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Conserved domains on  [gi|42571361|ref|NP_973771|]
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GSK3/SHAGGY-like protein kinase 1 [Arabidopsis thaliana]

Protein Classification

GSK family serine/threonine-protein kinase( domain architecture ID 10197641)

GSK (glycogen synthase kinase) family serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
65-357 0e+00

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: 597.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  65 KQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSR-DELFLNL 143
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKkDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVK 223
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSL-GICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNPNYT 303
Cdd:cd14137 160 GEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYT 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 304 DFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNEL 357
Cdd:cd14137 240 EFKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
65-357 0e+00

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: 597.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  65 KQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSR-DELFLNL 143
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKkDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVK 223
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSL-GICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNPNYT 303
Cdd:cd14137 160 GEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYT 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 304 DFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNEL 357
Cdd:cd14137 240 EFKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
59-396 9.66e-147

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 423.68  E-value: 9.66e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   59 GKNGEPKQTI----------SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLKH 128
Cdd:PTZ00036  47 GEDEDEEKMIdndinrspnkSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHINIIFLKD 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  129 CFFSTTSRDE---LFLNLVMEYVPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDP 205
Cdd:PTZ00036 127 YYYTECFKKNeknIFLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHS-KFICHRDLKPQNLLIDP 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  206 LTHQVKLCDFGSAKVLVKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK 285
Cdd:PTZ00036 206 NTHTLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQ 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  286 VLGTPTREEIRCMNPNYTDFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLP 365
Cdd:PTZ00036 286 VLGTPTEDQLKEMNPNYADIKFPDVKPKDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRDPCIKLP 365
                        330       340       350
                 ....*....|....*....|....*....|...
gi 42571361  366 NG-RPLPPLFNF-KQELGGASMELINRLIPEHV 396
Cdd:PTZ00036 366 KYiDKLPDLFNFcDAEIKEMSDACRRKIIPKCT 398
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
70-354 1.18e-81

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 250.91  E-value: 1.18e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361     70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV-----LQDRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLV 144
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIkkkkiKKDRERILREIKILKKLKHPNIVRLYDVF-----EDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    145 MEYVPE-TLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK 223
Cdd:smart00220  76 MEYCEGgDLFDLLK----KRGRLSEDEARFYLRQILSALEYLHSK-GIVHRDLKPENILLDE-DGHVKLADFGLARQLDP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    224 GEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIkvlgtptreeircMNPNYT 303
Cdd:smart00220 150 GEKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI-------------GKPKPP 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 42571361    304 DFRfpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:smart00220 216 FPP------------PEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
70-354 5.99e-52

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 173.20  E-value: 5.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFfsttsRDELFLNL 143
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKkdknilREIKILKKLNHPNIVRLYDAF-----EDKDNLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   144 VMEYVP-ETLYRVLRHYTSsnqrMPIFYVKLYTYQIFRGLAyihtvpgvchrdvkpqnllvdplthqvklcdfgsakvlv 222
Cdd:pfam00069  76 VLEYVEgGSLFDLLSEKGA----FSEREAKFIMKQILEGLE--------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   223 KGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIkvlgtptreeIRCMNPNY 302
Cdd:pfam00069 113 SGSSLTTFVGTPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGING-NEIYELI----------IDQPYAFP 180
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42571361   303 TdfrfpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:pfam00069 181 E---------------LPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
73-373 8.45e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 153.63  E-value: 8.45e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVAIKKVLQD--------RRYKnRELQLMRPMDHPNVISLKHCFfstTSRDELFLnlV 144
Cdd:COG0515  12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPElaadpearERFR-REARALARLNHPNIVRVYDVG---EEDGRPYL--V 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP-ETLYRVLRHytssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvk 223
Cdd:COG0515  86 MEYVEgESLADLLRR----RGPLPPAEALRILAQLAEALAAAHAA-GIVHRDIKPANILLTP-DGRVKLIDFGIARAL-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY----ICSRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREeircmn 299
Cdd:COG0515 158 GGATLTQtgtvVGTPGYMAPEQARGE-PVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSE------ 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 300 pnytdfrfpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLR-------CTALEACAHPFFNELREPNARLPNGRPLPP 372
Cdd:COG0515 231 -------------------LRPDLPPALDAIVLRALAKDPEERyqsaaelAAALRAVLRSLAAAAAAAAAAAAAAAAAAA 291

                .
gi 42571361 373 L 373
Cdd:COG0515 292 A 292
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
75-277 2.25e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   75 VVGTGSFGIVFQAKCLETGESVAIKkVLQD---------RRYKnRELQLMRPMDHPNVISLkhcfFSTTSRDELFLnLVM 145
Cdd:NF033483  14 RIGRGGMAEVYLAKDTRLDRDVAVK-VLRPdlardpefvARFR-REAQSAASLSHPNIVSV----YDVGEDGGIPY-IVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  146 EYVP-ETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkG 224
Cdd:NF033483  87 EYVDgRTLKDYIR----EHGPLSPEEAVEIMIQILSALEHAHRN-GIVHRDIKPQNILITK-DGRVKVTDFGIARAL--S 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361  225 EPNISY----ICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSV 277
Cdd:NF033483 159 STTMTQtnsvLGTVHYLSPEQARGGT-VDARSDIYSLGIVLYEMLTGRPPFDGDSPV 214
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
91-347 6.39e-11

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 64.48  E-value: 6.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361     91 ETGESVAIKKVLQD-----RRYK--NRELQLMRPMDHPNVISLkhcfFSTTSRDELFLNLVMEYVPEtlyRVLRHYTSSN 163
Cdd:TIGR03903    1 MTGHEVAIKLLRTDapeeeHQRArfRRETALCARLYHPNIVAL----LDSGEAPPGLLFAVFEYVPG---RTLREVLAAD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    164 QRMP-IFYVKLYTyQIFRGLAYIHTvPGVCHRDVKPQNLLVDP--LTHQVKLCDFGSAKVLVKGEPNI--------SYIC 232
Cdd:TIGR03903   74 GALPaGETGRLML-QVLDALACAHN-QGIVHRDLKPQNIMVSQtgVRPHAKVLDFGIGTLLPGVRDADvatltrttEVLG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    233 SRYYRAPELIFGATEyTASIDIWSAGCVLAELLLGQPLFPGENsvdqLVEIIKvlgtptreeiRCMNPnyTDFRFPQ-IK 311
Cdd:TIGR03903  152 TPTYCAPEQLRGEPV-TPNSDLYAWGLIFLECLTGQRVVQGAS----VAEILY----------QQLSP--VDVSLPPwIA 214
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 42571361    312 AHPWHKVFHKRM---PPEAIDLASRLLQYSPSLRCTALE 347
Cdd:TIGR03903  215 GHPLGQVLRKALnkdPRQRAASAPALAERFRALELCALV 253
 
Name Accession Description Interval E-value
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
65-357 0e+00

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: 597.18  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  65 KQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSR-DELFLNL 143
Cdd:cd14137   1 PVEISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRLKHPNIVKLKYFFYSSGEKkDEVYLNL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVK 223
Cdd:cd14137  81 VMEYMPETLYRVIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSL-GICHRDIKPQNLLVDPETGVLKLCDFGSAKRLVP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNPNYT 303
Cdd:cd14137 160 GEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTPTREQIKAMNPNYT 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 304 DFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNEL 357
Cdd:cd14137 240 EFKFPQIKPHPWEKVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
59-396 9.66e-147

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 423.68  E-value: 9.66e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   59 GKNGEPKQTI----------SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLKH 128
Cdd:PTZ00036  47 GEDEDEEKMIdndinrspnkSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHINIIFLKD 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  129 CFFSTTSRDE---LFLNLVMEYVPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDP 205
Cdd:PTZ00036 127 YYYTECFKKNeknIFLNVVMEFIPQTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHS-KFICHRDLKPQNLLIDP 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  206 LTHQVKLCDFGSAKVLVKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK 285
Cdd:PTZ00036 206 NTHTLKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQ 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  286 VLGTPTREEIRCMNPNYTDFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLP 365
Cdd:PTZ00036 286 VLGTPTEDQLKEMNPNYADIKFPDVKPKDLKKVFPKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLRDPCIKLP 365
                        330       340       350
                 ....*....|....*....|....*....|...
gi 42571361  366 NG-RPLPPLFNF-KQELGGASMELINRLIPEHV 396
Cdd:PTZ00036 366 KYiDKLPDLFNFcDAEIKEMSDACRRKIIPKCT 398
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
70-392 1.76e-92

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: 281.34  E-value: 1.76e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCF--FSTTSRDELFL 141
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKIsnvfddLIDAKRILREIKILRHLKHENIIGLLDILrpPSPEEFNDVYI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 nlVMEYVPETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVL 221
Cdd:cd07834  82 --VTELMETDLHKVIK----SPQPLTDDHIQYFLYQILRGLKYLHSA-GVIHRDLKPSNILVN-SNCDLKICDFGLARGV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNI---SYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCM 298
Cdd:cd07834 154 DPDEDKGfltEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEEDLKFI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 299 -NPNYTDF--RFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNaRLPNGRPLPPLFN 375
Cdd:cd07834 234 sSEKARNYlkSLPKKPKKPLSEVF-PGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDPE-DEPVAKPPFDFPF 311
                       330
                ....*....|....*..
gi 42571361 376 FkqELGGASMELINRLI 392
Cdd:cd07834 312 F--DDEELTIEELKELI 326
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
74-354 4.01e-88

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: 267.18  E-value: 4.01e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN---RELQLMR----PMDHPNVISLKHCFFSTTSRDelfLNLVME 146
Cdd:cd05118   5 RKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKaalREIKLLKhlndVEGHPNIVKLLDVFEHRGGNH---LCLVFE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKGEP 226
Cdd:cd05118  82 LMGMNLYELIKDY---PRGLPLDLIKSYLYQLLQALDFLHSN-GIIHRDLKPENILINLELGQLKLADFGLARSFTSPPY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NIsYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTptreeircmnpnytdfr 306
Cdd:cd05118 158 TP-YVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGT----------------- 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 307 fpqikahpwhkvfhkrmpPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd05118 220 ------------------PEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
76-355 3.37e-86

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: 263.81  E-value: 3.37e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPM-------DHPNVISLKHCFFSTTSrdelfLNLVMEYV 148
Cdd:cd07832   8 IGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIkalqacqGHPYVVKLRDVFPHGTG-----FVLVFEYM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNI 228
Cdd:cd07832  83 LSSLSEVLRD---EERPLTEAQVKRYMRMLLKGVAYMHAN-RIMHRDLKPANLLISS-TGVLKIADFGLARLFSEEDPRL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SY--ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTRE---EIRCMnPNYT 303
Cdd:cd07832 158 YShqVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTPNEKtwpELTSL-PDYN 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 304 DFRFPQIKAHPWHKVFHKrMPPEAIDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:cd07832 237 KITFPESKGIRLEEIFPD-CSPEAIDLLKGLLVYNPKKRLSAEEALRHPYFF 287
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
76-354 1.96e-85

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: 261.65  E-value: 1.96e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRyKN-------RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYV 148
Cdd:cd07829   7 LGEGTYGVVYKAKDKKTGEIVALKKIRLDNE-EEgipstalREISLLKELKHPNIVKLLDVIHTENK-----LYLVFEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkGEPNI 228
Cdd:cd07829  81 DQDLKKYLDKR---PGPLPPNLIKSIMYQLLRGLAYCHSH-RILHRDLKPQNLLINR-DGVLKLADFGLARAF--GIPLR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIR--CMNPNYt 303
Cdd:cd07829 154 TYtheVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWPgvTKLPDY- 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 304 DFRFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07829 233 KPTFPKWPKNDLEKVL-PRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
70-354 1.18e-81

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 250.91  E-value: 1.18e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361     70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV-----LQDRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLV 144
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIkkkkiKKDRERILREIKILKKLKHPNIVRLYDVF-----EDEDKLYLV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    145 MEYVPE-TLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK 223
Cdd:smart00220  76 MEYCEGgDLFDLLK----KRGRLSEDEARFYLRQILSALEYLHSK-GIVHRDLKPENILLDE-DGHVKLADFGLARQLDP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    224 GEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIkvlgtptreeircMNPNYT 303
Cdd:smart00220 150 GEKLTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKI-------------GKPKPP 215
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 42571361    304 DFRfpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:smart00220 216 FPP------------PEWDISPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
74-354 1.08e-79

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: 247.06  E-value: 1.08e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQdrRYKN-------RELQLMRPM-DHPNVISLKHCFfsttsRDELFLNLVM 145
Cdd:cd07830   5 KQLGDGTFGSVYLARNKETGELVAIKKMKK--KFYSweecmnlREVKSLRKLnEHPNIVKLKEVF-----RENDELYFVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVLRHYTssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLThQVKLCDFGSAKVLVKGE 225
Cdd:cd07830  78 EYMEGNLYQLMKDRK--GKPFSESVIRSIIYQILQGLAHIHKH-GFFHRDLKPENLLVSGPE-VVKIADFGLAREIRSRP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREE-------IRCM 298
Cdd:cd07830 154 PYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDwpegyklASKL 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 299 NpnytdFRFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07830 234 G-----FRFPQFAPTSLHQLI-PNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
75-354 1.21e-78

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: 244.53  E-value: 1.21e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFfstTSRDELFLnlVMEYV 148
Cdd:cd07833   8 VVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDvkktalREVKVLRQLRHENIVNLKEAF---RRKGRLYL--VFEYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHYTSSnqrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLV--KGEP 226
Cdd:cd07833  83 ERTLLELLEASPGG---LPPDAVRSYIWQLLQAIAYCHSH-NIIHRDIKPENILVSE-SGVLKLCDFGFARALTarPASP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLG--TPTREEIRCMNPNYTD 304
Cdd:cd07833 158 LTDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGplPPSHQELFSSNPRFAG 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 305 FRFPQIKA-HPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07833 238 VAFPEPSQpESLERRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
70-360 2.11e-76

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: 239.01  E-value: 2.11e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN---------RELQLMRPMDHPNVISLKHCFfstTSRDelF 140
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEAkdginftalREIKLLQELKHPNIIGLLDVF---GHKS--N 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVPETLYRVLRhytSSNQRMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd07841  77 INLVFEFMETDLEKVIK---DKSIVLTPADIKSYMLMTLRGLEYLH-SNWILHRDLKPNNLLIAS-DGVLKLADFGLARS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LvkGEPNISYIC---SRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRC 297
Cdd:cd07841 152 F--GSPNRKMTHqvvTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWPG 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 298 MN--PNYTDFRFpqIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREP 360
Cdd:cd07841 230 VTslPDYVEFKP--FPPTPLKQIF-PAASDDALDLLQRLLTLNPNKRITARQALEHPYFSNDPAP 291
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
76-362 4.98e-74

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: 234.37  E-value: 4.98e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVL------QD--RRYknRELQLMRPM-DHPNVISLKHCFFSTTSRDelfLNLVME 146
Cdd:cd07852  15 LGKGAYGIVWKAIDKKTGEVVALKKIFdafrnaTDaqRTF--REIMFLQELnDHPNIIKLLNVIRAENDKD---IYLVFE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHytssNQRMPIfYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEP 226
Cdd:cd07852  90 YMETDLHAVIRA----NILEDI-HKQYIMYQLLKALKYLHS-GGVIHRDLKPSNILLNSDCR-VKLADFGLARSLSQLEE 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NIS------YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNP 300
Cdd:cd07852 163 DDEnpvltdYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQLEKIIEVIGRPSAEDIESIQS 242
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 301 NYTD---FRFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHP----FFNELREPNA 362
Cdd:cd07852 243 PFAAtmlESLPPSRPKSLDELF-PKASPDALDLLKKLLVFNPNKRLTAEEALRHPyvaqFHNPADEPSL 310
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
76-354 7.11e-73

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: 229.76  E-value: 7.11e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLK---HCFFSTTSRDELFLnlVME 146
Cdd:cd07840   7 IGEGTYGQVYKARNKKTGELVALKKIRMENEKEGfpitaiREIKLLQKLDHPNVVRLKeivTSKGSAKYKGSIYM--VFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEP 226
Cdd:cd07840  85 YMDHDLTGLLDNP---EVKFTESQIKCYMKQLLEGLQYLHS-NGILHRDIKGSNILINN-DGVLKLADFGLARPYTKENN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NI--SYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTRE---EIRCMnPN 301
Cdd:cd07840 160 ADytNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEEnwpGVSDL-PW 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 302 YTDFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07840 239 FENLKPKKPYKRRLREVFKNVIDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
70-392 1.14e-72

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 230.72  E-value: 1.14e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDELFLNL 143
Cdd:cd07858   7 YVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIanafdnRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHREAFNDVYI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV-LV 222
Cdd:cd07858  87 VYELMDTDLHQIIR----SSQTLSDDHCQYFLYQLLRGLKYIHSA-NVLHRDLKPSNLLLNA-NCDLKICDFGLARTtSE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCM-NPN 301
Cdd:cd07858 161 KGDFMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEEDLGFIrNEK 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 302 YTDF--RFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLPNGRPlpplFNFKQE 379
Cdd:cd07858 241 ARRYirSLPYTPRQSFARLF-PHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLHDPSDEPVCQTP----FSFDFE 315
                       330
                ....*....|...
gi 42571361 380 LGGASMELINRLI 392
Cdd:cd07858 316 EDALTEEDIKELI 328
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
70-361 1.56e-72

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: 230.64  E-value: 1.56e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQ--------DRRYknRELQLMRPMDHPNVISLKHCFFSTTSRDElFL 141
Cdd:cd07851  17 YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRpfqsaihaKRTY--RELRLLKHMKHENVIGLLDVFTPASSLED-FQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 N--LVMEYVPETLYRVLRHytssnQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAK 219
Cdd:cd07851  94 DvyLVTHLMGADLNNIVKC-----QKLSDDHIQFLVYQILRGLKYIHSA-GIIHRDLKPSNLAVNE-DCELKILDFGLAR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VlvKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMN 299
Cdd:cd07851 167 H--TDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDEELLKKIS 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 300 P----NYTDfRFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPN 361
Cdd:cd07851 245 SesarNYIQ-SLPQMPKKDFKEVF-SGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLAEYHDPE 308
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
70-398 7.35e-72

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: 228.73  E-value: 7.35e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV-------LQDRRYknRELQLMRPMDHPNVISLKHCFFSTT--SRDELF 140
Cdd:cd07849   7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIspfehqtYCLRTL--REIKILLRFKHENIIGILDIQRPPTfeSFKDVY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LnlVMEYVPETLYRVLRHYTSSNQrmpifYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd07849  85 I--VQELMETDLYKLIKTQHLSND-----HIQYFLYQILRGLKYIHSA-NVLHRDLKPSNLLLNT-NCDLKICDFGLARI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNIS----YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIR 296
Cdd:cd07849 156 ADPEHDHTGflteYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPSQEDLN 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 297 CM-NPNYTDF--RFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLPNGRPLPPL 373
Cdd:cd07849 236 CIiSLKARNYikSLPFKPKVPWNKLF-PNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHDPSDEPVAEEPFPFD 314
                       330       340
                ....*....|....*....|....*
gi 42571361 374 FNFKQELggaSMELINRLIPEHVRR 398
Cdd:cd07849 315 MELFDDL---PKEKLKELIFEEIMR 336
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
69-392 7.56e-69

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: 220.70  E-value: 7.56e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHcFFSTTSRDELFLN 142
Cdd:cd07855   6 RYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnafdvVTTAKRTLRELKILRHFKHDNIIAIRD-ILRPKVPYADFKD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 --LVMEYVPETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV 220
Cdd:cd07855  85 vyVVLDLMESDLHHIIH----SDQPLTLEHIRYFLYQLLRGLKYIHSA-NVIHRDLKPSNLLVNENCE-LKIGDFGMARG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPN-----ISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEI 295
Cdd:cd07855 159 LCTSPEEhkyfmTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPSQAVI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 296 RCMNP----NYTDfRFPQIKAHPWHKVFHKRmPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNarlpNGRPLP 371
Cdd:cd07855 239 NAIGAdrvrRYIQ-NLPNKQPVPWETLYPKA-DQQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDPD----DEPDCA 312
                       330       340
                ....*....|....*....|.
gi 42571361 372 PLFNFKQELGGASMELINRLI 392
Cdd:cd07855 313 PPFDFDFDAEALTREALKEAI 333
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
76-354 6.96e-67

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: 214.08  E-value: 6.96e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLkHCFFSTTSRdelfLNLVMEYvp 149
Cdd:cd07835   7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGvpstaiREISLLKELNHPNIVRL-LDVVHSENK----LYLVFEF-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 etLYRVLRHY--TSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkGEPN 227
Cdd:cd07835  80 --LDLDLKKYmdSSPLTGLDPPLIKSYLYQLLQGIAFCHS-HRVLHRDLKPQNLLIDT-EGALKLADFGLARAF--GVPV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTRE---EIRCMnPN 301
Cdd:cd07835 154 RTYtheVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDvwpGVTSL-PD 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 302 YTDfRFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07835 233 YKP-TFPKWARQDLSKVV-PSLDEDGLDLLSQMLVYDPAKRISAKAALQHPYF 283
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
77-354 2.84e-65

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: 209.82  E-value: 2.84e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKKVLQdrRYKN-------RELQLMRPM-DHPNVISLKHCFF-STTSRdelfLNLVMEY 147
Cdd:cd07831   8 GEGTFSEVLKAQSRKTGKYYAIKCMKK--HFKSleqvnnlREIQALRRLsPHPNILRLIEVLFdRKTGR----LALVFEL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETLYRVL---RHYTSSNQrmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLThqVKLCDFGSAKVLVKG 224
Cdd:cd07831  82 MDMNLYELIkgrKRPLPEKR------VKNYMYQLLKSLDHMHR-NGIFHRDIKPENILIKDDI--LKLADFGSCRGIYSK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNP-NYT 303
Cdd:cd07831 153 PPYTEYISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVLKKFRKsRHM 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 304 DFRFPQIKAH--PWHKVfhkRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07831 233 NYNFPSKKGTglRKLLP---NASAEGLDLLKKLLAYDPDERITAKQALRHPYF 282
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
70-378 4.07e-62

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: 203.47  E-value: 4.07e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDELFLNL 143
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKIndvfehVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRREFKDIYV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK 223
Cdd:cd07859  82 VFELMESDLHQVIK----ANDDLTPEHHQFFLYQLLRALKYIHTA-NVFHRDLKPKNILANA-DCKLKICDFGLARVAFN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPN----ISYICSRYYRAPELIfGA--TEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEI-R 296
Cdd:cd07859 156 DTPTaifwTDYVATRWYRAPELC-GSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETIsR 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 297 CMNPNYTDFRFPQIKAHPwhKVFHKRMP---PEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNaRLPNGRPLPPL 373
Cdd:cd07859 235 VRNEKARRYLSSMRKKQP--VPFSQKFPnadPLALRLLERLLAFDPKDRPTAEEALADPYFKGLAKVE-REPSAQPITKL 311

                ....*.
gi 42571361 374 -FNFKQ 378
Cdd:cd07859 312 eFEFER 317
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
67-360 2.51e-61

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: 201.26  E-value: 2.51e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  67 TISYMAERVVGTGSFGIVFQAKCLETGESVAIKK--------VLQDRRYknRELQLMRPMDHPNVISLKHCFFSTtSRDE 138
Cdd:cd07856   9 TTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKimkpfstpVLAKRTY--RELKLLKHLRHENIISLSDIFISP-LEDI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 139 LFlnlVMEYVPETLYRVLRHYTSSNQrmpifYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSA 218
Cdd:cd07856  86 YF---VTELLGTDLHRLLTSRPLEKQ-----FIQYFLYQILRGLKYVHSA-GVIHRDLKPSNILVNE-NCDLKICDFGLA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVlvkGEPNIS-YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRC 297
Cdd:cd07856 156 RI---QDPQMTgYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTPPDDVINT 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 298 MNPNYTdFRF----PQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREP 360
Cdd:cd07856 233 ICSENT-LRFvqslPKRERVPFSEKF-KNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLAPYHDP 297
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
75-354 2.72e-61

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: 199.57  E-value: 2.72e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQD------RRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYV 148
Cdd:cd07846   8 LVGEGSYGMVMKCRHKETGQIVAIKKFLESeddkmvKKIAMREIKMLKQLRHENLVNLIEVF-----RRKKRWYLVFEFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHYTSSNQRMpifYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK-GEPN 227
Cdd:cd07846  83 DHTVLDDLEKYPNGLDES---RVRKYLFQILRGIDFCHS-HNIIHRDIKPENILVSQ-SGVVKLCDFGFARTLAApGEVY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGT--PTREEIRCMNPNYTDF 305
Cdd:cd07846 158 TDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNliPRHQELFQKNPLFAGV 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42571361 306 RFPQIK-AHPWHKVFHKrMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07846 238 RLPEVKeVEPLERRYPK-LSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
70-354 4.16e-61

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: 199.69  E-value: 4.16e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYK--NRELQLMRPM-DHPNVISLKHCFfsttsRDELFLN--LV 144
Cdd:cd14132  20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIK-VLKPVKKKkiKREIKILQNLrGGPNIVKLLDVV-----KDPQSKTpsLI 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPETLYRVLRHYTSSNQrmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKG 224
Cdd:cd14132  94 FEYVNNTDFKTLYPTLTDYD------IRYYMYELLKALDYCHSK-GIMHRDVKPHNIMIDHEKRKLRLIDWGLAEFYHPG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLG-QPLFPGENSVDQLVEIIKVLGTptrEEIrcMN---- 299
Cdd:cd14132 167 QEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRkEPFFHGHDNYDQLVKIAKVLGT---DDL--YAyldk 241
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 300 -----PNYTDFRFPQIKAHPWHKVFHKR----MPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14132 242 ygielPPRLNDILGRHSKKPWERFVNSEnqhlVTPEALDLLDKLLRYDHQERITAKEAMQHPYF 305
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
76-361 7.56e-61

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: 199.94  E-value: 7.56e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLET--GESVAIKKV--------LQDRRYknRELQLMRPM-DHPNVISLKHCFFSTTSR-DELFLnl 143
Cdd:cd07857   8 LGQGAYGIVCSARNAETseEETVAIKKItnvfskkiLAKRAL--RELKLLRHFrGHKNITCLYDMDIVFPGNfNELYL-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAK---- 219
Cdd:cd07857  84 YEELMEADLHQIIR----SGQPLTDAHFQSFIYQILCGLKYIHSA-NVLHRDLKPGNLLVN-ADCELKICDFGLARgfse 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEPNIS-YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEI-RC 297
Cdd:cd07857 158 NPGENAGFMTeYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPDEETLsRI 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 298 MNPNYTDF--RFPQIKAHPWHKVFHKrMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPN 361
Cdd:cd07857 238 GSPKAQNYirSLPNIPKKPFESIFPN-ANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIWHDPD 302
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
76-361 2.22e-60

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: 199.02  E-value: 2.22e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV--------LQDRRYknRELQLMRPMDHPNVISLKHCFFSTTSRDELF-LNLVME 146
Cdd:cd07880  23 VGSGAYGTVCSALDRRTGAKVAIKKLyrpfqselFAKRAY--RELRLLKHMKHENVIGLLDVFTPDLSLDRFHdFYLVMP 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVlvKGEP 226
Cdd:cd07880 101 FMGTDLGKLMKHEKLSEDR-----IQFLVYQMLKGLKYIHAA-GIIHRDLKPGNLAVNE-DCELKILDFGLARQ--TDSE 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNP----NY 302
Cdd:cd07880 172 MTGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLQSedakNY 251
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 303 TDfRFPQIKahpwHKVFHKRMP---PEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPN 361
Cdd:cd07880 252 VK-KLPRFR----KKDFRSLLPnanPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDPE 308
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
69-354 4.43e-60

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: 196.45  E-value: 4.43e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRR----YKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd07844   1 TYKKLDKLGEGSYATVYKGRSKLTGQLVALKEIrLEHEEgapfTAIREASLLKDLKHANIVTLHDIIHTKKT-----LTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRHYTSSnqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLThQVKLCDFGSAKVlvK 223
Cdd:cd07844  76 VFEYLDTDLKQYMDDCGGG---LSMHNVRLFLFQLLRGLAYCHQ-RRVLHRDLKPQNLLISERG-ELKLADFGLARA--K 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPG-ENSVDQLVEIIKVLGTPTREEIR--C 297
Cdd:cd07844 149 SVPSKTYsneVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGsTDVEDQLHKIFRVLGTPTEETWPgvS 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 298 MNPNYTDFRFPQIKAHPWHKVFHK-RMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07844 229 SNPEFKPYSFPFYPPRPLINHAPRlDRIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
76-354 5.35e-60

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: 196.34  E-value: 5.35e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVlqdrRYKN----------RELQLMRPMD---HPNVISLKH-CFFSTTSRdELFL 141
Cdd:cd07838   7 IGEGAYGTVYKARDLQDGRFVALKKV----RVPLseegiplstiREIALLKQLEsfeHPNVVRLLDvCHGPRTDR-ELKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPETLYRVLRHYTSSNqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd07838  82 TLVFEHVDQDLATYLDKCPKPG--LPPETIKDLMRQLLRGLDFLHS-HRIVHRDLKPQNILVTS-DGQVKLADFGLARIY 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEircmnpn 301
Cdd:cd07838 158 SFEMALTSVVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPSEEE------- 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 302 ytdfrFPQIKAHPWHKvFHKR-----------MPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07838 230 -----WPRNSALPRSS-FPSYtprpfksfvpeIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
76-356 6.75e-59

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: 194.12  E-value: 6.75e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSTtSRDELFLnlVMEYVP 149
Cdd:cd07845  15 IGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGipisslREITLLLNLRHPNIVELKEVVVGK-HLDSIFL--VMEYCE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVLRHYTSSnqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTHQ--VKLCDFGSAKVLvkGEPN 227
Cdd:cd07845  92 QDLASLLDNMPTP---FSESQVKCLMLQLLRGLQYLHE-NFIIHRDLKVSNLL---LTDKgcLKIADFGLARTY--GLPA 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTrEEI----RCMnP 300
Cdd:cd07845 163 KPMtpkVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPN-ESIwpgfSDL-P 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 301 NYTDFRFPQikaHPWHKVFHKrMP--PEA-IDLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd07845 241 LVGKFTLPK---QPYNNLKHK-FPwlSEAgLRLLNFLLMYDPKKRATAEEALESSYFKE 295
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
76-354 1.25e-58

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: 193.66  E-value: 1.25e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLE--TGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLVME 146
Cdd:cd07842   8 IGRGTYGRVYKAKRKNgkDGKEYAIKKFKGDKEQYTgisqsacREIALLRELKHENVVSLVEVFLEHADKS---VYLLFD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRM-PIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV---DPLTHQVKLCDFGSA---- 218
Cdd:cd07842  85 YAEHDLWQIIKFHRQAKRVSiPPSMVKSLLWQILNGIHYLHS-NWVLHRDLKPANILVmgeGPERGVVKIGDLGLArlfn 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 ---KVLVKGEPNISYIcsrYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENS---------VDQLVEIIKV 286
Cdd:cd07842 164 aplKPLADLDPVVVTI---WYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqRDQLERIFEV 240
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 287 LGTPTREE---IRCMnPNYTDF-------RFPQIKAHPW-HKvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07842 241 LGTPTEKDwpdIKKM-PEYDTLksdtkasTYPNSLLAKWmHK--HKKPDSQGFDLLRKLLEYDPTKRITAEEALEHPYF 316
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
76-354 2.35e-58

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: 192.20  E-value: 2.35e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQD------RRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYVP 149
Cdd:cd07847   9 IGEGSYGVVFKCRNRETGQIVAIKKFVESeddpviKKIALREIRMLKQLKHPNLVNLIEVF-----RRKRKLHLVFEYCD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVLRHYTssnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNIS 229
Cdd:cd07847  84 HTVLNELEKNP---RGVPEHLIKKIIWQTLQAVNFCHK-HNCIHRDVKPENILITK-QGQIKLCDFGFARILTGPGDDYT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 230 -YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLG--TPTREEIRCMNpNYtdFR 306
Cdd:cd07847 159 dYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGdlIPRHQQIFSTN-QF--FK 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 307 FPQIKAHPWHKVFHKRMP---PEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07847 236 GLSIPEPETREPLESKFPnisSPALSFLKGCLQMDPTERLSCEELLEHPYF 286
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
76-354 3.04e-58

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: 191.56  E-value: 3.04e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVP 149
Cdd:cd07860   8 IGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGvpstaiREISLLKELNHPNIVKLLDVIHTENK-----LYLVFEFLH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVLRhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLvkGEPNIS 229
Cdd:cd07860  83 QDLKKFMD--ASALTGIPLPLIKSYLFQLLQGLAFCHS-HRVLHRDLKPQNLLINTEGA-IKLADFGLARAF--GVPVRT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 230 Y---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREeircMNPNYT--- 303
Cdd:cd07860 157 YtheVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEV----VWPGVTsmp 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 304 DFR--FPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07860 233 DYKpsFPKWARQDFSKVV-PPLDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
79-354 3.12e-58

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: 192.05  E-value: 3.12e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  79 GSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSTTSrDELFLnlVMEYVPETL 152
Cdd:cd07843  16 GTYGVVYRARDKKTGEIVALKKLKMEKEKEGfpitslREINILLKLQHPNIVTVKEVVVGSNL-DKIYM--VMEYVEHDL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 153 YRVLRHytsSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTH--QVKLCDFGSAKVLvkGEPNISY 230
Cdd:cd07843  93 KSLMET---MKQPFLQSEVKCLMLQLLSGVAHLHD-NWILHRDLKTSNLL---LNNrgILKICDFGLAREY--GSPLKPY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 ---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIrcmnPNYTDFRF 307
Cdd:cd07843 164 tqlVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEKIW----PGFSELPG 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 308 PQIKAHPWH------KVF-HKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07843 240 AKKKTFTKYpynqlrKKFpALSLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
70-361 7.23e-58

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: 192.42  E-value: 7.23e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKK--------VLQDRRYknRELQLMRPMDHPNVISLKHCFFSTTSRDELF- 140
Cdd:cd07879  17 YTSLKQVGSGAYGSVCSAIDKRTGEKVAIKKlsrpfqseIFAKRAY--RELTLLKHMQHENVIGLLDVFTSAVSGDEFQd 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVPETLYRVLRHYTSSNQrmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKv 220
Cdd:cd07879  95 FYLVMPYMQTDLQKIMGHPLSEDK------VQYLVYQMLCGLKYIHSA-GIIHRDLKPGNLAVNE-DCELKILDFGLAR- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 lvKGEPNIS-YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMN 299
Cdd:cd07879 166 --HADAEMTgYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGPEFVQKLE 243
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 300 ----PNYTDfRFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPN 361
Cdd:cd07879 244 dkaaKSYIK-SLPKYPRKDFSTLF-PKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSFRDAD 307
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
70-365 1.69e-57

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: 191.53  E-value: 1.69e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVL--QDRRYKN--RELQLMRPMDHPNVISLKHCFFSTTSRDELFLN--- 142
Cdd:cd07854   7 YMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVltDPQSVKHalREIKIIRRLDHDNIVKVYEVLGPSGSDLTEDVGslt 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 ------LVMEYVPETLYRVLRHYTSSNQrmpifYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFG 216
Cdd:cd07854  87 elnsvyIVQEYMETDLANVLEQGPLSEE-----HARLFMYQLLRGLKYIHSA-NVLHRDLKPANVFINTEDLVLKIGDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 SAKVLvkgEPNISY-------ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQL---VEIIKV 286
Cdd:cd07854 161 LARIV---DPHYSHkgylsegLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMqliLESVPV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 287 LGTPTREEIRCMNPNYtdfrfpqIKAHPW--HKVFHKRMP---PEAIDLASRLLQYSPSLRCTALEACAHPFF----NEL 357
Cdd:cd07854 238 VREEDRNELLNVIPSF-------VRNDGGepRRPLRDLLPgvnPEALDFLEQILTFNPMDRLTAEEALMHPYMscysCPF 310

                ....*...
gi 42571361 358 REPNARLP 365
Cdd:cd07854 311 DEPVSLHP 318
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
76-354 1.94e-57

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: 189.61  E-value: 1.94e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLkHCFFSTTSRdelfLNLVMEYVPE 150
Cdd:cd07836   8 LGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTpstaiREISLMKELKHENIVRL-HDVIHTENK----LMLVFEYMDK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkGEPNISY 230
Cdd:cd07836  83 DLKKYMDTHGVRGA-LDPNTVKSFTYQLLKGIAFCHE-NRVLHRDLKPQNLLINK-RGELKLADFGLARAF--GIPVNTF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 ---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMN--PNYTDf 305
Cdd:cd07836 158 sneVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISqlPEYKP- 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 306 RFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07836 237 TFPRYPPQDLQQLF-PHADPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
76-354 3.42e-56

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: 186.48  E-value: 3.42e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSttsrdELFLNLVMEYVP 149
Cdd:cd07839   8 IGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGvpssalREICLLKELKHKNIVRLYDVLHS-----DKKLTLVFEYCD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRvlrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkGEPNIS 229
Cdd:cd07839  83 QDLKK---YFDSCNGDIDPEIVKSFMFQLLKGLAFCHS-HNVLHRDLKPQNLLINK-NGELKLADFGLARAF--GIPVRC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 230 Y---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELL-LGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMN--PNYT 303
Cdd:cd07839 156 YsaeVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELAnAGRPLFPGNDVDDQLKRIFRLLGTPTEESWPGVSklPDYK 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 304 DF-RFPQIKAhpWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07839 236 PYpMYPATTS--LVNVV-PKLNSTGRDLLQNLLVCNPVQRISAEEALQHPYF 284
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
70-358 3.45e-56

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 186.56  E-value: 3.45e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSttsrdELFLNL 143
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGvpstaiREISLLKEMQHGNIVRLQDVVHS-----EKRLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  144 VMEYVPETLYRvlrHYTSS-----NQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVKLCDFGSA 218
Cdd:PLN00009  79 VFEYLDLDLKK---HMDSSpdfakNPRL----IKTYLYQILRGIAYCHS-HRVLHRDLKPQNLLIDRRTNALKLADFGLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  219 KVLvkGEPNISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEI 295
Cdd:PLN00009 151 RAF--GIPVRTFtheVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETW 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361  296 RCMN--PNYTDfRFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELR 358
Cdd:PLN00009 229 PGVTslPDYKS-AFPKWPPKDLATVV-PTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLG 291
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
76-355 1.22e-54

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: 182.73  E-value: 1.22e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSTTSRDELFLNLVMEYVP 149
Cdd:cd07837   9 IGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGvpstalREVSLLQMLSQSIYIVRLLDVEHVEENGKPLLYLVFEYLD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVLRHYTSSNQR-MPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKgePNI 228
Cdd:cd07837  89 TDLKKFIDSYGRGPHNpLPAKTIQSFMYQLCKGVAHCHS-HGVMHRDLKPQNLLVDKQKGLLKIADLGLGRAFTI--PIK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIrcmnPNYTDF 305
Cdd:cd07837 166 SYtheIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPNEEVW----PGVSKL 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 306 R----FPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:cd07837 242 RdwheYPQWKPQDLSRAV-PDLEPEGVDLLTKMLAYDPAKRISAKAALQHPYFD 294
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
75-354 1.89e-54

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: 182.74  E-value: 1.89e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMR---PMDHPNVISLKHCFfstTSRDelFLNLVM 145
Cdd:cd14210  20 VLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQqalvevKILKHLNdndPDDKHNIVRYKDSF---IFRG--HLCIVF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVLRhytSSN-QRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDPLTHQVKLCDFGSAkvLVK 223
Cdd:cd14210  95 ELLSINLYELLK---SNNfQGLSLSLIRKFAKQILQALQFLHKL-NIIHCDLKPENiLLKQPSKSSIKVIDFGSS--CFE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNPNYT 303
Cdd:cd14210 169 GEKVYTYIQSRFYRAPEVILGL-PYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVLGVPPKSLIDKASRRKK 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 304 DFrFPQIKAHPWHKVFHKRMPPEA--------------IDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14210 248 FF-DSNGKPRPTTNSKGKKRRPGSkslaqvlkcddpsfLDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
70-369 2.11e-53

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: 181.02  E-value: 2.11e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDELF-LN 142
Cdd:cd07878  17 YQNLTPVGSGAYGSVCSAYDTRLRQKVAVKKLsrpfqsLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSIENFNeVY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPETLYRVLRHytssnQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVlv 222
Cdd:cd07878  97 LVTNLMGADLNNIVKC-----QKLSDEHVQFLIYQLLRGLKYIHSA-GIIHRDLKPSNVAVNE-DCELRILDFGLARQ-- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNPNY 302
Cdd:cd07878 168 ADDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKISSEH 247
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 303 TDFRF---PQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARlPNGRP 369
Cdd:cd07878 248 ARKYIqslPHMPQQDLKKIF-RGANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQYHDPEDE-PEAEP 315
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
76-361 3.91e-53

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: 180.24  E-value: 3.91e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQ--------DRRYknRELQLMRPMDHPNVISLKHCFFSTTSRDELF-LNLVME 146
Cdd:cd07877  25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRpfqsiihaKRTY--RELRLLKHMKHENVIGLLDVFTPARSLEEFNdVYLVTH 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRhytssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVlvKGEP 226
Cdd:cd07877 103 LMGADLNNIVK-----CQKLTDDHVQFLIYQILRGLKYIHSA-DIIHRDLKPSNLAVNE-DCELKILDFGLARH--TDDE 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNP----NY 302
Cdd:cd07877 174 MTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSesarNY 253
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 303 TDfRFPQIKAHPWHKVFHKrMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPN 361
Cdd:cd07877 254 IQ-SLTQMPKMNFANVFIG-ANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPD 310
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
74-354 1.10e-52

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 176.17  E-value: 1.10e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKN-----RELQLMRPMDHPNVIslkHCFFstTSRDELFLNLVMEY 147
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDTGELMAVKEVeLSGDSEEElealeREIRILSSLKHPNIV---RYLG--TERTENTLNIFLEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPEtlyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEpN 227
Cdd:cd06606  81 VPG---GSLASLLKKFGKLPEPVVRKYTRQILEGLEYLH-SNGIVHRDIKGANILVDS-DGVVKLADFGCAKRLAEIA-T 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYICSR----YYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPG-ENSVDQLVEIIkvlgtpTREEIrcmnpny 302
Cdd:cd06606 155 GEGTKSLrgtpYWMAPEVIRG-EGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIG------SSGEP------- 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 303 tdfrfPQIKAHpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06606 221 -----PPIPEH---------LSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
70-355 1.18e-52

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: 178.76  E-value: 1.18e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVlqDRRYKN--------RELQLMRPMDHPNVISLKHCFFSTTSRDELF- 140
Cdd:cd07850   2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKL--SRPFQNvthakrayRELVLMKLVNHKNIIGLLNVFTPQKSLEEFQd 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVPETLYRVLrHYTSSNQRMPIFyvklyTYQIFRGLAYIHTVpGVCHRDVKPQNLLV-DPLThqVKLCDFGSAK 219
Cdd:cd07850  80 VYLVMELMDANLCQVI-QMDLDHERMSYL-----LYQMLCGIKHLHSA-GIIHRDLKPSNIVVkSDCT--LKILDFGLAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMN 299
Cdd:cd07850 151 TAGTSFMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTPSDEFMSRLQ 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 300 P---NYTDFRfPQIKAHPWHKVF------------HKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:cd07850 230 PtvrNYVENR-PKYAGYSFEELFpdvlfppdseehNKLKASQARDLLSKMLVIDPEKRISVDDALQHPYIN 299
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
76-355 1.93e-52

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 178.03  E-value: 1.93e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   76 VGTGSFGIVFQAKCLETGESVAIKKV---------LQDRRYKN---------RELQLMRPMDHPNVISLKHCFFSttsrd 137
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVkiieisndvTKDRQLVGmcgihfttlRELKIMNEIKHENIMGLVDVYVE----- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  138 ELFLNLVMEYVPETLYRVLrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGS 217
Cdd:PTZ00024  92 GDFINLVMDIMASDLKKVV----DRKIRLTESQVKCILLQILNGLNVLHKW-YFMHRDLSPANIFINS-KGICKIADFGL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  218 AK-----VLVKGEPNISYICSR----------YYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVE 282
Cdd:PTZ00024 166 ARrygypPYSDTLSKDETMQRReemtskvvtlWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGR 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361  283 IIKVLGTPTRE---EIRCMnPNYTDFRFPQIKAhpwHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:PTZ00024 246 IFELLGTPNEDnwpQAKKL-PLYTEFTPRKPKD---LKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFK 317
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
69-366 3.26e-52

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: 176.35  E-value: 3.26e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd07873   3 TYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGApctaiREVSLLKDLKHANIVTLHDIIHTEKS-----LTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLrhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVlvK 223
Cdd:cd07873  78 VFEYLDKDLKQYL---DDCGNSINMHNVKLFLFQLLRGLAYCHR-RKVLHRDLKPQNLLINE-RGELKLADFGLARA--K 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCM-- 298
Cdd:cd07873 151 SIPTKTYsneVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGIls 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 299 NPNYTDFRFPQIKAHPWHKvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLPN 366
Cdd:cd07873 231 NEEFKSYNYPKYRADALHN-HAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHSLGERIHKLPD 297
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
74-353 3.82e-52

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: 174.97  E-value: 3.82e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIkKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd05117   6 KVLGRGSFGVVRLAVHKKTGEEYAV-KIIDKKKLKSedeemlrREIEILKRLDHPNIVKLYEVF-----EDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVLRHYTSSNQrmpifYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDP--LTHQVKLCDFGSAKVLv 222
Cdd:cd05117  80 LCTggELFDRIVKKGSFSER-----EAAKIMKQILSAVAYLHSQ-GIVHRDLKPENILLASkdPDSPIKIIDFGLAKIF- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsvdqLVEIIkvlgtptrEEIrcMNPN 301
Cdd:cd05117 153 EEGEKLKTVCgTPYYVAPE-VLKGKGYGKKCDIWSLGVILYILLCGYPPFYGET----EQELF--------EKI--LKGK 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 302 YtDFRFPqikahPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd05117 218 Y-SFDSP-----EWKNV-----SEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
Pkinase pfam00069
Protein kinase domain;
70-354 5.99e-52

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 173.20  E-value: 5.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFfsttsRDELFLNL 143
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKkdknilREIKILKKLNHPNIVRLYDAF-----EDKDNLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   144 VMEYVP-ETLYRVLRHYTSsnqrMPIFYVKLYTYQIFRGLAyihtvpgvchrdvkpqnllvdplthqvklcdfgsakvlv 222
Cdd:pfam00069  76 VLEYVEgGSLFDLLSEKGA----FSEREAKFIMKQILEGLE--------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   223 KGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIkvlgtptreeIRCMNPNY 302
Cdd:pfam00069 113 SGSSLTTFVGTPWYMAPEVL-GGNPYGPKVDVWSLGCILYELLTGKPPFPGING-NEIYELI----------IDQPYAFP 180
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42571361   303 TdfrfpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:pfam00069 181 E---------------LPSNLSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
76-354 6.01e-52

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: 175.30  E-value: 6.01e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVlqdrRYKN----------RELQLMRPMDHPNVISLKHCFFsttsrDELFLNLVM 145
Cdd:cd07861   8 IGEGTYGVVYKGRNKKTGQIVAMKKI----RLESeeegvpstaiREISLLKELQHPNIVCLEDVLM-----QENRLYLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVLRHyTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkGE 225
Cdd:cd07861  79 EFLSMDLKKYLDS-LPKGKYMDAELVKSYLYQILQGILFCHS-RRVLHRDLKPQNLLIDN-KGVIKLADFGLARAF--GI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMN--P 300
Cdd:cd07861 154 PVRVYtheVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGVTslP 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 301 NYTDfRFPQIKAhPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07861 234 DYKN-TFPKWKK-GSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
70-354 4.06e-51

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: 172.45  E-value: 4.06e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMR---PMDHPNVISLKHCFfstTSRDELF 140
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDYLDqsldeiRLLELLNkkdKADKYHIVRLKDVF---YFKNHLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LnlVMEYVPETLYRVLRHytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDPLTHQVKLCDFGSAK 219
Cdd:cd14133  78 I--VFELLSQNLYEFLKQ--NKFQYLSLPRIRKIAQQILEALVFLHSL-GLIHCDLKPENiLLASYSRCQIKIIDFGSSC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEPniSYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMN 299
Cdd:cd14133 153 FLTQRLY--SYIQSRYYRAPEVILG-LPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGK 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 300 PNYTDFrfpqikahpwhkvfhkrmppeaIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14133 230 ADDELF----------------------VDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
75-354 8.24e-51

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: 172.49  E-value: 8.24e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFfstTSRDELFLnlVMEYV 148
Cdd:cd07848   8 VVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEvkettlRELKMLRTLKQENIVELKEAF---RRRGKLYL--VFEYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHYTSSnqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKG-EPN 227
Cdd:cd07848  83 EKNMLELLEEMPNG---VPPEKVRSYIYQLIKAIHWCHK-NDIVHRDIKPENLLISH-NDVLKLCDFGFARNLSEGsNAN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 IS-YICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCM--NPNYTD 304
Cdd:cd07848 158 YTeYVATRWYRSPELLLGAP-YGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLPAEQMKLFysNPRFHG 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 305 FRFPQIkAHPwhKVFHKR----MPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07848 237 LRFPAV-NHP--QSLERRylgiLSGVLLDLMKNLLKLNPTDRYLTEQCLNHPAF 287
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
69-354 9.32e-51

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: 172.45  E-value: 9.32e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRR-----YKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd07870   1 SYLNLEKLGEGSYATVYKGISRINGQLVALKVISMKTEegvpfTAIREASLLKGLKHANIVLLHDIIHTKET-----LTF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRHYTSSnqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLThQVKLCDFGSAKVlvK 223
Cdd:cd07870  76 VFEYMHTDLAQYMIQHPGG---LHPYNVRLFMFQLLRGLAYIHG-QHILHRDLKPQNLLISYLG-ELKLADFGLARA--K 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSV-DQLVEIIKVLGTPTREEIRCMN 299
Cdd:cd07870 149 SIPSQTYsseVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVfEQLEKIWTVLGVPTEDTWPGVS 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 300 --PNYTDFRFPQIKAHPWHKVFhKRM--PPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07870 229 klPNYKPEWFLPCKPQQLRVVW-KRLsrPPKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
69-354 1.31e-50

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: 172.12  E-value: 1.31e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLkHCFFSTtsrdELFLNL 143
Cdd:cd07871   6 TYVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGApctaiREVSLLKNLKHANIVTL-HDIIHT----ERCLTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRHytsSNQRMPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVlvK 223
Cdd:cd07871  81 VFEYLDSDLKQYLDN---CGNLMSMHNVKIFMFQLLRGLSYCHKRK-ILHRDLKPQNLLINE-KGELKLADFGLARA--K 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIR--CM 298
Cdd:cd07871 154 SVPTKTYsneVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPgvTS 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 299 NPNYTDFRFPQIKAHPWhkVFH-KRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07871 234 NEEFRSYLFPQYRAQPL--INHaPRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
77-354 9.66e-50

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: 170.19  E-value: 9.66e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKKVLQdrryKN----------RELQLMRPMDHPNVISLKHCFFS---TTSRDELFLNL 143
Cdd:cd07866  17 GEGTFGEVYKARQIKTGRVVALKKILM----HNekdgfpitalREIKILKKLKHPNVVPLIDMAVErpdKSKRKRGSVYM 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLrHYTSSNQRMPifYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK 223
Cdd:cd07866  93 VTPYMDHDLSGLL-ENPSVKLTES--QIKCYMLQLLEGINYLHE-NHILHRDIKAANILIDN-QGILKIADFGLARPYDG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY------------ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPT 291
Cdd:cd07866 168 PPPNPKGgggggtrkytnlVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCGTPT 247
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 292 REEIrcmnPNYTDF-RFPQIKAHPWH-----KVFhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07866 248 EETW----PGWRSLpGCEGVHSFTNYprtleERF-GKLGPEGLDLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
73-358 1.02e-49

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: 172.24  E-value: 1.02e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVAIKK---VLQD-----RRYknRELQLMRPMDHPNVIS--------LKHCFfsttsr 136
Cdd:cd07853   5 DRPIGYGAFGVVWSVTDPRDGKRVALKKmpnVFQNlvsckRVF--RELKMLCFFKHDNVLSaldilqppHIDPF------ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 DELFLnlVMEYVPETLYRVLrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFG 216
Cdd:cd07853  77 EEIYV--VTELMQSDLHKII----VSPQPLSSDHVKVFLYQILRGLKYLHSA-GILHRDIKPGNLLVNS-NCVLKICDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 SAKVlvkGEPNISY-----ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPT 291
Cdd:cd07853 149 LARV---EEPDESKhmtqeVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPS 225
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 292 REEIRCMNPNYTDFRFPQIKAHPWHKVFHKRMPP---EAIDLASRLLQYSPSLRCTALEACAHPFFNELR 358
Cdd:cd07853 226 LEAMRSACEGARAHILRGPHKPPSLPVLYTLSSQathEAVHLLCRMLVFDPDKRISAADALAHPYLDEGR 295
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
69-357 6.90e-47

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: 162.85  E-value: 6.90e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd07872   7 TYIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGApctaiREVSLLKDLKHANIVTLHDIVHTDKS-----LTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLrhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVlvK 223
Cdd:cd07872  82 VFEYLDKDLKQYM---DDCGNIMSMHNVKIFLYQILRGLAYCHRRK-VLHRDLKPQNLLINE-RGELKLADFGLARA--K 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNP 300
Cdd:cd07872 155 SVPTKTYsneVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISS 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 301 N--YTDFRFPQIKAHPWhkVFHK-RMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNEL 357
Cdd:cd07872 235 NdeFKNYNFPKYKPQPL--INHApRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSL 292
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
70-348 3.50e-46

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: 159.29  E-value: 3.50e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQD--------RRYKnRELQLMRPMDHPNVISLKHCFFsttsrDELFL 141
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPElaedeefrERFL-REARALARLSHPNIVRVYDVGE-----DDGRP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVP-ETLYRVLRHytssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLThQVKLCDFGSAKV 220
Cdd:cd14014  76 YIVMEYVEgGSLADLLRE----RGPLPPREALRILAQIADALAAAHRA-GIVHRDIKPANILLTEDG-RVKLTDFGIARA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNIS--YICSRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREeircm 298
Cdd:cd14014 150 LGDSGLTQTgsVLGTPAYMAPEQARGG-PVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSP----- 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42571361 299 npnytdfrfpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEA 348
Cdd:cd14014 224 --------------------LNPDVPPALDAIILRALAKDPEERPQSAAE 253
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
60-355 1.19e-45

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: 160.56  E-value: 1.19e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  60 KNGEpKQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR---ELQLMRPMDHP------NVISLKHCF 130
Cdd:cd14226   6 KNGE-KWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIKNKKAFLNQaqiEVRLLELMNKHdtenkyYIVRLKRHF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 131 fstTSRDELFLnlVMEYVPETLYRVLRHytsSNQR-MPIFYVKLYTYQIFRGLAYIHTVP-GVCHRDVKPQN-LLVDPLT 207
Cdd:cd14226  85 ---MFRNHLCL--VFELLSYNLYDLLRN---TNFRgVSLNLTRKFAQQLCTALLFLSTPElSIIHCDLKPENiLLCNPKR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 208 HQVKLCDFGSAKVLvkGEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVL 287
Cdd:cd14226 157 SAIKIIDFGSSCQL--GQRIYQYIQSRFYRSPEVLLG-LPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 288 GTPTREEIRcmnpnytdfrfpqiKAHPWHKVFHK--------------------------------------RMPPEA-- 327
Cdd:cd14226 234 GMPPVHMLD--------------QAPKARKFFEKlpdgtyylkktkdgkkykppgsrklheilgvetggpggRRAGEPgh 299
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 42571361 328 --------IDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:cd14226 300 tvedylkfKDLILRMLDYDPKTRITPAEALQHSFFK 335
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
77-314 1.39e-45

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 156.28  E-value: 1.39e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYVPE- 150
Cdd:cd00180   2 GKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLleellREIEILKKLNHPNIVKLYDVF-----ETENFLYLVMEYCEGg 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLVKGEPNISY 230
Cdd:cd00180  77 SLKDLLK---ENKGPLSEEEALSILRQLLSALEYLHSN-GIIHRDLKPENILLD-SDGTVKLADFGLAKDLDSDDSLLKT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 IC--SRYYRAPELIFGATEYTASIDIWSAGCVLAELllgqplfpgensvDQLVEIIKvlgtptreeiRCMNPNYTDfR-- 306
Cdd:cd00180 152 TGgtTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------EELKDLIR----------RMLQYDPKK-Rps 207

                ....*...
gi 42571361 307 FPQIKAHP 314
Cdd:cd00180 208 AKELLEHL 215
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
70-353 5.84e-45

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: 156.14  E-value: 5.84e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK----KVLQDRRYKN--RELQLMRPMDHPNVISLKHcFFSTTSRdelfLNL 143
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKiidkSKLKEEIEEKikREIEIMKLLNHPNIIKLYE-VIETENK----IYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--EtlyrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd14003  77 VMEYASggE-----LFDYIVNNGRLSEDEARRFFQQLISAVDYCHSN-GIVHRDLKLENILLDK-NGNLKIIDFGLSNEF 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEIIKVlgtptreeircmnpn 301
Cdd:cd14003 150 RGGSLLKTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDN-DSKLFRKILK--------------- 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 302 yTDFRFPqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14003 214 -GKYPIP------------SHLSPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
74-353 6.26e-45

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: 156.10  E-value: 6.26e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKkVL---QDRRYKN-----RELQLMRPMDHPNVISLKHCFFsttsrDELFLNLVM 145
Cdd:cd14007   6 KPLGKGKFGNVYLAREKKSGFIVALK-VIsksQLQKSGLehqlrREIEIQSHLRHPNILRLYGYFE-----DKKRIYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLrhytssnQRMPIF---YVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVL 221
Cdd:cd14007  80 EYAPNgELYKEL-------KKQKRFdekEAAKYIYQLALALDYLHS-KNIIHRDIKPENILLG-SNGELKLADFGWSVHA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNIsyICSRY-YRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeircmnp 300
Cdd:cd14007 151 PSNRRKT--FCGTLdYLPPEMVEG-KEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNV-------------- 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 301 nytDFRFPqikahPWhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14007 214 ---DIKFP-----SS-------VSPEAKDLISKLLQKDPSKRLSLEQVLNHPW 251
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
76-354 2.01e-44

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: 154.60  E-value: 2.01e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIK----KVLQDRR---YKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYV 148
Cdd:cd05123   1 LGKGSFGKVLLVRKKDTGKLYAMKvlrkKEIIKRKeveHTLNERNILERVNHPFIVKLHYAFQTEEK-----LYLVLDYV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P--EtlyrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEP 226
Cdd:cd05123  76 PggE-----LFSHLSKEGRFPEERARFYAAEIVLALEYLHSL-GIIYRDLKPENILLDSDGH-IKLTDFGLAKELSSDGD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NISYIC-SRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEIIKvlgtptreeircmnpnYTDF 305
Cdd:cd05123 149 RTYTFCgTPEYLAPEVLLGK-GYGKAVDWWSLGVLLYEMLTGKPPFYAEN-RKEIYEKIL----------------KSPL 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 306 RFPQIkahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEAC---AHPFF 354
Cdd:cd05123 211 KFPEY------------VSPEAKSLISGLLQKDPTKRLGSGGAEeikAHPFF 250
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
74-354 2.83e-44

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: 154.28  E-value: 2.83e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKN---RELQLMRPMDHPNVISLKHCFFsttSRDELFlnLVMEYVP 149
Cdd:cd05122   6 EKIGKGGFGVVYKARHKKTGQIVAIKKInLESKEKKEsilNEIAILKKCKHPNIVKYYGSYL---KKDELW--IVMEFCS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLvdpLTH--QVKLCDFGSAKVLVKGEP 226
Cdd:cd05122  81 GgSLKDLLKNT---NKTLTEQQIAYVCKEVLKGLEYLHSH-GIIHRDIKAANIL---LTSdgEVKLIDFGLSAQLSDGKT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVeIIKVLGTPTreeircmnpnytdfr 306
Cdd:cd05122 154 RNTFVGTPYWMAPEVIQG-KPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALF-LIATNGPPG--------------- 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 307 FPQIKAhpWHKVFHkrmppeaiDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd05122 217 LRNPKK--WSKEFK--------DFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
76-354 1.03e-42

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: 151.27  E-value: 1.03e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVlqdrRYKN----------RELQLMRPM---DHPNVISLKH-CFFSTTSRdELFL 141
Cdd:cd07863   8 IGVGAYGTVYKARDPHSGHFVALKSV----RVQTnedglplstvREVALLKRLeafDHPNIVRLMDvCATSRTDR-ETKV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPETLYRVLRHYTSSNqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd07863  83 TLVFEHVDQDLRTYLDKVPPPG--LPAETIKDLMRQFLRGLDFLHA-NCIVHRDLKPENILVTS-GGQVKLADFGLARIY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIrcmnPn 301
Cdd:cd07863 159 SCQMALTPVVVTLWYRAPEVLLQST-YATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGLPPEDDW----P- 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 302 yTDFRFPqikahpwHKVFHKRMP-------PE----AIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07863 233 -RDVTLP-------RGAFSPRGPrpvqsvvPEieesGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
75-354 7.38e-42

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: 150.09  E-value: 7.38e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRE-------LQLMR----PMDHPNVISLkHCFFSTTSRdelfLNL 143
Cdd:cd14212   6 LLGQGTFGQVVKCQDLKTNKLVAVK-VLKNKPAYFRQamleiaiLTLLNtkydPEDKHHIVRL-LDHFMHHGH----LCI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDPLTHQVKLCDFGSAkvLV 222
Cdd:cd14212  80 VFELLGVNLYELLK--QNQFRGLSLQLIRKFLQQLLDALSVLKDA-RIIHCDLKPENiLLVNLDSPEIKLIDFGSA--CF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRcMNPNY 302
Cdd:cd14212 155 ENYTLYTYIQSRFYRSPEVLLG-LPYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRIIEMLGMPPDWMLE-KGKNT 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 303 TDF-------------RFPQ---------IKAHPWHKVF--------------HKRMPPEA----------IDLASRLLQ 336
Cdd:cd14212 233 NKFfkkvaksggrstyRLKTpeefeaennCKLEPGKRYFkyktlediimnypmKKSKKEQIdkemetrlafIDFLKGLLE 312
                       330
                ....*....|....*...
gi 42571361 337 YSPSLRCTALEACAHPFF 354
Cdd:cd14212 313 YDPKKRWTPDQALNHPFI 330
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
73-373 8.45e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 153.63  E-value: 8.45e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVAIKKVLQD--------RRYKnRELQLMRPMDHPNVISLKHCFfstTSRDELFLnlV 144
Cdd:COG0515  12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPElaadpearERFR-REARALARLNHPNIVRVYDVG---EEDGRPYL--V 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP-ETLYRVLRHytssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvk 223
Cdd:COG0515  86 MEYVEgESLADLLRR----RGPLPPAEALRILAQLAEALAAAHAA-GIVHRDIKPANILLTP-DGRVKLIDFGIARAL-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY----ICSRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREeircmn 299
Cdd:COG0515 158 GGATLTQtgtvVGTPGYMAPEQARGE-PVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSE------ 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 300 pnytdfrfpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLR-------CTALEACAHPFFNELREPNARLPNGRPLPP 372
Cdd:COG0515 231 -------------------LRPDLPPALDAIVLRALAKDPEERyqsaaelAAALRAVLRSLAAAAAAAAAAAAAAAAAAA 291

                .
gi 42571361 373 L 373
Cdd:COG0515 292 A 292
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
75-353 1.57e-41

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: 148.41  E-value: 1.57e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSTTS-----RDELFLNL 143
Cdd:cd07864  14 IIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGfpitaiREIKILRQLNHRSVVNLKEIVTDKQDaldfkKDKGAFYL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLR----HYTSSNqrmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAK 219
Cdd:cd07864  94 VFEYMDHDLMGLLEsglvHFSEDH-------IKSFMKQLLEGLNYCHK-KNFLHRDIKCSNILLNN-KGQIKLADFGLAR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGE--PNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREeirc 297
Cdd:cd07864 165 LYNSEEsrPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPA---- 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 298 MNPNYTdfRFPQIKAHPWHKVFHKR-------MPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd07864 241 VWPDVI--KLPYFNTMKPKKQYRRRlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALNSPW 301
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
69-354 2.74e-41

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: 146.54  E-value: 2.74e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV----LQDRRYKNR---ELQLMRPMDHPNVISLKHCFfsttsRDELFL 141
Cdd:cd14099   2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVpkssLTKPKQREKlksEIKIHRSLKHPNIVKFHDCF-----EDEENV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVP-ETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV 220
Cdd:cd14099  77 YILLELCSnGSLMELLK----RRKALTEPEVRYFMRQILSGVKYLHSN-RIIHRDLKLGNLFLDENMN-VKIGDFGLAAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 L---------VKGEPNisYIcsryyrAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPgensvdqlveiikvlgTPT 291
Cdd:cd14099 151 LeydgerkktLCGTPN--YI------APEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFE----------------TSD 206
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 292 REEI-RCMNPNytDFRFPQikahpwhkvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14099 207 VKETyKRIKKN--EYSFPS----------HLSISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
76-353 1.28e-40

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: 144.67  E-value: 1.28e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYK------NRELQLMRPMDHPNVISLKHCffsttSRDELFLNLVMEYVP 149
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKklqenlESEIAILKSIKHPNIVRLYDV-----QKTEDFIYLVLEYCA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRHYtssnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTH--QVKLCDFGSAKVLvkgeP 226
Cdd:cd14009  76 GgDLSQYIRKR----GRLPEAVARHFMQQLASGLKFLRS-KNIIHRDLKPQNLLLSTSGDdpVLKIADFGFARSL----Q 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NISY---IC-SRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENSVdQLVEIIKvlgtptreeircmnpnY 302
Cdd:cd14009 147 PASMaetLCgSPLYMAPEILQFQ-KYDAKADLWSVGAILFEMLVGKPPFRGSNHV-QLLRNIE----------------R 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 303 TDFRFPQIKAHPWHkvfhkrmpPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14009 209 SDAVIPFPIAAQLS--------PDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
76-301 2.19e-40

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: 143.83  E-value: 2.19e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLetGESVAIKKV----LQDRRYK--NRELQLMRPMDHPNVISLkhcFFSTTSRDELFLnlVMEYVP 149
Cdd:cd13999   1 IGSGSFGEVYKGKWR--GTDVAIKKLkvedDNDELLKefRREVSILSKLRHPNIVQF---IGACLSPPPLCI--VTEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRhytSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEPNI 228
Cdd:cd13999  74 GgSLYDLLH---KKKIPLSWSLRLKIALDIARGMNYLHS-PPIIHRDLKSLNILLDENFT-VKIADFGLSRIKNSTTEKM 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSRY-YRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQlveIIKVLGTPTREEI------------ 295
Cdd:cd13999 149 TGVVGTPrWMAPE-VLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSPIQI---AAAVVQKGLRPPIppdcppelskli 224

                ....*..
gi 42571361 296 -RCMNPN 301
Cdd:cd13999 225 kRCWNED 231
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
76-354 5.92e-40

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: 144.43  E-value: 5.92e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKH-CFFSTT--SRDELFLNLVME 146
Cdd:cd07865  20 IGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGfpitalREIKILQLLKHENVVNLIEiCRTKATpyNRYKGSIYLVFE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLrhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLV---K 223
Cdd:cd07865 100 FCEHDLAGLL---SNKNVKFTLSEIKKVMKMLLNGLYYIHR-NKILHRDMKAANILITK-DGVLKLADFGLARAFSlakN 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPN--ISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREeircMNPN 301
Cdd:cd07865 175 SQPNryTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPE----VWPG 250
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 302 ------YTDFRFPQ-IKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07865 251 vdklelFKKMELPQgQKRKVKERLKPYVKDPYALDLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
70-396 6.96e-40

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: 145.56  E-value: 6.96e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVlqDRRYKN--------RELQLMRPMDHPNVISLKHCFFSTTSRDELF- 140
Cdd:cd07876  23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKL--SRPFQNqthakrayRELVLLKCVNHKNIISLLNVFTPQKSLEEFQd 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVPETLYRVLrHYTSSNQRMPIFYvklytYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd07876 101 VYLVMELMDANLCQVI-HMELDHERMSYLL-----YQMLCGIKHLHSA-GIIHRDLKPSNIVVKS-DCTLKILDFGLART 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNP 300
Cdd:cd07876 173 ACTNFMMTPYVVTRYYRAPEVILG-MGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSAEFMNRLQP 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 301 ---NYTDFRfPQIKAHPWHKVFHKRMPP-----------EAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARlpn 366
Cdd:cd07876 252 tvrNYVENR-PQYPGISFEELFPDWIFPseserdklktsQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEA--- 327
                       330       340       350
                ....*....|....*....|....*....|
gi 42571361 367 GRPLPPLFNFKQELGGASMELINRLIPEHV 396
Cdd:cd07876 328 EAPPPQIYDAQLEEREHAIEEWKELIYKEV 357
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
70-354 9.29e-40

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: 142.60  E-value: 9.29e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIdlsnmsEKEREEALNEVKLLSKLKHPNIVKYYESFEENGK-----LCI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL- 221
Cdd:cd08215  77 VMEYADGgDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSR-KILHRDLKTQNIFLTK-DGVVKLGDFGISKVLe 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 --------VKGEPnisyicsrYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEIIkvlgtpTRE 293
Cdd:cd08215 155 sttdlaktVVGTP--------YYLSPELCENK-PYNYKSDIWALGCVLYELCTLKHPFEANN-LPALVYKI------VKG 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 294 EIRCMNPNYTDfrfpqikahpwhkvfhkrmppEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd08215 219 QYPPIPSQYSS---------------------ELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
69-357 1.34e-39

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: 143.29  E-value: 1.34e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRR----YKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd07869   6 SYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIrLQEEEgtpfTAIREASLLKGLKHANIVLLHDIIHTKET-----LTL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRHYTSSnqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVlvK 223
Cdd:cd07869  81 VFEYVHTDLCQYMDKHPGG---LHPENVKLFLFQLLRGLSYIHQ-RYILHRDLKPQNLLISD-TGELKLADFGLARA--K 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISY---ICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSV-DQLVEIIKVLGTPTREEIRCMN 299
Cdd:cd07869 154 SVPSHTYsneVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIqDQLERIFLVLGTPNEDTWPGVH 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 300 --PNYTDFRFPQIKA----HPWHKVFHKRmppEAIDLASRLLQYSPSLRCTALEACAHPFFNEL 357
Cdd:cd07869 234 slPHFKPERFTLYSPknlrQAWNKLSYVN---HAEDLASKLLQCFPKNRLSAQAALSHEYFSDL 294
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
79-357 2.24e-39

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: 141.97  E-value: 2.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  79 GSFGIVFQAKCLETGESVAIKKV-LQDRRYKNRELQLMRPMD------HPNVISLkhcFFSTTSRDELFLnlVMEYVPE- 150
Cdd:cd05579   4 GAYGRVYLAKKKSTGDLYAIKVIkKRDMIRKNQVDSVLAERNilsqaqNPFVVKL---YYSFQGKKNLYL--VMEYLPGg 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV-LVKGEPNIS 229
Cdd:cd05579  79 DLYSLLENVGALDEDV----ARIYIAEIVLALEYLHSH-GIIHRDLKPDNILIDANGH-LKLTDFGLSKVgLVRRQIKLS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 230 Y---------------ICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGEnsvdqlveiikvlgtpTREE 294
Cdd:cd05579 153 IqkksngapekedrriVGTPDYLAPEILLG-QGHGKTVDWWSLGVILYEFLVGIPPFHAE----------------TPEE 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 295 IrcmnpnytdfrFPQIKAH--PWHKVFHkrMPPEAIDLASRLLQYSPSLR---CTALEACAHPFFNEL 357
Cdd:cd05579 216 I-----------FQNILNGkiEWPEDPE--VSDEAKDLISKLLTPDPEKRlgaKGIEEIKNHPFFKGI 270
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
74-353 3.22e-39

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: 140.85  E-value: 3.22e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQ----DRRYKN--RELQLMRPMDHPNVISLKHCFfsTTSRDelfLNLVMEY 147
Cdd:cd14002   7 ELIGEGSFGKVYKGRRKYTGQVVALKFIPKrgksEKELRNlrQEIEILRKLNHPNIIEMLDSF--ETKKE---FVVVTEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETLYRVLrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAK-------V 220
Cdd:cd14002  82 AQGELFQIL----EDDGTLPEEEVRSIAKQLVSALHYLHS-NRIIHRDMKPQNILIGK-GGVVKLCDFGFARamscntlV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 L--VKGEPnisyicsrYYRAPELIfgaTE--YTASIDIWSAGCVLAELLLGQPLFpGENSVDQLVEIIKvlgtptreeir 296
Cdd:cd14002 156 LtsIKGTP--------LYMAPELV---QEqpYDHTADLWSLGCILYELFVGQPPF-YTNSIYQLVQMIV----------- 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 cmnpnYTDFRFPqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14002 213 -----KDPVKWP------------SNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPF 252
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
76-354 1.01e-38

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: 139.67  E-value: 1.01e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR------ELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYVP 149
Cdd:cd06627   8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDlksvmgEIDLLKKLNHPNIVKYIGSV-----KTKDSLYIILEYVE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 EtlyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVdPLTHQVKLCDFGSAKVL--VKGEPN 227
Cdd:cd06627  83 N---GSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHE-QGVIHRDIKGANILT-TKDGLVKLADFGVATKLneVEKDEN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 iSYICSRYYRAPELIFGATEYTASiDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircmnpnytdfrf 307
Cdd:cd06627 158 -SVVGTPYWMAPEVIEMSGVTTAS-DIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQ---------------------- 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42571361 308 pqiKAHPwhkVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06627 214 ---DDHP---PLPENISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
70-360 2.10e-38

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: 141.76  E-value: 2.10e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVlqDRRYKN--------RELQLMRPMDHPNVISLKHCFFSTTSRDELF- 140
Cdd:cd07874  19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKL--SRPFQNqthakrayRELVLMKCVNHKNIISLLNVFTPQKSLEEFQd 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVPETLYRVLRhYTSSNQRMPIFYvklytYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd07874  97 VYLVMELMDANLCQVIQ-MELDHERMSYLL-----YQMLCGIKHLHSA-GIIHRDLKPSNIVVKS-DCTLKILDFGLART 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNP 300
Cdd:cd07874 169 AGTSFMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPEFMKKLQP 247
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 301 ---NYTDFRfPQIKAHPWHKVFHKRMPP-----------EAIDLASRLLQYSPSLRCTALEACAHPFFNELREP 360
Cdd:cd07874 248 tvrNYVENR-PKYAGLTFPKLFPDSLFPadsehnklkasQARDLLSKMLVIDPAKRISVDEALQHPYINVWYDP 320
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
77-354 9.69e-38

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: 137.30  E-value: 9.69e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIK-----KVLQDRRYKN-------------RELQLMRPMDHPNVISLKHCFFSTTSrDE 138
Cdd:cd14008   2 GRGSFGKVKLALDTETGQLYAIKifnksRLRKRREGKNdrgkiknalddvrREIAIMKKLDHPNIVRLYEVIDDPES-DK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 139 LFLnlVMEYVP--ETLYRVLRHytsSNQRMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPlTHQVKLCDFG 216
Cdd:cd14008  81 LYL--VLEYCEggPVMELDSGD---RVPPLPEETARKYFRDLVLGLEYLH-ENGIVHRDIKPENLLLTA-DGTVKISDFG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 SAKVLVKGEPNIS-YICSRYYRAPELI-FGATEYTAS-IDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPtre 293
Cdd:cd14008 154 VSEMFEDGNDTLQkTAGTPAFLAPELCdGDSKTYSGKaADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEF--- 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 294 eircmnpnytdfrfpqikahpwhkVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14008 231 ------------------------PIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
70-354 1.52e-37

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: 137.35  E-value: 1.52e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIkKVLQDRR--------YKNRELQLMRPMDHPNVISLKHCFfsttsRDELFL 141
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKEKETGKEYAI-KVLDKRHiikekkvkYVTIEKEVLSRLAHPGIVKLYYTF-----QDESKL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPE-TLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV 220
Cdd:cd05581  77 YFVLEYAPNgDLLEYIRKYGSLDEKC----TRFYTAEIVLALEYLHSK-GIIHRDLKPENILLDEDMH-IKITDFGTAKV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNI------------------SYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVE 282
Cdd:cd05581 151 LGPDSSPEstkgdadsqiaynqaraaSFVGTAEYVSPELL-NEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQK 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 283 IIKVlgtptreeircmnpnytDFRFPQikahpwhkvfhkRMPPEAIDLASRLLQYSPSLRCTALEAC------AHPFF 354
Cdd:cd05581 230 IVKL-----------------EYEFPE------------NFPPDAKDLIQKLLVLDPSKRLGVNENGgydelkAHPFF 278
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
76-354 3.01e-37

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: 136.70  E-value: 3.01e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETG-ESVAIKKVLQDRRYKN------RELQLMRPMD---HPNVISL-KHCFFSTTSRdELFLNLV 144
Cdd:cd07862   9 IGEGAYGKVFKARDLKNGgRFVALKRVRVQTGEEGmplstiREVAVLRHLEtfeHPNVVRLfDVCTVSRTDR-ETKLTLV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPETLYRVLRhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKG 224
Cdd:cd07862  88 FEHVDQDLTTYLD--KVPEPGVPTETIKDMMFQLLRGLDFLHS-HRVVHRDLKPQNILVTS-SGQIKLADFGLARIYSFQ 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIrcmnPNytD 304
Cdd:cd07862 164 MALTSVVVTLWYRAPEVLLQSS-YATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIGLPGEEDW----PR--D 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 305 FRFPQIKAHPWHKVFHKRMPPEAIDLASRLL----QYSPSLRCTALEACAHPFF 354
Cdd:cd07862 237 VALPRQAFHSKSAQPIEKFVTDIDELGKDLLlkclTFNPAKRISAYSALSHPYF 290
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
70-366 3.73e-37

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: 138.64  E-value: 3.73e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVlqDRRYKN--------RELQLMRPMDHPNVISLKHCFFSTTSRDELF- 140
Cdd:cd07875  26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKL--SRPFQNqthakrayRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQd 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVPETLYRVLRhYTSSNQRMPIFYvklytYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd07875 104 VYIVMELMDANLCQVIQ-MELDHERMSYLL-----YQMLCGIKHLHSA-GIIHRDLKPSNIVVKS-DCTLKILDFGLART 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCMNP 300
Cdd:cd07875 176 AGTSFMMTPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCPEFMKKLQP 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 301 ---NYTDFRfPQIKAHPWHKVFHKRMPP-----------EAIDLASRLLQYSPSLRCTALEACAHPFFN------ELREP 360
Cdd:cd07875 255 tvrTYVENR-PKYAGYSFEKLFPDVLFPadsehnklkasQARDLLSKMLVIDASKRISVDEALQHPYINvwydpsEAEAP 333

                ....*.
gi 42571361 361 NARLPN 366
Cdd:cd07875 334 PPKIPD 339
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
70-354 4.98e-37

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


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 135.07  E-value: 4.98e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFfstTSRDELFLn 142
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKEsvlmkveREIAIMKLIEHPNVLKLYDVY---ENKKYLYL- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 lVMEYVP--EtlyrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLThQVKLCDFGSAKV 220
Cdd:cd14081  79 -VLEYVSggE-----LFDYLVKKGRLTEKEARKFFRQIISALDYCHSH-SICHRDLKPENLLLDEKN-NIKIADFGMASL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEIIKVlGTptreeircmnp 300
Cdd:cd14081 151 QPEGSLLETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDN-LRQLLEKVKR-GV----------- 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 301 nytdFRFPQIkahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14081 218 ----FHIPHF------------ISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
74-353 3.48e-36

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: 133.20  E-value: 3.48e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYK-----NRELQLMRPMDHPNVISlkhCFFSTTSRDELflNLVMEY 147
Cdd:cd06626   6 NKIGEGTFGKVYTAVNLDTGELMAMKEIrFQDNDPKtikeiADEMKVLEGLDHPNLVR---YYGVEVHREEV--YIFMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPE-TLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTHQ--VKLCDFGSAKVLVKG 224
Cdd:cd06626  81 CQEgTLEELLRHGRILDEAV----IRVYTLQLLEGLAYLHE-NGIVHRDIKPANIF---LDSNglIKLGDFGSAVKLKNN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 ------EPNISYICSRYYRAPELIFGATE--YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTreeir 296
Cdd:cd06626 153 tttmapGEVNSLVGTPAYMAPEVITGNKGegHGRAADIWSLGCVVLEMATGKRPWSELDNEWAIMYHVGMGHKPP----- 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 cmnpnytdfrFPQikahpwhkvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06626 228 ----------IPD----------SLQLSPEGKDFLSRCLESDPKKRPTASELLDHPF 264
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
74-354 5.49e-36

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: 134.61  E-value: 5.49e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN---RELQLMR------PMDHPNVISLKHCFfsttsrdeLFLN-- 142
Cdd:cd14134  18 RLLGEGTFGKVLECWDRKRKRYVAVKIIRNVEKYREaakIEIDVLEtlaekdPNGKSHCVQLRDWF--------DYRGhm 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 -LVMEYVPETLYRVLRHYtsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVD---------------- 204
Cdd:cd14134  90 cIVFELLGPSLYDFLKKN--NYGPFPLEHVQHIAKQLLEAVAFLHDL-KLTHTDLKPENiLLVDsdyvkvynpkkkrqir 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 205 -PLTHQVKLCDFGSAkvLVKGEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEI 283
Cdd:cd14134 167 vPKSTDIKLIDFGSA--TFDDEYHSSIVSTRHYRAPEVILG-LGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHLAMM 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 284 IKVLGTP----TREEIRCMNPNYTD---FRFPQ-------IKAHPwhKVFHKRMP------PEAIDLASRLLQYSPSLRC 343
Cdd:cd14134 244 ERILGPLpkrmIRRAKKGAKYFYFYhgrLDWPEgsssgrsIKRVC--KPLKRLMLlvdpehRLLFDLIRKMLEYDPSKRI 321
                       330
                ....*....|.
gi 42571361 344 TALEACAHPFF 354
Cdd:cd14134 322 TAKEALKHPFF 332
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
68-354 1.28e-35

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: 133.67  E-value: 1.28e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  68 ISYMAE--RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDH---------PNVISLKHCFFSttsR 136
Cdd:cd14225  41 IAYRYEilEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQALVEVKILDAlrrkdrdnsHNVIHMKEYFYF---R 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 DELFLNLvmEYVPETLYRVLRHytSSNQRMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPL-THQVKLCDF 215
Cdd:cd14225 118 NHLCITF--ELLGMNLYELIKK--NNFQGFSLSLIRRFAISLLQCLRLLY-RERIIHCDLKPENILLRQRgQSSIKVIDF 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 216 GSA-----KVLvkgepniSYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTP 290
Cdd:cd14225 193 GSScyehqRVY-------TYIQSRFYRSPEVILG-LPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGLP 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 291 TREEI----------------RCMNPNYTDFRFPQIK--AHPWhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14225 265 PPELIenaqrrrlffdskgnpRCITNSKGKKRRPNSKdlASAL-----KTSDPLFLDFIRRCLEWDPSKRMTPDEALQHE 339

                ..
gi 42571361 353 FF 354
Cdd:cd14225 340 WI 341
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
76-354 1.91e-35

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: 132.73  E-value: 1.91e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETG-ESVAIKKVLQD---RRYKNRELQLMR------PMDHPNVISLKHCFFSttsRDELFLnlVM 145
Cdd:cd14135   8 LGKGVFSNVVRARDLARGnQEVAIKIIRNNelmHKAGLKELEILKklndadPDDKKHCIRLLRHFEH---KNHLCL--VF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVLRHYTSsNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKGE 225
Cdd:cd14135  83 ESLSMNLREVLKKYGK-NVGLNIKAVRSYAQQLFLALKHLKKC-NILHADIKPDNILVNEKKNTLKLCDFGSASDIGENE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PnISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQL------------------------- 280
Cdd:cd14135 161 I-TPYLVSRFYRAPEIILGLP-YDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLklmmdlkgkfpkkmlrkgqfkdqhf 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 281 --------VEIIKVLGTPTREEIRCMNPNyTDFRfPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14135 239 denlnfiyREVDKVTKKEVRRVMSDIKPT-KDLK-TLLIGKQRLPDEDRKKLLQLKDLLDKCLMLDPEKRITPNEALQHP 316

                ..
gi 42571361 353 FF 354
Cdd:cd14135 317 FI 318
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
74-353 2.80e-35

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: 130.60  E-value: 2.80e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVL---QDRRYK------NRELQLMRPMDHPNVISlkhcfFSTTSRDELFLNLV 144
Cdd:cd06632   6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSlvdDDKKSResvkqlEQEIALLSKLRHPNIVQ-----YYGTEREEDNLYIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLRHYtssnQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK 223
Cdd:cd06632  81 LEYVPGgSIHKLLQRY----GAFEEPVIRLYTRQILSGLAYLHSR-NTVHRDIKGANILVDT-NGVVKLADFGMAKHVEA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPELIFGA-TEYTASIDIWSAGCVLAELLLGQPLFpgeNSVDQLVEIIKVlgtptreeircmnpny 302
Cdd:cd06632 155 FSFAKSFKGSPYWMAPEVIMQKnSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAIFKI---------------- 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 303 tdFRFPQIKAHPWHkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06632 216 --GNSGELPPIPDH------LSPDAKDFIRLCLQRDPEDRPTASQLLEHPF 258
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
75-356 1.16e-34

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: 129.25  E-value: 1.16e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRElQLMRPM------DHPNVISLKHCFFSTTSrdelfLNLVMEYV 148
Cdd:cd06623   8 VLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRK-QLLRELktlrscESPYVVKCYGAFYKEGE-----ISIVLEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PE-TLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLvkgePN 227
Cdd:cd06623  82 DGgSLADLLK----KVGKIPEPVLAYIARQILKGLDYLHTKRHIIHRDIKPSNLLIN-SKGEVKIADFGISKVL----EN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYICSRY-----YRAPELIFGATeYTASIDIWSAGCVLAELLLGQ-P-LFPGENSVDQLVEIIkvlgtptreeirCMNP 300
Cdd:cd06623 153 TLDQCNTFvgtvtYMSPERIQGES-YSYAADIWSLGLTLLECALGKfPfLPPGQPSFFELMQAI------------CDGP 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 301 NYtdfrFPQikahpwhkvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd06623 220 PP----SLP----------AEEFSPEFRDFISACLQKDPKKRPSAAELLQHPFIKK 261
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
75-353 1.49e-34

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: 130.65  E-value: 1.49e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQL---------MRPMDHPNVISLKHCFfsttsRDELFLNLVM 145
Cdd:cd14211   6 FLGRGTFGQVVKCWKRGTNEIVAIK-ILKNHPSYARQGQIevsilsrlsQENADEFNFVRAYECF-----QHKNHTCLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVLRHytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDPLT--HQVKLCDFGSAKVLV 222
Cdd:cd14211  80 EMLEQNLYDFLKQ--NKFSPLPLKYIRPILQQVLTALLKLKSL-GLIHADLKPENiMLVDPVRqpYRVKVIDFGSASHVS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNiSYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTP-----------T 291
Cdd:cd14211 157 KAVCS-TYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPaehllnaatktS 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 292 REEIRCMNPNYTDFRFP---------QIKAHPWHKVFHK--------RMPP---------------EAIDLASRLLQYSP 339
Cdd:cd14211 235 RFFNRDPDSPYPLWRLKtpeeheaetGIKSKEARKYIFNclddmaqvNGPSdlegsellaekadrrEFIDLLKRMLTIDQ 314
                       330
                ....*....|....
gi 42571361 340 SLRCTALEACAHPF 353
Cdd:cd14211 315 ERRITPGEALNHPF 328
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
70-352 3.05e-34

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 128.28  E-value: 3.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKN-------------RELQLMRPMDHPNVISLKHCFfstTSR 136
Cdd:cd14084   8 YIMSRTLGSGACGEVKLAYDKSTCKKVAIK-IINKRKFTIgsrreinkprnieTEIEILKKLSHPCIIKIEDFF---DAE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 DELFLnlVMEYVP--ETLYRVlrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLV-----DPLthq 209
Cdd:cd14084  84 DDYYI--VLELMEggELFDRV-----VSNKRLKEAICKLYFYQMLLAVKYLHSN-GIIHRDLKPENVLLssqeeECL--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 VKLCDFGSAKVLVK--------GEPNisyicsryYRAPELI--FGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvdq 279
Cdd:cd14084 153 IKITDFGLSKILGEtslmktlcGTPT--------YLAPEVLrsFGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYT--- 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 280 lveiikvlGTPTREEIrcMNPNYTdfrfpqikahpWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14084 222 --------QMSLKEQI--LSGKYT-----------FIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHP 273
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
70-354 4.28e-34

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: 127.34  E-value: 4.28e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLET-------GESVAIKKVlqdrrYKN-------RELQ-LMRPMDHPNVISLKHCFfstt 134
Cdd:cd14019   3 YRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHI-----YPTsspsrilNELEcLERLGGSNNVSGLITAF---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 135 sRDELFLNLVMEYVPETLYRVLRHytssnqRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCD 214
Cdd:cd14019  74 -RNEDQVVAVLPYIEHDDFRDFYR------KMSLTDIRIYLRNLFKALKHVHSF-GIIHRDVKPGNFLYNRETGKGVLVD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 215 FGSAKVLvKGEPNISYIC--SRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQ-PLFPGENSVDQLVEIIKVLGTpt 291
Cdd:cd14019 146 FGLAQRE-EDRPEQRAPRagTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRfPFFFSSDDIDALAEIATIFGS-- 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 292 reeircmnpnytdfrfpqikahpwhkvfhkrmpPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14019 223 ---------------------------------DEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
70-353 3.26e-33

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: 125.28  E-value: 3.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN--------RELQLMRPMDHPNVISLKHCFFSTtsrDELFL 141
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNdknlqlfqREINILKSLEHPGIVRLIDWYEDD---QHIYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 nlVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLV---DPLThqVKLCDFGSA 218
Cdd:cd14098  79 --VMEYVEGG---DLMDFIMAWGAIPEQHARELTKQILEAMAYTHSM-GITHRDLKPENILItqdDPVI--VKISDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEPNISYICSRYYRAPELIFGAT-----EYTASIDIWSAGCVLAELLLGQPLFPGeNSVDQLVEIIkvlgtptre 293
Cdd:cd14098 151 KVIHTGTFLVTFCGTMAYLAPEILMSKEqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDG-SSQLPVEKRI--------- 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 294 eircmnpnyTDFRFPQikahPWHKVFhkRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14098 221 ---------RKGRYTQ----PPLVDF--NISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
74-353 4.96e-33

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: 124.44  E-value: 4.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVME 146
Cdd:cd14663   6 RTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREgmveqikREIAIMKLLRHPNIVELHEVMATKTK-----IFFVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVlrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVL--V 222
Cdd:cd14663  81 LVTggELFSKI-----AKNGRLKEDKARKYFQQLIDAVDYCHS-RGVFHRDLKPENLLLDEDGN-LKISDFGLSALSeqF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYIC-SRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeircmnpn 301
Cdd:cd14663 154 RQDGLLHTTCgTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKG--------------- 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 302 ytDFRFPqikahPWhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14663 219 --EFEYP-----RW-------FSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
76-354 1.14e-32

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: 125.56  E-value: 1.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGES--VAIKKVLQD--RRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLVMEYVPET 151
Cdd:cd07868  25 VGRGTYGHVYKAKRKDGKDDkdYALKQIEGTgiSMSACREIALLRELKHPNVISLQKVFLSHADRK---VWLLFDYAEHD 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 152 LYRVLRHYTSSNQ-----RMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV---DPLTHQVKLCDFGSAKV--- 220
Cdd:cd07868 102 LWHIIKFHRASKAnkkpvQLPRGMVKSLLYQILDGIHYLHA-NWVLHRDLKPANILVmgeGPERGRVKIADMGFARLfns 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 ----LVKGEPnisYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENS---------VDQLVEIIKVL 287
Cdd:cd07868 181 plkpLADLDP---VVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpyhHDQLDRIFNVM 257
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 288 GTPTR---EEIRCMNPNYT---DFR------FPQIKAHPWHKVfhkRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07868 258 GFPADkdwEDIKKMPEHSTlmkDFRrntytnCSLIKYMEKHKV---KPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYF 333
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
74-357 1.31e-32

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: 124.23  E-value: 1.31e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK-----KVLQDRRYK--NRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd05580   7 KTLGTGSFGRVRLVKHKDSGKYYALKilkkaKIIKLKQVEhvLNEKRILSEVRHPFIVNLLGSF-----QDDRNLYMVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--EtLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK- 223
Cdd:cd05580  82 YVPggE-LFSLLR----RSGRFPNDVAKFYAAEVVLALEYLHSL-DIVYRDLKPENLLLDSDGH-IKITDFGFAKRVKDr 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 -----GEPNisyicsryYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircm 298
Cdd:cd05580 155 tytlcGTPE--------YLAPEIILS-KGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILE------------- 212
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 299 npnyTDFRFPqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACA-----HPFFNEL 357
Cdd:cd05580 213 ----GKIRFP------------SFFDPDAKDLIKRLLVVDLTKRLGNLKNGVediknHPWFAGI 260
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
76-354 1.80e-32

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: 124.80  E-value: 1.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGES--VAIKKVLQD--RRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLVMEYVPET 151
Cdd:cd07867  10 VGRGTYGHVYKAKRKDGKDEkeYALKQIEGTgiSMSACREIALLRELKHPNVIALQKVFLSHSDRK---VWLLFDYAEHD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 152 LYRVLRHYTSSN-----QRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV---DPLTHQVKLCDFGSAKV--- 220
Cdd:cd07867  87 LWHIIKFHRASKankkpMQLPRSMVKSLLYQILDGIHYLHA-NWVLHRDLKPANILVmgeGPERGRVKIADMGFARLfns 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 ----LVKGEPnisYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENS---------VDQLVEIIKVL 287
Cdd:cd07867 166 plkpLADLDP---VVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVM 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 288 GTPTR---EEIRCMnPNY----TDFRFPQIKAHPWHKVFHK-RMPPEA--IDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd07867 243 GFPADkdwEDIRKM-PEYptlqKDFRRTTYANSSLIKYMEKhKVKPDSkvFLLLQKLLTMDPTKRITSEQALQDPYF 318
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
70-352 2.58e-32

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: 122.43  E-value: 2.58e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNR------ELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKATDKEYALK-IIDKAKCKGKehmienEVAILRRVKHPNIVQLIEEYDTDTE-----LYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVpeTLYRVLRHYTSSNqRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPltHQ-----VKLCDFGSA 218
Cdd:cd14095  76 VMELV--KGGDLFDAITSST-KFTERDASRMVTDLAQALKYLHSL-SIVHRDIKPENLLVVE--HEdgsksLKLADFGLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVkgEPnISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGE-NSVDQLVEIIKvLGtptreeir 296
Cdd:cd14095 150 TEVK--EP-LFTVCgTPTYVAPE-ILAETGYGLKVDIWAAGVITYILLCGFPPFRSPdRDQEELFDLIL-AG-------- 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 cmnpnytDFRFPQikahP-WHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14095 217 -------EFEFLS----PyWDNI-----SDSAKDLISRMLVVDPEKRYSAGQVLDHP 257
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
79-354 2.75e-32

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: 122.59  E-value: 2.75e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  79 GSFGIVFQAKCLETGESVAIK-----KVLQDRRYKNRELQ---LMRPMDHPNVISLkhcFFSTTSRDELFLnlVMEYVP- 149
Cdd:cd05611   7 GAFGSVYLAKKRSTGDYFAIKvlkksDMIAKNQVTNVKAEraiMMIQGESPYVAKL---YYSFQSKDYLYL--VMEYLNg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ---ETLYRVLRHytssnqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEP 226
Cdd:cd05611  82 gdcASLIKTLGG-------LPEDWAKQYIAEVVLGVEDLHQ-RGIIHRDIKPENLLIDQTGH-LKLTDFGLSRNGLEKRH 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NISYICSRYYRAPELIFGATEyTASIDIWSAGCVLAELLLGQPLFPGEnSVDQLVEIIkvlgtptreEIRCMNpnytdfr 306
Cdd:cd05611 153 NKKFVGTPDYLAPETILGVGD-DKMSDWWSLGCVIFEFLFGYPPFHAE-TPDAVFDNI---------LSRRIN------- 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 307 fpqikahpWHKVFHKRMPPEAIDLASRLLQYSPSLRCTA---LEACAHPFF 354
Cdd:cd05611 215 --------WPEEVKEFCSPEAVDLINRLLCMDPAKRLGAngyQEIKSHPFF 257
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
70-354 3.18e-32

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: 123.84  E-value: 3.18e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR---ELQLMRPMDH--PNVISLKHC-----FFSTTSRDEL 139
Cdd:cd14136  12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTEAaldEIKLLKCVREadPKDPGREHVvqlldDFKHTGPNGT 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 FLNLVMEYVPETLYRVLRHYtssNQR-MPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPLTHQVKLCDFGSA 218
Cdd:cd14136  92 HVCMVFEVLGPNLLKLIKRY---NYRgIPLPLVKKIARQVLQGLDYLHTKCGIIHTDIKPENVLLCISKIEVKIADLGNA 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKgePNISYICSRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLF---PGEN---SVDQLVEIIKVLGTPTR 292
Cdd:cd14136 169 CWTDK--HFTEDIQTRQYRSPEVILGA-GYGTPADIWSTACMAFELATGDYLFdphSGEDysrDEDHLALIIELLGRIPR 245
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 293 EEIRC-------MNPNYTDFRFPQIKAHPWHKVF---HKRMPPEAIDLASRL---LQYSPSLRCTALEACAHPFF 354
Cdd:cd14136 246 SIILSgkysrefFNRKGELRHISKLKPWPLEDVLvekYKWSKEEAKEFASFLlpmLEYDPEKRATAAQCLQHPWL 320
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
58-353 3.80e-32

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: 125.24  E-value: 3.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  58 GGKNGEPKQTISYMAE--RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHC 129
Cdd:cd14224  53 GSYIHVPHDHIAYRYEvlKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRFHRqaaeeiRILEHLKKQDKDNTMNVIHM 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 130 FFSTTSRDELFLNLvmEYVPETLYRVLRHytSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTHQ 209
Cdd:cd14224 133 LESFTFRNHICMTF--ELLSMNLYELIKK--NKFQGFSLQLVRKFAHSILQCLDALHR-NKIIHCDLKPENIL---LKQQ 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 ----VKLCDFGSAkvLVKGEPNISYICSRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK 285
Cdd:cd14224 205 grsgIKVIDFGSS--CYEHQRIYTYIQSRFYRAPEVILGA-RYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIE 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 286 VLGTPTREEI----RCMNpnytdfrFPQIKAHPWH------------------KVFHKRMPPEA---------------I 328
Cdd:cd14224 282 LLGMPPQKLLetskRAKN-------FISSKGYPRYctvttlpdgsvvlnggrsRRGKMRGPPGSkdwvtalkgcddplfL 354
                       330       340
                ....*....|....*....|....*
gi 42571361 329 DLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14224 355 DFLKRCLEWDPAARMTPSQALRHPW 379
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
75-355 1.29e-31

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: 120.78  E-value: 1.29e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVL---QDRRYKNRELQLMRPMDHPNVISLKHCFFsttSRDELFlnLVMEYVPE- 150
Cdd:cd06614   7 KIGEGASGEVYKATDRATGKEVAIKKMRlrkQNKELIINEILIMKECKHPNIVDYYDSYL---VGDELW--VVMEYMDGg 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRMPIFYVKLytyQIFRGLAYIHTVpGVCHRDVKPQNLLvdpLTHQ--VKLCDFGSAKVLVKGEPN- 227
Cdd:cd06614  82 SLTDIITQNPVRMNESQIAYVCR---EVLQGLEYLHSQ-NVIHRDIKSDNIL---LSKDgsVKLADFGFAAQLTKEKSKr 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvLGTPTREEircmnpnytdfrf 307
Cdd:cd06614 155 NSVVGTPYWMAPEVIKR-KDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLITT-KGIPPLKN------------- 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 308 pqikAHPWHKVFhkrmppeaIDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:cd06614 220 ----PEKWSPEF--------KDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
74-355 1.83e-31

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: 122.39  E-value: 1.83e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ-------LMRPMDHPNVISLkHCFFsttsRDELFLNLVME 146
Cdd:cd05573   7 KVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAhvraerdILADADSPWIVRL-HYAF----QDEDHLYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE-TLYRVLRHYtssnQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGE 225
Cdd:cd05573  82 YMPGgDLMNLLIKY----DVFPEETARFYIAELVLALDSLHKL-GFIHRDIKPDNILLDADGH-IKLADFGLCTKMNKSG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRY------------------------------YRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd05573 156 DRESYLNDSVntlfqdnvlarrrphkqrrvraysavgtpdYIAPEVLRG-TGYGPECDWWSLGVILYEMLYGFPPFYSDS 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 276 SVDqlveiikvlgtpTREEIrcMNPNyTDFRFPQikahpwhkvfHKRMPPEAIDLASRLLQySPSLR-CTALEACAHPFF 354
Cdd:cd05573 235 LVE------------TYSKI--MNWK-ESLVFPD----------DPDVSPEAIDLIRRLLC-DPEDRlGSAEEIKAHPFF 288

                .
gi 42571361 355 N 355
Cdd:cd05573 289 K 289
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
74-355 3.35e-31

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: 119.76  E-value: 3.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVL-----QDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYV 148
Cdd:cd06605   7 GELGEGNGGVVSKVRHRPSGQIMAVKVIRleideALQKQILRELDVLHKCNSPYIVGFYGAFYSEGD-----ISICMEYM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPLThQVKLCDFGSAKVLVKGEPNi 228
Cdd:cd06605  82 DGG---SLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHKIIHRDVKPSNILVNSRG-QVKLCDFGVSGQLVDSLAK- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVeIIKVLgtptrEEIRCMNPnytdfrfP 308
Cdd:cd06605 157 TFVGTRSYMAPERISG-GKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMM-IFELL-----SYIVDEPP-------P 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42571361 309 QIKAHPWhkvfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:cd06605 223 LLPSGKF--------SPDFQDFVSQCLQKDPTERPSYKELMEHPFIK 261
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
74-347 7.24e-31

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: 118.93  E-value: 7.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKN----RELQLMRPMDHPNVIslkHCFFSTTSRDELFLNlvMEYV 148
Cdd:cd13996  12 ELLGSGGFGSVYKVRNKVDGVTYAIKKIrLTEKSSASekvlREVKALAKLNHPNIV---RYYTAWVEEPPLYIQ--MELC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P-ETLYRVLRHYTSSNQRMPIFYVKLyTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKGEP- 226
Cdd:cd13996  87 EgGTLRDWIDRRNSSSKNDRKLALEL-FKQILKGVSYIHSK-GIVHRDLKPSNIFLDNDDLQVKIGDFGLATSIGNQKRe 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 --------------NISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGqplfpgensvdqlveiikvlGTPTR 292
Cdd:cd13996 165 lnnlnnnnngntsnNSVGIGTPLYASPEQLDG-ENYNEKADIYSLGIILFEMLHP--------------------FKTAM 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 293 EEIRCMnpnyTDFR---FPQIkahpwhkvFHKRMPPEAiDLASRLLQYSPSLRCTALE 347
Cdd:cd13996 224 ERSTIL----TDLRngiLPES--------FKAKHPKEA-DLIQSLLSKNPEERPSAEQ 268
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
70-353 1.52e-30

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: 118.02  E-value: 1.52e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVL--------QDRRYK-----NRELQLMRPMDHPNVISlkhcfFSTTSR 136
Cdd:cd06628   2 WIKGALIGSGSFGSVYLGMNASSGELMAVKQVElpsvsaenKDRKKSmldalQREIALLRELQHENIVQ-----YLGSSS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 DELFLNLVMEYVPE-TLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDF 215
Cdd:cd06628  77 DANHLNIFLEYVPGgSVATLLNNYGAFEESL----VRNFVRQILKGLNYLHN-RGIIHRDIKGANILVDN-KGGIKISDF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 216 GSAKvlvKGEPNI----------SYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPgenSVDQLVEIIK 285
Cdd:cd06628 151 GISK---KLEANSlstknngarpSLQGSVFWMAPEVV-KQTSYTRKADIWSLGCLVVEMLTGTHPFP---DCTQMQAIFK 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 286 V--LGTPTreeircmnpnytdfrFPQIKAHpwhkvfhkrmppEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06628 224 IgeNASPT---------------IPSNISS------------EARDFLEKTFEIDHNKRPTADELLKHPF 266
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
68-353 6.80e-30

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: 116.33  E-value: 6.80e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  68 ISYMAERVVGTGSFGIVFQAKCLETGESVAIKKV--------LQDRRYK------NRELQLMRPMDHPNVISLKHCffst 133
Cdd:cd06629   1 FKWVKGELIGKGTYGRVYLAMNATTGEMLAVKQVelpktssdRADSRQKtvvdalKSEIDTLKDLDHPNIVQYLGF---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 134 tSRDELFLNLVMEYVPE-TLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKL 212
Cdd:cd06629  77 -EETEDYFSIFLEYVPGgSIGSCLRKYGKFEEDL----VRFFTRQILDGLAYLHS-KGILHRDLKADNILVD-LEGICKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 213 CDFG---SAKVLVKGEPNISYICSRYYRAPELIFGATE-YTASIDIWSAGCVLAELLLGQ-PLfpgenSVDQLVEIIKVL 287
Cdd:cd06629 150 SDFGiskKSDDIYGNNGATSMQGSVFWMAPEVIHSQGQgYSAKVDIWSLGCVVLEMLAGRrPW-----SDDEAIAAMFKL 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 288 GT-----PTREEIrcmnpnytdfrfpqikahpwhkvfhkRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06629 225 GNkrsapPVPEDV--------------------------NLSPEALDFLNACFAIDPRDRPTAAELLSHPF 269
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
70-275 3.08e-29

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 114.29  E-value: 3.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV----LQDRRYKN---RELQLMRPMDHPNVISLKHCFFsttsrDELFLN 142
Cdd:cd08224   2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVqifeMMDAKARQdclKEIDLLQQLNHPNIIKYLASFI-----ENNELN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFG----- 216
Cdd:cd08224  77 IVLELADAgDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHS-KRIMHRDIKPANVFIT-ANGVVKLGDLGlgrff 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 217 SAKVLVK----GEPnisyicsrYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd08224 155 SSKTTAAhslvGTP--------YYMSPERIRE-QGYDFKSDIWSLGCLLYEMAALQSPFYGEK 208
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
73-359 3.53e-29

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: 114.18  E-value: 3.53e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361     73 ERVVGTGSFGIVFQAKCL----ETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCffsTTSRDELFlnL 143
Cdd:smart00221   4 GKKLGEGAFGEVYKGTLKgkgdGKEVEVAVKTLKEDASEQQieeflREARIMRKLDHPNIVKLLGV---CTEEEPLM--I 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    144 VMEYVPetlYRVLRHY--TSSNQRMPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVL 221
Cdd:smart00221  79 VMEYMP---GGDLLDYlrKNRPKELSLSDLLSFALQIARGMEYLESKN-FIHRDLAARNCLVG-ENLVVKISDFGLSRDL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    222 VKGEpnisyicsrYYR-----------APELIFGATEYTASiDIWSAGCVLAELL-LGQPLFPGEnSVDQLVEIIKvlgt 289
Cdd:smart00221 154 YDDD---------YYKvkggklpirwmAPESLKEGKFTSKS-DVWSFGVLLWEIFtLGEEPYPGM-SNAEVLEYLK---- 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    290 ptreeircmnpnyTDFRFPQIkahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTaleacahpfFNELRE 359
Cdd:smart00221 219 -------------KGYRLPKP----------PNCPPELYKLMLQCWAEDPEDRPT---------FSELVE 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
74-354 7.99e-29

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 113.19  E-value: 7.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISlkhcfFSTTSRDELFLNLVMEY 147
Cdd:cd14069   7 QTLGEGAFGEVFLAVNRNTEEAVAVKFVdmkrapGDCPENIKKEVCIQKMLSHKNVVR-----FYGHRREGEFQYLFLEY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VP--ETLYRVLRHYTssnqrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL-VKG 224
Cdd:cd14069  82 ASggELFDKIEPDVG-----MPEDVAQFYFQQLMAGLKYLHSC-GITHRDIKPENLLLDE-NDNLKISDFGLATVFrYKG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNI--SYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQplfpgensvdqlveiikvlgTPTREEI-RCmnPN 301
Cdd:cd14069 155 KERLlnKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGE--------------------LPWDQPSdSC--QE 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 302 YTDFRFPQ-IKAHPWhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14069 213 YSDWKENKkTYLTPW-----KKIDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
70-354 1.05e-28

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: 112.75  E-value: 1.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKN--------RELQLMRPMDHPNVISLKHCFFSTTsrdELFL 141
Cdd:cd14079   4 YILGKTLGVGSFGKVKLAEHELTGHKVAVK-ILNRQKIKSldmeekirREIQILKLFRHPHIIRLYEVIETPT---DIFM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 nlVMEYVP--EtlyrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAK 219
Cdd:cd14079  80 --VMEYVSggE-----LFDYIVQKGRLSEDEARRFFQQIISGVEYCHR-HMVVHRDLKPENLLLDS-NMNVKIADFGLSN 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGE--------PNisyicsryYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsvdqlveiIKVLgtpt 291
Cdd:cd14079 151 IMRDGEflktscgsPN--------YAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFDDEH--------IPNL---- 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 292 reeircmnpnytdfrFPQIKahpwHKVFH--KRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14079 211 ---------------FKKIK----SGIYTipSHLSPGARDLIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
75-354 1.23e-28

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 112.74  E-value: 1.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN--RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVpeTL 152
Cdd:cd06612  10 KLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQEiiKEISILKQCDSPYIVKYYGSYFKNTD-----LWIVMEYC--GA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 153 YRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK--GEPNiSY 230
Cdd:cd06612  83 GSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSN-KKIHRDIKAGNILLNE-EGQAKLADFGVSGQLTDtmAKRN-TV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 ICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircmNPnytdfrfPQI 310
Cdd:cd06612 160 IGTPFWMAPEVIQE-IGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPN-------------KP-------PPT 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42571361 311 KAHPwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06612 219 LSDP------EKWSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
76-353 3.24e-28

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: 111.62  E-value: 3.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYK-NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEY-VPETLY 153
Cdd:cd14010   8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPEvLNEVRLTHELKHPNVLKFYEWYETSNH-----LWLVVEYcTGGDLE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 154 RVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL----------VK 223
Cdd:cd14010  83 TLLR----QDGNLPESSVRKFGRDLVRGLHYIHSK-GIIYCDLKPSNILLDG-NGTLKLSDFGLARREgeilkelfgqFS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYIC-------SRYYRAPELIFGATEYTASiDIWSAGCVLAELLLGQPLFPGEnSVDQLVEiikvlgtptreEIR 296
Cdd:cd14010 157 DEGNVNKVSkkqakrgTPYYMAPELFQGGVHSFAS-DLWALGCVLYEMFTGKPPFVAE-SFTELVE-----------KIL 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 CMNPNYtdfrfpqikahPWHKVFHKrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14010 224 NEDPPP-----------PPPKVSSK-PSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
70-315 3.31e-28

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: 111.62  E-value: 3.31e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK-----KVLQDRRYK--NRELQLMRPMDHPNVISLKHCfFSTTSRdelfLN 142
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKivskkKAPEDYLQKflPREIEVIKGLKHPNLICFYEA-IETTSR----VY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAK--- 219
Cdd:cd14162  77 IIMELAENG---DLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSK-GVVHRDLKCENLLLDKNNN-LKITDFGFARgvm 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEPNIS--YICSRYYRAPELIFGaTEYTASI-DIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTR---- 292
Cdd:cd14162 152 KTKDGKPKLSetYCGSYAYASPEILRG-IPYDPFLsDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRVVFPKNptvs 230
                       250       260
                ....*....|....*....|....*...
gi 42571361 293 EEIRCM-----NPNYTDFRFPQIKAHPW 315
Cdd:cd14162 231 EECKDLilrmlSPVKKRITIEEIKRDPW 258
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
75-285 4.25e-28

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: 111.48  E-value: 4.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNRELQ-------LMRPMDHPNVISLKHCFFSTTSRDelfLNLVMEY 147
Cdd:cd08217   7 TIGKGSFGTVRKVRRKSDGKILVWKE-IDYGKMSEKEKQqlvsevnILRELKHPNIVRYYDRIVDRANTT---LYIVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIH--TVPG--VCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLv 222
Cdd:cd08217  83 CEGgDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHnrSVGGgkILHRDLKPANIFLDS-DNNVKLGDFGLARVL- 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 223 kGEPN---ISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIK 285
Cdd:cd08217 161 -SHDSsfaKTYVGTPYYMSPELLNEQS-YDEKSDIWSLGCLIYELCALHPPFQAANQ-LELAKKIK 223
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
76-354 5.26e-28

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 110.86  E-value: 5.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVL----QDRRYKNRELQLMRPMDHPNVIslkHCFFSTTSRDELFlnLVMEYVP-- 149
Cdd:cd06613   8 IGSGTYGDVYKARNIATGELAAVKVIKlepgDDFEIIQQEISMLKECRHPNIV---AYFGSYLRRDKLW--IVMEYCGgg 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 --ETLYRVLRHYTSSNqrmpIFYVklyTYQIFRGLAYIHTVpGVCHRDVKPQNLLvdpLTHQ--VKLCDFGSAKVLVK-- 223
Cdd:cd06613  83 slQDIYQVTGPLSELQ----IAYV---CRETLKGLAYLHST-GKIHRDIKGANIL---LTEDgdVKLADFGVSAQLTAti 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNiSYICSRYYRAPELIfgATE----YTASIDIWSAGCVLAELLLGQ-PLFPgensvdqlVEIIKVLgtptreeircM 298
Cdd:cd06613 152 AKRK-SFIGTPYWMAPEVA--AVErkggYDGKCDIWALGITAIELAELQpPMFD--------LHPMRAL----------F 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 299 NPNYTDFRFPQIKA-HPWHKVFHkrmppeaiDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06613 211 LIPKSNFDPPKLKDkEKWSPDFH--------DFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
69-267 6.92e-28

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: 110.90  E-value: 6.92e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQD-----------RRYKNRELQLMRPM-DHPNVISLkHCFFSTtsr 136
Cdd:cd13993   1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnskdgndfqKLPQLREIDLHRRVsRHPNIITL-HDVFET--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 dELFLNLVMEYVPET-LYRVLRhytsSNQRMPI--FYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLC 213
Cdd:cd13993  77 -EVAIYIVLEYCPNGdLFEAIT----ENRIYVGktELIKNVFLQLIDAVKHCHSL-GIYHRDIKPENILLSQDEGTVKLC 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 214 DFGSAKvlvkgEPNISY---ICSRYYRAPELI-----FGATEYTASIDIWSAGCVLAELLLG 267
Cdd:cd13993 151 DFGLAT-----TEKISMdfgVGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGIILLNLTFG 207
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
73-359 7.78e-28

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 110.31  E-value: 7.78e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361     73 ERVVGTGSFGIVFQAK----CLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCffsTTSRDELFlnL 143
Cdd:smart00219   4 GKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDASEQQieeflREARIMRKLDHPNVVKLLGV---CTEEEPLY--I 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    144 VMEYVPetlYRVLRHYTSSNQ-RMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLV 222
Cdd:smart00219  79 VMEYME---GGDLLSYLRKNRpKLSLSDLLSFALQIARGMEYLESKNFI-HRDLAARNCLVGE-NLVVKISDFGLSRDLY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    223 KGEpnisyicsrYYR-----------APELIFGATEYTASiDIWSAGCVLAELL-LGQPLFPGEnSVDQLVEIIKvlgtp 290
Cdd:smart00219 154 DDD---------YYRkrggklpirwmAPESLKEGKFTSKS-DVWSFGVLLWEIFtLGEQPYPGM-SNEEVLEYLK----- 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361    291 treeircmnpnyTDFRFPQIkahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTaleacahpfFNELRE 359
Cdd:smart00219 218 ------------NGYRLPQP----------PNCPPELYDLMLQCWAEDPEDRPT---------FSELVE 255
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
74-354 7.79e-28

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: 110.52  E-value: 7.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDR---------RYKNRELQLMRPMDHPNVISLKHCffsttSRDELFLNLV 144
Cdd:cd06625   6 KLLGQGAFGQVYLCYDADTGRELAVKQVEIDPinteaskevKALECEIQLLKNLQHERIVQYYGC-----LQDEKSLSIF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP-ETLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDpLTHQVKLCDFGSAKVL-- 221
Cdd:cd06625  81 MEYMPgGSVKDEIKAYGALTENV----TRKYTRQILEGLAYLHSNMIV-HRDIKGANILRD-SNGNVKLGDFGASKRLqt 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 ---------VKGEPnisyicsrYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFpgeNSVDQLVEIIKVLGTPTR 292
Cdd:cd06625 155 icsstgmksVTGTP--------YWMSPEVINGEG-YGRKADIWSVGCTVVEMLTTKPPW---AEFEPMAAIFKIATQPTN 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 293 eeircmnpnytdfrfPQIKAHpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06625 223 ---------------PQLPPH---------VSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
76-313 9.44e-28

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: 112.04  E-value: 9.44e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVfqAKCLETG--ESVAIKkVLQDRRYKNRELQLMRPM---------DHPNVISLKHCFfstTSRDELFLnlV 144
Cdd:cd14229   8 LGRGTFGQV--VKCWKRGtnEIVAVK-ILKNHPSYARQGQIEVGIlarlsnenaDEFNFVRAYECF---QHRNHTCL--V 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPETLYRVLRHYTSSNqrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDPL--THQVKLCDFGSAKVL 221
Cdd:cd14229  80 FEMLEQNLYDFLKQNKFSP--LPLKVIRPILQQVATALKKLKSL-GLIHADLKPENiMLVDPVrqPYRVKVIDFGSASHV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNiSYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIR----- 296
Cdd:cd14229 157 SKTVCS-TYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLPGEQLLNvgtkt 234
                       250       260
                ....*....|....*....|...
gi 42571361 297 ----CMNPN--YTDFRFPQIKAH 313
Cdd:cd14229 235 srffCRETDapYSSWRLKTLEEH 257
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
76-355 1.69e-27

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: 109.62  E-value: 1.69e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV----LQDRRYKN---RELQLMRPMDHPNVISLkHCFFsttsRDELFLNLVMEYV 148
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTFALKCVkkrhIVQTRQQEhifSEKEILEECNSPFIVKL-YRTF----KDKKYLYMLMEYC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P-ETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpltHQ--VKLCDFGSAKVLVKGE 225
Cdd:cd05572  76 LgGELWTILR----DRGLFDEYTARFYTACVVLAFEYLHSR-GIIYRDLKPENLLLD---SNgyVKLVDFGFAKKLGSGR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFpGENSVDQLVeiikvlgtpTREEIRCMNPNYTdf 305
Cdd:cd05572 148 KTWTFCGTPEYVAPEIILNKG-YDFSVDYWSLGILLYELLTGRPPF-GGDDEDPMK---------IYNIILKGIDKIE-- 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 306 rFPQIkahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACA-----HPFFN 355
Cdd:cd05572 215 -FPKY------------IDKNAKNLIKQLLRRNPEERLGYLKGGIrdikkHKWFE 256
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
77-352 1.71e-27

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: 109.28  E-value: 1.71e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVA---IKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYV--PET 151
Cdd:cd14006   2 GRGRFGVVKRCIEKATGREFAakfIPKRDKKKEAVLREISILNQLQHPRIIQLHEAYESPTE-----LVLILELCsgGEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 152 LYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTH-QVKLCDFGSAKVLVKGEPNISY 230
Cdd:cd14006  77 LDRLAERGSLSEEE-----VRTYMRQLLEGLQYLHNH-HILHLDLKPENILLADRPSpQIKIIDFGLARKLNPGEELKEI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 ICSRYYRAPELIFG--ATEYTasiDIWSAGcVLAELLL-GQPLFPGENSVDQLVEIIKVlgtptreeircmnpNYtDFRF 307
Cdd:cd14006 151 FGTPEFVAPEIVNGepVSLAT---DMWSIG-VLTYVLLsGLSPFLGEDDQETLANISAC--------------RV-DFSE 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42571361 308 PqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14006 212 E----------YFSSVSQEAKDFIRKLLVKEPRKRPTAQEALQHP 246
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
77-315 1.98e-27

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: 109.27  E-value: 1.98e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKkVLQDRRYKN---------RELQLMRPMDHPNVISLkHCFFSTTSRDELFlnLVMEY 147
Cdd:cd14119   2 GEGSYGKVKEVLDTETLCRRAVK-ILKKRKLRRipngeanvkREIQILRRLNHRNVIKL-VDVLYNEEKQKLY--MVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETLYRVLRhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLVKGEPN 227
Cdd:cd14119  78 CVGGLQEMLD--SAPDKRLPIWQAHGYFVQLIDGLEYLHSQ-GIIHKDIKPGNLLLT-TDGTLKISDFGVAEALDLFAED 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 isYICSRYY-----RAPELIFGATEYTA-SIDIWSAGCVLAELLLGQPLFPGENsVDQLVEII--------KVLGTPTRE 293
Cdd:cd14119 154 --DTCTTSQgspafQPPEIANGQDSFSGfKVDIWSAGVTLYNMTTGKYPFEGDN-IYKLFENIgkgeytipDDVDPDLQD 230
                       250       260
                ....*....|....*....|....*
gi 42571361 294 EIRCM---NPNyTDFRFPQIKAHPW 315
Cdd:cd14119 231 LLRGMlekDPE-KRFTIEQIRQHPW 254
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
75-305 2.29e-27

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 109.87  E-value: 2.29e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-----RELQLM---RPMDHPNVISLKHCFFSTTSrdelfLNLVME 146
Cdd:cd06917   8 LVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvsdiqKEVALLsqlKLGQPKNIIKYYGSYLKGPS-----LWIIMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRmpifYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLVKGE- 225
Cdd:cd06917  83 YCEGGSIRTLMRAGPIAER----YIAVIMREVLVALKFIHKD-GIIHRDIKAANILVT-NTGNVKLCDFGVAASLNQNSs 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlGTPTREEIRCMNPNYTDF 305
Cdd:cd06917 157 KRSTFVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPK--SKPPRLEGNGYSPLLKEF 234
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
75-354 2.65e-27

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: 109.44  E-value: 2.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN----------RELQLMRPMDHPNVISLkhcfFSTTSRDELFlNLV 144
Cdd:cd06630   7 LLGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSeqeevveairEEIRMMARLNHPNIVRM----LGATQHKSHF-NIF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVKLCDFGSA----- 218
Cdd:cd06630  82 VEWMAGgSVASLLSKYGAFSENV----IINYTLQILRGLAYLHD-NQIIHRDLKGANLLVDSTGQRLRIADFGAAarlas 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeIRCM 298
Cdd:cd06630 157 KGTGAGEFQGQLLGTIAFMAPEVLRG-EQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFK---------IASA 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 299 NpnytdfRFPQIKAHpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06630 227 T------TPPPIPEH---------LSPGLRDVTLRCLELQPEDRPPARELLKHPVF 267
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
67-290 6.01e-27

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: 110.18  E-value: 6.01e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  67 TISYMAERVVGTGSFGIVfqAKCLE--TGESVAIKKVLQDRRYKNR---ELQLMRPM-----DHPNVISLKHCFfsttsR 136
Cdd:cd14228  14 TNSYEVLEFLGRGTFGQV--AKCWKrsTKEIVAIKILKNHPSYARQgqiEVSILSRLssenaDEYNFVRSYECF-----Q 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 DELFLNLVMEYVPETLYRVLRHYTSSNqrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDPL--THQVKLC 213
Cdd:cd14228  87 HKNHTCLVFEMLEQNLYDFLKQNKFSP--LPLKYIRPILQQVATALMKLKSL-GLIHADLKPENiMLVDPVrqPYRVKVI 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 214 DFGSAKVLVKGEPNiSYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTP 290
Cdd:cd14228 164 DFGSASHVSKAVCS-TYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLP 238
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
74-352 6.53e-27

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: 107.86  E-value: 6.53e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKNR-----ELQLMRPMDHPNVISLKHCFFsttsrDELFLNLVMEY 147
Cdd:cd08530   6 KKLGKGSYGSVYKVKRLSDNQVYALKEVnLGSLSQKERedsvnEIRLLASVNHPNIIRYKEAFL-----DGNRLCIVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDPltHQVKLCDFGSAKVLVKGE 225
Cdd:cd08530  81 APFgDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQ-KILHRDLKSANiLLSAG--DLVKIGDLGISKVLKKNL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNiSYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVeiiKVLGTptreeircmnpnytdf 305
Cdd:cd08530 158 AK-TQIGTPLYAAPE-VWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRY---KVCRG---------------- 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42571361 306 RFPQIkahpwhkvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd08530 217 KFPPI---------PPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
74-357 1.04e-26

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: 108.84  E-value: 1.04e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK-----KVLQDR-----RYKNRELQLMRpmDHPNVISLkHCFFSTTSRdeLFLnl 143
Cdd:cd05570   1 KVLGKGSFGKVMLAERKKTDELYAIKvlkkeVIIEDDdvectMTEKRVLALAN--RHPFLTGL-HACFQTEDR--LYF-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--ETLYRVLRhytssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVL 221
Cdd:cd05570  74 VMEYVNggDLMFHIQR-----ARRFTEERARFYAAEICLALQFLHER-GIIYRDLKLDNVLLDAEGH-IKIADFGMCKEG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYIC-SRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEIIKvlgtptreeircmnp 300
Cdd:cd05570 147 IWGGNTTSTFCgTPDYIAPEILRE-QDYGFSVDWWALGVLLYEMLAGQSPFEGDD-EDELFEAIL--------------- 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 301 nYTDFRFPqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLR--CT---ALEACAHPFFNEL 357
Cdd:cd05570 210 -NDEVLYP------------RWLSREAVSILKGLLTKDPARRlgCGpkgEADIKAHPFFRNI 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
70-354 1.41e-26

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: 107.27  E-value: 1.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKC--LETGESVAIKKVlqDRR-----YKN----RELQLMRPMDHPNVISLkHCFFSTTSRde 138
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYtkSGLKEKVACKII--DKKkapkdFLEkflpRELEILRKLRHPNIIQV-YSIFERGSK-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 139 LFlnLVMEYVPETlyRVLRhYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSA 218
Cdd:cd14080  77 VF--IFMEYAEHG--DLLE-YIQKRGALSESQARIWFRQLALAVQYLHSL-DIAHRDLKCENILLDSNNN-VKLSDFGFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEPNI---SYICSRYYRAPELIFGaTEYTASI-DIWSAGCVLAELLLGQPLFPGENsVDQLVEiikvlgtptree 294
Cdd:cd14080 150 RLCPDDDGDVlskTFCGSAAYAAPEILQG-IPYDPKKyDIWSLGVILYIMLCGSMPFDDSN-IKKMLK------------ 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 295 iRCMNPNytdFRFPQIKAHPwhkvfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14080 216 -DQQNRK---VRFPSSVKKL---------SPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
67-290 1.75e-26

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: 109.02  E-value: 1.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  67 TISYMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQL---------MRPMDHPNVISLKHCFfsttsRD 137
Cdd:cd14227  14 TNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIK-ILKNHPSYARQGQIevsilarlsTESADDYNFVRAYECF-----QH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 138 ELFLNLVMEYVPETLYRVLRHYTSSNqrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDP--LTHQVKLCD 214
Cdd:cd14227  88 KNHTCLVFEMLEQNLYDFLKQNKFSP--LPLKYIRPILQQVATALMKLKSL-GLIHADLKPENiMLVDPsrQPYRVKVID 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 215 FGSAKVLVKGEPNiSYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTP 290
Cdd:cd14227 165 FGSASHVSKAVCS-TYLQSRYYRAPEIILG-LPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLP 238
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
70-354 2.12e-26

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: 107.05  E-value: 2.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFqaKCLE--TGESVAIK--KVLQDRRYKN----------RELQLMRPMD-HPNVISLkHCFFSTT 134
Cdd:cd14093   5 YEPKEILGRGVSSTVR--RCIEkeTGQEFAVKiiDITGEKSSENeaeelreatrREIEILRQVSgHPNIIEL-HDVFESP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 135 SrdelFLNLVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLC 213
Cdd:cd14093  82 T----FIFLVFELCRKgELFDYLTEVVTLSEKKTRRIMR----QLFEAVEFLHSL-NIVHRDLKPENILLDD-NLNVKIS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 214 DFGSAKVLVKGEpNISYIC-SRYYRAPELI-----FGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIikvl 287
Cdd:cd14093 152 DFGFATRLDEGE-KLRELCgTPGYLAPEVLkcsmyDNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNI---- 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 288 gtptreeircMNPNYTdFRFPQikahpWHKVFHkrmppEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14093 227 ----------MEGKYE-FGSPE-----WDDISD-----TAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
77-353 3.24e-26

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: 105.83  E-value: 3.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQA-KCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFsttsrDELFLNLVMEYVP 149
Cdd:cd14121   4 GSGTYATVYKAyRKSGAREVVAVKCVSKSSLNKAstenllTEIELLKKLKHPHIVELKDFQW-----DEEHIYLIMEYCS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQN-LLVDPLTHQVKLCDFGSAKVLVKGEPNI 228
Cdd:cd14121  79 GG---DLSRFIRSRRTLPESTVRRFLQQLASALQFLRE-HNISHMDLKPQNlLLSSRYNPVLKLADFGFAQHLKPNDEAH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFpGENSVDQLVEIIKvlgtpTREEIrcmnpnytdfrfp 308
Cdd:cd14121 155 SLRGSPLYMAPEMILKKK-YDARVDLWSVGVILYECLFGRAPF-ASRSFEELEEKIR-----SSKPI------------- 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42571361 309 QIKAHPwhkvfhkRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14121 215 EIPTRP-------ELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
74-354 3.87e-26

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: 105.80  E-value: 3.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK-----KVLQDRRYKN--RELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd05578   6 RVIGKGSFGKVCIVQKKDTKKMFAMKymnkqKCIEKDSVRNvlNELEILQELEHPFLVNLWYSF-----QDEEDMYMVVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVpetLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEP 226
Cdd:cd05578  81 LL---LGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHS-KNIIHRDIKPDNILLDEQGH-VHITDFNIATKLTDGTL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSvdqlveiikvlgtPTREEIRCMnpnytdfr 306
Cdd:cd05578 156 ATSTSGTKPYMAPEVFMRAG-YSFAVDWWSLGVTAYEMLRGKRPYEIHSR-------------TSIEEIRAK-------- 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 307 fpQIKAHPwhkVFHKRMPPEAIDLASRLLQYSPSLRCTALEAC-AHPFF 354
Cdd:cd05578 214 --FETASV---LYPAGWSEEAIDLINKLLERDPQKRLGDLSDLkNHPYF 257
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
75-354 5.61e-26

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: 105.52  E-value: 5.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLkHCFFstTSRDELFLnlVMEYVP 149
Cdd:cd06610   8 VIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSmdelrKEIQAMSQCNHPNVVSY-YTSF--VVGDELWL--VMPLLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRH-YTSSNQRMPIFYVKLYtyQIFRGLAYIHTvPGVCHRDVKPQNLLVDplTH-QVKLCDFGSAKVLVKGEP 226
Cdd:cd06610  83 GgSLLDIMKSsYPRGGLDEAIIATVLK--EVLKGLEYLHS-NGQIHRDVKAGNILLG--EDgSVKIADFGVSASLATGGD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 NIS-----YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQP----LFPgensvdqlveiIKVLgtptreeirc 297
Cdd:cd06610 158 RTRkvrktFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAApyskYPP-----------MKVL---------- 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 298 MNPNYTDfrFPQIKAHPWHKVFHKRMPpeaiDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06610 217 MLTLQND--PPSLETGADYKKYSKSFR----KMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
76-360 6.11e-26

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: 106.66  E-value: 6.11e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFFSTTSRdelflNLVMEYV 148
Cdd:cd06633  29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNekwqdiiKEVKFLQQLKHPNTIEYKGCYLKDHTA-----WLVMEYC 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHYTSSNQRMPIFYVklyTYQIFRGLAYIHTvPGVCHRDVKPQN-LLVDPltHQVKLCDFGSAKVlvkGEPN 227
Cdd:cd06633 104 LGSASDLLEVHKKPLQEVEIAAI---THGALQGLAYLHS-HNMIHRDIKAGNiLLTEP--GQVKLADFGSASI---ASPA 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYICSRYYRAPELIFGATE--YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircmNPNytdf 305
Cdd:cd06633 175 NSFVGTPYWMAPEVILAMDEgqYDGKVDIWSLGITCIELAERKPPLFNMNAMSALYHIAQ-------------NDS---- 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 306 rfPQIKAHPWHKVFHKrmppeaidLASRLLQYSPSLRCTALEACAHPFFNELREP 360
Cdd:cd06633 238 --PTLQSNEWTDSFRG--------FVDYCLQKIPQERPSSAELLRHDFVRRERPP 282
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
76-342 6.27e-26

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: 105.43  E-value: 6.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKcLETGESVAIKKV-----LQDRRYKNRELQLMRPMDHPNVISLKHCFFSttsRDELFLnlVMEYVPE 150
Cdd:cd14066   1 IGSGGFGTVYKGV-LENGTVVAVKRLnemncAASKKEFLTELEMLGRLRHPNLVRLLGYCLE---SDEKLL--VYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 -TLYRVLRHYTSSN-----QRMPIfyvklyTYQIFRGLAYIHT--VPGVCHRDVKPQNLLVDPLThQVKLCDFGSAKVLV 222
Cdd:cd14066  75 gSLEDRLHCHKGSPplpwpQRLKI------AKGIARGLEYLHEecPPPIIHGDIKSSNILLDEDF-EPKLTDFGLARLIP 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYICSRY---YRAPELIFGAtEYTASIDIWSAGCVLAELLLGQP---LFPGENSVDQLVEIIKVLGTPTREEI- 295
Cdd:cd14066 148 PSESVSKTSAVKGtigYLAPEYIRTG-RVSTKSDVYSFGVVLLELLTGKPavdENRENASRKDLVEWVESKGKEELEDIl 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 296 -RCMNPNYTDFRfPQIKAhpwhkvfhkrmppeAIDLASRLLQYSPSLR 342
Cdd:cd14066 227 dKRLVDDDGVEE-EEVEA--------------LLRLALLCTRSDPSLR 259
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
70-352 1.48e-25

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: 104.39  E-value: 1.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK----KVLQDR--RYKnRELQLMRPMDHPNVISLKHCFfstTSRDELFLnl 143
Cdd:cd14078   5 YELHETIGSGGFAKVKLATHILTGEKVAIKimdkKALGDDlpRVK-TEIEALKNLSHQHICRLYHVI---ETDNKIFM-- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--EtlyrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFG-SAKV 220
Cdd:cd14078  79 VLEYCPggE-----LFDYIVAKDRLSEDEARVFFRQIVSAVAYVHS-QGYAHRDLKPENLLLDE-DQNLKLIDFGlCAKP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYIC-SRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK-VLGTPtreeircm 298
Cdd:cd14078 152 KGGMDHHLETCCgSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSgKYEEP-------- 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 299 npnytdfrfpqikahPWhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14078 224 ---------------EW-------LSPSSKLLLDQMLQVDPKKRITVKELLNHP 255
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
73-353 2.23e-25

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: 104.03  E-value: 2.23e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVV-GTGSFGIVFQAKCLETGESVAIKKV-LQDRRYK---NRELQLMRPMDHPNVISlkhcFFSTTSRDELFLnLVMEY 147
Cdd:cd06624  12 ERVVlGKGTFGVVYAARDLSTQVRIAIKEIpERDSREVqplHEEIALHSRLSHKNIVQ----YLGSVSEDGFFK-IFMEQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPE-TLYRVLRHY---TSSNQRMPIFYVKlytyQIFRGLAYIHTVPGVcHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVK 223
Cdd:cd06624  87 VPGgSLSALLRSKwgpLKDNENTIGYYTK----QILEGLKYLHDNKIV-HRDIKGDNVLVNTYSGVVKISDFGTSKRLAG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNI-SYICSRYYRAPELI-FGATEYTASIDIWSAGCVLAELLLGQPLFpgensvdqlveiikvlgtptreeIRCMNPN 301
Cdd:cd06624 162 INPCTeTFTGTLQYMAPEVIdKGQRGYGPPADIWSLGCTIIEMATGKPPF-----------------------IELGEPQ 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 302 YTDFRFPQIKAHPwhkVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06624 219 AAMFKVGMFKIHP---EIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPF 267
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
69-342 5.73e-25

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: 102.80  E-value: 5.73e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVL----QDRRYKNRELQLMRPM-DHPNVISLKHCFFSTTSRDELFLnL 143
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYfndeEQLRVAIKEIEIMKRLcGHPNIVQYYDSAILSSEGRKEVL-L 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRH----YTSSNQRMPIFYvklytyQIFRGLAYIHTV-PGVCHRDVKPQNLLVDPlTHQVKLCDFGSA 218
Cdd:cd13985  80 LMEYCPGSLVDILEKsppsPLSEEEVLRIFY------QICQAVGHLHSQsPPIIHRDIKIENILFSN-TGRFKLCDFGSA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KvlvkgepNISYICSRY-----------------YRAPELI--FGATEYTASIDIWSAGCVLAELLLGQPLFpGENSVdq 279
Cdd:cd13985 153 T-------TEHYPLERAeevniieeeiqknttpmYRAPEMIdlYSKKPIGEKADIWALGCLLYKLCFFKLPF-DESSK-- 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 280 lveiikvlgtptreeIRCMNPNYTdfrfpqIKAHPwhkvfhkRMPPEAIDLASRLLQYSPSLR 342
Cdd:cd13985 223 ---------------LAIVAGKYS------IPEQP-------RYSPELHDLIRHMLTPDPAER 257
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
74-353 1.02e-24

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: 101.76  E-value: 1.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFFSttsrdELFLNLVME 146
Cdd:cd06607   7 REIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTekwqdiiKEVKFLRQLRHPNTIEYKGCYLR-----EHTAWLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRMPIFYVklyTYQIFRGLAYIHTVpGVCHRDVKPQNLLvdpLTH--QVKLCDFGSAKVLvkg 224
Cdd:cd06607  82 YCLGSASDIVEVHKKPLQEVEIAAI---CHGALQGLAYLHSH-NRIHRDVKAGNIL---LTEpgTVKLADFGSASLV--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELIFGATE--YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircMNPny 302
Cdd:cd06607 152 CPANSFVGTPYWMAPEVILAMDEgqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQ------------NDS-- 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 303 tdfrfPQIKAHPWHKVFHKrmppeaidLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06607 218 -----PTLSSGEWSDDFRN--------FVDSCLQKIPQDRPSAEDLLKHPF 255
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
71-354 1.33e-24

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: 101.97  E-value: 1.33e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  71 MAERVVGTGSFG-IVFQAKcLEtGESVAIKKVLQD-RRYKNRELQLMRPMD-HPNVISLkHCffstTSRDELFLNLVMEY 147
Cdd:cd13982   4 FSPKVLGYGSEGtIVFRGT-FD-GRPVAVKRLLPEfFDFADREVQLLRESDeHPNVIRY-FC----TEKDRQFLYIALEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETLYRVLRHYTSSNQRM-PIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTH----QVKLCDFGSAKVLV 222
Cdd:cd13982  77 CAASLQDLVESPRESKLFLrPGLEPVRLLRQIASGLAHLHSL-NIVHRDLKPQNILISTPNAhgnvRAMISDFGLCKKLD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPniSYIC------SRYYRAPELIFGATEY--TASIDIWSAGCVLAELLLGqplfpGENSvdqlveiikvLGTPTREE 294
Cdd:cd13982 156 VGRS--SFSRrsgvagTSGWIAPEMLSGSTKRrqTRAVDIFSLGCVFYYVLSG-----GSHP----------FGDKLERE 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 295 IRCMNPNYTDFRFPQIKAHpwhkvfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd13982 219 ANILKGKYSLDKLLSLGEH----------GPEAQDLIERMIDFDPEKRPSAEEVLNHPFF 268
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
70-352 1.59e-24

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: 101.31  E-value: 1.59e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVL-------QDRRYKNRELQLMRPMDHPNVISLKHCFfstTSRDELFLn 142
Cdd:cd14073   3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKkdkiedeQDMVRIRREIEIMSSLNHPHIIRIYEVF---ENKDKIVI- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 lVMEYVPE-TLYrvlrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd14073  79 -VMEYASGgELY----DYISERRRLPEREARRIFRQIVSAVHYCHK-NGVVHRDLKLENILLDQ-NGNAKIADFGLSNLY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsvdqlveiIKVLgtptREEIRCmnpn 301
Cdd:cd14073 152 SKDKLLQTFCGSPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSD--------FKRL----VKQISS---- 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 302 yTDFRFPqikahpwhkvfhkRMPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14073 216 -GDYREP-------------TQPSDASGLIRWMLTVNPKRRATIEDIANHW 252
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
76-354 1.68e-24

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: 101.37  E-value: 1.68e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVlqDRRYKNR------ELQLMRPMDHPNVISLkhcFFSTTSRDELFLnlVMEYVP 149
Cdd:cd06648  15 IGEGSTGIVCIATDKSTGRQVAVKKM--DLRKQQRrellfnEVVIMRDYQHPNIVEM---YSSYLVGDELWV--VMEFLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRHytssnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTH--QVKLCDFGSAKVLVKGEP 226
Cdd:cd06648  88 GgALTDIVTH-----TRMNEEQIATVCRAVLKALSFLHS-QGVIHRDIKSDSIL---LTSdgRVKLSDFGFCAQVSKEVP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 227 N-ISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLveiikvlgtptrEEIRCMNPnytdf 305
Cdd:cd06648 159 RrKSLVGTPYWMAPEVI-SRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAM------------KRIRDNEP----- 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 306 rfPQIKAHpwHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06648 221 --PKLKNL--HKV-----SPRLRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
76-285 1.75e-24

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 101.33  E-value: 1.75e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV-LQ--DRRYKN---RELQLMRPMDHPNVISLKHCFFsttsrDELFLNLVMEYVP 149
Cdd:cd08529   8 LGKGSFGVVYKVVRKVDGRVYALKQIdISrmSRKMREeaiDEARVLSKLNSPYVIKYYDSFV-----DKGKLNIVMEYAE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRHYTSsnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL------- 221
Cdd:cd08529  83 NgDLHSLIKSQRG--RPLPEDQIWKFFIQTLLGLSHLHS-KKILHRDIKSMNIFLDK-GDNVKIGDLGVAKILsdttnfa 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 222 --VKGEPnisyicsrYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK 285
Cdd:cd08529 159 qtIVGTP--------YYLSPELCEDKP-YNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVR 215
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
75-277 2.72e-24

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: 100.92  E-value: 2.72e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKclETGESVAIKKVlqDRRYKNR--------ELQLMRpMDHPNVISLkhcFFSTTSRDELFLNLV-M 145
Cdd:cd13979  10 PLGSGGFGSVYKAT--YKGETVAVKIV--RRRRKNRasrqsfwaELNAAR-LRHENIVRV---LAAETGTDFASLGLIiM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYV-PETLYRVLrhYTSSnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkG 224
Cdd:cd13979  82 EYCgNGTLQQLI--YEGS-EPLPLAHRILISLDIARALRFCHS-HGIVHLDVKPANILISE-QGVCKLCDFGCSVKL--G 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 225 EPN-----ISYICSRY-YRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSV 277
Cdd:cd13979 155 EGNevgtpRSHIGGTYtYRAPELLKGER-VTPKADIYSFGITLWQMLTRELPYAGLRQH 212
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
72-353 3.32e-24

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: 100.56  E-value: 3.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  72 AERVVGTGSFGIVFQAKCLETGESVAIKKV-------LQDRRYKNrELQLMRPMDHPNVISLKhCFFSTTSRdeLFlnLV 144
Cdd:cd14082   7 PDEVLGSGQFGIVYGGKHRKTGRDVAIKVIdklrfptKQESQLRN-EVAILQQLSHPGVVNLE-CMFETPER--VF--VV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP-ETLYRVLrhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTH--QVKLCDFGSAKVL 221
Cdd:cd14082  81 MEKLHgDMLEMIL---SSEKGRLPERITKFLVTQILVALRYLHS-KNIVHCDLKPENVLLASAEPfpQVKLCDFGFARII 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEiikvlgtptreeircmnpn 301
Cdd:cd14082 157 GEKSFRRSVVGTPAYLAPE-VLRNKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQ------------------- 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 302 YTDFRFPqikAHPWhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14082 217 NAAFMYP---PNPW-----KEISPDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
74-354 5.58e-24

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: 99.62  E-value: 5.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVL--QDRRYKN--------RELQLMR---PMDHPNVISLKHCFfsttSRDELF 140
Cdd:cd14005   6 DLLGKGGFGTVYSGVRIRDGLPVAVKFVPksRVTEWAMingpvpvpLEIALLLkasKPGVPGVIRLLDWY----ERPDGF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LnLVMEYvPE---TLYRVLRHYTSSNQRMpifyvklyTYQIFRGLayIHTV-----PGVCHRDVKPQNLLVDPLTHQVKL 212
Cdd:cd14005  82 L-LIMER-PEpcqDLFDFITERGALSENL--------ARIIFRQV--VEAVrhchqRGVLHRDIKDENLLINLRTGEVKL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 213 CDFGSAKVLvKGEPNISYICSRYYRAPELI----FGATEYTasidIWSAGCVLAELLLGQplFPGENsvdqlveiikvlg 288
Cdd:cd14005 150 IDFGCGALL-KDSVYTDFDGTRVYSPPEWIrhgrYHGRPAT----VWSLGILLYDMLCGD--IPFEN------------- 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 289 tptREEIrcmnpnytdfrfpqIKAHPWhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14005 210 ---DEQI--------------LRGNVL---FRPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
76-352 6.20e-24

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: 99.61  E-value: 6.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFqaKCLE--TGESVAIKKV----LQDRRYKNRELQLMRPMDHPNVISLKHCFfstTSRDELFlnLVMEYVP 149
Cdd:cd14103   1 LGRGKFGTVY--RCVEkaTGKELAAKFIkcrkAKDREDVRNEIEIMNQLRHPRLLQLYDAF---ETPREMV--LVMEYVA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 --ETLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLL-VDPLTHQVKLCDFGSA-------- 218
Cdd:cd14103  74 ggELFERVVDDDFELTERDCILFMR----QICEGVQYMHK-QGILHLDLKPENILcVSRTGNQIKIIDFGLArkydpdkk 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 -KVLVkGEPNisyicsryYRAPELI-FGATEYTAsiDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeir 296
Cdd:cd14103 149 lKVLF-GTPE--------FVAPEVVnYEPISYAT--DMWSVGVICYVLLSGLSPFMGDNDAETLANVTRA---------- 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 297 cmNPNYTDFRFPQIKahpwhkvfhkrmpPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14103 208 --KWDFDDEAFDDIS-------------DEAKDFISKLLVKDPRKRMSAAQCLQHP 248
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
74-389 6.81e-24

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: 100.90  E-value: 6.81e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFFSttsrdELFLNLVME 146
Cdd:cd06635  31 REIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNekwqdiiKEVKFLQRIKHPNSIEYKGCYLR-----EHTAWLVME 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRMPIFYVklyTYQIFRGLAYIHTvPGVCHRDVKPQN-LLVDPltHQVKLCDFGSAKVLvkgE 225
Cdd:cd06635 106 YCLGSASDLLEVHKKPLQEIEIAAI---THGALQGLAYLHS-HNMIHRDIKAGNiLLTEP--GQVKLADFGSASIA---S 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIFGATE--YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircmNPNyt 303
Cdd:cd06635 177 PANSFVGTPYWMAPEVILAMDEgqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQ-------------NES-- 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 304 dfrfPQIKAHPWHKVFHkrmppeaiDLASRLLQYSPSLRCTALEACAHPFFneLREpnarlpngRPLPPLFNFKQELGGA 383
Cdd:cd06635 242 ----PTLQSNEWSDYFR--------NFVDSCLQKIPQDRPTSEELLKHMFV--LRE--------RPETVLIDLIQRTKDA 299

                ....*.
gi 42571361 384 SMELIN 389
Cdd:cd06635 300 VRELDN 305
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
70-315 9.22e-24

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


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 99.00  E-value: 9.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSTTsrdelFLNL 143
Cdd:cd14071   2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEEnlkkiyREVQIMKMLNHPHIIKLYQVMETKD-----MLYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLVK 223
Cdd:cd14071  77 VTEYASNG---EIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKR-HIVHRDLKAENLLLD-ANMNIKIADFGFSNFFKP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPELiFGATEYTA-SIDIWSAGCVLAELLLGQPLFPGEN--SVDQLV-----EIIKVLGTPTREEI 295
Cdd:cd14071 152 GELLKTWCGSPPYAAPEV-FEGKEYEGpQLDIWSLGVVLYVLVCGALPFDGSTlqTLRDRVlsgrfRIPFFMSTDCEHLI 230
                       250       260
                ....*....|....*....|...
gi 42571361 296 RCM---NPNyTDFRFPQIKAHPW 315
Cdd:cd14071 231 RRMlvlDPS-KRLTIEQIKKHKW 252
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
77-365 1.01e-23

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: 99.81  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKKV---LQDRRYKnrelQLMRPMDhpnvISLK--HCFFSTTSRDELFLN----LVMEY 147
Cdd:cd06617  10 GRGAYGVVDKMRHVPTGTIMAVKRIratVNSQEQK----RLLMDLD----ISMRsvDCPYTVTFYGALFREgdvwICMEV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPLThQVKLCDFGSAKVLVKGEPN 227
Cdd:cd06617  82 MDTSLDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKLSVIHRDVKPSNVLINRNG-QVKLCDFGISGYLVDSVAK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYICSRYYRAPELIFGATE---YTASIDIWSAGCVLAELLLGQplFPGENsvdqlveiikvLGTPtreeircmnpnytd 304
Cdd:cd06617 161 TIDAGCKPYMAPERINPELNqkgYDVKSDVWSLGITMIELATGR--FPYDS-----------WKTP-------------- 213
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 305 frFPQIKA---HPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLP 365
Cdd:cd06617 214 --FQQLKQvveEPSPQLPAEKFSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKNTDVA 275
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
76-353 1.09e-23

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 99.82  E-value: 1.09e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLE-TGESVAIKKV---------LQDRRYKN--RELQLMRPMDHPNVISLKHcFFSTTSrdelFLNL 143
Cdd:cd14096   9 IGEGAFSNVYKAVPLRnTGKPVAIKVVrkadlssdnLKGSSRANilKEVQIMKRLSHPNIVKLLD-FQESDE----YYYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--ETLYRVLRhYTSSNQRMPIFYVKlytyQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTH------------- 208
Cdd:cd14096  84 VLELADggEIFHQIVR-LTYFSEDLSRHVIT----QVASAVKYLHEI-GVVHRDIKPENLLFEPIPFipsivklrkaddd 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 209 -------------------QVKLCDFGSAKVLvkGEPNISYICSRY-YRAPElIFGATEYTASIDIWSAGCVLAELLLGQ 268
Cdd:cd14096 158 etkvdegefipgvggggigIVKLADFGLSKQV--WDSNTKTPCGTVgYTAPE-VVKDERYSKKVDMWALGCVLYTLLCGF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 269 PLFPgENSVDQLVEiiKVLgtptreeircmNPNYTdFRFPQikahpWHKVFHkrmppEAIDLASRLLQYSPSLRCTALEA 348
Cdd:cd14096 235 PPFY-DESIETLTE--KIS-----------RGDYT-FLSPW-----WDEISK-----SAKDLISHLLTVDPAKRYDIDEF 289

                ....*
gi 42571361 349 CAHPF 353
Cdd:cd14096 290 LAHPW 294
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
70-353 2.12e-23

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: 98.25  E-value: 2.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV----LQD--RRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd14074   5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIdktkLDDvsKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTK-----LYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYR-VLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVL 221
Cdd:cd14074  80 ILELGDGgDMYDyIMKHENGLNEDL----ARKYFRQIVSAISYCHKL-HVVHRDLKPENVVFFEKQGLVKLTDFGFSNKF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEpNISYIC-SRYYRAPELIFGaTEYTA-SIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIikvlgtptreeircMN 299
Cdd:cd14074 155 QPGE-KLETSCgSLAYSAPEILLG-DEYDApAVDIWSLGVILYMLVCGQPPFQEANDSETLTMI--------------MD 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 300 PNYTdfrfpqIKAHpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14074 219 CKYT------VPAH---------VSPECKDLIRRMLIRDPKKRASLEEIENHPW 257
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
74-377 2.24e-23

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: 99.63  E-value: 2.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ--------LMRPMDHPNVISLkHCFFSTtsRDELFLnlVM 145
Cdd:cd05620   1 KVLGKGSFGKVLLAELKGKGEYFAVKALKKDVVLIDDDVEctmvekrvLALAWENPFLTHL-YCTFQT--KEHLFF--VM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGE 225
Cdd:cd05620  76 EFLNGG---DLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHS-KGIIYRDLKLDNVMLDRDGH-IKIADFGMCKENVFGD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYIC-SRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKVlGTPtreeircmnpnytd 304
Cdd:cd05620 151 NRASTFCgTPDYIAPEILQG-LKYTFSVDWWSFGVLLYEMLIGQSPFHGDDE-DELFESIRV-DTP-------------- 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 305 fRFPQikahpWhkvfhkrMPPEAIDLASRLLQYSPSLRCTAL-EACAHPFFNELrepNARLPNGRPLPPLFNFK 377
Cdd:cd05620 214 -HYPR-----W-------ITKESKDILEKLFERDPTRRLGVVgNIRGHPFFKTI---NWTALEKRELDPPFKPK 271
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
75-353 2.54e-23

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: 98.28  E-value: 2.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFqakC--LETGESVAIKKVLQDRRYKNR----------ELQLMRPMDHPNVISlkhcfFSTTSRDELFLN 142
Cdd:cd06631   8 VLGKGAYGTVY---CglTSTGQLIAVKQVELDTSDKEKaekeyeklqeEVDLLKTLKHVNIVG-----YLGTCLEDNVVS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVLRHYTSSNQrmPIFyvKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd06631  80 IFMEFVPGgSIASILARFGALEE--PVF--CRYTKQILEGVAYLHN-NNVIHRDIKGNNIMLMP-NGVIKLIDFGCAKRL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 ---------------VKGEPnisyicsrYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPlfPGENsvdqlveiikv 286
Cdd:cd06631 154 cinlssgsqsqllksMRGTP--------YWMAPEVI-NETGHGRKSDIWSIGCTVFEMATGKP--PWAD----------- 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 287 lgtptreeircMNPNYTDFrfpQIKAHpwhkvfHKRMP-------PEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06631 212 -----------MNPMAAIF---AIGSG------RKPVPrlpdkfsPEARDFVHACLTRDQDERPSAEQLLKHPF 265
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
73-356 2.99e-23

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: 98.91  E-value: 2.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVfqAKC--LETGESVAIKKVlqDRRYK-NRELQLMRPMD-HPNVISLKHCFfsttsRDELFLNLVMEYV 148
Cdd:cd14092  11 EEALGDGSFSVC--RKCvhKKTGQEFAVKIV--SRRLDtSREVQLLRLCQgHPNIVKLHEVF-----QDELHTYLVMELL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P--ETLYRV--LRHYTSSNQRmpifyvklytyQIFRGLA----YIHTVpGVCHRDVKPQNLLV--DPLTHQVKLCDFGSA 218
Cdd:cd14092  82 RggELLERIrkKKRFTESEAS-----------RIMRQLVsavsFMHSK-GVVHRDLKPENLLFtdEDDDAEIKIVDFGFA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEPNISYICSRYYRAPELI---FGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreEI 295
Cdd:cd14092 150 RLKPENQPLKTPCFTLPYAAPEVLkqaLSTQGYDESCDLWSLGVILYTMLSGQVPFQSPSRNESAAEIMK--------RI 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 296 RcmnpnYTDFRFpqiKAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd14092 222 K-----SGDFSF---DGEEWKNV-----SSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQG 269
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
77-283 4.45e-23

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: 97.90  E-value: 4.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKK--VLQDRRYKNR-----ELQLMRPMDHPNVISLK----HCFFSTTSRDELflnLVM 145
Cdd:cd13989   2 GSGGFGYVTLWKHQDTGEYVAIKKcrQELSPSDKNRerwclEVQIMKKLNHPNVVSARdvppELEKLSPNDLPL---LAM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLRHYTSSNQrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQV--KLCDFGSAKVLV 222
Cdd:cd13989  79 EYCSGgDLRKVLNQPENCCG-LKESEVRTLLSDISSAISYLHEN-RIIHRDLKPENIVLQQGGGRViyKLIDLGYAKELD 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 223 KGEPNISYICSRYYRAPELiFGATEYTASIDIWSAGCVLAELLLG-QPLFPGENSVDQLVEI 283
Cdd:cd13989 157 QGSLCTSFVGTLQYLAPEL-FESKKYTCTVDYWSFGTLAFECITGyRPFLPNWQPVQWHGKV 217
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
74-283 4.70e-23

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: 98.56  E-value: 4.70e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFFSttsrdELFLNLVME 146
Cdd:cd06634  21 REIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSNekwqdiiKEVKFLQKLRHPNTIEYRGCYLR-----EHTAWLVME 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRMPIFYVklyTYQIFRGLAYIHTvPGVCHRDVKPQN-LLVDPltHQVKLCDFGSAKVLvkgE 225
Cdd:cd06634  96 YCLGSASDLLEVHKKPLQEVEIAAI---THGALQGLAYLHS-HNMIHRDVKAGNiLLTEP--GLVKLGDFGSASIM---A 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIFGATE--YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEI 283
Cdd:cd06634 167 PANSFVGTPYWMAPEVILAMDEgqYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHI 226
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
74-357 5.00e-23

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: 97.86  E-value: 5.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKNR------ELQLMRPMDHPNVISLkHCFFSTTSrdelFLNLVME 146
Cdd:cd05609   6 KLISNGAYGAVYLVRHRETRQRFAMKKInKQNLILRNQiqqvfvERDILTFAENPFVVSM-YCSFETKR----HLCMVME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP----ETLyrvLRHYTSsnqrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV-L 221
Cdd:cd05609  81 YVEggdcATL---LKNIGP----LPVDMARMYFAETVLALEYLHSY-GIVHRDLKPDNLLITSMGH-IKLTDFGLSKIgL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNI--------------SYIC-SRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKv 286
Cdd:cd05609 152 MSLTTNLyeghiekdtrefldKQVCgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVIS- 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 287 lgtptrEEIrcMNPNYTDFrfpqikahpwhkvfhkrMPPEAIDLASRLLQYSPSLR---CTALEACAHPFFNEL 357
Cdd:cd05609 230 ------DEI--EWPEGDDA-----------------LPDDAQDLITRLLQQNPLERlgtGGAEEVKQHPFFQDL 278
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
74-362 5.02e-23

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: 98.46  E-value: 5.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQ-DRRYKNR------ELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd05599   7 KVIGRGAFGEVRLVRKKDTGHVYAMKKLRKsEMLEKEQvahvraERDILAEADNPWVVKLYYSF-----QDEENLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP----ETLyrVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLV 222
Cdd:cd05599  82 FLPggdmMTL--LMKKDTLTEEE-----TRFYIAETVLAIESIHKL-GYIHRDIKPDNLLLDARGH-IKLSDFGLCTGLK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIikvlgtptreeircMNPNY 302
Cdd:cd05599 153 KSHLAYSTVGTPDYIAPE-VFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKI--------------MNWRE 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 303 TdFRFPQikahpwhkvfHKRMPPEAIDLASRLLQySPSLRCTAL---EACAHPFFN-----ELREPNA 362
Cdd:cd05599 218 T-LVFPP----------EVPISPEAKDLIERLLC-DAEHRLGANgveEIKSHPFFKgvdwdHIRERPA 273
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
74-354 5.97e-23

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: 98.23  E-value: 5.97e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKK-----VLQD-----RRYKNRELQLmrPMDHPNVISLkHCFFSTTSrdELFLnl 143
Cdd:cd05592   1 KVLGKGSFGKVMLAELKGTNQYFAIKAlkkdvVLEDddvecTMIERRVLAL--ASQHPFLTHL-FCTFQTES--HLFF-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK 223
Cdd:cd05592  74 VMEYLNGG---DLMFHIQQSGRFDEDRARFYGAEIICGLQFLHS-RGIIYRDLKLDNVLLDREGH-IKIADFGMCKENIY 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYIC-SRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIkvlgtptreeircMNPNy 302
Cdd:cd05592 149 GENKASTFCgTPDYIAPEILKG-QKYNQSVDWWSFGVLLYEMLIGQSPFHGEDE-DELFWSI-------------CNDT- 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 303 tdfrfpqikahPWhkvFHKRMPPEAIDLASRLLQYSPSLR-----CTALEACAHPFF 354
Cdd:cd05592 213 -----------PH---YPRWLTKEAASCLSLLLERNPEKRlgvpeCPAGDIRDHPFF 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
70-353 6.66e-23

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: 96.94  E-value: 6.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRE------LQLMRPMDHPNVISLkHCFFSTtsrdELFLNL 143
Cdd:cd14185   2 YEIGRTIGDGNFAVVKECRHWNENQEYAMK-IIDKSKLKGKEdmieseILIIKSLSHPNIVKL-FEVYET----EKEIYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV---DPLTHQVKLCDFGSAK 219
Cdd:cd14185  76 ILEYVRGgDLFDAI----IESVKFTEHDAALMIIDLCEALVYIHS-KHIVHRDLKPENLLVqhnPDKSTTLKLADFGLAK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKgePNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPG-ENSVDQLVEIIKVlgtptreeircm 298
Cdd:cd14185 151 YVTG--PIFTVCGTPTYVAPE-ILSEKGYGLEVDMWAAGVILYILLCGFPPFRSpERDQEELFQIIQL------------ 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 299 npNYTDFRFPQikahpWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14185 216 --GHYEFLPPY-----WDNI-----SEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
74-273 8.36e-23

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 96.84  E-value: 8.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKC---LETGESVAIKKVLQDRRYKNR-----ELQLMRPMDHPNVISLKHCffsTTSRDELFlnLVM 145
Cdd:cd00192   1 KKLGEGAFGEVYKGKLkggDGKTVDVAVKTLKEDASESERkdflkEARVMKKLGHPNVVRLLGV---CTEEEPLY--LVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE----TLYRVLRHYTSSNQRMPIFYVKL--YTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAK 219
Cdd:cd00192  76 EYMEGgdllDFLRKSRPVFPSPEPSTLSLKDLlsFAIQIAKGMEYLASKKFV-HRDLAARNCLVGE-DLVVKISDFGLSR 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 220 VLVKGEpnisyicsrYYR------------APELIFGATeYTASIDIWSAGCVLAELL-LGQPLFPG 273
Cdd:cd00192 154 DIYDDD---------YYRkktggklpirwmAPESLKDGI-FTSKSDVWSFGVLLWEIFtLGATPYPG 210
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
76-354 9.45e-23

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: 97.12  E-value: 9.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISlkhcFFSTtsrdelFLN------LV 144
Cdd:cd06620  13 LGAGNGGSVSKVLHIPTGTIMAKKVIHIDakssvRKQILRELQILHECHSPYIVS----FYGA------FLNennniiIC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP-ETLYRVLRHYTSsnqrMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK 223
Cdd:cd06620  83 MEYMDcGSLDKILKKKGP----FPEEVLGKIAVAVLEGLTYLYNVHRIIHRDIKPSNILVNS-KGQIKLCDFGVSGELIN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNiSYICSRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVE----IIKVLGTPTREEircmN 299
Cdd:cd06620 158 SIAD-TFVGTSTYMSPERIQGG-KYSVKSDVWSLGLSIIELALGEFPFAGSNDDDDGYNgpmgILDLLQRIVNEP----P 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 300 PnytdfRFPQikahpwhkvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06620 232 P-----RLPK----------DRIFPKDLRDFVDRCLLKDPRERPSPQLLLDHDPF 271
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
70-353 1.07e-22

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: 96.55  E-value: 1.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV-----LQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLV 144
Cdd:cd06609   3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIdleeaEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGSK-----LWII 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLRHYtssnqRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGsakvlVK 223
Cdd:cd06609  78 MEYCGGgSVLDLLKPG-----PLDETYIAFILREVLLGLEYLHS-EGKIHRDIKAANILLSE-EGDVKLADFG-----VS 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNiSYICSR-------YYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeir 296
Cdd:cd06609 146 GQLT-STMSKRntfvgtpFWMAPEVIKQ-SGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPK----------- 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 cMNPnytdfrfPQIKAHPWHKVFHkrmppeaiDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06609 213 -NNP-------PSLEGNKFSKPFK--------DFVELCLNKDPKERPSAKELLKHKF 253
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
64-285 1.26e-22

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: 96.68  E-value: 1.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMaeRVVGTGSFGIVFQAkCLE-----TGESVAIKK-----VLQDRRYKNRELQLMRPMDHPNVISLKHCffsT 133
Cdd:cd05038   2 EERHLKFI--KQLGEGHFGSVELC-RYDplgdnTGEQVAVKSlqpsgEEQHMSDFKREIEILRTLDHEYIVKYKGV---C 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 134 TSRDELFLNLVMEYVPetlYRVLRHYTSSNQ-RMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKL 212
Cdd:cd05038  76 ESPGRRSLRLIMEYLP---SGSLRDYLQRHRdQIDLKRLLLFASQICKGMEYLGSQ-RYIHRDLAARNILVES-EDLVKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 213 CDFGSAKVLVKG-------EPNISYIcsRYYrAPELIFGATEYTASiDIWSAGCVLAELL---------LGQPL-----F 271
Cdd:cd05038 151 SDFGLAKVLPEDkeyyyvkEPGESPI--FWY-APECLRESRFSSAS-DVWSFGVTLYELFtygdpsqspPALFLrmigiA 226
                       250
                ....*....|....
gi 42571361 272 PGENSVDQLVEIIK 285
Cdd:cd05038 227 QGQMIVTRLLELLK 240
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
70-315 1.36e-22

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


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 96.25  E-value: 1.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVfqAKCLE--TGESVAIK-----KVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTsrdELFLn 142
Cdd:cd14184   3 YKIGKVIGDGNFAVV--KECVErsTGKEFALKiidkaKCCGKEHLIENEVSILRRVKHPNIIMLIEEMDTPA---ELYL- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 lVMEYVPE-TLYRVLRHYTSSNQRMPIFYVklytYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPL---THQVKLCDFGSA 218
Cdd:cd14184  77 -VMELVKGgDLFDAITSSTKYTERDASAMV----YNLASALKYLHGL-CIVHRDIKPENLLVCEYpdgTKSLKLGDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVlVKGePNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSV-----DQLveIIKVLGTPT-- 291
Cdd:cd14184 151 TV-VEG-PLYTVCGTPTYVAPEII-AETGYGLKVDIWAAGVITYILLCGFPPFRSENNLqedlfDQI--LLGKLEFPSpy 225
                       250       260       270
                ....*....|....*....|....*....|....
gi 42571361 292 --------REEIRCMNPNYTDFRFP--QIKAHPW 315
Cdd:cd14184 226 wdnitdsaKELISHMLQVNVEARYTaeQILSHPW 259
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
69-275 3.17e-22

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: 94.80  E-value: 3.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLN 142
Cdd:cd08220   1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqmtKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKA-----LM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVLRHYTS---SNQRMPIFYVklytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVKLCDFGSA 218
Cdd:cd08220  76 IVMEYAPGgTLFEYIQQRKGsllSEEEILHFFV-----QILLALHHVHS-KQILHRDLKTQNILLNKKRTVVKIGDFGIS 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 219 KVLVKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd08220 150 KILSSKSKAYTVVGTPCYISPELCEGKP-YNQKSDIWALGCVLYELASLKRAFEAAN 205
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
74-354 3.51e-22

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: 96.27  E-value: 3.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAI----KKVLQDRR------YKNRELQLMRpmdHPNVISLKHCfFSTTSRdelfLNL 143
Cdd:cd05571   1 KVLGKGTFGKVILCREKATGELYAIkilkKEVIIAKDevahtlTENRVLQNTR---HPFLTSLKYS-FQTNDR----LCF 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGsakvL 221
Cdd:cd05571  73 VMEYVNggELFFHLSRERVFSEDR-----TRFYGAEIVLALGYLHSQ-GIVYRDLKLENLLLDKDGH-IKITDFG----L 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEpnISY------IC-SRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKVlgtptrEE 294
Cdd:cd05571 142 CKEE--ISYgattktFCgTPEYLAPEVLED-NDYGRAVDWWGLGVVMYEMMCGRLPFYNRDH-EVLFELILM------EE 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 295 IrcmnpnytdfRFPqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRC-----TALEACAHPFF 354
Cdd:cd05571 212 V----------RFP------------STLSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPFF 254
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
74-275 5.17e-22

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: 95.19  E-value: 5.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV-------LQDRRYKNRELQLMRPMDHPNVISLKhcffsTTSRDELFLNLVME 146
Cdd:cd05612   7 KTIGTGTFGRVHLVRDRISEHYYALKVMaipevirLKQEQHVHNEKRVLKEVSHPFIIRLF-----WTEHDQRFLYMLME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE-TLYRVLRHYTSSNQRMPIFYvklyTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK-- 223
Cdd:cd05612  82 YVPGgELFSYLRNSGRFSNSTGLFY----ASEIVCALEYLHSK-EIVYRDLKPENILLDKEGH-IKLTDFGFAKKLRDrt 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 224 ----GEPNisyicsryYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd05612 156 wtlcGTPE--------YLAPEVI-QSKGHNKAVDWWALGILIYEMLVGYPPFFDDN 202
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
76-354 5.48e-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: 94.30  E-value: 5.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIV--FQAKCLETGESVAIKKV------LQDRRYKNR---ELQLMRPMDHPNVI---------SLKHCFfstts 135
Cdd:cd13994   1 IGKGATSVVriVTKKNPRSGVLYAVKEYrrrddeSKRKDYVKRltsEYIISSKLHHPNIVkvldlcqdlHGKWCL----- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 136 rdelflnlVMEYVPE-TLYRVLRHYTSsnqrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLtHQVKLCD 214
Cdd:cd13994  76 --------VMEYCPGgDLFTLIEKADS----LSLEEKDCFFKQILRGVAYLHSH-GIAHRDLKPENILLDED-GVLKLTD 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 215 FGSAKVL-VKGEPNISYIC----SRYYRAPElIFGATEYTA-SIDIWSAGCVLAELLLGQPLFPGENSVDQlveiikvlg 288
Cdd:cd13994 142 FGTAEVFgMPAEKESPMSAglcgSEPYMAPE-VFTSGSYDGrAVDVWSCGIVLFALFTGRFPWRSAKKSDS--------- 211
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 289 tptREEIRCMNPNYTDFRFPQIKAHpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd13994 212 ---AYKAYEKSGDFTNGPYEPIENL---------LPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
76-383 6.16e-22

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: 94.80  E-value: 6.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQ-------LMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYV 148
Cdd:cd14086   9 LGKGAFSVVRRCVQKSTGQEFAAK-IINTKKLSARDHQklerearICRLLKHPNIVRLHDSI-----SEEGFHYLVFDLV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PE-TLYR--VLR-HYTSSNQRMPIfyvklytYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTH--QVKLCDFGSAkVLV 222
Cdd:cd14086  83 TGgELFEdiVAReFYSEADASHCI-------QQILESVNHCHQ-NGIVHRDLKPENLLLASKSKgaAVKLADFGLA-IEV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISY--ICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKvlgtptreeircmNP 300
Cdd:cd14086 154 QGDQQAWFgfAGTPGYLSPEVL-RKDPYGKPVDIWACGVILYILLVGYPPFWDEDQ-HRLYAQIK-------------AG 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 301 NYtDFRFPQikahpWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLPNGRPLPPL--FNFKQ 378
Cdd:cd14086 219 AY-DYPSPE-----WDTV-----TPEAKDLINQMLTVNPAKRITAAEALKHPWICQRDRVASMVHRQETVDCLkkFNARR 287

                ....*
gi 42571361 379 ELGGA 383
Cdd:cd14086 288 KLKGA 292
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
70-353 7.68e-22

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: 93.94  E-value: 7.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK----KVLQDRRYK-NRELQLMRPMDHPNVISLKHCFfstTSRDELFLnlV 144
Cdd:cd14167   5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKciakKALEGKETSiENEIAVLHKIKHPNIVALDDIY---ESGGHLYL--I 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVLRH--YTSSNQRMPIFyvklytyQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKL--CDFGSA 218
Cdd:cd14167  80 MQLVSggELFDRIVEKgfYTERDASKLIF-------QILDAVKYLHDM-GIVHRDLKPENLLYYSLDEDSKImiSDFGLS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreEIRCM 298
Cdd:cd14167 152 KIEGSGSVMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKA-------EYEFD 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 299 NPNYTDfrfpqikahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14167 224 SPYWDD------------------ISDSAKDFIQHLMEKDPEKRFTCEQALQHPW 260
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
69-354 7.85e-22

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


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 93.65  E-value: 7.85e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdeLFLN 142
Cdd:cd08221   1 HYIPVRVLGRGAFGEAVLYRKTEDNSLVVWKEVnlsrlsEKERRDALNEIDILSLLNHDNIITYYNHFLDGES---LFIE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 lvMEYVPE-TLYRVLRHytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd08221  78 --MEYCNGgNLHDKIAQ--QKNQLFPEEVVLWYLYQIVSAVSHIHKA-GILHRDIKTLNIFLTK-ADLVKLGDFGISKVL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 -VKGEPNISYICSRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtPTREEIrcmNP 300
Cdd:cd08221 152 dSESSMAESIVGTPYYMSPELVQGV-KYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQ----GEYEDI---DE 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 301 NYTDfrfpqikahpwhkvfhkrmppEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd08221 224 QYSE---------------------EIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
69-373 8.07e-22

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: 95.38  E-value: 8.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ--------LMRPMDHPnviSLKHCFFSTTSRDELF 140
Cdd:cd05619   6 DFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVEctmvekrvLSLAWEHP---FLTHLFCTFQTKENLF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LnlVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV 220
Cdd:cd05619  83 F--VMEYLNGG---DLMFHIQSCHKFDLPRATFYAAEIICGLQFLHS-KGIVYRDLKLDNILLDKDGH-IKIADFGMCKE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYIC-SRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLveiikvlgtptrEEIRCMN 299
Cdd:cd05619 156 NMLGDAKTSTFCgTPDYIAPEILLG-QKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELF------------QSIRMDN 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 300 PNYTDFrfpqikahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTAL-EACAHPFFNELREpnARLPNGRPLPPL 373
Cdd:cd05619 223 PFYPRW-----------------LEKEAKDILVKLFVREPERRLGVRgDIRQHPFFREINW--EALEEREIEPPF 278
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
74-281 9.14e-22

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 93.87  E-value: 9.14e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLkhcFFSTTSRDELFLnlVMEY 147
Cdd:cd08225   6 KKIGEGSFGKIYLAKAKSDSEHCVIKEIdltkmpVKEKEASKKEVILLAKMKHPNIVTF---FASFQENGRLFI--VMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VP--ETLYRVLRHYT---SSNQRMPIFYvklytyQIFRGLAYIHTVPgVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLv 222
Cdd:cd08225  81 CDggDLMKRINRQRGvlfSEDQILSWFV------QISLGLKHIHDRK-ILHRDIKSQNIFLSKNGMVAKLGDFGIARQL- 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 223 KGEPNISYIC--SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGeNSVDQLV 281
Cdd:cd08225 153 NDSMELAYTCvgTPYYLSPE-ICQNRPYNNKTDIWSLGCVLYELCTLKHPFEG-NNLHQLV 211
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
74-273 1.17e-21

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: 93.33  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    74 RVVGTGSFGIVFQAKCLETGES----VAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFfstTSRDELFlnLV 144
Cdd:pfam07714   5 EKLGEGAFGEVYKGTLKGEGENtkikVAVKTLKEGADEEEredflEEASIMKKLDHPNIVKLLGVC---TQGEPLY--IV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   145 MEYVPE-TLYRVLRhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDpLTHQVKLCDFGSAKVLvk 223
Cdd:pfam07714  80 TEYMPGgDLLDFLR---KHKRKLTLKDLLSMALQIAKGMEYLESKNFV-HRDLAARNCLVS-ENLVVKISDFGLSRDI-- 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361   224 gEPNISYICS-------RYYrAPELIFGATEYTASiDIWSAGCVLAELL-LGQPLFPG 273
Cdd:pfam07714 153 -YDDDYYRKRgggklpiKWM-APESLKDGKFTSKS-DVWSFGVLLWEIFtLGEQPYPG 207
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
74-295 1.74e-21

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: 93.18  E-value: 1.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR---------ELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLV 144
Cdd:cd06652   8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETskevnalecEIQLLKNLLHERIVQYYGCLRDPQERT---LSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLRHYTSSNQrmpiFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL-- 221
Cdd:cd06652  85 MEYMPGgSIKDQLKSYGALTE----NVTRKYTRQILEGVHYLHS-NMIVHRDIKGANILRDS-VGNVKLGDFGASKRLqt 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 222 --VKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPgenSVDQLVEIIKVLGTPTREEI 295
Cdd:cd06652 159 icLSGTGMKSVTGTPYWMSPEVISGEG-YGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKIATQPTNPQL 230
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
75-277 2.25e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   75 VVGTGSFGIVFQAKCLETGESVAIKkVLQD---------RRYKnRELQLMRPMDHPNVISLkhcfFSTTSRDELFLnLVM 145
Cdd:NF033483  14 RIGRGGMAEVYLAKDTRLDRDVAVK-VLRPdlardpefvARFR-REAQSAASLSHPNIVSV----YDVGEDGGIPY-IVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  146 EYVP-ETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkG 224
Cdd:NF033483  87 EYVDgRTLKDYIR----EHGPLSPEEAVEIMIQILSALEHAHRN-GIVHRDIKPQNILITK-DGRVKVTDFGIARAL--S 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361  225 EPNISY----ICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSV 277
Cdd:NF033483 159 STTMTQtnsvLGTVHYLSPEQARGGT-VDARSDIYSLGIVLYEMLTGRPPFDGDSPV 214
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
75-357 2.47e-21

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: 93.79  E-value: 2.47e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ-------LMRPMDHPNVISLKhcfFSTTSRDELFLNLVMEY 147
Cdd:cd05585   1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVThtlaertVLAQVDCPFIVPLK---FSFQSPEKLYLVLAFIN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPEtlyrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEPN 227
Cdd:cd05585  78 GGE-----LFHHLQREGRFDLSRARFYTAELLCALECLHKF-NVIYRDLKPENILLDYTGH-IALCDFGLCKLNMKDDDK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYIC-SRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEiiKVLGTPTReeircmnpnytdfr 306
Cdd:cd05585 151 TNTFCgTPEYLAPELLLGHG-YTKAVDWWTLGVLLYEMLTGLPPFYDEN-TNEMYR--KILQEPLR-------------- 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 307 fpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRC---TALEACAHPFFNEL 357
Cdd:cd05585 213 ------------FPDGFDRDAKDLLIGLLNRDPTKRLgynGAQEIKNHPFFDQI 254
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
75-354 2.56e-21

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: 93.65  E-value: 2.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVP 149
Cdd:cd06615   8 ELGAGNGGVVTKVLHRPSGLIMARKLIHLEikpaiRNQIIRELKVLHECNSPYIVGFYGAFYSDGE-----ISICMEHMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNi 228
Cdd:cd06615  83 GgSLDQVLK----KAGRIPENILGKISIAVLRGLTYLREKHKIMHRDVKPSNILVNS-RGEIKLCDFGVSGQLIDSMAN- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGENSvdqlVEIIKVLGTP-----TREEIRCMNPNYT 303
Cdd:cd06615 157 SFVGTRSYMSPERLQG-THYTVQSDIWSLGLSLVEMAIGRYPIPPPDA----KELEAMFGRPvsegeAKESHRPVSGHPP 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 304 DFRFPQ--------IKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd06615 232 DSPRPMaifelldyIVNEPPPKLPSGAFSDEFQDFVDKCLKKNPKERADLKELTKHPFI 290
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
76-268 2.67e-21

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: 91.79  E-value: 2.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCleTGESVAIKKVlqdRRYKNRELQLMRPMDHPNVISLKH------CFFsttsrdelflnLVMEYVP 149
Cdd:cd14059   1 LGSGAQGAVFLGKF--RGEEVAVKKV---RDEKETDIKHLRKLNHPNIIKFKGvctqapCYC-----------ILMEYCP 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRhytSSNQRMPIFYVKlYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLVKGEPNI 228
Cdd:cd14059  65 YgQLYEVLR---AGREITPSLLVD-WSKQIASGMNYLHLHK-IIHRDLKSPNVLVT-YNDVLKISDFGTSKELSEKSTKM 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQ 268
Cdd:cd14059 139 SFAGTVAWMAPEVIRNEP-CSEKVDIWSFGVVLWELLTGE 177
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
62-365 2.95e-21

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: 93.13  E-value: 2.95e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  62 GEPKQTI-SYMAervVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQ-----LMRPMDHPNVISLkhcFFSTTS 135
Cdd:cd06659  17 GDPRQLLeNYVK---IGEGSTGVVCIAREKHSGRQVAVK-MMDLRKQQRRELLfnevvIMRDYQHPNVVEM---YKSYLV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 136 RDELFLnlVMEYVPE-TLYRVLrhytsSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCD 214
Cdd:cd06659  90 GEELWV--LMEYLQGgALTDIV-----SQTRLNEEQIATVCEAVLQALAYLHS-QGVIHRDIKSDSILLT-LDGRVKLSD 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 215 FGSAKVLVKGEPN-ISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIikvlgtptRE 293
Cdd:cd06659 161 FGFCAQISKDVPKrKSLVGTPYWMAPEVI-SRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRL--------RD 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 294 EircmnpnytdfrfPQIKAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLP 365
Cdd:cd06659 232 S-------------PPPKLKNSHKA-----SPVLRDFLERMLVRDPQERATAQELLDHPFLLQTGLPECLVP 285
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
76-373 3.10e-21

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: 92.59  E-value: 3.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNR--------ELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEY 147
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYACKK-LDKKRIKKKkgetmalnEKIILEKVSSPFIVSLAYAFETKDK-----LCLVLTL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETLYrvlrHYTSSNQRMPIF---YVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKG 224
Cdd:cd05577  75 MNGGDL----KYHIYNVGTRGFseaRAIFYAAEIICGLEHLHNR-FIVYRDLKPENILLDDHGH-VRISDLGLAVEFKGG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFpgensvDQLVEIIKvlgtptREEIRCMnpnytd 304
Cdd:cd05577 149 KKIKGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPF------RQRKEKVD------KEELKRR------ 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 305 frfpqIKAHPwhKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACA-----HPFFNELREPnaRLPNGRPLPPL 373
Cdd:cd05577 211 -----TLEMA--VEYPDSFSPEARSLCEGLLQKDPERRLGCRGGSAdevkeHPFFRSLNWQ--RLEAGMLEPPF 275
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
65-355 3.15e-21

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: 92.75  E-value: 3.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  65 KQTISYMaeRVVGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYKN--RELQLMRPMDHPNVISLKHCFFSTTSrdelf 140
Cdd:cd14166   2 RETFIFM--EVLGSGAFSEVYLVKQRSTGKLYALKciKKSPLSRDSSleNEIAVLKRIKHENIVTLEDIYESTTH----- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVP--ETLYRVLRH--YTSSNQRMPIfyvklytYQIFRGLAYIHTvPGVCHRDVKPQNLL-VDPLTH-QVKLCD 214
Cdd:cd14166  75 YYLVMQLVSggELFDRILERgvYTEKDASRVI-------NQVLSAVKYLHE-NGIVHRDLKPENLLyLTPDENsKIMITD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 215 FGSAKVLVKGEpnISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKvlgtptre 293
Cdd:cd14166 147 FGLSKMEQNGI--MSTACgTPGYVAPE-VLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETE-SRLFEKIK-------- 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 294 eircmnPNYTDFRFPqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:cd14166 215 ------EGYYEFESP----------FWDDISESAKDFIRHLLEKNPSKRYTCEKALSHPWII 260
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
70-354 3.99e-21

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: 92.03  E-value: 3.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAE-RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN--RELQ-----LMRPMDHPNVISLkHCFFSTTSRdelfL 141
Cdd:cd14106   9 YTVEsTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDcrNEILheiavLELCKDCPRVVNL-HEVYETRSE----L 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVP--EtlyrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLvdpLTHQ-----VKLCD 214
Cdd:cd14106  84 ILILELAAggE-----LQTLLDEEECLTEADVRRLMRQILEGVQYLHER-NIVHLDLKPQNIL---LTSEfplgdIKLCD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 215 FGSAKVLVKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptree 294
Cdd:cd14106 155 FGISRVIGEGEEIREILGTPDYVAPE-ILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQ--------- 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 295 ircMNPNYTDFRFPQIKahpwhkvfhkrmpPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14106 225 ---CNLDFPEELFKDVS-------------PLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
76-265 4.30e-21

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: 92.39  E-value: 4.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVfqAKCL------ETGESVAIKKVLQDR----RYKNRELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLVM 145
Cdd:cd14205  12 LGKGNFGSV--EMCRydplqdNTGEVVAVKKLQHSTeehlRDFEREIEILKSLQHDNIVKYKGVCYSAGRRN---LRLIM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPetlYRVLRHYTSSN-QRMPIFYVKLYTYQIFRGLAYIhTVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKG 224
Cdd:cd14205  87 EYLP---YGSLRDYLQKHkERIDHIKLLQYTSQICKGMEYL-GTKRYIHRDLATRNILVEN-ENRVKIGDFGLTKVLPQD 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 225 -------EPNISYIcsrYYRAPELIfGATEYTASIDIWSAGCVLAELL 265
Cdd:cd14205 162 keyykvkEPGESPI---FWYAPESL-TESKFSVASDVWSFGVVLYELF 205
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
74-375 5.89e-21

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: 92.77  E-value: 5.89e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQ---------LMRPMDHPNVISLKhcfFSTTSRDELFLnlV 144
Cdd:cd05575   1 KVIGKGSFGKVLLARHKAEGKLYAVK-VLQKKAILKRNEVkhimaernvLLKNVKHPFLVGLH---YSFQTKDKLYF--V 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLV 222
Cdd:cd05575  75 LDYVNggELFFHLQRERHFPEPR-----ARFYAAEIASALGYLHSL-NIIYRDLKPENILLDSQGH-VVLTDFGLCKEGI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYIC-SRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEiiKVLGTPTReeircMNPN 301
Cdd:cd05575 148 EPSDTTSTFCgTPEYLAPEVLR-KQPYDRTVDWWCLGAVLYEMLYGLPPFYSRD-TAEMYD--NILHKPLR-----LRTN 218
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 302 YTdfrfpqikahpwhkvfhkrmpPEAIDLASRLLQYSPSLRCTA----LEACAHPFFNELrepNARLPNGRPLPPLFN 375
Cdd:cd05575 219 VS---------------------PSARDLLEGLLQKDRTKRLGSgndfLEIKNHSFFRPI---NWDDLEAKKIPPPFN 272
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
76-272 6.46e-21

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: 91.95  E-value: 6.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR-----ELQLMRPMDHPNVISLKHC--FFSTTSRDELFLnLVMEYV 148
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRerwclEIQIMKRLNHPNVVAARDVpeGLQKLAPNDLPL-LAMEYC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETlyrVLRHYTSSNQR---MPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDP----LTHqvKLCDFGSAKVL 221
Cdd:cd14038  81 QGG---DLRKYLNQFENccgLREGAILTLLSDISSALRYLHENR-IIHRDLKPENIVLQQgeqrLIH--KIIDLGYAKEL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 222 VKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLG-QPLFP 272
Cdd:cd14038 155 DQGSLCTSFVGTLQYLAPELL-EQQKYTVTVDYWSFGTLAFECITGfRPFLP 205
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
74-275 6.67e-21

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: 91.04  E-value: 6.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVlqDRRYKN--------RELQLMRPMDHPNVISLkhcfFSTTSRDELfLNLVM 145
Cdd:cd14072   6 KTIGKGNFAKVKLARHVLTGREVAIKII--DKTQLNpsslqklfREVRIMKILNHPNIVKL----FEVIETEKT-LYLVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVP--ETLyrvlrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK 223
Cdd:cd14072  79 EYASggEVF-----DYLVAHGRMKEKEARAKFRQIVSAVQYCHQ-KRIVHRDLKAENLLLDADMN-IKIADFGFSNEFTP 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 224 GEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd14072 152 GNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQN 203
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
62-305 6.79e-21

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: 91.53  E-value: 6.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  62 GEPKQtiSYMAERVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKN---RELQLMRPMDHPNVISLKHCFFSTtsrD 137
Cdd:cd06647   3 GDPKK--KYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMnLQQQPKKEliiNEILVMRENKNPNIVNYLDSYLVG---D 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 138 ELFLnlVMEYVPE-TLYRVLrhytsSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFG 216
Cdd:cd06647  78 ELWV--VMEYLAGgSLTDVV-----TETCMDEGQIAAVCRECLQALEFLHS-NQVIHRDIKSDNILLG-MDGSVKLTDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 -SAKVLVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVeIIKVLGTPTREEI 295
Cdd:cd06647 149 fCAQITPEQSKRSTMVGTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQNP 226
                       250
                ....*....|
gi 42571361 296 RCMNPNYTDF 305
Cdd:cd06647 227 EKLSAIFRDF 236
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
76-265 6.92e-21

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: 90.96  E-value: 6.92e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCleTGESVAIKKV--LQDRRYKNRELQLMRPMDHPNVISLkHCFFSTTSRDelflNLVMEYVPE-TL 152
Cdd:cd14058   1 VGRGSFGVVCKARW--RNQIVAVKIIesESEKKAFEVEVRQLSRVDHPNIIKL-YGACSNQKPV----CLVMEYAEGgSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 153 YRVLR------HYTSSNqrmpifyVKLYTYQIFRGLAYIHTVP--GVCHRDVKPQNLLvdpLTHQ---VKLCDFGSA--- 218
Cdd:cd14058  74 YNVLHgkepkpIYTAAH-------AMSWALQCAKGVAYLHSMKpkALIHRDLKPPNLL---LTNGgtvLKICDFGTAcdi 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 ---KVLVKGepnisyicSRYYRAPElIFGATEYTASIDIWSAGCVLAELL 265
Cdd:cd14058 144 sthMTNNKG--------SAAWMAPE-VFEGSKYSEKCDVFSWGIILWEVI 184
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
75-271 6.96e-21

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: 91.59  E-value: 6.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYK-NRELQLMRPM-DHPNVISLKHCFF---STTSRDELFlnLVMEY 147
Cdd:cd06608  13 VIGEGTYGKVYKARHKKTGQLAAIKimDIIEDEEEEiKLEINILRKFsNHPNIATFYGAFIkkdPPGGDDQLW--LVMEY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 -----VPETLYRVLRhytsSNQRMP---IFYVklyTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTHQ--VKLCDFG- 216
Cdd:cd06608  91 cgggsVTDLVKGLRK----KGKRLKeewIAYI---LRETLRGLAYLHE-NKVIHRDIKGQNIL---LTEEaeVKLVDFGv 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 217 SAKVLVKGEPNISYICSRYYRAPELIfgATE------YTASIDIWSAGCVLAELLLGQPLF 271
Cdd:cd06608 160 SAQLDSTLGRRNTFIGTPYWMAPEVI--ACDqqpdasYDARCDVWSLGITAIELADGKPPL 218
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
74-353 7.67e-21

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: 91.17  E-value: 7.67e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYK-------NRELQLMRPMDHPNVISLkHCFFSTTSRdelfLNLVME 146
Cdd:cd14116  11 RPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKagvehqlRREVEIQSHLRHPNILRL-YGYFHDATR----VYLILE 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE-TLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAkvLVKGE 225
Cdd:cd14116  86 YAPLgTVYRELQKLSKFDEQRTATYIT----ELANALSYCHS-KRVIHRDIKPENLLLGS-AGELKIADFGWS--VHAPS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRY-YRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeircmnpnytD 304
Cdd:cd14116 158 SRRTTLCGTLdYLPPEMIEGRM-HDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRV-----------------E 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 305 FRFPQIkahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14116 220 FTFPDF------------VTEGARDLISRLLKHNPSQRPMLREVLEHPW 256
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
74-357 8.53e-21

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: 92.29  E-value: 8.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVF--------------QAKCLETGESVAIKKVLQDRRYKNRELQLMRpmDHPNVISLkHCFFSTTSRdel 139
Cdd:cd05614   6 KVLGTGAYGKVFlvrkvsghdanklyAMKVLRKAALVQKAKTVEHTRTERNVLEHVR--QSPFLVTL-HYAFQTDAK--- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 fLNLVMEYVP-----ETLYRvlRHYTSSNQrmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVkLCD 214
Cdd:cd05614  80 -LHLILDYVSggelfTHLYQ--RDHFSEDE------VRFYSGEIILALEHLHKL-GIVYRDIKLENILLDSEGHVV-LTD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 215 FGSAKVLV--KGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIikvlgtpTR 292
Cdd:cd05614 149 FGLSKEFLteEKERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSEV-------SR 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 293 EEIRCMNPnytdfrFPQikahpwhkvfhkRMPPEAIDLASRLLQYSPSLRC-----TALEACAHPFFNEL 357
Cdd:cd05614 222 RILKCDPP------FPS------------FIGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKGL 273
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
63-351 1.02e-20

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: 91.09  E-value: 1.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  63 EPKQtisymaerVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRElQLMRP------MDHPNVISLKHCFFST--- 133
Cdd:cd14048   9 EPIQ--------CLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELARE-KVLREvralakLDHPGIVRYFNAWLERppe 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 134 ---TSRDELFLNLVMEYV-PETLYRVLRHYTSSNQRmPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQ 209
Cdd:cd14048  80 gwqEKMDEVYLYIQMQLCrKENLKDWMNRRCTMESR-ELFVCLNIFKQIASAVEYLHS-KGLIHRDLKPSNVFFS-LDDV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 VKLCDFGSAKVLVKGEPNISY-------------ICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGqplfpgens 276
Cdd:cd14048 157 VKVGDFGLVTAMDQGEPEQTVltpmpayakhtgqVGTRLYMSPEQIHGNQ-YSEKVDIFALGLILFELIYS--------- 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 277 vdqlveiikvLGTPTrEEIRcmnpNYTDFR---FPQIkahpwhkvFHKRMPPEAiDLASRLLQYSPSLRCTALEACAH 351
Cdd:cd14048 227 ----------FSTQM-ERIR----TLTDVRklkFPAL--------FTNKYPEER-DMVQQMLSPSPSERPEAHEVIEH 280
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
69-274 1.25e-20

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: 90.86  E-value: 1.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV----LQDRRYKN---RELQLMRPMDHPNVISLKHCFFSTTSrdelfL 141
Cdd:cd08228   3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVqifeMMDAKARQdcvKEIDLLKQLNHPNVIKYLDSFIEDNE-----L 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd08228  78 NIVLELADAgDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHS-RRVMHRDIKPANVFITA-TGVVKLGDLGLGRF 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 221 L-VKGEPNISYICSRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGE 274
Cdd:cd08228 156 FsSKTTAAHSLVGTPYYMSPERIH-ENGYNFKSDIWSLGCLLYEMAALQSPFYGD 209
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
73-354 1.35e-20

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: 90.36  E-value: 1.35e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVA-----IKKVL-QDRRYKNRELQLMRPMDHPNVISLKHCFFSTtSRDELflNLVME 146
Cdd:cd13983   6 NEVLGRGSFKTVYRAFDTEEGIEVAwneikLRKLPkAERQRFKQEIEILKSLKHPNIIKFYDSWESK-SKKEV--IFITE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHT-VPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKGE 225
Cdd:cd13983  83 LMTSG---TLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTrDPPIIHRDLKCDNIFINGNTGEVKIGDLGLATLLRQSF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNiSYICSRYYRAPELIFGatEYTASIDIWSAGCVLAELLLGQplfpgensvdqlveiikvlgTPTREeirCMNPNytdf 305
Cdd:cd13983 160 AK-SVIGTPEFMAPEMYEE--HYDEKVDIYAFGMCLLEMATGE--------------------YPYSE---CTNAA---- 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 306 rfpQIkahpWHKVFHKRMP--------PEAIDLASRLLQySPSLRCTALEACAHPFF 354
Cdd:cd13983 210 ---QI----YKKVTSGIKPeslskvkdPELKDFIEKCLK-PPDERPSARELLEHPFF 258
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
70-354 1.42e-20

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: 90.33  E-value: 1.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ---LMRPMDHPNVISLKHcFFSTtsRDELFLNLVME 146
Cdd:cd14107   4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRARAFQerdILARLSHRRLTCLLD-QFET--RKTLILILELC 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQN-LLVDPLTHQVKLCDFGSAKVLVKGE 225
Cdd:cd14107  81 SSEELLDRLFLKGVVTEAE-----VKLYIQQVLEGIGYLHGM-NILHLDIKPDNiLMVSPTREDIKICDFGFAQEITPSE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIkvlgtptREEIRCMNPNYTdf 305
Cdd:cd14107 155 HQFSKYGSPEFVAPEIV-HQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVA-------EGVVSWDTPEIT-- 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 306 rfpqikahpwhkvfhkRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14107 225 ----------------HLSEDAKDFIKRVLQPDPEKRPSASECLSHEWF 257
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
76-352 1.74e-20

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: 90.77  E-value: 1.74e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFqaKCLE--TGESVAIKKVLQDRRYKNRELQ-LMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYVP--E 150
Cdd:cd14091   8 IGKGSYSVCK--RCIHkaTGKEYAVKIIDKSKRDPSEEIEiLLRYGQHPNIITLRDVY-----DDGNSVYLVTELLRggE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRH-YTSSNQRMPIFYVKLYTyqifrgLAYIHTvPGVCHRDVKPQNLLV-----DPLThqVKLCDFGSAKVLvKG 224
Cdd:cd14091  81 LLDRILRQkFFSEREASAVMKTLTKT------VEYLHS-QGVVHRDLKPSNILYadesgDPES--LRICDFGFAKQL-RA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 E------PnisyiCsrY---YRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFP-GENsvDQLVEIIKVLGtptree 294
Cdd:cd14091 151 EngllmtP-----C--YtanFVAPE-VLKKQGYDAACDIWSLGVLLYTMLAGYTPFAsGPN--DTPEVILARIG------ 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 295 ircmnpnytDFRFPQIKAHpWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14091 215 ---------SGKIDLSGGN-WDHV-----SDSAKDLVRKMLHVDPSQRPTAAQVLQHP 257
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
74-325 1.92e-20

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: 91.18  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQ---------LMRPMDHPNVISLkHCFFSTTSRdelfLNLV 144
Cdd:cd05603   1 KVIGKGSFGKVLLAKRKCDGKFYAVK-VLQKKTILKKKEQnhimaernvLLKNLKHPFLVGL-HYSFQTSEK----LYFV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVkLCDFGSAKVLV 222
Cdd:cd05603  75 LDYVNggELFFHLQRERCFLEPR-----ARFYAAEVASAIGYLHSL-NIIYRDLKPENILLDCQGHVV-LTDFGLCKEGM 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEII--KVLGTP--------- 290
Cdd:cd05603 148 EPEETTSTFCgTPEYLAPE-VLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRD-VSQMYDNIlhKPLHLPggktvaacd 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42571361 291 -----TREEIRCMNPNYTDFRfpQIKAH------PWHKVFHKRMPP 325
Cdd:cd05603 226 llqglLHKDQRRRLGAKADFL--EIKNHvffspiNWDDLYHKRITP 269
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
74-374 1.99e-20

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 90.31  E-value: 1.99e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFFsttsrDELFLNLVME 146
Cdd:cd14117  12 RPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEgvehqlrREIEIQSHLRHPNILRLYNYFH-----DRKRIYLILE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE-TLYRVL-RHYTSSNQRMPIFYVKLYTyqifrGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFG---SAKVL 221
Cdd:cd14117  87 YAPRgELYKELqKHGRFDEQRTATFMEELAD-----ALHYCHE-KKVIHRDIKPENLLMG-YKGELKIADFGwsvHAPSL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKgepniSYICSRY-YRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeircmnp 300
Cdd:cd14117 160 RR-----RTMCGTLdYLPPEMIEGRT-HDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKV-------------- 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 301 nytDFRFPqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFnelrEPNARlpngRPLPPLF 374
Cdd:cd14117 220 ---DLKFP------------PFLSDGSRDLISKLLRYHPSERLPLKGVMEHPWV----KANSR----RVLPPVY 270
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
76-354 2.05e-20

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: 91.22  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGES-VAIKKVLQDRRYKNRE------LQLMRPMDHPNVislkhcFFSTTSRDELFLNLVMEYV 148
Cdd:cd14214  21 LGEGTFGKVVECLDHARGKSqVALKIIRNVGKYREAArleinvLKKIKEKDKENK------FLCVLMSDWFNFHGHMCIA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHYTSSN--QRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV-----DPLTHQVKLC-------- 213
Cdd:cd14214  95 FELLGKNTFEFLKENnfQPYPLPHIRHMAYQLCHALKFLHE-NQLTHTDLKPENILFvnsefDTLYNESKSCeeksvknt 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 214 -----DFGSAKVlvKGEPNISYICSRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLG 288
Cdd:cd14214 174 sirvaDFGSATF--DHEHHTTIVATRHYRPPEVIL-ELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLVMMEKILG 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 289 -TPTREEIRCMNPNY------------TDFRFPQIKAHPWHKVFHKRMPPEA--IDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14214 251 pIPSHMIHRTRKQKYfykgslvwdensSDGRYVSENCKPLMSYMLGDSLEHTqlFDLLRRMLEFDPALRITLKEALLHPF 330

                .
gi 42571361 354 F 354
Cdd:cd14214 331 F 331
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
67-353 2.43e-20

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: 90.46  E-value: 2.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  67 TISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ-LMRPMDHPNVISLKHCFfsttsRDELFLNLVM 145
Cdd:cd14178   2 TDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEiLLRYGQHPNIITLKDVY-----DDGKFVYLVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYV--PETLYRVLRH-YTSSNQRMPIFYVklytyqIFRGLAYIHTvPGVCHRDVKPQNLLV-----DPltHQVKLCDFGS 217
Cdd:cd14178  77 ELMrgGELLDRILRQkCFSEREASAVLCT------ITKTVEYLHS-QGVVHRDLKPSNILYmdesgNP--ESIRICDFGF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 218 AKVLVKGEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGqpLFPGENSVDQlveiikvlgtpTREEI- 295
Cdd:cd14178 148 AKQLRAENGLLMTPCyTANFVAPE-VLKRQGYDAACDIWSLGILLYTMLAG--FTPFANGPDD-----------TPEEIl 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 296 -RCMNPNYTdfrfpqIKAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14178 214 aRIGSGKYA------LSGGNWDSI-----SDAAKDIVSKMLHVDPHQRLTAPQVLRHPW 261
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
74-325 2.55e-20

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: 90.79  E-value: 2.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQ---------LMRPMDHPNVISLkHCFFSTTsrDELFLnlV 144
Cdd:cd05604   2 KVIGKGSFGKVLLAKRKRDGKYYAVK-VLQKKVILNRKEQkhimaernvLLKNVKHPFLVGL-HYSFQTT--DKLYF--V 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVkLCDFGSAKVLV 222
Cdd:cd05604  76 LDFVNggELFFHLQRERSFPEPR-----ARFYAAEIASALGYLHSI-NIVYRDLKPENILLDSQGHIV-LTDFGLCKEGI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYIC-SRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEII-KVLGT---------PT 291
Cdd:cd05604 149 SNSDTTTTFCgTPEYLAPEVIR-KQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILhKPLVLrpgisltawSI 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42571361 292 REEIRCMNPN----YTDfRFPQIKAHP------WHKVFHKRMPP 325
Cdd:cd05604 228 LEELLEKDRQlrlgAKE-DFLEIKNHPffesinWTDLVQKKIPP 270
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
69-354 2.80e-20

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: 89.37  E-value: 2.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIK-----KVLQDRRYKNR-------ELQLM---RPMDHPNVISLKHCFfst 133
Cdd:cd14004   1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkeRILVDTWVRDRklgtvplEIHILdtlNKRSHPNIVKLLDFF--- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 134 tsRDELFLNLVMEyvPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLC 213
Cdd:cd14004  78 --EDDEFYYLVME--KHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHD-QGIVHRDIKDENVILDGNGT-IKLI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 214 DFGSAKVLVKGePNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGqplfpgENSVDQLVEIIKvlgtptre 293
Cdd:cd14004 152 DFGSAAYIKSG-PFDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFK------ENPFYNIEEILE-------- 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 294 eircmnpnyTDFRFPqikahpwhKVFHKrmppEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14004 217 ---------ADLRIP--------YAVSE----DLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
70-285 3.32e-20

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: 89.53  E-value: 3.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDR------RYKNRELQLMRPMDHPNVISLKHCfFSTTSRdelfLNL 143
Cdd:cd14097   3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKagssavKLLEREVDILKHVNHAHIIHLEEV-FETPKR----MYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLRH--YTSSNQRMPIFyvklytYQIFRGLAYIHTvPGVCHRDVKPQNLLV-----DP-LTHQVKLCD 214
Cdd:cd14097  78 VMELCEDgELKELLLRkgFFSENETRHII------QSLASAVAYLHK-NDIVHRDLKLENILVkssiiDNnDKLNIKVTD 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 215 FG-SAKVLVKGEPNISYIC-SRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGEnSVDQLVEIIK 285
Cdd:cd14097 151 FGlSVQKYGLGEDMLQETCgTPIYMAPEVI-SAHGYSQQCDIWSIGVIMYMLLCGEPPFVAK-SEEKLFEEIR 221
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
75-352 4.20e-20

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: 88.97  E-value: 4.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIK----KVLQDRRYK-NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVP 149
Cdd:cd14083  10 VLGTGAFSEVVLAEDKATGKLVAIKcidkKALKGKEDSlENEIAVLRKIKHPNIVQLLDIYESKSH-----LYLVMELVT 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 --ETLYRVLRH--YTSSNQRMPIFyvklytyQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKL--CDFGSAKVLVK 223
Cdd:cd14083  85 ggELFDRIVEKgsYTEKDASHLIR-------QVLEAVDYLHSL-GIVHRDLKPENLLYYSPDEDSKImiSDFGLSKMEDS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEpnISYIC-SRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircmnpNY 302
Cdd:cd14083 157 GV--MSTACgTPGYVAPEVL-AQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILK---------------AE 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42571361 303 TDFRFPQikahpWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14083 219 YEFDSPY-----WDDI-----SDSAKDFIRHLMEKDPNKRYTCEQALEHP 258
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
76-361 4.93e-20

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: 89.52  E-value: 4.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV---LQDRRYKN--RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVPE 150
Cdd:cd06622   9 LGKGNYGSVYKVLHRPTGVTMAMKEIrleLDESKFNQiiMELDILHKAVSPYIVDFYGAFFIEGA-----VYMCMEYMDA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNISY 230
Cdd:cd06622  84 GSLDKLYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEHNIIHRDVKPTNVLVNG-NGQVKLCDFGVSGNLVASLAKTNI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 ICSRYYrAPELI-----FGATEYTASIDIWSAGCVLAELLLGQPLFPGE---NSVDQLVEIIKvlGTPTReeircMNPNY 302
Cdd:cd06622 163 GCQSYM-APERIksggpNQNPTYTVQSDVWSLGLSILEMALGRYPYPPEtyaNIFAQLSAIVD--GDPPT-----LPSGY 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 303 TdfrfpqikahpwhkvfhkrmpPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPN 361
Cdd:cd06622 235 S---------------------DDAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNAD 272
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
63-354 6.77e-20

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: 88.45  E-value: 6.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  63 EPKQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQ-------DRRYKNRELQLMRPMDHPNVISLkHCFFstts 135
Cdd:cd14187   2 DPRTRRRYVRGRFLGKGGFAKCYEITDADTKEVFAGKIVPKslllkphQKEKMSMEIAIHRSLAHQHVVGF-HGFF---- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 136 RDELFLNLVMEYVPEtlyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDF 215
Cdd:cd14187  77 EDNDFVYVVLELCRR---RSLLELHKRRKALTEPEARYYLRQIILGCQYLHR-NRVIHRDLKLGNLFLND-DMEVKIGDF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 216 GSA-KVLVKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFpgensvdqlveiikvlgtptreE 294
Cdd:cd14187 152 GLAtKVEYDGERKKTLCGTPNYIAPE-VLSKKGHSFEVDIWSIGCIMYTLLVGKPPF----------------------E 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 295 IRCMNPNYTdfrfpQIKAHPWHkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14187 209 TSCLKETYL-----RIKKNEYS--IPKHINPVAASLIQKMLQTDPTARPTINELLNDEFF 261
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
76-300 7.42e-20

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: 89.34  E-value: 7.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVPE 150
Cdd:cd06650  13 LGAGNGGVVFKVSHKPSGLVMARKLIHLEikpaiRNQIIRELQVLHECNSPYIVGFYGAFYSDGE-----ISICMEHMDG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 -TLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNiS 229
Cdd:cd06650  88 gSLDQVLK----KAGRIPEQILGKVSIAVIKGLTYLREKHKIMHRDVKPSNILVNS-RGEIKLCDFGVSGQLIDSMAN-S 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 230 YICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQ-PLFPGENSVDQLVEIIKVLGTPTREEIRCMNP 300
Cdd:cd06650 162 FVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVEMAVGRyPIPPPDAKELELMFGCQVEGDAAETPPRPRTP 232
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
74-352 7.87e-20

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 88.50  E-value: 7.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQL-MRPMDHPNVISLKHCFFSTTSRDELFLnLVMEYVP--E 150
Cdd:cd14089   7 QVLGLGINGKVLECFHKKTGEKFALK-VLRDNPKARREVELhWRASGCPHIVRIIDVYENTYQGRKCLL-VVMECMEggE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRV----LRHYTSSNqrmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLV--DPLTHQVKLCDFGSAKVLVKG 224
Cdd:cd14089  85 LFSRIqeraDSAFTERE-------AAEIMRQIGSAVAHLHSM-NIAHRDLKPENLLYssKGPNAILKLTDFGFAKETTTK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLF---------PGENSvdqlveiikvlgtptreei 295
Cdd:cd14089 157 KSLQTPCYTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYILLCGYPPFysnhglaisPGMKK------------------- 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 296 RCMNPNYTdfrFPqikaHP-WhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHP 352
Cdd:cd14089 217 RIRNGQYE---FP----NPeW-----SNVSEEAKDLIRGLLKTDPSERLTIEEVMNHP 262
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
70-353 7.90e-20

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: 88.36  E-value: 7.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYK---NRELQLMRPMDHPNVISLKHCFfstTSRDELFLNLVME 146
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGRevcESELNVLRRVRHTNIIQLIEVF---ETKERVYMVMELA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLR--HYTSSNQRMPIfyvklytYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKL--CDFGSAKVLV 222
Cdd:cd14087  80 TGGELFDRIIAkgSFTERDATRVL-------QMVLDGVKYLHGL-GITHRDLKPENLLYYHPGPDSKImiTDFGLASTRK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPN-ISYIC-SRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeircmnp 300
Cdd:cd14087 152 KGPNClMKTTCgTPEYIAPEILL-RKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRA-------------- 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 301 NYTdfrfpqIKAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14087 217 KYS------YSGEPWPSV-----SNLAKDFIDRLLTVNPGERLSATQALKHPW 258
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
76-360 8.27e-20

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: 90.09  E-value: 8.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV-------LQDRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYV 148
Cdd:cd05600  19 VGQGGYGSVFLARKKDTGEICALKIMkkkvlfkLNEVNHVLTERDILTTTNSPWLVKLLYAF-----QDPENVYLAMEYV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P----ETL---YRVLRHYtssnqrmpifYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSA--- 218
Cdd:cd05600  94 PggdfRTLlnnSGILSEE----------HARFYIAEMFAAISSLHQL-GYIHRDLKPENFLIDSSGH-IKLTDFGLAsgt 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 ---------------------------------KVLVKGEPNISYIC--SRYYRAPELIFGaTEYTASIDIWSAGCVLAE 263
Cdd:cd05600 162 lspkkiesmkirleevkntafleltakerrniyRAMRKEDQNYANSVvgSPDYMAPEVLRG-EGYDLTVDYWSLGCILFE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 264 LLLGQPLFPGeNSVDQLVEII----KVLGTPTREEiRCMNPNYTDfrfpqikahpwhkvfhkrmppEAIDLASRLLQYSP 339
Cdd:cd05600 241 CLVGFPPFSG-STPNETWANLyhwkKTLQRPVYTD-PDLEFNLSD---------------------EAWDLITKLITDPQ 297
                       330       340
                ....*....|....*....|....*.
gi 42571361 340 SLRCTALEACAHPFF-----NELREP 360
Cdd:cd05600 298 DRLQSPEQIKNHPFFknidwDRLREG 323
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
74-324 1.08e-19

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 88.25  E-value: 1.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLVMEYV 148
Cdd:cd06621   7 SSLGEGAGGSVTKCRLRNTKTIFALKTITTDpnpdvQKQILRELEINKSCASPYIVKYYGAFLDEQDSS---IGIAMEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P----ETLYRVLRHYTSSNQRMPIFYVklyTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFGsakvlVKG 224
Cdd:cd06621  84 EggslDSIYKKVKKKGGRIGEKVLGKI---AESVLKGLSYLHS-RKIIHRDIKPSNILLT-RKGQVKLCDFG-----VSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNIS----YICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVD----QLVEIIKVLGTPT----- 291
Cdd:cd06621 154 ELVNSlagtFTGTSYYMAPERIQGGP-YSITSDVWSLGLTLLEVAQNRFPFPPEGEPPlgpiELLSYIVNMPNPElkdep 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42571361 292 ------REEIR-----CMNPNYTDFRFP-QIKAHPWHKVFHKRMP 324
Cdd:cd06621 233 engikwSESFKdfiekCLEKDGTRRPGPwQMLAHPWIKAQEKKKV 277
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
75-348 1.27e-19

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: 88.19  E-value: 1.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFFSttsRDELFLNlvMEYVP 149
Cdd:cd14046  13 VLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNnsrilREVMLLSRLNHQHVVRYYQAWIE---RANLYIQ--MEYCE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRHYTSSNQRmpiFYVKLYTyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAK------VLV 222
Cdd:cd14046  88 KsTLRDLIDSGLFQDTD---RLWRLFR-QILEGLAYIHS-QGIIHRDLKPVNIFLDSNGN-VKIGDFGLATsnklnvELA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISY-------------ICSRYYRAPELIFGATE-YTASIDIWSAGCVLAELLlgQPLFPGensvdqlVEIIKVLG 288
Cdd:cd14046 162 TQDINKSTsaalgssgdltgnVGTALYVAPEVQSGTKStYNEKVDMYSLGIIFFEMC--YPFSTG-------MERVQILT 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 289 TptreeIRCMNPNytdfrFPQIkahpWHKVFHkrmpPEAIDLASRLLQYSPSLRCTALEA 348
Cdd:cd14046 233 A-----LRSVSIE-----FPPD----FDDNKH----SKQAKLIRWLLNHDPAKRPSAQEL 274
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
74-295 1.31e-19

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 87.77  E-value: 1.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR---------ELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLV 144
Cdd:cd06653   8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETskevnalecEIQLLKNLRHDRIVQYYGCLRDPEEKK---LSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP-ETLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAK---- 219
Cdd:cd06653  85 VEYMPgGSVKDQLKAYGALTENV----TRRYTRQILQGVSYLHS-NMIVHRDIKGANILRDS-AGNVKLGDFGASKriqt 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 220 VLVKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPgenSVDQLVEIIKVLGTPTREEI 295
Cdd:cd06653 159 ICMSGTGIKSVTGTPYWMSPEVISGEG-YGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKIATQPTKPQL 230
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
75-357 1.61e-19

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: 88.52  E-value: 1.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKV-------LQDRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEY 147
Cdd:cd05601   8 VIGRGHFGEVQVVKEKATGDIYAMKVLkksetlaQEEVSFFEEERDIMAKANSPWITKLQYAF-----QDSENLYLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VP--ETLYRVLRHYTSSNQRMPIFYVKLYTyqifrgLAyIHTVP--GVCHRDVKPQNLLVDPLTHqVKLCDFGSA----- 218
Cdd:cd05601  83 HPggDLLSLLSRYDDIFEESMARFYLAELV------LA-IHSLHsmGYVHRDIKPENILIDRTGH-IKLADFGSAaklss 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 --KVLVK---GEPNisyicsryYRAPELIFGATEYTAS-----IDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIkvlg 288
Cdd:cd05601 155 dkTVTSKmpvGTPD--------YIAPEVLTSMNGGSKGtygveCDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIM---- 222
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 289 tptreeircmnpNYTDF-RFPQikahpwhkvfHKRMPPEAIDLASRLLQySPSLRCTALEACAHPFFNEL 357
Cdd:cd05601 223 ------------NFKKFlKFPE----------DPKVSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGI 269
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
76-353 1.66e-19

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 87.35  E-value: 1.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYK---NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVP--E 150
Cdd:cd14665   8 IGSGNFGVARLMRDKQTKELVAVKYIERGEKIDenvQREIINHRSLRHPNIVRFKEVILTPTH-----LAIVMEYAAggE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRMPIFYvklytYQIFRGLAYIHTVPgVCHRDVKPQNLLVDPLTH-QVKLCDFGSAKVLVKGEPNIS 229
Cdd:cd14665  83 LFERICNAGRFSEDEARFFF-----QQLISGVSYCHSMQ-ICHRDLKLENTLLDGSPApRLKICDFGYSKSSVLHSQPKS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 230 YICSRYYRAPELIFgATEYTASI-DIWSAGCVLAELLLGQplFPGENSvDQLVEIIKVLGtptreeiRCMNPNYTdfrFP 308
Cdd:cd14665 157 TVGTPAYIAPEVLL-KKEYDGKIaDVWSCGVTLYVMLVGA--YPFEDP-EEPRNFRKTIQ-------RILSVQYS---IP 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42571361 309 QikahpwhkvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14665 223 D----------YVHISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
76-275 2.20e-19

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: 86.93  E-value: 2.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKcLETGESVAIKKVLQDR-------RYKNRELQLMRPMDHPNVISLkHCFFSTTSRdelfLNLVMEYV 148
Cdd:cd14161  11 LGKGTYGRVKKAR-DSSGRLVAIKSIRKDRikdeqdlLHIRREIEIMSSLNHPHIISV-YEVFENSSK----IVIVMEYA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PE-TLYrvlrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPN 227
Cdd:cd14161  85 SRgDLY----DYISERQRLSELEARHFFRQIVSAVHYCHA-NGIVHRDLKLENILLDA-NGNIKIADFGLSNLYNQDKFL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 228 ISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd14161 159 QTYCGSPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHD 206
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
74-374 2.99e-19

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: 87.66  E-value: 2.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKK-----VLQD-----RRYKNRELQLMRpmDHPNVISLKHCFFSTtsrDELFlnL 143
Cdd:cd05590   1 RVLGKGSFGKVMLARLKESGRLYAVKVlkkdvILQDddvecTMTEKRILSLAR--NHPFLTQLYCCFQTP---DRLF--F 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK 223
Cdd:cd05590  74 VMEFVNGG---DLMFHIQKSRRFDEARARFYAAEITSALMFLHD-KGIIYRDLKLDNVLLDHEGH-CKLADFGMCKEGIF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIkvlgtpTREEIrcmnpny 302
Cdd:cd05590 149 NGKTTSTFCgTPDYIAPE-ILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENE-DDLFEAI------LNDEV------- 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 303 tdfrfpqikahpwhkVFHKRMPPEAIDLASRLLQYSPSLR--CTALEA----CAHPFFNELrepNARLPNGRPLPPLF 374
Cdd:cd05590 214 ---------------VYPTWLSQDAVDILKAFMTKNPTMRlgSLTLGGeeaiLRHPFFKEL---DWEKLNRRQIEPPF 273
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
74-261 3.05e-19

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 87.18  E-value: 3.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN----RELQLMRPMD-HPNVISLkhCFFSTTSRDEL------FLn 142
Cdd:cd14036   6 RVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNkaiiQEINFMKKLSgHPNIVQF--CSAASIGKEESdqgqaeYL- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPETLYRVLRHYTSSNQRMPIFYVKLYtYQIFRGLAYIHT-VPGVCHRDVKPQNLLvdpLTHQ--VKLCDFGSAK 219
Cdd:cd14036  83 LLTELCKGQLVDFVKKVEAPGPFSPDTVLKIF-YQTCRAVQHMHKqSPPIIHRDLKIENLL---IGNQgqIKLCDFGSAT 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 220 VLV-------------KGEPNISYICSRYYRAPELIFGATEY--TASIDIWSAGCVL 261
Cdd:cd14036 159 TEAhypdyswsaqkrsLVEDEITRNTTPMYRTPEMIDLYSNYpiGEKQDIWALGCIL 215
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
75-357 4.55e-19

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: 86.29  E-value: 4.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQA--------------KCLETGESVAIKKVLQDRRYKNRELQLMRpmDHPNVISLkHCFFSTTSRdelf 140
Cdd:cd05583   1 VLGTGAYGKVFLVrkvgghdagklyamKVLKKATIVQKAKTAEHTMTERQVLEAVR--QSPFLVTL-HYAFQTDAK---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVP-----ETLYRVlRHYTSSNqrmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDF 215
Cdd:cd05583  74 LHLILDYVNggelfTHLYQR-EHFTESE-------VRIYIGEIVLALEHLHKL-GIIYRDIKLENILLDSEGH-VVLTDF 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 216 GSAKVLVKGEPNISY-ICSRY-YRAPELIFGATE-YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptr 292
Cdd:cd05583 144 GLSKEFLPGENDRAYsFCGTIeYMAPEVVRGGSDgHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISK------- 216
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 293 eeiRCMnpnytdfrfpqiKAHPwhkVFHKRMPPEAIDLASRLLQYSPSLR-----CTALEACAHPFFNEL 357
Cdd:cd05583 217 ---RIL------------KSHP---PIPKTFSAEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPFFKGL 268
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
69-353 6.00e-19

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: 85.96  E-value: 6.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIK-----------KVLQDRRYKN--------RELQLMRPMDHPNVISLKHC 129
Cdd:cd14077   2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKiiprasnaglkKEREKRLEKEisrdirtiREAALSSLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 130 FFSTTSRDELFlnlvmEYVPEtlyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQ 209
Cdd:cd14077  82 LRTPNHYYMLF-----EYVDG---GQLLDYIISHGKLKEKQARKFARQIASALDYLHR-NSIVHRDLKIENILISK-SGN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 VKLCDFGSAKVLVKGEPNISYICSRYYRAPELIfGATEYTA-SIDIWSAGCVLAELLLGQPLFPGENsVDQLVEIIKvlg 288
Cdd:cd14077 152 IKIIDFGLSNLYDPRRLLRTFCGSLYFAAPELL-QAQPYTGpEVDVWSFGVVLYVLVCGKVPFDDEN-MPALHAKIK--- 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 289 tptreeircmnpnYTDFRFPqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14077 227 -------------KGKVEYP------------SYLSSECKSLISRMLVVDPKKRATLEQVLNHPW 266
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
74-284 6.17e-19

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: 86.30  E-value: 6.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ-------LMRPMDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd14209   7 KTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEhtlnekrILQAINFPFLVKLEYSF-----KDNSNLYMVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--EtlyrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKvLVKG 224
Cdd:cd14209  82 YVPggE-----MFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSL-DLIYRDLKPENLLIDQQGY-IKVTDFGFAK-RVKG 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 225 EpnISYIC-SRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVdQLVEII 284
Cdd:cd14209 154 R--TWTLCgTPEYLAPEIIL-SKGYNKAVDWWALGVLIYEMAAGYPPFFADQPI-QIYEKI 210
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
70-275 7.54e-19

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: 85.30  E-value: 7.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDR-------RYKNRELQLMRPMDHPNVISLKHCFFSTTSRdelfLN 142
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRaspdfvqKFLPRELSILRRVNHPNIVQMFECIEVANGR----LY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPETLYRVLRHytssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKvLV 222
Cdd:cd14164  78 IVMEAAATDLLQKIQE----VHHIPKDLARDMFAQMVGAVNYLHDM-NIVHRDLKCENILLSADDRKIKIADFGFAR-FV 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 223 KGEPNIS--YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd14164 152 EDYPELSttFCGSRAYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETN 206
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
67-353 7.86e-19

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: 87.00  E-value: 7.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  67 TISYMAERVVGTGSFGIVfqAKCLE--TGESVAIKKVLQDRRYKNRELQ-LMRPMDHPNVISLKHCFfsttsRDELFLNL 143
Cdd:cd14176  18 TDGYEVKEDIGVGSYSVC--KRCIHkaTNMEFAVKIIDKSKRDPTEEIEiLLRYGQHPNIITLKDVY-----DDGKYVYV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--ETLYRVLRH-YTSSNQRMPIFYVklytyqIFRGLAYIHTvPGVCHRDVKPQNLL-VDPLTH--QVKLCDFGS 217
Cdd:cd14176  91 VTELMKggELLDKILRQkFFSEREASAVLFT------ITKTVEYLHA-QGVVHRDLKPSNILyVDESGNpeSIRICDFGF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 218 AKVLVKGEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFpGENSVDQLVEIIKVLGTPtreeir 296
Cdd:cd14176 164 AKQLRAENGLLMTPCyTANFVAPE-VLERQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIGSG------ 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 cmnpnytdfRFpQIKAHPWHKVFHkrmppEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14176 236 ---------KF-SLSGGYWNSVSD-----TAKDLVSKMLHVDPHQRLTAALVLRHPW 277
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
74-372 9.07e-19

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: 85.87  E-value: 9.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNR--------ELQLMRPMDHPNVISLKHCFfstTSRDELFLNLVM 145
Cdd:cd05605   6 RVLGKGGFGEVCACQVRATGKMYACKK-LEKKRIKKRkgeamalnEKQILEKVNSRFVVSLAYAY---ETKDALCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVlrhYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGE 225
Cdd:cd05605  82 MNGGDLKFHI---YNMGNPGFEEERAVFYAAEITCGLEHLHS-ERIVYRDLKPENILLDDHGH-VRISDLGLAVEIPEGE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENsvdqlvEIIKvlgtptREEIrcmnpnytDF 305
Cdd:cd05605 157 TIRGRVGTVGYMAPEVV-KNERYTFSPDWWGLGCLIYEMIEGQAPFRARK------EKVK------REEV--------DR 215
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 306 RfpqIKAHPwhKVFHKRMPPEAIDLASRLLQYSPSLR--CT---ALEACAHPFFNELREpnARLPNGRPLPP 372
Cdd:cd05605 216 R---VKEDQ--EEYSEKFSEEAKSICSQLLQKDPKTRlgCRgegAEDVKSHPFFKSINF--KRLEAGLLEPP 280
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
70-315 9.17e-19

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 85.21  E-value: 9.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVlqDRRYK-----NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLV 144
Cdd:cd14662   2 YELVKDIGSGNFGVARLMRNKETKELVAVKYI--ERGLKidenvQREIINHRSLRHPNIIRFKEVVLTPTH-----LAIV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVlrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVD-PLTHQVKLCDFGSAKVL 221
Cdd:cd14662  75 MEYAAggELFERI-----CNAGRFSEDEARYFFQQLISGVSYCHSMQ-ICHRDLKLENTLLDgSPAPRLKICDFGYSKSS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYICSRYYRAPElIFGATEYTASI-DIWSAGCVLAELLLGQplFPGENSVD------QLVEIIKV-------- 286
Cdd:cd14662 149 VLHSQPKSTVGTPAYIAPE-VLSRKEYDGKVaDVWSCGVTLYVMLVGA--YPFEDPDDpknfrkTIQRIMSVqykipdyv 225
                       250       260       270
                ....*....|....*....|....*....|...
gi 42571361 287 -LGTPTREEIRCM---NPnYTDFRFPQIKAHPW 315
Cdd:cd14662 226 rVSQDCRHLLSRIfvaNP-AKRITIPEIKNHPW 257
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
69-354 1.02e-18

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: 84.98  E-value: 1.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR-------ELQLMRPMDHPNVISLKHcFFSTTSRDELFL 141
Cdd:cd14189   2 SYCKGRLLGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHqrekivnEIELHRDLHHKHVVKFSH-HFEDAENIYIFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEyvpetlyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd14189  81 ELCSR-------KSLAHIWKARHTLLEPEVRYYLKQIISGLKYLH-LKGILHRDLKLGNFFINE-NMELKVGDFGLAARL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYIC-SRYYRAPELIFGATEYTASiDIWSAGCVLAELLLGQPLFpgeNSVDqlveiikvlgtpTREEIRCMNP 300
Cdd:cd14189 152 EPPEQRKKTICgTPNYLAPEVLLRQGHGPES-DVWSLGCVMYTLLCGNPPF---ETLD------------LKETYRCIKQ 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 301 nyTDFRFPQIkahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14189 216 --VKYTLPAS------------LSLPARHLLAGILKRNPGDRLTLDQILEHEFF 255
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
73-353 1.04e-18

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: 84.97  E-value: 1.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFqaKCLETGESVAIK-KVLQDRRYKNR-----ELQLMRPMDHPNVISLKHCFfstTSRDELFLnlVME 146
Cdd:cd14193   9 EEILGGGRFGQVH--KCEEKSSGLKLAaKIIKARSQKEKeevknEIEVMNQLNHANLIQLYDAF---ESRNDIVL--VME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVPgVCHRDVKPQNLL-VDPLTHQVKLCDFGSAKVLVK 223
Cdd:cd14193  82 YVDggELFDRIIDENYNLTELDTILFIK----QICEGIQYMHQMY-ILHLDLKPENILcVSREANQVKIIDFGLARRYKP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPELIfgATEYTA-SIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeirCmNPNY 302
Cdd:cd14193 157 REKLRVNFGTPEFLAPEVV--NYEFVSfPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILA-----------C-QWDF 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 303 TDFRFPQIKAhpwhkvfhkrmppEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14193 223 EDEEFADISE-------------EAKDFISKLLIKEKSWRMSASEALKHPW 260
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
64-295 1.04e-18

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 85.52  E-value: 1.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR---------ELQLMRPMDHPNVISLKHCFfstT 134
Cdd:cd06651   3 PSAPINWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETskevsalecEIQLLKNLQHERIVQYYGCL---R 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 135 SRDELFLNLVMEYVPE-TLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLC 213
Cdd:cd06651  80 DRAEKTLTIFMEYMPGgSVKDQLKAYGALTESV----TRKYTRQILEGMSYLHS-NMIVHRDIKGANILRDS-AGNVKLG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 214 DFGSAKVL----VKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPgenSVDQLVEIIKVLGT 289
Cdd:cd06651 154 DFGASKRLqticMSGTGIRSVTGTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKIATQ 229

                ....*.
gi 42571361 290 PTREEI 295
Cdd:cd06651 230 PTNPQL 235
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
70-264 1.13e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 85.03  E-value: 1.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV--------LQDRRyknRELQLMRPMDHPNVISLKHCFfsttsRDELFL 141
Cdd:cd08219   2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIrlpksssaVEDSR---KEAVLLAKMKHPNIVAFKESF-----EADGHL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVP--ETLYRVlrhytsSNQRMPIF---YVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTH--QVKLCD 214
Cdd:cd08219  74 YIVMEYCDggDLMQKI------KLQRGKLFpedTILQWFVQMCLGVQHIHE-KRVLHRDIKSKNIF---LTQngKVKLGD 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 215 FGSAKVLVK-GEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAEL 264
Cdd:cd08219 144 FGSARLLTSpGAYACTYVGTPYYVPPE-IWENMPYNNKSDIWSLGCILYEL 193
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
69-267 1.18e-18

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: 84.87  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIkKVLQDRRYKN---------RELQLMRPMDHPNVISLKHCFFSTTSrdel 139
Cdd:cd14070   3 SYLIGRKLGEGSFAKVREGLHAVTGEKVAI-KVIDKKKAKKdsyvtknlrREGRIQQMIRHPNITQLLDILETENS---- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 fLNLVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFG--- 216
Cdd:cd14070  78 -YYLVMELCPGG---NLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRA-GVVHRDLKIENLLLDE-NDNIKLIDFGlsn 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 217 SAKVLVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLG 267
Cdd:cd14070 152 CAGILGYSDPFSTQCGSPAYAAPELL-ARKKYGPKVDVWSIGVNMYAMLTG 201
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
62-305 1.32e-18

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: 85.55  E-value: 1.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  62 GEPKQtiSYMAERVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKN---RELQLMRPMDHPNVISLKHCFFSTtsrD 137
Cdd:cd06655  15 GDPKK--KYTRYEKIGQGASGTVFTAIDVATGQEVAIKQInLQKQPKKEliiNEILVMKELKNPNIVNFLDSFLVG---D 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 138 ELFLnlVMEYVPE-TLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFG 216
Cdd:cd06655  90 ELFV--VMEYLAGgSLTDVVTETCMDEAQ-----IAAVCRECLQALEFLHA-NQVIHRDIKSDNVLLG-MDGSVKLTDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 -SAKVLVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVeIIKVLGTPTREEI 295
Cdd:cd06655 161 fCAQITPEQSKRSTMVGTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQNP 238
                       250
                ....*....|
gi 42571361 296 RCMNPNYTDF 305
Cdd:cd06655 239 EKLSPIFRDF 248
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
70-353 1.45e-18

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: 84.96  E-value: 1.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKClETGESVAIKKV-LQDRR------YKNrELQLMRPM-DHPNVISLkhcFFSTTSRDELFL 141
Cdd:cd14131   3 YEILKQLGKGGSSKVYKVLN-PKKKIYALKRVdLEGADeqtlqsYKN-EIELLKKLkGSDRIIQL---YDYEVTDEDDYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPETLYRVLRHYTSSNqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQN-LLVDpltHQVKLCDFGSAKV 220
Cdd:cd14131  78 YMVMECGEIDLATILKKKRPKP--IDPNFIRYYWKQMLEAVHTIHE-EGIVHSDLKPANfLLVK---GRLKLIDFGIAKA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNI---SYICSRYYRAPELIFGaTEYTASI----------DIWSAGCVLAELLLGQPLFPgenSVDQLVEIIKVL 287
Cdd:cd14131 152 IQNDTTSIvrdSQVGTLNYMSPEAIKD-TSASGEGkpkskigrpsDVWSLGCILYQMVYGKTPFQ---HITNPIAKLQAI 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 288 gtptreeircMNPNYtDFRFPQIKahpwhkvfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14131 228 ----------IDPNH-EIEFPDIP------------NPDLIDVMKRCLQRDPKKRPSIPELLNHPF 270
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
75-265 1.53e-18

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: 84.94  E-value: 1.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIV----FQAKCLETGESVAIKKVLQD----RRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLVME 146
Cdd:cd05081  11 QLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSgpdqQRDFQREIQILKALHSDFIVKYRGVSYGPGRRS---LRLVME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETlyrVLRHYTSSNQ-RMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPLTHqVKLCDFGSAKVL---- 221
Cdd:cd05081  88 YLPSG---CLRDFLQRHRaRLDASRLLLYSSQICKGMEYLGSRRCV-HRDLAARNILVESEAH-VKIADFGLAKLLpldk 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 42571361 222 ---VKGEPNISYIcsrYYRAPELIfGATEYTASIDIWSAGCVLAELL 265
Cdd:cd05081 163 dyyVVREPGQSPI---FWYAPESL-SDNIFSRQSDVWSFGVVLYELF 205
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
69-267 1.57e-18

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: 85.04  E-value: 1.57e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKVL----QDRRYKNRELQLMRPMDHPNVISL-KHCFFSTTSRDElFLNL 143
Cdd:cd13986   1 RYRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILchskEDVKEAMREIENYRLFNHPNILRLlDSQIVKEAGGKK-EVYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGV--CHRDVKPQNLLVDPLTHQVkLCDFGS--- 217
Cdd:cd13986  80 LLPYYKRgSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELVpyAHRDIKPGNVLLSEDDEPI-LMDLGSmnp 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 218 AKVLVKGEPNISYI-------CSRYYRAPELIfgATEYTASI----DIWSAGCVLAELLLG 267
Cdd:cd13986 159 ARIEIEGRREALALqdwaaehCTMPYRAPELF--DVKSHCTIdektDIWSLGCTLYALMYG 217
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
74-284 2.27e-18

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: 85.24  E-value: 2.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK-----KVLQD-----RRYKNRELQLMRpmDHPNVISLkHCFFSTtsRDELFLnl 143
Cdd:cd05591   1 KVLGKGSFGKVMLAERKGTDEVYAIKvlkkdVILQDddvdcTMTEKRILALAA--KHPFLTAL-HSCFQT--KDRLFF-- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV- 220
Cdd:cd05591  74 VMEYVNggDLMFQIQRARKFDEPR-----ARFYAAEVTLALMFLHR-HGVIYRDLKLDNILLDAEGH-CKLADFGMCKEg 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 221 LVKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEII 284
Cdd:cd05591 147 ILNGKTTTTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE-DDLFESI 208
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
93-356 2.94e-18

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


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 84.20  E-value: 2.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  93 GESVAIKKVLQDRRYKNRELQLMRPMD-HPNVISLKHCFFSTTsrdelFLNLVMEYVPE-TLYRVLRHYTSSNQRMpify 170
Cdd:cd14182  41 GGSFSPEEVQELREATLKEIDILRKVSgHPNIIQLKDTYETNT-----FFFLVFDLMKKgELFDYLTEKVTLSEKE---- 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 171 vklyTYQIFRGL----AYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEpNISYIC-SRYYRAPELIFGA 245
Cdd:cd14182 112 ----TRKIMRALleviCALHKL-NIVHRDLKPENILLDD-DMNIKLTDFGFSCQLDPGE-KLREVCgTPGYLAPEIIECS 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 246 TE-----YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIikvlgtptreeircMNPNYtdfrfpQIKAHPWHKvfh 320
Cdd:cd14182 185 MDdnhpgYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMI--------------MSGNY------QFGSPEWDD--- 241
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 42571361 321 krMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd14182 242 --RSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
73-273 2.94e-18

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 83.94  E-value: 2.94e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAkcLETGESVAIKKVLQD------RRYKN--RELQLMRPMDHPNVISLKH-CFfsttsrDELFLNL 143
Cdd:cd14145  11 EEIIGIGGFGKVYRA--IWIGDEVAVKAARHDpdedisQTIENvrQEAKLFAMLKHPNIIALRGvCL------KEPNLCL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLrhytsSNQRMPIFYVKLYTYQIFRGLAYIHT---VPgVCHRDVKPQNLLV------DPLTHQV-KL 212
Cdd:cd14145  83 VMEFARGgPLNRVL-----SGKRIPPDILVNWAVQIARGMNYLHCeaiVP-VIHRDLKSSNILIlekvenGDLSNKIlKI 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 213 CDFGSAKVLVKgEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPG 273
Cdd:cd14145 157 TDFGLAREWHR-TTKMSAAGTYAWMAPEVIRSSM-FSKGSDVWSYGVLLWELLTGEVPFRG 215
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
69-274 3.45e-18

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 84.31  E-value: 3.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV----LQDRRYKN---RELQLMRPMDHPNVISLKHCFFsttsrDELFL 141
Cdd:cd08229  25 NFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVqifdLMDAKARAdciKEIDLLKQLNHPNVIKYYASFI-----EDNEL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd08229 100 NIVLELADAgDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHS-RRVMHRDIKPANVFITA-TGVVKLGDLGLGRF 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 221 L-VKGEPNISYICSRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGE 274
Cdd:cd08229 178 FsSKTTAAHSLVGTPYYMSPERIH-ENGYNFKSDIWSLGCLLYEMAALQSPFYGD 231
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
70-351 3.78e-18

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 84.30  E-value: 3.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ-LMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYV 148
Cdd:cd14177   6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEiLMRYGQHPNIITLKDVY-----DDGRYVYLVTELM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P--ETLYRVLRH-YTSSNQRMPIFYVklytyqIFRGLAYIHtVPGVCHRDVKPQNLL-VDPLTH--QVKLCDFGSAKVLv 222
Cdd:cd14177  81 KggELLDRILRQkFFSEREASAVLYT------ITKTVDYLH-CQGVVHRDLKPSNILyMDDSANadSIRICDFGFAKQL- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPN--ISYICSRYYRAPELIFgATEYTASIDIWSAGCVLAELLLG-QPLFPGENSvdqlveiikvlgTPTREEIRCMN 299
Cdd:cd14177 153 RGENGllLTPCYTANFVAPEVLM-RQGYDAACDIWSLGVLLYTMLAGyTPFANGPND------------TPEEILLRIGS 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 300 PNYTdfrfpqIKAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAH 351
Cdd:cd14177 220 GKFS------LSGGNWDTV-----SDAAKDLLSHMLHVDPHQRYTAEQVLKH 260
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
74-362 3.95e-18

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: 85.29  E-value: 3.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNREL-------QLMRPMDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd05629   7 KVIGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMFKKDQLahvkaerDVLAESDSPWVVSLYYSF-----QDAQYLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE-TLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFG--------- 216
Cdd:cd05629  82 FLPGgDLMTMLIKYDTFSEDVTRFYMA----ECVLAIEAVHKL-GFIHRDIKPDNILIDRGGH-IKLSDFGlstgfhkqh 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 ---SAKVLVKGEPNISYICSRY------------------------------------YRAPElIFGATEYTASIDIWSA 257
Cdd:cd05629 156 dsaYYQKLLQGKSNKNRIDNRNsvavdsinltmsskdqiatwkknrrlmaystvgtpdYIAPE-IFLQQGYGQECDWWSL 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 258 GCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptREEIrcmnpnytdfRFPQiKAHpwhkvfhkrMPPEAIDLASRLLQY 337
Cdd:cd05629 235 GAIMFECLIGWPPFCSENSHETYRKIINW-----RETL----------YFPD-DIH---------LSVEAEDLIRRLITN 289
                       330       340       350
                ....*....|....*....|....*....|..
gi 42571361 338 SPSL--RCTALEACAHPFF-----NELREPNA 362
Cdd:cd05629 290 AENRlgRGGAHEIKSHPFFrgvdwDTIRQIRA 321
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
76-353 4.13e-18

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: 83.19  E-value: 4.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLE-TGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVP 149
Cdd:cd14120   1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSqnllgKEIKILKELSHENVVALLDCQETSSS-----VYLVMEYCN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 etlYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTH-----------QVKLCDFGSA 218
Cdd:cd14120  76 ---GGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHS-KGIVHRDLKPQNIL---LSHnsgrkpspndiRLKIADFGFA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGeNSVDQLVEIIkvlgtptrEEIRCM 298
Cdd:cd14120 149 RFLQDGMMAATLCGSPMYMAPEVIMS-LQYDAKADLWSIGTIVYQCLTGKAPFQA-QTPQELKAFY--------EKNANL 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 299 NPNYTDFRFPQIKahpwhkvfhkrmppeaiDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14120 219 RPNIPSGTSPALK-----------------DLLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
70-353 4.13e-18

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: 83.91  E-value: 4.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK-----------KVLQDRRYKNRELQLMRPMDHPNVISLKHCF------FS 132
Cdd:cd13990   2 YLLLNLLGKGGFSEVYKAFDLVEQRYVACKihqlnkdwseeKKQNYIKHALREYEIHKSLDHPRIVKLYDVFeidtdsFC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 133 TtsrdelflnlVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTV-PGVCHRDVKPQNLLVDPLTH--Q 209
Cdd:cd13990  82 T----------VLEYCDGN---DLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIkPPIIHYDLKPGNILLHSGNVsgE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 VKLCDFGSAKVLVKGEPNISYI-------CSRYYRAPE-LIFGATEYTAS--IDIWSAGCVLAELLLGQ-PLFPGENSVD 278
Cdd:cd13990 149 IKITDFGLSKIMDDESYNSDGMeltsqgaGTYWYLPPEcFVVGKTPPKISskVDVWSVGVIFYQMLYGRkPFGHNQSQEA 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 279 QLVEIIKVlgtptreeircmnpNYTDFRFPqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd13990 229 ILEENTIL--------------KATEVEFP----------SKPVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
76-356 4.73e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 84.48  E-value: 4.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   76 VGTGSFGIVFQAKCLETGESVAIkKVLQDR---RYK-----NRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEY 147
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGTGEYYAI-KCLKKReilKMKqvqhvAQEKSILMELSHPFIVNMMCSF-----QDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  148 V-PETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLvkgeP 226
Cdd:PTZ00263 100 VvGGELFTHLR----KAGRFPNDVAKFYHAELVLAFEYLHSK-DIIYRDLKPENLLLDNKGH-VKVTDFGFAKKV----P 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  227 NISY-IC-SRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGEnsvdqlveiikvlgTPTR--EEI---RCMN 299
Cdd:PTZ00263 170 DRTFtLCgTPEYLAPEVI-QSKGHGKAVDWWTMGVLLYEFIAGYPPFFDD--------------TPFRiyEKIlagRLKF 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361  300 PNYTDFRfpqikahpwhkvfhkrmppeAIDLASRLLQYSPSLRCTALEACA-----HPFFNE 356
Cdd:PTZ00263 235 PNWFDGR--------------------ARDLVKGLLQTDHTKRLGTLKGGVadvknHPYFHG 276
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
75-284 5.64e-18

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: 84.28  E-value: 5.64e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ-------LMRPMDHPNVISLKHCFFSTTSRdelfLNLVMEY 147
Cdd:cd05615  17 VLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVEctmvekrVLALQDKPPFLTQLHSCFQTVDR----LYFVMEY 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VP--ETLYRVlRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV-LVKG 224
Cdd:cd05615  93 VNggDLMYHI-QQVGKFKEPQAVFYAA----EISVGLFFLHK-KGIIYRDLKLDNVMLDSEGH-IKIADFGMCKEhMVEG 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEII 284
Cdd:cd05615 166 VTTRTFCGTPDYIAPEII-AYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDE-DELFQSI 223
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
75-284 6.19e-18

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: 83.09  E-value: 6.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIK----KVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVP- 149
Cdd:cd14192  11 VLGGGRFGQVHKCTELSTGLTLAAKiikvKGAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTN-----LTLIMEYVDg 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 -ETLYRVlrhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLL-VDPLTHQVKLCDFGSAkvlvkgepn 227
Cdd:cd14192  86 gELFDRI----TDESYQLTELDAILFTRQICEGVHYLHQ-HYILHLDLKPENILcVNSTGNQIKIIDFGLA--------- 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 228 isyicsRYYRAPELI---FGATEYTAS-----------IDIWSAGCVLAELLLGQPLFPGENSVDQLVEII 284
Cdd:cd14192 152 ------RRYKPREKLkvnFGTPEFLAPevvnydfvsfpTDMWSVGVITYMLLSGLSPFLGETDAETMNNIV 216
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
73-336 7.81e-18

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 82.77  E-value: 7.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCleTGESVAIKKVLQD--------RRYKNRELQLMRPMDHPNVISLKhcffsTTSRDELFLNLV 144
Cdd:cd14147   8 EEVIGIGGFGKVYRGSW--RGELVAVKAARQDpdedisvtAESVRQEARLFAMLAHPNIIALK-----AVCLEEPNLCLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLrhytsSNQRMPIFYVKLYTYQIFRGLAYIHT---VPgVCHRDVKPQNLLV------DPLTHQ-VKLC 213
Cdd:cd14147  81 MEYAAGgPLSRAL-----AGRRVPPHVLVNWAVQIARGMHYLHCealVP-VIHRDLKSNNILLlqpienDDMEHKtLKIT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 214 DFGSAKVLVKgEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGEN--SVDQLVEIIKV-LGTP 290
Cdd:cd14147 155 DFGLAREWHK-TTQMSAAGTYAWMAPEVIKAST-FSKGSDVWSFGVLLWELLTGEVPYRGIDclAVAYGVAVNKLtLPIP 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42571361 291 TreeiRCMNPnytdfrFPQIKAHPWHKVFHKRmPpeaiDLASRLLQ 336
Cdd:cd14147 233 S----TCPEP------FAQLMADCWAQDPHRR-P----DFASILQQ 263
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
74-356 7.81e-18

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: 83.91  E-value: 7.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK-----KVLQDRR--YKNRELQLMRPMDHPNVISLkhcFFSTTSRDELFLnlVME 146
Cdd:cd05598   7 KTIGVGAFGEVSLVRKKDTNALYAMKtlrkkDVLKRNQvaHVKAERDILAEADNEWVVKL---YYSFQDKENLYF--VMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE-TLYRVLrhytssnQRMPIF---YVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFG------ 216
Cdd:cd05598  82 YIPGgDLMSLL-------IKKGIFeedLARFYIAELVCAIESVHKM-GFIHRDIKPDNILIDRDGH-IKLTDFGlctgfr 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 --------SAKVLVkGEPNisYIcsryyrAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGEnsvdqlveiikvlg 288
Cdd:cd05598 153 wthdskyyLAHSLV-GTPN--YI------APE-VLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQ-------------- 208
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 289 TPTREEIRCMNpNYTDFRFPQikahpwhkvfHKRMPPEAIDLASRLLQySPSLRC---TALEACAHPFFNE 356
Cdd:cd05598 209 TPAETQLKVIN-WRTTLKIPH----------EANLSPEAKDLILRLCC-DAEDRLgrnGADEIKAHPFFAG 267
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
74-354 7.87e-18

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: 83.61  E-value: 7.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAI--KKVLQ---------DRRYKNRELQLMRPMDHPNVISLkHCFFSTTSRdelfLN 142
Cdd:cd05584   2 KVLGKGGYGKVFQVRKTTGSDKGKIfaMKVLKkasivrnqkDTAHTKAERNILEAVKHPFIVDL-HYAFQTGGK----LY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVLrhytssnQRMPIFY---VKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSA 218
Cdd:cd05584  77 LILEYLSGgELFMHL-------EREGIFMedtACFYLAEITLALGHLHSL-GIIYRDLKPENILLDAQGH-VKLTDFGLC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEPNISYICSRY-YRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvdqlveiikvlgtptREEIRc 297
Cdd:cd05584 148 KESIHDGTVTHTFCGTIeYMAPE-ILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENR---------------KKTID- 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 298 mnpnytdfrfpqikahpwhKVFHKRM--PP----EAIDLASRLLQYSPSLRC-----TALEACAHPFF 354
Cdd:cd05584 211 -------------------KILKGKLnlPPyltnEARDLLKKLLKRNVSSRLgsgpgDAEEIKAHPFF 259
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
76-269 7.93e-18

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


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 82.77  E-value: 7.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVL----QDRRYKNRELQLMRPMDHPNVISLkhcFFSTTSRDELFlnLVMEYVPET 151
Cdd:cd06646  17 VGSGTYGDVYKARNLHTGELAAVKIIKlepgDDFSLIQQEIFMVKECKHCNIVAY---FGSYLSREKLW--ICMEYCGGG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 152 LYRVLRHYTSSNQRMPIFYVKLYTYQifrGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFG-SAKVLVKGEPNISY 230
Cdd:cd06646  92 SLQDIYHVTGPLSELQIAYVCRETLQ---GLAYLHS-KGKMHRDIKGANILLTD-NGDVKLADFGvAAKITATIAKRKSF 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42571361 231 ICSRYYRAPELifGATE----YTASIDIWSAGCVLAELLLGQP 269
Cdd:cd06646 167 IGTPYWMAPEV--AAVEknggYNQLCDIWAVGITAIELAELQP 207
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
71-354 9.39e-18

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: 82.17  E-value: 9.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  71 MAERVVGTGSFGIVFQAKCLETGESVAiKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYVPE 150
Cdd:cd14109   7 IGEEDEKRAAQGAPFHVTERSTGRNFL-AQLRYGDPFLMREVDIHNSLDHPNIVQMHDAY-----DDEKLAVTVIDNLAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDplTHQVKLCDFGSAKVLVKGEPNISY 230
Cdd:cd14109  81 TIELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDL-GIAHLDLRPEDILLQ--DDKLKLADFGQSRRLLRGKLTTLI 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 ICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIikvlgtptrEEIRCmnpnytdfrfpQI 310
Cdd:cd14109 158 YGSPEFVSPEIVNSYP-VTLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNV---------RSGKW-----------SF 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 42571361 311 KAHPWHKVFHkrmppEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14109 217 DSSPLGNISD-----DARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
71-342 9.51e-18

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: 83.17  E-value: 9.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  71 MAERVVGTGSFGIVfqAKCL--ETGESVAIKkVLQDRRYKN--RELQLMRPMD-HPNVISLKHCFfsttsRDELFLNLVM 145
Cdd:cd14179  10 LKDKPLGEGSFSIC--RKCLhkKTNQEYAVK-IVSKRMEANtqREIAALKLCEgHPNIVKLHEVY-----HDQLHTFLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVP--ETLYRVLRHYTSSNQRMPIFYVKLYTyqifrGLAYIHTVpGVCHRDVKPQNLLVDPLTH--QVKLCDFGSAKVL 221
Cdd:cd14179  82 ELLKggELLERIKKKQHFSETEASHIMRKLVS-----AVSHMHDV-GVVHRDLKPENLLFTDESDnsEIKIIDFGFARLK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYIC-SRYYRAPELiFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsvdqlveiiKVLGTPTREEIRcMNP 300
Cdd:cd14179 156 PPDNQPLKTPCfTLHYAAPEL-LNYNGYDESCDLWSLGVILYTMLSGQVPFQCHD---------KSLTCTSAEEIM-KKI 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42571361 301 NYTDFRFpqiKAHPWhkvfhKRMPPEAIDLASRLLQYSPSLR 342
Cdd:cd14179 225 KQGDFSF---EGEAW-----KNVSQEAKDLIQGLLTVDPNKR 258
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
74-357 1.06e-17

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: 83.13  E-value: 1.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNREL-------QLMRPMDHPNVISLKHCFfSTTSRdelfLNLVME 146
Cdd:cd05595   1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVahtvtesRVLQNTRHPFLTALKYAF-QTHDR----LCFVME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKG 224
Cdd:cd05595  76 YANggELFFHLSRERVFTEDR-----ARFYGAEIVSALEYLHS-RDVVYRDIKLENLMLDKDGH-IKITDFGLCKEGITD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKVlgtptrEEIrcmnpnyt 303
Cdd:cd05595 149 GATMKTFCgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-ERLFELILM------EEI-------- 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 304 dfRFPqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRC-----TALEACAHPFFNEL 357
Cdd:cd05595 213 --RFP------------RTLSPEAKSLLAGLLKKDPKQRLgggpsDAKEVMEHRFFLSI 257
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
62-365 1.09e-17

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: 82.78  E-value: 1.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  62 GEPKQTISYMAErvVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNRELQ-----LMRPMDHPNVISLkhcFFSTTSR 136
Cdd:cd06658  18 GDPREYLDSFIK--IGEGSTGIVCIATEKHTGKQVAVKK-MDLRKQQRRELLfnevvIMRDYHHENVVDM---YNSYLVG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 DELFLnlVMEYVPETLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFG 216
Cdd:cd06658  92 DELWV--VMEFLEGGALTDIVTHTRMNEEQ----IATVCLSVLRALSYLHN-QGVIHRDIKSDSILLTS-DGRIKLSDFG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 SAKVLVKGEPN-ISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGEnsvdqlveiikvlgtPTREEI 295
Cdd:cd06658 164 FCAQVSKEVPKrKSLVGTPYWMAPEVI-SRLPYGTEVDIWSLGIMVIEMIDGEPPYFNE---------------PPLQAM 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 296 RCMNPNYTdfrfPQIKAHpwHKVfhKRMPPEAIDLasrLLQYSPSLRCTALEACAHPFFNELREPNARLP 365
Cdd:cd06658 228 RRIRDNLP----PRVKDS--HKV--SSVLRGFLDL---MLVREPSQRATAQELLQHPFLKLAGPPSCIVP 286
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
77-356 1.14e-17

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: 82.48  E-value: 1.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKKV-------LQDRRYknrELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVP 149
Cdd:cd06611  14 GDGAFGKVYKAQHKETGLFAAAKIIqieseeeLEDFMV---EIDILSECKHPNIVGLYEAYFYENK-----LWILIEFCD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ----ETLYRVLRHYTSSNQrmpIFYVklyTYQIFRGLAYIHTvPGVCHRDVKPQNLLVdPLTHQVKLCDFG-SAKVLVKG 224
Cdd:cd06611  86 ggalDSIMLELERGLTEPQ---IRYV---CRQMLEALNFLHS-HKVIHRDLKAGNILL-TLDGDVKLADFGvSAKNKSTL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELI----FGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlGTPTREeircmNP 300
Cdd:cd06611 158 QKRDTFIGTPYWMAPEVVacetFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKS-EPPTLD-----QP 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 301 nytdfrfpqikaHPWHKVFHkrmppeaiDLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd06611 232 ------------SKWSSSFN--------DFLKSCLVKDPDDRPTAAELLKHPFVSD 267
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
74-354 1.20e-17

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: 83.06  E-value: 1.20e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK----KVLQDRRYKNR---ELQLMRPMDHPNVISLKHCFFSTTsrdelFLNLVME 146
Cdd:cd05574   7 KLLGKGDVGRVYLVRLKGTGKLFAMKvldkEEMIKRNKVKRvltEREILATLDHPFLPTLYASFQTST-----HLCFVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP-ETLYRVLRhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDF---------- 215
Cdd:cd05574  82 YCPgGELFRLLQ--KQPGKRLPEEVARFYAAEVLLALEYLHLL-GFVYRDLKPENILLHESGH-IMLTDFdlskqssvtp 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 216 ---------GSAKVLVKGEPNISYICSRYYR-----------APELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd05574 158 ppvrkslrkGSRRSSVKSIEKETFVAEPSARsnsfvgteeyiAPEVIKGDG-HGSAVDWWTLGILLYEMLYGTTPFKGSN 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 276 SVDQLVEIIKvlgtptreeircmnpnyTDFRFPQikahpwhkvfHKRMPPEAIDLASRLLQYSPSLRC----TALEACAH 351
Cdd:cd05574 237 RDETFSNILK-----------------KELTFPE----------SPPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRH 289

                ...
gi 42571361 352 PFF 354
Cdd:cd05574 290 PFF 292
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
76-354 1.27e-17

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: 83.36  E-value: 1.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQakCLE---TGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDEL----FLNLVMEYV 148
Cdd:cd14213  20 LGEGAFGKVVE--CIDhkmGGMHVAVKIVKNVDRYREAARSEIQVLEHLNTTDPNSTFRCVQMLEWFdhhgHVCIVFELL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHytSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV---------------DPLTHQ---V 210
Cdd:cd14213  98 GLSTYDFIKE--NSFLPFPIDHIRNMAYQICKSVNFLHH-NKLTHTDLKPENILFvqsdyvvkynpkmkrDERTLKnpdI 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 211 KLCDFGSAKVlvKGEPNISYICSRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTP 290
Cdd:cd14213 175 KVVDFGSATY--DDEHHSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHLAMMERILGPL 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 291 TREEI------RCMNPNYTDF-------RFPQIKAHPW------HKVFHKRMppeaIDLASRLLQYSPSLRCTALEACAH 351
Cdd:cd14213 252 PKHMIqktrkrKYFHHDQLDWdehssagRYVRRRCKPLkefmlsQDVDHEQL----FDLIQKMLEYDPAKRITLDEALKH 327

                ...
gi 42571361 352 PFF 354
Cdd:cd14213 328 PFF 330
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-353 1.37e-17

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: 82.51  E-value: 1.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIkKVLQDRRYKNRELQL-MRPMDHPNVISLKHCF-----FSTTSRDELFLNLVMEY 147
Cdd:cd14171  12 QKLGTGISGPVRVCVKKSTGERFAL-KILLDRPKARTEVRLhMMCSGHPNIVQIYDVYansvqFPGESSPRARLLIVMEL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VP--ETLYRVL--RHYTSSNQRMpifyvklYTYQIFRGLAYIHTVpGVCHRDVKPQNLLV--DPLTHQVKLCDFGSAKV- 220
Cdd:cd14171  91 MEggELFDRISqhRHFTEKQAAQ-------YTKQIALAVQHCHSL-NIAHRDLKPENLLLkdNSEDAPIKLCDFGFAKVd 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 ---LVKgePNIsyicSRYYRAPEL--------------IFGATEYT--ASIDIWSAGCVLAELLLGQPLFPGENSVDQLv 281
Cdd:cd14171 163 qgdLMT--PQF----TPYYVAPQVleaqrrhrkersgiPTSPTPYTydKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTI- 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 282 eiikvlgtPTREEIRCMNpnyTDFRFPQikaHPWhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14171 236 --------TKDMKRKIMT---GSYEFPE---EEW-----SQISEMAKDIVRKLLCVDPEERMTIEEVLHHPW 288
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
63-354 1.42e-17

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: 82.33  E-value: 1.42e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  63 EPKQTI----SYMAERVVGTGSfGIVFQAKCLE-TGESVAIKKVLQDRRYKNRELQLMRPM-DHPNVISLKHCFFSTTsr 136
Cdd:cd14181  13 DPKEVIgrgvSSVVRRCVHRHT-GQEFAVKIIEvTAERLSPEQLEEVRSSTLKEIHILRQVsGHPSIITLIDSYESST-- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 delFLNLVMEYVPE-TLYRVLRHYTSSNQRMpifyvklyTYQIFRGL----AYIHTVpGVCHRDVKPQNLLVDPLTHqVK 211
Cdd:cd14181  90 ---FIFLVFDLMRRgELFDYLTEKVTLSEKE--------TRSIMRSLleavSYLHAN-NIVHRDLKPENILLDDQLH-IK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 212 LCDFGSAKVLVKGEpNISYIC-SRYYRAPELIFGATE-----YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK 285
Cdd:cd14181 157 LSDFGFSCHLEPGE-KLRELCgTPGYLAPEILKCSMDethpgYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIME 235
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 286 vlgtptrEEIRCMNPNYTDfRFPQIKahpwhkvfhkrmppeaiDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14181 236 -------GRYQFSSPEWDD-RSSTVK-----------------DLISRLLVVDPEIRLTAEQALQHPFF 279
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
76-356 1.46e-17

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: 82.02  E-value: 1.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVL----QDRRYKNRELQLMRPMDHPNVISLkhcFFSTTSRDELFLNlvMEYVPET 151
Cdd:cd06645  19 IGSGTYGDVYKARNVNTGELAAIKVIKlepgEDFAVVQQEIIMMKDCKHSNIVAY---FGSYLRRDKLWIC--MEFCGGG 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 152 LYRVLRHYTSSNQRMPIFYVKLYTYQifrGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFG-SAKVLVKGEPNISY 230
Cdd:cd06645  94 SLQDIYHVTGPLSESQIAYVSRETLQ---GLYYLHS-KGKMHRDIKGANILLTDNGH-VKLADFGvSAQITATIAKRKSF 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 ICSRYYRAPELifGATE----YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircmnpnyTDFR 306
Cdd:cd06645 169 IGTPYWMAPEV--AAVErkggYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTK-----------------SNFQ 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 307 FPQIKAH-PWHKVFHKrmppeaidLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd06645 230 PPKLKDKmKWSNSFHH--------FVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
70-353 1.55e-17

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: 81.83  E-value: 1.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAI----KKVLQDRRYKNR---ELQLMRPMDHPNVISLKHCFfsttsRDELFLN 142
Cdd:cd14186   3 FKVLNLLGKGSFACVYRARSLHTGLEVAIkmidKKAMQKAGMVQRvrnEVEIHCQLKHPSILELYNYF-----EDSNYVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVLRH----YTSSNQRMpifyvklYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGS 217
Cdd:cd14186  78 LVLEMCHNgEMSRYLKNrkkpFTEDEARH-------FMHQIVTGMLYLHS-HGILHRDLTLSNLLLTRNMN-IKIADFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 218 AKVL-VKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIkvlgtptreeir 296
Cdd:cd14186 149 ATQLkMPHEKHFTMCGTPNYISPE-IATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVV------------ 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 cmnpnYTDFRFPqikAHpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14186 216 -----LADYEMP---AF---------LSREAQDLIHQLLRKNPADRLSLSSVLDHPF 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
70-283 1.66e-17

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: 81.49  E-value: 1.66e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN---RELQLMRPMDHPNVIslkhcFFSTTSRDELFLNLVME 146
Cdd:cd14108   4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKTsarRELALLAELDHKSIV-----RFHDAFEKRRVVIIVTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPET-LYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV-DPLTHQVKLCDFGSAKVLVKG 224
Cdd:cd14108  79 LCHEElLERITKRPTVCESE-----VRSYMRQLLEGIEYLHQ-NDVLHLDLKPENLLMaDQKTDQVRICDFGNAQELTPN 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 225 EPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEI 283
Cdd:cd14108 153 EPQYCKYGTPEFVAPE-IVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNI 210
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
76-265 1.90e-17

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: 81.77  E-value: 1.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFF-------------STTSRDELFLN 142
Cdd:cd14047  14 IGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVKALAKLDHPNIVRYNGCWDgfdydpetsssnsSRSKTKCLFIQ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 lvMEYVPE-TLYRVLRHyTSSNQRMPIFYVKLYtYQIFRGLAYIHTvPGVCHRDVKPQN-LLVDPLthQVKLCDFGSAKV 220
Cdd:cd14047  94 --MEFCEKgTLESWIEK-RNGEKLDKVLALEIF-EQITKGVEYIHS-KKLIHRDLKPSNiFLVDTG--KVKIGDFGLVTS 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 42571361 221 LVKGEPNISYICSRYYRAPELiFGATEYTASIDIWSAGCVLAELL 265
Cdd:cd14047 167 LKNDGKRTKSKGTLSYMSPEQ-ISSQDYGKEVDIYALGLILFELL 210
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
74-373 1.91e-17

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: 81.99  E-value: 1.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNR--------ELQLMRPMDHPNVISLKHCFfstTSRDELFLNLVM 145
Cdd:cd05630   6 RVLGKGGFGEVCACQVRATGKMYACKK-LEKKRIKKRkgeamalnEKQILEKVNSRFVVSLAYAY---ETKDALCLVLTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVlrhYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGE 225
Cdd:cd05630  82 MNGGDLKFHI---YHMGQAGFPEARAVFYAAEICCGLEDLHR-ERIVYRDLKPENILLDDHGH-IRISDLGLAVHVPEGQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFpgensvDQLVEIIKvlgtptREEIRCMnpnytdf 305
Cdd:cd05630 157 TIKGRVGTVGYMAPEVV-KNERYTFSPDWWALGCLLYEMIAGQSPF------QQRKKKIK------REEVERL------- 216
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 306 rfpqIKAHPwhKVFHKRMPPEAIDLASRLLQYSPSLR--C---TALEACAHPFFNELRepNARLPNGRPLPPL 373
Cdd:cd05630 217 ----VKEVP--EEYSEKFSPQARSLCSMLLCKDPAERlgCrggGAREVKEHPLFKKLN--FKRLGAGMLEPPF 281
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
70-364 1.91e-17

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: 82.00  E-value: 1.91e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVfqAKCLETGESV--AIKKVLQDRRYKNRELQ-LMRPMDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd14175   3 YVVKETIGVGSYSVC--KRCVHKATNMeyAVKVIDKSKRDPSEEIEiLLRYGQHPNIITLKDVY-----DDGKHVYLVTE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVLRHYTSSNQRMPIFyvkLYTyqIFRGLAYIHTvPGVCHRDVKPQNLLV-----DPltHQVKLCDFGSAK 219
Cdd:cd14175  76 LMRggELLDKILRQKFFSEREASSV---LHT--ICKTVEYLHS-QGVVHRDLKPSNILYvdesgNP--ESLRICDFGFAK 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKVLGTPtreeircm 298
Cdd:cd14175 148 QLRAENGLLMTPCyTANFVAPE-VLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPS-DTPEEILTRIGSG-------- 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 299 npnytdfRFpQIKAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELRE-PNARL 364
Cdd:cd14175 218 -------KF-TLSGGNWNTV-----SDAAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKlPQSQL 271
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
63-353 2.30e-17

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: 82.00  E-value: 2.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  63 EPKQTISYMAErvVGTGSFGIVFQAKCLETGeSVAIKKVLQDRRYKNR-----ELQLMRPMDHPNVISLKHCFFSTTSrd 137
Cdd:cd06644   9 DPNEVWEIIGE--LGDGAFGKVYKAKNKETG-ALAAAKVIETKSEEELedymvEIEILATCNHPYIVKLLGAFYWDGK-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 138 elfLNLVMEYVP-----ETLYRVLRHYTSSNqrmpifyVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDpLTHQVKL 212
Cdd:cd06644  84 ---LWIMIEFCPggavdAIMLELDRGLTEPQ-------IQVICRQMLEALQYLHSMK-IIHRDLKAGNVLLT-LDGDIKL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 213 CDFG-SAKVLVKGEPNISYICSRYYRAPELIFGAT----EYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK-- 285
Cdd:cd06644 152 ADFGvSAKNVKTLQRRDSFIGTPYWMAPEVVMCETmkdtPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKse 231
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 286 --VLGTPTReeircmnpnytdfrfpqikahpWHKVFHkrmppeaiDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd06644 232 ppTLSQPSK----------------------WSMEFR--------DFLKTALDKHPETRPSAAQLLEHPF 271
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
70-354 3.23e-17

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: 80.80  E-value: 3.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQD-------RRYKNRELQLMRPMDHPNVISLKHCFFSTTSRdelfLN 142
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSggpeefiQRFLPRELQIVERLDHKNIIHVYEMLESADGK----IY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLThqVKLCDFGSAKVLV 222
Cdd:cd14163  78 LVMELAEDG---DVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGC-GVAHRDLKCENALLQGFT--LKLTDFGFAKQLP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNIS--YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLlgqplfpgensvdqlveiikvlgtptreeirCMNP 300
Cdd:cd14163 152 KGGRELSqtFCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVML-------------------------------CAQL 200
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 301 NYTDFRFPQIKAHPWHKVF---HKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14163 201 PFDDTDIPKMLCQQQKGVSlpgHLGVSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
70-353 3.54e-17

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: 81.31  E-value: 3.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQ----DRRYKNRELQLM-RPMDHPNVISLKHcFFSTtsrDELFLnLV 144
Cdd:cd14090   4 KLTGELLGEGAYASVQTCINLYTGKEYAVKIIEKhpghSRSRVFREVETLhQCQGHPNILQLIE-YFED---DERFY-LV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 ME--YVPETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLL------VDPlthqVKLCDF- 215
Cdd:cd14090  79 FEkmRGGPLLSHIEKRVHFTEQE-----ASLVVRDIASALDFLHD-KGIAHRDLKPENILcesmdkVSP----VKICDFd 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 216 -GSAKVLVKGE------PNISYIC-SRYYRAPEL----IFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDqlvei 283
Cdd:cd14090 149 lGSGIKLSSTSmtpvttPELLTPVgSAEYMAPEVvdafVGEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGED----- 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 284 ikvLGTPTREEIR-CMNPNYT-----DFRFPQIKahpWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14090 224 ---CGWDRGEACQdCQELLFHsiqegEYEFPEKE---WSHI-----SAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
70-353 5.02e-17

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 80.67  E-value: 5.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFqaKCLET-GESVAIKKVLQ----DRRYKNRELQLMRPMDHPNVISLKHCFfstTSRDELFLnlV 144
Cdd:cd14104   2 YMIAEELGRGQFGIVH--RCVETsSKKTYMAKFVKvkgaDQVLVKKEISILNIARHRNILRLHESF---ESHEELVM--I 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLLVdpLTHQ---VKLCDFGSAK 219
Cdd:cd14104  75 FEFISgvDIFERITTARFELNEREIVSYVR----QVCEALEFLHS-KNIGHFDIRPENIIY--CTRRgsyIKIIEFGQSR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEP-NISYICSRYYrAPELIFGATEYTASiDIWSAGCVLAELLLGQPLFPGENSVDqlveiikvlgtpTREEIRCM 298
Cdd:cd14104 148 QLKPGDKfRLQYTSAEFY-APEVHQHESVSTAT-DMWSLGCLVYVLLSGINPFEAETNQQ------------TIENIRNA 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 299 NPNYTDFRFpqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14104 214 EYAFDDEAF-------------KNISIEALDFVDRLLVKERKSRMTAQEALNHPW 255
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
62-365 5.09e-17

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: 80.84  E-value: 5.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  62 GEPKQTISYMAErvVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNRELQ-----LMRPMDHPNVISLKHCFFSTtsr 136
Cdd:cd06657  16 GDPRTYLDNFIK--IGEGSTGIVCIATVKSSGKLVAVKK-MDLRKQQRRELLfnevvIMRDYQHENVVEMYNSYLVG--- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 DELFLnlVMEYVPETLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTH--QVKLCD 214
Cdd:cd06657  90 DELWV--VMEFLEGGALTDIVTHTRMNEEQ----IAAVCLAVLKALSVLHA-QGVIHRDIKSDSIL---LTHdgRVKLSD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 215 FGSAKVLVKGEPN-ISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGEnsvdqlveiikvlgtPTRE 293
Cdd:cd06657 160 FGFCAQVSKEVPRrKSLVGTPYWMAPELI-SRLPYGPEVDIWSLGIMVIEMVDGEPPYFNE---------------PPLK 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 294 EIRCMNPNYTdfrfPQIKAhpWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLP 365
Cdd:cd06657 224 AMKMIRDNLP----PKLKN--LHKV-----SPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPSCIVP 284
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
75-268 5.33e-17

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


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 80.03  E-value: 5.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAkcLETGESVAIKKVLQDRRYK--------NRELQLMRPMDHPNVISLKH-CFfsttsrDELFLNLVM 145
Cdd:cd14148   1 IIGVGGFGKVYKG--LWRGEEVAVKAARQDPDEDiavtaenvRQEARLFWMLQHPNIIALRGvCL------NPPHLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLrhytsSNQRMPIFYVKLYTYQIFRGLAYIHT---VPgVCHRDVKPQNLLV-------DPLTHQVKLCD 214
Cdd:cd14148  73 EYARGgALNRAL-----AGKKVPPHVLVNWAVQIARGMNYLHNeaiVP-IIHRDLKSSNILIlepiendDLSGKTLKITD 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 215 FGSAKVLVKgEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQ 268
Cdd:cd14148 147 FGLAREWHK-TTKMSAAGTYAWMAPEVI-RLSLFSKSSDVWSFGVLLWELLTGE 198
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
70-383 5.88e-17

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: 80.64  E-value: 5.88e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQ--DRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEY 147
Cdd:cd14085   5 FEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKtvDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTE-----ISLVLEL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VP--ETLYRVL-RHYTSsnQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLL-VDPLTHQ-VKLCDFGSAKVlV 222
Cdd:cd14085  80 VTggELFDRIVeKGYYS--ERDAADAVK----QILEAVAYLHE-NGIVHRDLKPENLLyATPAPDApLKIADFGLSKI-V 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYIC-SRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIkvlgtptreeIRCmnpn 301
Cdd:cd14085 152 DQQVTMKTVCgTPGYCAPEILRGCA-YGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKRI----------LNC---- 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 302 ytDFRFpqikAHPWhkvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNARLPNGRPLPPLFNFKQELG 381
Cdd:cd14085 217 --DYDF----VSPW----WDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWVTGKAANFAHMDTAQKKLQEFNARRKLK 286

                ..
gi 42571361 382 GA 383
Cdd:cd14085 287 AA 288
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
76-276 6.28e-17

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: 80.50  E-value: 6.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVlqdRRYKNRELQ---------LMRPMDHPNVISLKHCFFSTTSrdelfLNLVME 146
Cdd:cd06618  23 IGSGTCGQVYKMRHKKTGHVMAVKQM---RRSGNKEENkrilmdldvVLKSHDCPYIVKCYGYFITDSD-----VFICME 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHytsSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLVKGEP 226
Cdd:cd06618  95 LMSTCLDKLLKR---IQGPIPEDILGKMTVSIVKALHYLKEKHGVIHRDVKPSNILLD-ESGNVKLCDFGISGRLVDSKA 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 227 NI-SYICSRYYrAPELIFGAT--EYTASIDIWSAGCVLAELLLGQPLFPGENS 276
Cdd:cd06618 171 KTrSAGCAAYM-APERIDPPDnpKYDIRADVWSLGISLVELATGQFPYRNCKT 222
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
75-273 7.29e-17

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 79.74  E-value: 7.29e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAkcLETGESVAIKKVLQD------RRYKN--RELQLMRPMDHPNVISLKH-CFfsttsrDELFLNLVM 145
Cdd:cd14061   1 VIGVGGFGKVYRG--IWRGEEVAVKAARQDpdedisVTLENvrQEARLFWMLRHPNIIALRGvCL------QPPNLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVP-ETLYRVLrhytsSNQRMPIFYVKLYTYQIFRGLAYIHT---VPgVCHRDVKPQNLLV-------DPLTHQVKLCD 214
Cdd:cd14061  73 EYARgGALNRVL-----AGRKIPPHVLVDWAIQIARGMNYLHNeapVP-IIHRDLKSSNILIleaieneDLENKTLKITD 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 215 FGSAKVLVKgEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPG 273
Cdd:cd14061 147 FGLAREWHK-TTRMSAAGTYAWMAPEVIKSST-FSKASDVWSYGVLLWELLTGEVPYKG 203
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
62-364 7.57e-17

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 80.54  E-value: 7.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  62 GEPKQtiSYMAERVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKN---RELQLMRPMDHPNVISLKHCFFSTtsrD 137
Cdd:cd06656  15 GDPKK--KYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMnLQQQPKKEliiNEILVMRENKNPNIVNYLDSYLVG---D 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 138 ELFLnlVMEYVPE-TLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFG 216
Cdd:cd06656  90 ELWV--VMEYLAGgSLTDVVTETCMDEGQ-----IAAVCRECLQALDFLHS-NQVIHRDIKSDNILLG-MDGSVKLTDFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 -SAKVLVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVeIIKVLGTPTREei 295
Cdd:cd06656 161 fCAQITPEQSKRSTMVGTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALY-LIATNGTPELQ-- 236
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 296 rcmNPnytdfrfpqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFnELREPNARL 364
Cdd:cd06656 237 ---NP--------------------ERLSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL-KLAKPLSSL 281
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
70-278 8.84e-17

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 79.67  E-value: 8.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLE-TGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLkhcFFSTTSRDELFLnl 143
Cdd:cd14201   8 YSRKDLVGHGAFAVVFKGRHRKkTDWEVAIKSINKKNLSKSqillgKEIKILKELQHENIVAL---YDVQEMPNSVFL-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQ--------VKLCDF 215
Cdd:cd14201  83 VMEYCNGG---DLADYLQAKGTLSEDTIRVFLQQIAAAMRILHS-KGIIHRDLKPQNILLSYASRKkssvsgirIKIADF 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 216 GSAKVLVKGEPNISYICSRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVD 278
Cdd:cd14201 159 GFARYLQSNMMAATLCGSPMYMAPEVIM-SQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQD 220
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
76-265 9.89e-17

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 79.61  E-value: 9.89e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVL----QDRRYKNRELQLMRPMDHPNVISlkhcFFSTTSRDELfLNLVMEYVP-E 150
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGEVMVMKELIrfdeETQRTFLKEVKVMRCLEHPNVLK----FIGVLYKDKR-LNFITEYIKgG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSS---NQRMPifyvklYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPN 227
Cdd:cd14221  76 TLRGIIKSMDSHypwSQRVS------FAKDIASGMAYLHSM-NIIHRDLNSHNCLVRE-NKSVVVADFGLARLMVDEKTQ 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 228 ISYICSR---------------YYRAPELIFGATeYTASIDIWSAGCVLAELL 265
Cdd:cd14221 148 PEGLRSLkkpdrkkrytvvgnpYWMAPEMINGRS-YDEKVDVFSFGIVLCEII 199
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
62-305 1.02e-16

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: 80.15  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  62 GEPKQtiSYMAERVVGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYKN---RELQLMRPMDHPNVISLKHCFFSTtsrD 137
Cdd:cd06654  16 GDPKK--KYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMnLQQQPKKEliiNEILVMRENKNPNIVNYLDSYLVG---D 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 138 ELFLnlVMEYVPE-TLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFG 216
Cdd:cd06654  91 ELWV--VMEYLAGgSLTDVVTETCMDEGQ-----IAAVCRECLQALEFLHS-NQVIHRDIKSDNILLG-MDGSVKLTDFG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 -SAKVLVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVeIIKVLGTPTREEI 295
Cdd:cd06654 162 fCAQITPEQSKRSTMVGTPYWMAPEVV-TRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALY-LIATNGTPELQNP 239
                       250
                ....*....|
gi 42571361 296 RCMNPNYTDF 305
Cdd:cd06654 240 EKLSAIFRDF 249
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
73-265 1.08e-16

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: 79.63  E-value: 1.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVAIKKVL----QDRRYKNRELQLMRPM-DHPNVISLKHCFFSTTSRD--ELFlnLVM 145
Cdd:cd14037   8 EKYLAEGGFAHVYLVKTSNGGNRAALKRVYvndeHDLNVCKREIEIMKRLsGHKNIVGYIDSSANRSGNGvyEVL--LLM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EY-----VPETLYRVLRHYTSSNQRMPIFyvklytYQIFRGLAYIHTV-PGVCHRDVKPQNLLVDPLTHqVKLCDFGSA- 218
Cdd:cd14037  86 EYckgggVIDLMNQRLQTGLTESEILKIF------CDVCEAVAAMHYLkPPLIHRDLKVENVLISDSGN-YKLCDFGSAt 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 219 -KVL-VKGEPNISYI---CSRY----YRAPELI--FGATEYTASIDIWSAGCVLAELL 265
Cdd:cd14037 159 tKILpPQTKQGVTYVeedIKKYttlqYRAPEMIdlYRGKPITEKSDIWALGCLLYKLC 216
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
74-284 1.19e-16

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: 80.45  E-value: 1.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKcLETGESVAIKKVLQDRR-YKNRELQ--------LMRPMDHPNVISLkHCFFSTTSRdelfLNLV 144
Cdd:cd05602  13 KVIGKGSFGKVLLAR-HKSDEKFYAVKVLQKKAiLKKKEEKhimsernvLLKNVKHPFLVGL-HFSFQTTDK----LYFV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVkLCDFGSAKVLV 222
Cdd:cd05602  87 LDYINggELFYHLQRERCFLEPR-----ARFYAAEIASALGYLHSL-NIVYRDLKPENILLDSQGHIV-LTDFGLCKENI 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 223 KGEPNISYIC-SRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEII 284
Cdd:cd05602 160 EPNGTTSTFCgTPEYLAPEVLH-KQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNIL 221
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
73-353 1.37e-16

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: 79.71  E-value: 1.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVAIK----KVLQDRRYK-NRELQLMRPMDHPNVISLKHCFfstTSRDELFLNLVMEY 147
Cdd:cd14168  15 KEVLGTGAFSEVVLAEERATGKLFAVKcipkKALKGKESSiENEIAVLRKIKHENIVALEDIY---ESPNHLYLVMQLVS 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETLYRVLRH--YTSSNQRMPIfyvklytYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVK--LCDFGSAKVLVK 223
Cdd:cd14168  92 GGELFDRIVEKgfYTEKDASTLI-------RQVLDAVYYLHRM-GIVHRDLKPENLLYFSQDEESKimISDFGLSKMEGK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircmnpnyT 303
Cdd:cd14168 164 GDVMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILK-----------------A 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 42571361 304 DFRFpqiKAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14168 226 DYEF---DSPYWDDI-----SDSAKDFIRNLMEKDPNKRYTCEQALRHPW 267
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
75-275 1.40e-16

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: 80.13  E-value: 1.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIK-----KVLQD-----RRYKNRELQLMrpmDHPNVISLKHCFFSTTSRdelfLNLV 144
Cdd:cd05587   3 VLGKGSFGKVMLAERKGTDELYAIKilkkdVIIQDddvecTMVEKRVLALS---GKPPFLTQLHSCFQTMDR----LYFV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVlRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLV 222
Cdd:cd05587  76 MEYVNggDLMYHI-QQVGKFKEPVAVFYAA----EIAVGLFFLHS-KGIIYRDLKLDNVMLDAEGH-IKIADFGMCKEGI 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 223 KGEPNISYIC-SRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd05587 149 FGGKTTRTFCgTPDYIAPEIIA-YQPYGKSVDWWAYGVLLYEMLAGQPPFDGED 201
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
76-272 1.46e-16

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: 80.09  E-value: 1.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVPE 150
Cdd:cd06649  13 LGAGNGGVVTKVQHKPSGLIMARKLIHLEikpaiRNQIIRELQVLHECNSPYIVGFYGAFYSDGE-----ISICMEHMDG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 -TLYRVLRHytssNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNiS 229
Cdd:cd06649  88 gSLDQVLKE----AKRIPEEILGKVSIAVLRGLAYLREKHQIMHRDVKPSNILVNS-RGEIKLCDFGVSGQLIDSMAN-S 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42571361 230 YICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFP 272
Cdd:cd06649 162 FVGTRSYMSPERLQG-THYSVQSDIWSMGLSLVELAIGRYPIP 203
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
75-278 1.49e-16

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: 78.90  E-value: 1.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGE-SVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHcfFSTTSRDelfLNLVMEYV 148
Cdd:cd14202   9 LIGHGAFAVVFKGRHKEKHDlEVAVKCINKKNLAKSqtllgKEIKILKELKHENIVALYD--FQEIANS---VYLVMEYC 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV--------DPLTHQVKLCDFGSAKV 220
Cdd:cd14202  84 NGG---DLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHS-KGIIHRDLKPQNILLsysggrksNPNNIRIKIADFGFARY 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 221 LvKGEPNISYIC-SRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVD 278
Cdd:cd14202 160 L-QNNMMAATLCgSPMYMAPEVIM-SQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQD 216
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
75-273 1.65e-16

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 78.93  E-value: 1.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCleTGESVAIKKVLQDRRYK--------NRELQLMRPMDHPNVISLKH-CFfsttsrDELFLNLVM 145
Cdd:cd14146   1 IIGVGGFGKVYRATW--KGQEVAVKAARQDPDEDikataesvRQEAKLFSMLRHPNIIKLEGvCL------EEPNLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLRHYTSS-----NQRMPIFYVKLYTYQIFRGLAYIH---TVPgVCHRDVKPQN-LLVDPLTHQ------ 209
Cdd:cd14146  73 EFARGgTLNRALAAANAApgprrARRIPPHILVNWAVQIARGMLYLHeeaVVP-ILHRDLKSSNiLLLEKIEHDdicnkt 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 210 VKLCDFGSAKVLVKgEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPG 273
Cdd:cd14146 152 LKITDFGLAREWHR-TTKMSAAGTYAWMAPEVI-KSSLFSKGSDIWSYGVLLWELLTGEVPYRG 213
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
74-285 1.73e-16

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: 79.08  E-value: 1.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFqaKCLETGESVAIKKV-------LQDRRYK-NRELQLMRPMDHPNVISLKHCffsttSRDELFLNLVM 145
Cdd:cd14158  21 NKLGEGGFGVVF--KGYINDKNVAVKKLaamvdisTEDLTKQfEQEIQVMAKCQHENLVELLGY-----SCDGPQLCLVY 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETlyRVLRHYTSSNQRMPIFYVKL--YTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK 223
Cdd:cd14158  94 TYMPNG--SLLDRLACLNDTPPLSWHMRckIAQGTANGINYLHE-NNHIHRDIKSANILLDE-TFVPKISDFGLARASEK 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 224 GEPNI---SYICSRYYRAPELIFGatEYTASIDIWSAGCVLAELLLGQPLFpGENSVDQLVEIIK 285
Cdd:cd14158 170 FSQTImteRIVGTTAYMAPEALRG--EITPKSDIFSFGVVLLEIITGLPPV-DENRDPQLLLDIK 231
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
70-285 1.83e-16

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: 78.70  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEIniskmsPKEREESRKEVAVLSKMKHPNIVQYQESFEENGN-----LYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLrhytssNQRMPIFY----VKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLvdpLTHQ--VKLCDFG 216
Cdd:cd08218  77 VMDYCDGgDLYKRI------NAQRGVLFpedqILDWFVQLCLALKHVHDRK-ILHRDIKSQNIF---LTKDgiIKLGDFG 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 SAKVL-VKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK 285
Cdd:cd08218 147 IARVLnSTVELARTCIGTPYYLSPE-ICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIR 215
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
76-292 1.91e-16

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: 78.95  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVlqdrRYKNRELQLMR-PMDHPNVISLKHC-----FFSTTSRD-------ELfln 142
Cdd:cd06616  14 IGRGAFGTVNKMLHKPSGTIMAVKRI----RSTVDEKEQKRlLMDLDVVMRSSDCpyivkFYGALFREgdcwicmEL--- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 lvMEYVPETLYRVLrhYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLV 222
Cdd:cd06616  87 --MDISLDKFYKYV--YEVLDSVIPEEILGKIAVATVKALNYLKEELKIIHRDVKPSNILLD-RNGNIKLCDFGISGQLV 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 223 KGEPNISYICSRYYRAPELI--FGATE-YTASIDIWSAGCVLAELLLGQPLFPGENSV-DQLVEIIKvlGTPTR 292
Cdd:cd06616 162 DSIAKTRDAGCRPYMAPERIdpSASRDgYDVRSDVWSLGITLYEVATGKFPYPKWNSVfDQLTQVVK--GDPPI 233
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
76-267 1.94e-16

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: 79.19  E-value: 1.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR-----ELQLMRPMDHPNVISLKhcffSTTSRDELFLN----LVME 146
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKdrwchEIQIMKKLNHPNVVKAC----DVPEEMNFLVNdvplLAME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQV--KLCDFGSAKVLVKG 224
Cdd:cd14039  77 YCSGGDLRKLLNKPENCCGLKESQVLSLLSDIGSGIQYLHE-NKIIHRDLKPENIVLQEINGKIvhKIIDLGYAKDLDQG 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42571361 225 EPNISYICSRYYRAPELiFGATEYTASIDIWSAGCVLAELLLG 267
Cdd:cd14039 156 SLCTSFVGTLQYLAPEL-FENKSYTVTVDYWSFGTMVFECIAG 197
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
76-353 1.98e-16

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: 78.46  E-value: 1.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVfqAKCLE--TGESVAIK---KVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVPE 150
Cdd:cd14115   1 IGRGRFSIV--KKCLHkaTRKDVAVKfvsKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTS-----YILVLELMDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TlyRVLRHYTSSNQRMPIfYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVD---PlTHQVKLCDFGSAkVLVKGEPN 227
Cdd:cd14115  74 G--RLLDYLMNHDELMEE-KVAFYIRDIMEALQYLHNCR-VAHLDIKPENLLIDlriP-VPRVKLIDLEDA-VQISGHRH 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYICSR-YYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPGEnsvdqlveiikvlgtpTREEIrCMNPNYTDFR 306
Cdd:cd14115 148 VHHLLGNpEFAAPEVIQG-TPVSLATDIWSIGVLTYVMLSGVSPFLDE----------------SKEET-CINVCRVDFS 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42571361 307 FPqikahpwHKVFHKrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14115 210 FP-------DEYFGD-VSQAARDFINVILQEDPRRRPTAATCLQHPW 248
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
76-285 2.16e-16

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: 78.69  E-value: 2.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKcLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFFSTTSRdelflNLVMEYVPE 150
Cdd:cd14664   1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGdhgfqAEIQTLGMIRHRNIVRLRGYCSNPTTN-----LLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQrMPIFYVKLY--TYQIFRGLAYIH--TVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEP 226
Cdd:cd14664  75 GSLGELLHSRPESQ-PPLDWETRQriALGSARGLAYLHhdCSPLIIHRDVKSNNILLDE-EFEAHVADFGLAKLMDDKDS 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 227 NISYIC--SRYYRAPELIFG--ATEYTasiDIWSAGCVLAELLLGQPLFpGENSVDQLVEIIK 285
Cdd:cd14664 153 HVMSSVagSYGYIAPEYAYTgkVSEKS---DVYSYGVVLLELITGKRPF-DEAFLDDGVDIVD 211
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
74-265 2.66e-16

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: 78.79  E-value: 2.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIV----FQAKCLETGESVAIKKVLQDRRYKNR-----ELQLMRPMDHPNVISLKHCffsTTSRDELFLNLV 144
Cdd:cd05080  10 RDLGEGHFGKVslycYDPTNDGTGEMVAVKALKADCGPQHRsgwkqEIDILKTLYHENIVKYKGC---CSEQGGKSLQLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPetlYRVLRHYTSSNqRMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKG 224
Cdd:cd05080  87 MEYVP---LGSLRDYLPKH-SIGLAQLLLFAQQICEGMAYLHSQHYI-HRDLAARNVLLDN-DRLVKIGDFGLAKAVPEG 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 225 EpnisyicsRYYRAPE-----LIFGATE-------YTASiDIWSAGCVLAELL 265
Cdd:cd05080 161 H--------EYYRVREdgdspVFWYAPEclkeykfYYAS-DVWSFGVTLYELL 204
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
73-280 2.71e-16

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: 77.81  E-value: 2.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVAIKKVL------QDRRYKNRELQLMRPM-DHPNVISLkhcfFSTTSRDElFLNLVM 145
Cdd:cd13997   5 LEQIGSGSFSEVFKVRSKVDGCLYAVKKSKkpfrgpKERARALREVEAHAALgQHPNIVRY----YSSWEEGG-HLYIQM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EY--------VPETLYRVlrhytssnQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGS 217
Cdd:cd13997  80 ELcengslqdALEELSPI--------SKLSEAEVWDLLLQVALGLAFIHSK-GIVHLDIKPDNIFISN-KGTCKIGDFGL 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 218 AKVLVKGePNISYICSRYYrAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQL 280
Cdd:cd13997 150 ATRLETS-GDVEEGDSRYL-APELLNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQL 210
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
76-347 2.97e-16

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: 78.26  E-value: 2.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYVP 149
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLhsspncIEERKALLKEAEKMERARHSYVLPLLGVC-----VERRSLGLVMEYME 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVLRHYTSSNQRMPIFYVKLYtyQIFRGLAYIHTV-PGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEPNI 228
Cdd:cd13978  76 NGSLKSLLEREIQDVPWSLRFRIIH--EIALGMNFLHNMdPPLLHHDLKPENILLDNHFH-VKISDFGLSKLGMKSISAN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSR------YYRAPELI-FGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVdQLVEIIKVLGTptreeircmNPN 301
Cdd:cd13978 153 RRRGTEnlggtpIYMAPEAFdDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINP-LLIMQIVSKGD---------RPS 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42571361 302 YTDFRFPQikahpwhkvfHKRMPPEAIDLASRLLQYSPSLRCTALE 347
Cdd:cd13978 223 LDDIGRLK----------QIENVQELISLMIRCWDGNPDARPTFLE 258
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
70-356 3.10e-16

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 78.74  E-value: 3.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV----------LQDRRYKnRELQLMRPMDHPNVISLKHCFFSttsrdEL 139
Cdd:cd14094   5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVdvakftsspgLSTEDLK-REASICHMLKHPHIVELLETYSS-----DG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 FLNLVMEYVP------ETLYRVLRHYTSSNqrmpiFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQ--VK 211
Cdd:cd14094  79 MLYMVFEFMDgadlcfEIVKRADAGFVYSE-----AVASHYMRQILEALRYCHD-NNIIHRDVKPHCVLLASKENSapVK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 212 LCDFGSAKVLVKGEpniSYICSR----YYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGenSVDQLVEIIKVL 287
Cdd:cd14094 153 LGGFGVAIQLGESG---LVAGGRvgtpHFMAPEVV-KREPYGKPVDVWGCGVILFILLSGCLPFYG--TKERLFEGIIKG 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 288 GTPtreeircMNPnytdFRFPQIKAhpwhkvfhkrmppEAIDLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd14094 227 KYK-------MNP----RQWSHISE-------------SAKDLVRRMLMLDPAERITVYEALNHPWIKE 271
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
74-373 3.15e-16

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: 78.86  E-value: 3.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNR--------ELQLMRPMDHPNVISLKHCFfstTSRDELFLNLVM 145
Cdd:cd05632   8 RVLGKGGFGEVCACQVRATGKMYACKR-LEKKRIKKRkgesmalnEKQILEKVNSQFVVNLAYAY---ETKDALCLVLTI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVlrhYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGE 225
Cdd:cd05632  84 MNGGDLKFHI---YNMGNPGFEEERALFYAAEILCGLEDLHR-ENTVYRDLKPENILLDDYGH-IRISDLGLAVKIPEGE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENsvdqlvEIIKvlgtptREEIrcmnpnytDF 305
Cdd:cd05632 159 SIRGRVGTVGYMAPEVL-NNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRK------EKVK------REEV--------DR 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 306 RFPQIKahpwhKVFHKRMPPEAIDLASRLLQYSPSLR--CT---ALEACAHPFFNELRepNARLPNGRPLPPL 373
Cdd:cd05632 218 RVLETE-----EVYSAKFSEEAKSICKMLLTKDPKQRlgCQeegAGEVKRHPFFRNMN--FKRLEAGMLDPPF 283
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
76-265 3.98e-16

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 77.93  E-value: 3.98e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQ--DRRYKN--RELQLMRPMDHPNVISlkhcFFSTTSRDELfLNLVMEYVP-E 150
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGEVMVMKELIRfdEEAQRNflKEVKVMRSLDHPNVLK----FIGVLYKDKK-LNLITEYIPgG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLV---KGEPN 227
Cdd:cd14154  76 TLKDVLK---DMARPLPWAQRVRFAKDIASGMAYLHSM-NIIHRDLNSHNCLVR-EDKTVVVADFGLARLIVeerLPSGN 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 228 ISYICSR------------------YYRAPELIFGaTEYTASIDIWSAGCVLAELL 265
Cdd:cd14154 151 MSPSETLrhlkspdrkkrytvvgnpYWMAPEMLNG-RSYDEKVDIFSFGIVLCEII 205
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
64-353 4.12e-16

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: 77.57  E-value: 4.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMAErvVGTGSFGIVFQA--KCLETGESVAIK--KVLQDRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDEL 139
Cdd:cd14112   1 PTGRFSFGSE--IFRGRFSVIVKAvdSTTETDAHCAVKifEVSDEASEAVREFESLRTLQHENVQRLIAAF-----KPSN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 FLNLVMEYVPETL--YRVLRHYTSSNQrmpifyVKLYTYQIFRGLAYIHtVPGVCHRDVKPQN-LLVDPLTHQVKLCDFG 216
Cdd:cd14112  74 FAYLVMEKLQEDVftRFSSNDYYSEEQ------VATTVRQILDALHYLH-FKGIAHLDVQPDNiMFQSVRSWQVKLVDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 SAKVlVKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvdqlveiikvlgtpTREEIR 296
Cdd:cd14112 147 RAQK-VSKLGKVPVDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFTSEYD--------------DEEETK 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 cMNPNYTDFRFPQIkahpwhkvfHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14112 212 -ENVIFVKCRPNLI---------FVEATQEALRFATWALKKSPTRRMRTDEALEHRW 258
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
76-347 4.71e-16

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 77.36  E-value: 4.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDR-RYKN--RELQLMRPM-DHPNVISLKHCFFSTTSrdelFLNLVMEYVPet 151
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPStKLKDflREYNISLELsVHPHIIKTYDVAFETED----YYVFAQEYAP-- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 152 lYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQN-LLVDPLTHQVKLCDFG---SAKVLVKgepN 227
Cdd:cd13987  75 -YGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHS-KNLVHRDIKPENvLLFDKDCRRVKLCDFGltrRVGSTVK---R 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISYICSryYRAPEL--IFGATEYTA--SIDIWSAGCVLAELLLGQplFPGENSVDqlveiikvlgtptreeircMNPNYT 303
Cdd:cd13987 150 VSGTIP--YTAPEVceAKKNEGFVVdpSIDVWAFGVLLFCCLTGN--FPWEKADS-------------------DDQFYE 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42571361 304 DF-RFPQIKAHPWHKVFhKRMPPEAIDLASRLLQYSPSLRCTALE 347
Cdd:cd13987 207 EFvRWQKRKNTAVPSQW-RRFTPKALRMFKKLLAPEPERRCSIKE 250
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
70-356 4.73e-16

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: 77.73  E-value: 4.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDR-RYK----NRELQLMRPMDHPNVISLKHcffSTTSRDELFLnlV 144
Cdd:cd14183   8 YKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKcRGKehmiQNEVSILRRVKHPNIVLLIE---EMDMPTELYL--V 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLrhyTSSNQrmpifyvklYT--------YQIFRGLAYIHTVpGVCHRDVKPQNLLVdpLTHQ-----V 210
Cdd:cd14183  83 MELVKGgDLFDAI---TSTNK---------YTerdasgmlYNLASAIKYLHSL-NIVHRDIKPENLLV--YEHQdgsksL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 211 KLCDFGSAKVlVKGePNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKVLgtp 290
Cdd:cd14183 148 KLGDFGLATV-VDG-PLYTVCGTPTYVAPEII-AETGYGLKVDIWAAGVITYILLCGFPPFRGSGD-DQEVLFDQIL--- 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 291 treeircmnPNYTDFRFPQikahpWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd14183 221 ---------MGQVDFPSPY-----WDNV-----SDSAKELITMMLQVDVDQRYSALQVLEHPWVND 267
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
75-284 5.09e-16

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: 78.50  E-value: 5.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ--------LMRPMDHPNVISLKHCFfstTSRDELFLnlVME 146
Cdd:cd05616   7 VLGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVEctmvekrvLALSGKPPFLTQLHSCF---QTMDRLYF--VME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVlrhytssnQRMPIF---YVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV- 220
Cdd:cd05616  82 YVNggDLMYHI--------QQVGRFkepHAVFYAAEIAIGLFFLQS-KGIIYRDLKLDNVMLDSEGH-IKIADFGMCKEn 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 221 LVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEII 284
Cdd:cd05616 152 IWDGVTTKTFCGTPDYIAPEII-AYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDE-DELFQSI 213
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
74-372 5.10e-16

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: 77.64  E-value: 5.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNR--------ELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVM 145
Cdd:cd05607   8 RVLGKGGFGEVCAVQVKNTGQMYACKK-LDKKRLKKKsgekmallEKEILEKVNSPFIVSLAYAFETKTH-----LCLVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVP--ETLYRVlrhYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLThQVKLCDFGSAKVLVK 223
Cdd:cd05607  82 SLMNggDLKYHI---YNVGERGIEMERVIFYSAQITCGILHLHSL-KIVYRDMKPENVLLDDNG-NCRLSDLGLAVEVKE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFpgeNSVDQLVEIIKVLGTPTREEIRCMNPNYT 303
Cdd:cd05607 157 GKPITQRAGTNGYMAPE-ILKEESYSYPVDWFAMGCSIYEMVAGRTPF---RDHKEKVSKEELKRRTLEDEVKFEHQNFT 232
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 304 DfrfpqiKAHPWHKVFHKRMPPEAidLASRLLQYSPSlrctaleacAHPFFNELREPnaRLPNGRPLPP 372
Cdd:cd05607 233 E------EAKDICRLFLAKKPENR--LGSRTNDDDPR---------KHEFFKSINFP--RLEAGLIDPP 282
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
74-354 5.16e-16

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: 78.92  E-value: 5.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQD----------RRYKNRELQLMRpmdHPNVISLKHCFfSTTSRdelfLNL 143
Cdd:cd05594  31 KLLGKGTFGKVILVKEKATGRYYAMKILKKEvivakdevahTLTENRVLQNSR---HPFLTALKYSF-QTHDR----LCF 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVL 221
Cdd:cd05594 103 VMEYANggELFFHLSRERVFSEDR-----ARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGH-IKITDFGLCKEG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKVlgtptrEEIRcmnp 300
Cdd:cd05594 177 IKDGATMKTFCgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELILM------EEIR---- 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 301 nytdfrfpqikahpwhkvFHKRMPPEAIDLASRLLQYSPSLRC-----TALEACAHPFF 354
Cdd:cd05594 245 ------------------FPRTLSPEAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKFF 285
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
70-353 5.75e-16

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: 77.62  E-value: 5.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK----KVLQDRRYK-NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLV 144
Cdd:cd14169   5 YELKEKLGEGAFSEVVLAQERGSQRLVALKcipkKALRGKEAMvENEIAVLRRINHENIVSLEDIYESPTH-----LYLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP--ETLYRVLR--HYTSSNQRMPIfyvklytYQIFRGLAYIHTVpGVCHRDVKPQNLLVD-PLT-HQVKLCDFGSA 218
Cdd:cd14169  80 MELVTggELFDRIIErgSYTEKDASQLI-------GQVLQAVKYLHQL-GIVHRDLKPENLLYAtPFEdSKIMISDFGLS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEpnISYIC-SRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreEIRC 297
Cdd:cd14169 152 KIEAQGM--LSTACgTPGYVAPELLEQKP-YGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKA-------EYEF 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 298 MNPNYTDfrfpqikahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14169 222 DSPYWDD------------------ISESAKDFIRHLLERDPEKRFTCEQALQHPW 259
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
76-270 5.82e-16

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: 77.55  E-value: 5.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVL------QDRRYKNRELQLMRPMDHPNVISLKHCFfsttsrdelflnlvMEYVP 149
Cdd:cd14049  14 LGKGGYGKVYKVRNKLDGQYYAIKKILikkvtkRDCMKVLREVKVLAGLQHPNIVGYHTAW--------------MEHVQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLY-------RVLRHYTSSNQRMPIFYVK---LYTY-----------QIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTH 208
Cdd:cd14049  80 LMLYiqmqlceLSLWDWIVERNKRPCEEEFksaPYTPvdvdvttkilqQLLEGVTYIHSM-GIVHRDLKPRNIFLHGSDI 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 209 QVKLCDFGSAKVLVKGEPNISYICSRY-------------YRAPELIFGaTEYTASIDIWSAGCVLAELLlgQPL 270
Cdd:cd14049 159 HVRIGDFGLACPDILQDGNDSTTMSRLnglthtsgvgtclYAAPEQLEG-SHYDFKSDMYSIGVILLELF--QPF 230
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
74-357 6.13e-16

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: 77.73  E-value: 6.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCL---ETGESVAIK-----------KVLQDRRYKNRELQLMRpmDHPNVISLKHCFFSTTSrdel 139
Cdd:cd05613   6 KVLGTGAYGKVFLVRKVsghDAGKLYAMKvlkkativqkaKTAEHTRTERQVLEHIR--QSPFLVTLHYAFQTDTK---- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 fLNLVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVkLCDFGSAK 219
Cdd:cd05613  80 -LHLILDYINGG---ELFTHLSQRERFTENEVQIYIGEIVLALEHLHKL-GIIYRDIKLENILLDSSGHVV-LTDFGLSK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEPNISY-ICSRY-YRAPELIFGA-TEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLgtptreeir 296
Cdd:cd05613 154 EFLLDENERAYsFCGTIeYMAPEIVRGGdSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKNSQAEISRRI--------- 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 297 cmnpnytdfrfpqIKAHPwhkVFHKRMPPEAIDLASRLLQYSPSLRC-----TALEACAHPFFNEL 357
Cdd:cd05613 225 -------------LKSEP---PYPQEMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQKI 274
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
70-271 6.60e-16

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: 77.29  E-value: 6.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKcleTGESVAIKKVL--QD-----RRYKNR-ELQLMRPMDHPNVISLKHcfFSTTSRdelFL 141
Cdd:cd13980   2 YLYDKSLGSTRFLKVARAR---HDEGLVVVKVFvkPDpalplRSYKQRlEEIRDRLLELPNVLPFQK--VIETDK---AA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPETLY-RV-LRHYTSSNQRmpifyvKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAK 219
Cdd:cd13980  74 YLIRQYVKYNLYdRIsTRPFLNLIEK------KWIAFQLLHALNQCHKR-GVCHGDIKTENVLVTS-WNWVYLTDFASFK 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 220 VLVKGEPN---ISY--------ICsryYRAPELIFGATEY-----------TASIDIWSAGCVLAELLL-GQPLF 271
Cdd:cd13980 146 PTYLPEDNpadFSYffdtsrrrTC---YIAPERFVDALTLdaeserrdgelTPAMDIFSLGCVIAELFTeGRPLF 217
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
76-280 7.02e-16

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: 76.99  E-value: 7.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIK---KVLQD---RRYKNRELQLMRPMDHPNVISLKHCfFSTTSRdelfLNLVMEYVP 149
Cdd:cd14075  10 LGSGNFSQVKLGIHQLTKEKVAIKildKTKLDqktQRLLSREISSMEKLHHPNIIRLYEV-VETLSK----LHLVMEYAS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYrvlrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEPNI 228
Cdd:cd14075  85 GgELY----TKISTEGKLSESEAKPLFAQIVSAVKHMHEN-NIIHRDLKAENVFYASNNC-VKVGDFGFSTHAKRGETLN 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 229 SYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQL 280
Cdd:cd14075 159 TFCGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAET-VAKL 209
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
76-305 7.46e-16

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: 77.37  E-value: 7.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGeSVAIKKVLQDRRYKNR-----ELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEY--- 147
Cdd:cd06643  13 LGDGAFGKVYKAQNKETG-ILAAAKVIDTKSEEELedymvEIDILASCDHPNIVKLLDAFYYENN-----LWILIEFcag 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 --VPETLYRVLRHYTSSNqrmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFG-SAKVLVKG 224
Cdd:cd06643  87 gaVDAVMLELERPLTEPQ-------IRVVCKQTLEALVYLHE-NKIIHRDLKAGNILFT-LDGDIKLADFGvSAKNTRTL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELIFGATE----YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIK----VLGTPTReeir 296
Cdd:cd06643 158 QRRDSFIGTPYWMAPEVVMCETSkdrpYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKseppTLAQPSR---- 233

                ....*....
gi 42571361 297 cMNPNYTDF 305
Cdd:cd06643 234 -WSPEFKDF 241
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
69-315 7.59e-16

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: 77.14  E-value: 7.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIV-----FQAKCLETGESVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHcfFSTTSR 136
Cdd:cd14076   2 PYILGRTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRDTQQENcqtskimREINILKGLTHPNIVRLLD--VLKTKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 137 delFLNLVMEYVP--ETLYRVLRH-YTSSNQRMPIFYvklytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLC 213
Cdd:cd14076  80 ---YIGIVLEFVSggELFDYILARrRLKDSVACRLFA------QLISGVAYLHK-KGVVHRDLKLENLLLDK-NRNLVIT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 214 DFGSAKVLVKGEPNI-SYIC-SRYYRAPELIFGATEYTAS-IDIWSAGCVLAELLLG------QPLFPGENSVDQLV--- 281
Cdd:cd14076 149 DFGFANTFDHFNGDLmSTSCgSPCYAAPELVVSDSMYAGRkADIWSCGVILYAMLAGylpfddDPHNPNGDNVPRLYryi 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 42571361 282 --------EIIKVLGTPTREEIRCMNPNYTdFRFPQIKAHPW 315
Cdd:cd14076 229 cntplifpEYVTPKARDLLRRILVPNPRKR-IRLSAIMRHAW 269
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
69-354 8.78e-16

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: 76.94  E-value: 8.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAErvVGTGSFGIVfqAKCLETG--ESVAIK---KVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNL 143
Cdd:cd14113  10 SEVAE--LGRGRFSVV--KKCDQRGtkRAVATKfvnKKLMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTS-----YIL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETlyRVLrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVD--PLTHQVKLCDFGSAKVL 221
Cdd:cd14113  81 VLEMADQG--RLL-DYVVRWGNLTEEKIRFYLREILEALQYLHNCR-IAHLDLKPENILVDqsLSKPTIKLADFGDAVQL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 vkgepNISY-----ICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFpgensVDQLVEIIkvlgtptreeir 296
Cdd:cd14113 157 -----NTTYyihqlLGSPEFAAPEIILG-NPVSLTSDLWSIGVLTYVLLSGVSPF-----LDESVEET------------ 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 297 CMNPNYTDFRFPQIkahpwhkvFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14113 214 CLNICRLDFSFPDD--------YFKGVSQKAKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
76-354 9.75e-16

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 76.47  E-value: 9.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQ----DRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYVP-- 149
Cdd:cd14114  10 LGTGAFGVVHRCTERATGNNFAAKFIMTphesDKETVRKEIQIMNQLHHPKLINLHDAF-----EDDNEMVLILEFLSgg 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVlrhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPL-THQVKLCDFGSAKVLVKGEPNI 228
Cdd:cd14114  85 ELFERI----AAEHYKMSEAEVINYMRQVCEGLCHMHE-NNIVHLDIKPENIMCTTKrSNEVKLIDFGLATHLDPKESVK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSRYYRAPELIFGATE--YTasiDIWSAGCVLAELLLGQPLFPGENSvDQLVEIIKvlgtptreeiRCmNPNYTDFR 306
Cdd:cd14114 160 VTTGTAEFAAPEIVEREPVgfYT---DMWAVGVLSYVLLSGLSPFAGEND-DETLRNVK----------SC-DWNFDDSA 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 307 FPQIKahpwhkvfhkrmpPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14114 225 FSGIS-------------EEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
75-362 1.35e-15

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 76.46  E-value: 1.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISLKHCFFSttsrdELFLNLVMEYVP 149
Cdd:cd06619   8 ILGHGNGGTVYKAYHLLTRRILAVKVIPLDitvelQKQIMSELEILYKCDSPYIIGFYGAFFV-----ENRISICTEFMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVLRhytssnqRMPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNiS 229
Cdd:cd06619  83 GGSLDVYR-------KIPEHVLGRIAVAVVKGLTYLWSLK-ILHRDVKPSNMLVNT-RGQVKLCDFGVSTQLVNSIAK-T 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 230 YICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPgensvdqlvEIIKVLGTPTREEI-RCMnpnyTDFRFP 308
Cdd:cd06619 153 YVGTNAYMAPERISG-EQYGIHSDVWSLGISFMELALGRFPYP---------QIQKNQGSLMPLQLlQCI----VDEDPP 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 309 QIKAHPWHKVFhkrmppeaIDLASRLLQYSPSLRCTALEACAHPFFNELREPNA 362
Cdd:cd06619 219 VLPVGQFSEKF--------VHFITQCMRKQPKERPAPENLMDHPFIVQYNDGNA 264
PTZ00284 PTZ00284
protein kinase; Provisional
75-372 1.46e-15

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 78.08  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   75 VVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR---ELQLMR------PMDHPNVISLKHCFFSTTSRdelfLNLVM 145
Cdd:PTZ00284 136 LLGEGTFGKVVEAWDRKRKEYCAVKIVRNVPKYTRDakiEIQFMEkvrqadPADRFPLMKIQRYFQNETGH----MCIVM 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  146 -EYVPETLYRVLRHYTSSNQrmpifYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLL-------VDPLTHQ-------- 209
Cdd:PTZ00284 212 pKYGPCLLDWIMKHGPFSHR-----HLAQIIFQTGVALDYFHTELHLMHTDLKPENILmetsdtvVDPVTNRalppdpcr 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  210 VKLCDFGSAkvLVKGEPNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGT 289
Cdd:PTZ00284 287 VRICDLGGC--CDERHSRTAIVSTRHYRSPEVVLGLG-WMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLMEKTLGR 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  290 -PTREEIRCMNPN----YTDFRFPQIKAHPWH--KVFHKRMPPEAI------DLASRLLQYSPSLRCTALEACAHP---- 352
Cdd:PTZ00284 364 lPSEWAGRCGTEEarllYNSAGQLRPCTDPKHlaRIARARPVREVIrddllcDLIYGLLHYDRQKRLNARQMTTHPyvlk 443
                        330       340
                 ....*....|....*....|..
gi 42571361  353 FFNELRE-PNArlPNGRP-LPP 372
Cdd:PTZ00284 444 YYPECRQhPNY--PDNRSmLRP 463
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
67-354 1.81e-15

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: 75.73  E-value: 1.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  67 TISYMAERVVGTGSFGIVfqAKCLE--TGESVAiKKVLQDRRYKNR-----ELQLMRPMDHPNVISLKHCFfsTTSRDel 139
Cdd:cd14190   3 TFSIHSKEVLGGGKFGKV--HTCTEkrTGLKLA-AKVINKQNSKDKemvllEIQVMNQLNHRNLIQLYEAI--ETPNE-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 fLNLVMEYVP--ETLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVPgVCHRDVKPQN-LLVDPLTHQVKLCDFG 216
Cdd:cd14190  76 -IVLFMEYVEggELFERIVDEDYHLTEVDAMVFVR----QICEGIQFMHQMR-VLHLDLKPENiLCVNRTGHQVKIIDFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 SAKVLVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvdqlveiikvlgTPTREEIR 296
Cdd:cd14190 150 LARRYNPREKLKVNFGTPEFLSPEVV-NYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDD------------TETLNNVL 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 297 CMNPNYTDFRFPQIKAhpwhkvfhkrmppEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14190 217 MGNWYFDEETFEHVSD-------------EAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
76-353 1.89e-15

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: 75.83  E-value: 1.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAiKKVLQDRRYKN-----------RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLV 144
Cdd:cd14194  13 LGSGQFAVVKKCREKSTGLQYA-AKFIKKRRTKSsrrgvsredieREVSILKEIQHPNVITLHEVYENKTD-----VILI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVPgVCHRDVKPQNLLV---DPLTHQVKLCDFGSAKV 220
Cdd:cd14194  87 LELVAGgELFDFLAEKESLTEEEATEFLK----QILNGVYYLHSLQ-IAHFDLKPENIMLldrNVPKPRIKIIDFGLAHK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeircmnp 300
Cdd:cd14194 162 IDFGNEFKNIFGTPEFVAPEIV-NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAV-------------- 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 301 nytDFRFPQikahpwhkVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14194 227 ---NYEFED--------EYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPW 268
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
74-357 1.96e-15

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 77.36  E-value: 1.96e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNR--------ELQLMRPMDHPNVISLkhcFFSTTSRDELFLnlVM 145
Cdd:cd05626   7 KTLGIGAFGEVCLACKVDTHALYAMK-TLRKKDVLNRnqvahvkaERDILAEADNEWVVKL---YYSFQDKDNLYF--VM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIfrglAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFG-------- 216
Cdd:cd05626  81 DYIPGgDMMSLLIRMEVFPEVLARFYIAELTLAI----ESVHKM-GFIHRDIKPDNILID-LDGHIKLTDFGlctgfrwt 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 -SAKVLVKG--------EPNI-------------------------------SYICSRYYRAPELIFgATEYTASIDIWS 256
Cdd:cd05626 155 hNSKYYQKGshirqdsmEPSDlwddvsncrcgdrlktleqratkqhqrclahSLVGTPNYIAPEVLL-RKGYTQLCDWWS 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 257 AGCVLAELLLGQPLFpgensvdqlveiikVLGTPTREEIRCMNPNYTDFRFPQIKahpwhkvfhkrMPPEAIDLASRLLQ 336
Cdd:cd05626 234 VGVILFEMLVGQPPF--------------LAPTPTETQLKVINWENTLHIPPQVK-----------LSPEAVDLITKLCC 288
                       330       340
                ....*....|....*....|...
gi 42571361 337 YSPSL--RCTALEACAHPFFNEL 357
Cdd:cd05626 289 SAEERlgRNGADDIKAHPFFSEV 311
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
76-325 2.04e-15

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: 76.84  E-value: 2.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRE----------LQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVM 145
Cdd:cd05586   1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEvahtigerniLVRTALDESPFIVGLKFSFQTPTD-----LYLVT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK 223
Cdd:cd05586  76 DYMSggELFWHLQKEGRFSEDR-----AKFYIAELVLALEHLHK-NDIVYRDLKPENILLDANGH-IALCDFGLSKADLT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYIC-SRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsVDQLVEII---------KVLGTPTRE 293
Cdd:cd05586 149 DNKTTNTFCgTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAED-TQQMYRNIafgkvrfpkDVLSDEGRS 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42571361 294 EIRCM---NPNY-----TDFRfpQIKAHP------WHKVFHKRMPP 325
Cdd:cd05586 228 FVKGLlnrNPKHrlgahDDAV--ELKEHPffadidWDLLSKKKITP 271
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
74-325 2.18e-15

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: 76.29  E-value: 2.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCL---ETGESVAIK-------KVlQDRRYKNRELQLMRPMDHPNVISLkHCFFSTTSRdelfLNL 143
Cdd:cd05582   1 KVLGQGSFGKVFLVRKItgpDAGTLYAMKvlkkatlKV-RDRVRTKMERDILADVNHPFIVKL-HYAFQTEGK----LYL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVL 221
Cdd:cd05582  75 ILDFLRggDLFTRLSKEVMFTEED-----VKFYLAELALALDHLHSL-GIIYRDLKPENILLDEDGH-IKLTDFGLSKES 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYIC-SRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKV-LGTP---TREE-- 294
Cdd:cd05582 148 IDHEKKAYSFCgTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAkLGMPqflSPEAqs 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 42571361 295 -IRCM---NPN----YTDFRFPQIKAHP------WHKVFHKRMPP 325
Cdd:cd05582 227 lLRALfkrNPAnrlgAGPDGVEEIKRHPffatidWNKLYRKEIKP 271
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
70-353 2.22e-15

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: 75.54  E-value: 2.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVF---QAKCLETGESVAIKKV----LQ--DRRYKNRELQLMRPMDHPNVISLKHCFFSttsrDELF 140
Cdd:cd08222   2 YRVVRKLGSGNFGTVYlvsDLKATADEELKVLKEIsvgeLQpdETVDANREAKLLSKLDHPAIVKFHDSFVE----KESF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LnLVMEYVP-ETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDplTHQVKLCDFGSAK 219
Cdd:cd08222  78 C-IVTEYCEgGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMH-ERRILHRDLKAKNIFLK--NNVIKVGDFGISR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVkGEPNI--SYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIkvlgtptreeirc 297
Cdd:cd08222 154 ILM-GTSDLatTFTGTPYYMSPEVLKHEG-YNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIV------------- 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 298 mnpnytDFRFPQIKAHpwhkvFHKrmppEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd08222 219 ------EGETPSLPDK-----YSK----ELNAIYSRMLNKDPALRPSAAEILKIPF 259
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
5-272 2.32e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 76.79  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    5 PLGPQPHALAPPLQLHDGDA-LKRRPELD---SDKEMSAAV---IEGNDAVTGHIISTTIGGKNGEPKQTISYMaERV-- 75
Cdd:PLN00034   3 PIQPPPGVPLPSTARHTTKSrPRRRPDLTlplPQRDPSLAVplpLPPPSSSSSSSSSSSASGSAPSAAKSLSEL-ERVnr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   76 VGTGSFGIVFQAKCLETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISLkHCFFSTTSRDELFLNLVMEYVPE 150
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNhedtvRRQICREIEILRDVNHPNVVKC-HDMFDHNGEIQVLLEFMDGGSLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  151 TLYRVLRHYTSSNQRmpifyvklytyQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKG-EPNIS 229
Cdd:PLN00034 161 GTHIADEQFLADVAR-----------QILSGIAYLHRRHIV-HRDIKPSNLLINS-AKNVKIADFGVSRILAQTmDPCNS 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 42571361  230 YICSRYYRAPELI-----FGATEYTASiDIWSAGCVLAELLLGQplFP 272
Cdd:PLN00034 228 SVGTIAYMSPERIntdlnHGAYDGYAG-DIWSLGVSILEFYLGR--FP 272
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
77-298 2.43e-15

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: 75.73  E-value: 2.43e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCleTGESVAIKkVLQDRRYKNR--------------------------ELQLMRPMDHPNVISLKHCF 130
Cdd:cd14000   3 GDGGFGSVYRASY--KGEPVAVK-IFNKHTSSNFanvpadtmlrhlratdamknfrllrqELTVLSHLHHPSIVYLLGIG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 131 FSTtsrdelfLNLVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV---DPL 206
Cdd:cd14000  80 IHP-------LMLVLELAPLgSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHS-AMIIYRDLKSHNVLVwtlYPN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 207 TH-QVKLCDFGSAKVL-------VKGEPNisyicsryYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVD 278
Cdd:cd14000 152 SAiIIKIADYGISRQCcrmgakgSEGTPG--------FRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFP 223
                       250       260
                ....*....|....*....|....
gi 42571361 279 QLVEIIK----VLGTPTREEIRCM 298
Cdd:cd14000 224 NEFDIHGglrpPLKQYECAPWPEV 247
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
74-282 2.60e-15

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 75.53  E-value: 2.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGES----VAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFFSTTsrdelfLNLV 144
Cdd:cd05057  13 KVLGSGAFGTVYKGVWIPEGEKvkipVAIKVLREETGPKAneeilDEAYVMASVDHPHLVRLLGICLSSQ------VQLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPetLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKG 224
Cdd:cd05057  87 TQLMP--LGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEK-RLVHRDLAARNVLVKTPNH-VKITDFGLAKLLDVD 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 225 EPNISYICSRY---YRAPELIFgATEYTASIDIWSAGCVLAELL-LGQPLFPGENSVD--QLVE 282
Cdd:cd05057 163 EKEYHAEGGKVpikWMALESIQ-YRIYTHKSDVWSYGVTVWELMtFGAKPYEGIPAVEipDLLE 225
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
74-271 3.74e-15

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: 76.26  E-value: 3.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK---KVLQDRR------YKNRELqlmrpMDHPN---VISLKHCFfsttsRDELFL 141
Cdd:cd05596  32 KVIGRGAFGEVQLVRHKSTKKVYAMKllsKFEMIKRsdsaffWEERDI-----MAHANsewIVQLHYAF-----QDDKYL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPE-TLYRVLrhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGS--- 217
Cdd:cd05596 102 YMVMDYMPGgDLVNLM-----SNYDVPEKWARFYTAEVVLALDAIHSM-GFVHRDVKPDNMLLDASGH-LKLADFGTcmk 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 218 --AKVLVK-----GEPNisyicsryYRAPELIF---GATEYTASIDIWSAGCVLAELLLGQPLF 271
Cdd:cd05596 175 mdKDGLVRsdtavGTPD--------YISPEVLKsqgGDGVYGRECDWWSVGVFLYEMLVGDTPF 230
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
70-275 3.74e-15

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: 74.66  E-value: 3.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYK-------NRELQLMRPMDHPNVISLKHCFfsttsRDELFLN 142
Cdd:cd14188   3 YCRGKVLGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKphqrekiDKEIELHRILHHKHVVQFYHYF-----EDKENIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPEtlyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLV 222
Cdd:cd14188  78 ILLEYCSR---RSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQE-ILHRDLKLGNFFINE-NMELKVGDFGLAARLE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 223 KGEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGEN 275
Cdd:cd14188 153 PLEHRRRTICgTPNYLSPE-VLNKQGHGCESDIWALGCVMYTMLLGRPPFETTN 205
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
70-279 3.80e-15

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: 75.87  E-value: 3.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRE-----------LQLMRPMDHPNVISLKHCFFSTtsrDE 138
Cdd:cd05633   7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMK-CLDKKRIKMKQgetlalnerimLSLVSTGDCPFIVCMTYAFHTP---DK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 139 LFLNLVMEYVPETLYRVLRHYTSSNQRMpifyvKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSA 218
Cdd:cd05633  83 LCFILDLMNGGDLHYHLSQHGVFSEKEM-----RFYATEIILGLEHMHN-RFVVYRDLKPANILLDEHGH-VRISDLGLA 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 219 KVLVKGEPNISyICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQ 279
Cdd:cd05633 156 CDFSKKKPHAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 215
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
71-373 4.28e-15

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: 75.29  E-value: 4.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  71 MAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKN--RELQLMRPMD-HPNVISLKHCFfsttsRDELFLNLVMEY 147
Cdd:cd14180   9 LEEPALGEGSFSVCRKCRHRQSGQEYAVK-IISRRMEANtqREVAALRLCQsHPNIVALHEVL-----HDQYHTYLVMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VP--ETLYRVLRhytssnQRMpifYVKLYTYQIFRGL----AYIHTVpGVCHRDVKPQNLLVDPLTHQ--VKLCDFGSAK 219
Cdd:cd14180  83 LRggELLDRIKK------KAR---FSESEASQLMRSLvsavSFMHEA-GVVHRDLKPENILYADESDGavLKVIDFGFAR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEPNISYIC-SRYYRAPELiFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsvdqlveiiKVLGTPTREEIRCm 298
Cdd:cd14180 153 LRPQGSRPLQTPCfTLQYAAPEL-FSNQGYDESCDLWSLGVILYTMLSGQVPFQSKR---------GKMFHNHAADIMH- 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 299 npNYTDFRFpQIKAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTaleacahpfFNELREpNARLPNGRPL--PPL 373
Cdd:cd14180 222 --KIKEGDF-SLEGEAWKGV-----SEEAKDLVRGLLTVDPAKRLK---------LSELRE-SDWLQGGSALssTPL 280
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
77-273 6.99e-15

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: 73.84  E-value: 6.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKKVLQdrryKNRELQLMRPMDHPNVISlkhcfFSTTSRDELFLNLVMEYVPetlYRVL 156
Cdd:cd14060   2 GGGSFGSVYRAIWVSQDKEVAVKKLLK----IEKEAEILSVLSHRNIIQ-----FYGAILEAPNYGIVTEYAS---YGSL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 157 RHYTSSN--QRMPIFYVKLYTYQIFRGLAYIHT-VP-GVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkGEPNISYIC 232
Cdd:cd14060  70 FDYLNSNesEEMDMDQIMTWATDIAKGMHYLHMeAPvKVIHRDLKSRNVVIAA-DGVLKICDFGASRFH--SHTTHMSLV 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42571361 233 SRY-YRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLFPG 273
Cdd:cd14060 147 GTFpWMAPEVIQS-LPVSETCDTYSYGVVLWEMLTREVPFKG 187
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
73-264 7.12e-15

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: 73.88  E-value: 7.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVAIKKVL------QDRRYKNREL-QLMRPMDHPNVISlkhcfFSTTSRDELFLNLVM 145
Cdd:cd14050   6 LSKLGEGSFGEVFKVRSREDGKLYAVKRSRsrfrgeKDRKRKLEEVeRHEKLGEHPNCVR-----FIKAWEEKGILYIQT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRvlrhYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGsakVLVK-G 224
Cdd:cd14050  81 ELCDTSLQQ----YCEETHSLPESEVWNILLDLLKGLKHLHD-HGLIHLDIKPANIFLSK-DGVCKLGDFG---LVVElD 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42571361 225 EPNISYIC---SRYYrAPELIFGatEYTASIDIWSAGCVLAEL 264
Cdd:cd14050 152 KEDIHDAQegdPRYM-APELLQG--SFTKAADIFSLGITILEL 191
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
70-354 7.26e-15

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: 74.05  E-value: 7.26e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK-----KVLQD--RRYKNRELQLMRPMDHPNVISLKHCFFSTTSRdelfLN 142
Cdd:cd14165   3 YILGINLGEGSYAKVKSAYSERLKCNVAIKiidkkKAPDDfvEKFLPRELEILARLNHKSIIKTYEIFETSDGK----VY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEY-VPETLYRvlrhYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd14165  79 IVMELgVQGDLLE----FIKLRGALPEDVARKMFHQLSSAIKYCHEL-DIVHRDLKCENLLLDK-DFNIKLTDFGFSKRC 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VK---GEPNIS--YICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENsvdqlveIIKVLgtptREEIR 296
Cdd:cd14165 153 LRdenGRIVLSktFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSN-------VKKML----KIQKE 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 297 cmnpnyTDFRFPQIKAhpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14165 222 ------HRVRFPRSKN----------LTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
74-366 7.39e-15

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: 74.64  E-value: 7.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFG--IVFQAKCLETGESVAIKKVLQDRRYKNR------ELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVM 145
Cdd:cd08216   4 YEIGKCFKGggVVHLAKHKPTNTLVAVKKINLESDSKEDlkflqqEILTSRQLQHPNILPYVTSFVVDND-----LYVVT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVL--RHYTSSnqrMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK 223
Cdd:cd08216  79 PLMAYGSCRDLlkTHFPEG---LPELAIAFILRDVLNALEYIHSK-GYIHRSVKASHILISGDGK-VVLSGLRYAYSMVK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 G--------EPNISYICSRYYRAPEL----IFGateYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEiiKVLGTP- 290
Cdd:cd08216 154 HgkrqrvvhDFPKSSEKNLPWLSPEVlqqnLLG---YNEKSDIYSVGITACELANGVVPFSDMPATQMLLE--KVRGTTp 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 291 --------TREEIRCMNPNYTDFRFPQIKAHPwHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNELREPNA 362
Cdd:cd08216 229 qlldcstyPLEEDSMSQSEDSSTEHPNNRDTR-DIPYQRTFSEAFHQFVELCLQRDPELRPSASQLLAHSFFKQCRRSNT 307

                ....
gi 42571361 363 RLPN 366
Cdd:cd08216 308 SLLD 311
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
71-353 8.90e-15

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: 74.30  E-value: 8.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  71 MAERVVGTGSFGIVFQAKCLETGESVAIKKVLQD----RRYKNRELQ-LMRPMDHPNVISLKHcFFSTTSRdelfLNLVM 145
Cdd:cd14174   5 LTDELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNaghsRSRVFREVEtLYQCQGNKNILELIE-FFEDDTR----FYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETlyRVLRHYTSS---NQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLL------VDPlthqVKLCDF- 215
Cdd:cd14174  80 EKLRGG--SILAHIQKRkhfNEREASRVVR----DIASALDFLHT-KGIAHRDLKPENILcespdkVSP----VKICDFd 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 216 -GSAKVLVKG-----EPNISYIC-SRYYRAPELI--FG--ATEYTASIDIWSAGCVLAELLLGQPLFPGENSVD---QLV 281
Cdd:cd14174 149 lGSGVKLNSActpitTPELTTPCgSAEYMAPEVVevFTdeATFYDKRCDLWSLGVILYIMLSGYPPFVGHCGTDcgwDRG 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 282 EIIKVLGTPTREEIRCMNPNYTDFRFPQIKAhpwhkvfhkrmppEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14174 229 EVCRVCQNKLFESIQEGKYEFPDKDWSHISS-------------EAKDLISKLLVRDAKERLSAAQVLQHPW 287
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
76-265 1.04e-14

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: 73.29  E-value: 1.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYKNRELQLMRPMDHPNVISlkhcFFSTTSRDELfLNLVMEYVP-ETL 152
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGKVMVMKelKRFDEQRSFLKEVKLMRRLSHPNILR----FIGVCVKDNK-LNFITEYVNgGTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 153 YRVL-RHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVpGVCHRDVKPQNLLV--DPLTHQVKLCDFGSAKVLVKGEPN-- 227
Cdd:cd14065  76 EELLkSMDEQLPWSQRVSLAK----DIASGMAYLHSK-NIIHRDLNSKNCLVreANRGRNAVVADFGLAREMPDEKTKkp 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42571361 228 -----ISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELL 265
Cdd:cd14065 151 drkkrLTVVGSPYWMAPEMLRGES-YDEKVDVFSFGIVLCEII 192
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
70-354 1.14e-14

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: 74.68  E-value: 1.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR---ELQLMRPM-----DHPN---VISLKHCFfSTTSRDE 138
Cdd:cd14216  12 YHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVKSAEHYTETaldEIKLLKSVrnsdpNDPNremVVQLLDDF-KISGVNG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 139 LFLNLVMEYVPETLyrvLRHYTSSN-QRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQN----------------- 200
Cdd:cd14216  91 THICMVFEVLGHHL---LKWIIKSNyQGLPLPCVKKIIRQVLQGLDYLHTKCRIIHTDIKPENillsvneqyirrlaaea 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 201 ------LLVDPLTHQ------VKLCDFGSAKVLVKGepNISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELLLGQ 268
Cdd:cd14216 168 tewqrnFLVNPLEPKnaeklkVKIADLGNACWVHKH--FTEDIQTRQYRSLEVLIGSG-YNTPADIWSTACMAFELATGD 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 269 PLF---PGEN---SVDQLVEIIKVLGTPTREEIrcMNPNYTDFRFPQ-------IKAHPW---HKVFHKRMPPEA----- 327
Cdd:cd14216 245 YLFephSGEDysrDEDHIALIIELLGKVPRKLI--VAGKYSKEFFTKkgdlkhiTKLKPWglfEVLVEKYEWSQEeaagf 322
                       330       340
                ....*....|....*....|....*..
gi 42571361 328 IDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14216 323 TDFLLPMLELIPEKRATAAECLRHPWL 349
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
70-315 1.42e-14

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: 73.08  E-value: 1.42e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQ--LMRPMD----------HPNVISLKHCFfsttSRD 137
Cdd:cd14100   2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPngTRVPMEivllkkvgsgFRGVIRLLDWF----ERP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 138 ELFLnLVMEYvPETLyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGS 217
Cdd:cd14100  78 DSFV-LVLER-PEPV-QDLFDFITERGALPEELARSFFRQVLEAVRHCHNC-GVLHRDIKDENILIDLNTGELKLIDFGS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 218 AkVLVKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQ-PLFPGENSVDQLVEIIKVLGTPTREEIR 296
Cdd:cd14100 154 G-ALLKDTVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDiPFEHDEEIIRGQVFFRQRVSSECQHLIK 232
                       250       260
                ....*....|....*....|.
gi 42571361 297 -CMNPNYTDF-RFPQIKAHPW 315
Cdd:cd14100 233 wCLALRPSDRpSFEDIQNHPW 253
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
74-292 1.51e-14

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: 74.29  E-value: 1.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDH--------PNVISLKHCFfSTTSRdelfLNLVM 145
Cdd:cd05617  21 RVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHvfeqassnPFLVGLHSCF-QTTSR----LFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVP--ETLYRVLRHytssnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK 223
Cdd:cd05617  96 EYVNggDLMFHMQRQ-----RKLPEEHARFYAAEICIALNFLHE-RGIIYRDLKLDNVLLDADGH-IKLTDYGMCKEGLG 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 224 GEPNISYIC-SRYYRAPELIFGAtEYTASIDIWSAGCVLAELLLGQPLF------PGENSVDQLVEIIkvLGTPTR 292
Cdd:cd05617 169 PGDTTSTFCgTPNYIAPEILRGE-EYGFSVDWWALGVLMFEMMAGRSPFdiitdnPDMNTEDYLFQVI--LEKPIR 241
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
76-353 1.63e-14

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: 73.29  E-value: 1.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVfqAKCLE--TGESVAiKKVLQDRRYK-----------NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLN 142
Cdd:cd14105  13 LGSGQFAVV--KKCREksTGLEYA-AKFIKKRRSKasrrgvsrediEREVSILRQVLHPNIITLHDVFENKTD-----VV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVpGVCHRDVKPQNLL-----VDPltHQVKLCDFG 216
Cdd:cd14105  85 LILELVAGgELFDFLAEKESLSEEEATEFLK----QILDGVNYLHTK-NIAHFDLKPENIMlldknVPI--PRIKLIDFG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 SAKVLVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeir 296
Cdd:cd14105 158 LAHKIEDGNEFKNIFGTPEFVAPEIV-NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV---------- 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 297 cmNPNYTDFRFPQIKAHpwhkvfhkrmppeAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14105 227 --NYDFDDEYFSNTSEL-------------AKDFIRQLLVKDPRKRMTIQESLRHPW 268
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
70-279 1.76e-14

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: 73.93  E-value: 1.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRE-----------LQLMRPMDHPNVISLKHCFFSTtsrDE 138
Cdd:cd14223   2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMK-CLDKKRIKMKQgetlalnerimLSLVSTGDCPFIVCMSYAFHTP---DK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 139 LFLNLVMEYVPETLYRVLRHYTSSNQRMpifyvKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSA 218
Cdd:cd14223  78 LSFILDLMNGGDLHYHLSQHGVFSEAEM-----RFYAAEIILGLEHMHS-RFVVYRDLKPANILLDEFGH-VRISDLGLA 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 219 KVLVKGEPNISyICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQ 279
Cdd:cd14223 151 CDFSKKKPHAS-VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDK 210
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
76-261 1.89e-14

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: 73.68  E-value: 1.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIK-----KVLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTSRDELflnLVMEYVP- 149
Cdd:cd13988   1 LGQGATANVFRGRHKKTGDLYAVKvfnnlSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEELTTRHKV---LVMELCPc 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVLRHYTSSnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNL---LVDPLTHQVKLCDFGSAKVLVKGEP 226
Cdd:cd13988  78 GSLYTVLEEPSNA-YGLPESEFLIVLRDVVAGMNHLRE-NGIVHRDIKPGNImrvIGEDGQSVYKLTDFGAARELEDDEQ 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42571361 227 NISYICSRYYRAPELIFGAT-------EYTASIDIWSAGCVL 261
Cdd:cd13988 156 FVSLYGTEEYLHPDMYERAVlrkdhqkKYGATVDLWSIGVTF 197
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
75-275 1.93e-14

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: 73.55  E-value: 1.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFqaKCLETGESVAIKKVLQD-RRYKNRELQLMR-P-MDHPNVIslkHCFFS-----TTSRDELFLnlVME 146
Cdd:cd14054   2 LIGQGRYGTVW--KGSLDERPVAVKVFPARhRQNFQNEKDIYElPlMEHSNIL---RFIGAderptADGRMEYLL--VLE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP-ETLYRVLRHYTS---SNQRMpifyvklyTYQIFRGLAYIHTV--------PGVCHRDVKPQNLLVDPLTHQVkLCD 214
Cdd:cd14054  75 YAPkGSLCSYLRENTLdwmSSCRM--------ALSLTRGLAYLHTDlrrgdqykPAIAHRDLNSRNVLVKADGSCV-ICD 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 215 FGSAKVL-----VKGEPN------ISYICSRYYRAPELIFGATE------YTASIDIWSAGCVLAELLLGQP-LFPGEN 275
Cdd:cd14054 146 FGLAMVLrgsslVRGRPGaaenasISEVGTLRYMAPEVLEGAVNlrdcesALKQVDVYALGLVLWEIAMRCSdLYPGES 224
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
74-284 1.96e-14

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: 73.61  E-value: 1.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVA---IKKVL----QDRRYKNRELQLMRPM-DHPNVISLKHCfFSTTSRdeLFlnLVM 145
Cdd:cd05588   1 RVIGRGSYAKVLMVELKKTKRIYAmkvIKKELvnddEDIDWVQTEKHVFETAsNHPFLVGLHSC-FQTESR--LF--FVI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVP--ETLYRVLRHytssnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVK 223
Cdd:cd05588  76 EFVNggDLMFHMQRQ-----RRLPEEHARFYSAEISLALNFLHE-KGIIYRDLKLDNVLLDSEGH-IKLTDYGMCKEGLR 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYIC-SRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLF--------PGENSVDQLVEII 284
Cdd:cd05588 149 PGDTTSTFCgTPNYIAPEILRG-EDYGFSVDWWALGVLMFEMLAGRSPFdivgssdnPDQNTEDYLFQVI 217
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
99-353 2.14e-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: 72.39  E-value: 2.14e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  99 KKVLQDRRYKNRELQLMRpmdHPNVIS-LKHCFFSTTSRDELFLNLVMEYVPETLyrvLRHYTSSNQRMPIFYVKLYTYQ 177
Cdd:cd14012  39 KKQIQLLEKELESLKKLR---HPNLVSyLAFSIERRGRSDGWKVYLLTEYAPGGS---LSELLDSVGSVPLDTARRWTLQ 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 178 IFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQ--VKLCDFGSAKVL--VKGEPNISYICSRYYRAPELIFGATEYTASID 253
Cdd:cd14012 113 LLEALEYLHRN-GVVHKSLHAGNVLLDRDAGTgiVKLTDYSLGKTLldMCSRGSLDEFKQTYWLPPELAQGSKSPTRKTD 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 254 IWSAGCVLAELLLGQPLFPGENSVDQLveiikvlgtptreeircMNPnytdfrfpqikahpwhkvfhKRMPPEAIDLASR 333
Cdd:cd14012 192 VWDLGLLFLQMLFGLDVLEKYTSPNPV-----------------LVS--------------------LDLSASLQDFLSK 234
                       250       260
                ....*....|....*....|
gi 42571361 334 LLQYSPSLRCTALEACAHPF 353
Cdd:cd14012 235 CLSLDPKKRPTALELLPHEF 254
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
76-269 2.15e-14

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: 72.38  E-value: 2.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGES---VAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLkhcffSTTSRDELFLnLVMEY 147
Cdd:cd05060   3 LGHGNFGSVRKGVYLMKSGKeveVAVKTLKQEHEKAGkkeflREASVMAQLDHPCIVRL-----IGVCKGEPLM-LVMEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQN-LLVDplTHQVKLCDFGSAKVLVKGep 226
Cdd:cd05060  77 APLG---PLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFV-HRDLAARNvLLVN--RHQAKISDFGMSRALGAG-- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 227 nisyicSRYYR------------APELIFGATEYTASiDIWSAGCVLAELL-LGQP 269
Cdd:cd05060 149 ------SDYYRattagrwplkwyAPECINYGKFSSKS-DVWSYGVTLWEAFsYGAK 197
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
70-286 2.19e-14

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 72.68  E-value: 2.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYK--------NRELQLMRPMDHPNVISLKHCFFSTTSrdel 139
Cdd:cd14196   7 YDIGEELGSGQFAIVKKCREKSTGLEYAAKfiKKRQSRASRrgvsreeiEREVSILRQVLHPNIITLHDVYENRTD---- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 fLNLVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQN-LLVD---PLTHqVKLCD 214
Cdd:cd14196  83 -VVLILELVSGgELFDFLAQKESLSEEEATSFIK----QILDGVNYLHT-KKIAHFDLKPENiMLLDkniPIPH-IKLID 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 215 FGSAKVLVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKV 286
Cdd:cd14196 156 FGLAHEIEDGVEFKNIFGTPEFVAPEIV-NYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAV 226
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
70-284 2.52e-14

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: 73.89  E-value: 2.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQ-------DRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLN 142
Cdd:cd05622  75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemikrsDSAFFWEERDIMAFANSPWVVQLFYAF-----QDDRYLY 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVLrhytsSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVL 221
Cdd:cd05622 150 MVMEYMPGgDLVNLM-----SNYDVPEKWARFYTAEVVLALDAIHSM-GFIHRDVKPDNMLLDKSGH-LKLADFGTCMKM 222
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 222 VK----------GEPNisyicsryYRAPELIF---GATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEII 284
Cdd:cd05622 223 NKegmvrcdtavGTPD--------YISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIM 290
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
70-315 2.53e-14

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: 72.30  E-value: 2.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYK---------NRELQLMR--PMDHPNVISLKHCFfsttSRDE 138
Cdd:cd14102   2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEwgtlngvmvPLEIVLLKkvGSGFRGVIKLLDWY----ERPD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 139 LFLnLVMEYvPEtLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSA 218
Cdd:cd14102  78 GFL-IVMER-PE-PVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSC-GVVHRDIKDENLLVDLRTGELKLIDFGSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLvKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFpgensvDQLVEIIKV-------LGTPT 291
Cdd:cd14102 154 ALL-KDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPF------EQDEEILRGrlyfrrrVSPEC 226
                       250       260
                ....*....|....*....|....*.
gi 42571361 292 REEIR-CMNPNYTDF-RFPQIKAHPW 315
Cdd:cd14102 227 QQLIKwCLSLRPSDRpTLEQIFDHPW 252
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
70-317 2.57e-14

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 72.19  E-value: 2.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYK----------NRELQLMRPM----DHPNVISLKHCFfsttS 135
Cdd:cd14101   2 YTMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQwsklpgvnpvPNEVALLQSVgggpGHRGVIRLLDWF----E 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 136 RDELFLnLVMEYvPETLyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVKLCDF 215
Cdd:cd14101  78 IPEGFL-LVLER-PQHC-QDLFDYITERGALDESLARRFFKQVVEAVQHCHS-KGVVHRDIKDENILVDLRTGDIKLIDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 216 GSAKVLvKGEPNISYICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQ-PLFPGENSVDQLVEIIKVLGTPTREE 294
Cdd:cd14101 154 GSGATL-KDSMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDiPFERDTDILKAKPSFNKRVSNDCRSL 232
                       250       260
                ....*....|....*....|....*
gi 42571361 295 IR-CMNPNYTDF-RFPQIKAHPWHK 317
Cdd:cd14101 233 IRsCLAYNPSDRpSLEQILLHPWMM 257
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
74-269 2.62e-14

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 72.73  E-value: 2.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYK-NRELQLMRPMDHPNVISLKHCFFSTTS----RDELFlnLVME 146
Cdd:cd06636  22 EVVGNGTYGQVYKGRHVKTGQLAAIKvmDVTEDEEEEiKLEINMLKKYSHHRNIATYYGAFIKKSppghDDQLW--LVME 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQrMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK--G 224
Cdd:cd06636 100 FCGAGSVTDLVKNTKGNA-LKEDWIAYICREILRGLAHLH-AHKVIHRDIKGQNVLLTE-NAEVKLVDFGVSAQLDRtvG 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 225 EPNiSYICSRYYRAPELIF----GATEYTASIDIWSAGCVLAELLLGQP 269
Cdd:cd06636 177 RRN-TFIGTPYWMAPEVIAcdenPDATYDYRSDIWSLGITAIEMAEGAP 224
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
79-357 2.91e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 73.37  E-value: 2.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   79 GSFGIVFQAKCLETGESVAIKkvLQDRRYKNRELQLMRPMDHPNVISLKHCFFSTTsrdelFLNLVMEYVPETLYRVLrh 158
Cdd:PHA03209  77 GSEGRVFVATKPGQPDPVVLK--IGQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGA-----ITCMVLPHYSSDLYTYL-- 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  159 yTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDPLThQVKLCDFGSAKVLVKGEPNISYICSRYYRA 238
Cdd:PHA03209 148 -TKRSRPLPIDQALIIEKQILEGLRYLHAQR-IIHRDVKTENIFINDVD-QVCIGDLGAAQFPVVAPAFLGLAGTVETNA 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  239 PElIFGATEYTASIDIWSAGCVLAELLL----------GQPLFPGENSVDQLVEIIKVLGT-----PTREEIRcMNPNYT 303
Cdd:PHA03209 225 PE-VLARDKYNSKADIWSAGIVLFEMLAypstifedppSTPEEYVKSCHSHLLKIISTLKVhpeefPRDPGSR-LVRGFI 302
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361  304 DFRFPQIKAHPWHKVFHK-RMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNEL 357
Cdd:PHA03209 303 EYASLERQPYTRYPCFQRvNLPIDGEFLVHKMLTFDAAMRPSAEEILNYPMFAQL 357
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
69-265 3.78e-14

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: 71.70  E-value: 3.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  69 SYMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLMRPMDHPNVISLKHCFfsttSRDELFLN 142
Cdd:cd08223   1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLnlknasKRERKAAEQEAKLLSKLKHPNIVSYKESF----EGEDGFLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVP-ETLYRVLRHYT----SSNQRMPIFyvklytYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGS 217
Cdd:cd08223  77 IVMGFCEgGDLYTRLKEQKgvllEERQVVEWF------VQIAMALQYMHE-RNILHRDLKTQNIFLTK-SNIIKVGDLGI 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 218 AKVLVKGEPNIS-YICSRYYRAPELiFGATEYTASIDIWSAGCVLAELL 265
Cdd:cd08223 149 ARVLESSSDMATtLIGTPYYMSPEL-FSNKPYNHKSDVWALGCCVYEMA 196
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
74-284 3.80e-14

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 73.50  E-value: 3.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVfQAKCLETGESVAIKKVLQ--------DRRYKNRELQLMRPMDHPNVISLkHCFFsttsRDELFLNLVM 145
Cdd:cd05621  58 KVIGRGAFGEV-QLVRHKASQKVYAMKLLSkfemikrsDSAFFWEERDIMAFANSPWVVQL-FCAF----QDDKYLYMVM 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVLrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVL---- 221
Cdd:cd05621 132 EYMPGGDLVNL----MSNYDVPEKWAKFYTAEVVLALDAIHSM-GLIHRDVKPDNMLLDKYGH-LKLADFGTCMKMdetg 205
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 222 ------VKGEPNisyicsryYRAPELIF---GATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEII 284
Cdd:cd05621 206 mvhcdtAVGTPD--------YISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIM 269
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
74-351 4.22e-14

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 71.98  E-value: 4.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISLKHCFfstTSRDELFLNLVMEYV 148
Cdd:cd14088   7 QVIKTEEFCEIFRAKDKTTGKLYTCKKFLKRdgrkvRKAAKNEINILKMVKHPNILQLVDVF---ETRKEYFIFLELATG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLR--HYTSSNQRMPIfyvklytYQIFRGLAYIHTVPgVCHRDVKPQNLL-VDPLTH-QVKLCDFGSAKV---L 221
Cdd:cd14088  84 REVFDWILDqgYYSERDTSNVI-------RQVLEAVAYLHSLK-IVHRNLKLENLVyYNRLKNsKIVISDFHLAKLengL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKgEPnisyiC-SRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGEnsvdqlveiikvlgtptREEIRCMNP 300
Cdd:cd14088 156 IK-EP-----CgTPEYLAPEVV-GRQRYGRPVDCWAIGVIMYILLSGNPPFYDE-----------------AEEDDYENH 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 301 NYTDFRFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAH 351
Cdd:cd14088 212 DKNLFRKILAGDYEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISH 262
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
70-219 4.33e-14

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: 71.72  E-value: 4.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkvLQDRRYKN----RELQLMRPM-DHPNVISLKHCFfsttsRDELFLNLV 144
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIK--IEKKDSKHpqleYEAKVYKLLqGGPGIPRLYWFG-----QEGDYNVMV 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 145 MEYVPETLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLL--VDPLTHQVKLCDFGSAK 219
Cdd:cd14016  75 MDLLGPSLEDLFNKC---GRKFSLKTVLMLADQMISRLEYLHSK-GYIHRDIKPENFLmgLGKNSNKVYLIDFGLAK 147
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
70-285 5.11e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 74.00  E-value: 5.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKV----LQDRRYKNR--ELQLMRPMDHPNVISLKHCFFSTTSRDelfLNL 143
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAIsyrgLKEREKSQLviEVNVMRELKHKNIVRYIDRFLNKANQK---LYI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   144 VMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPG------VCHRDVKPQNLL-------VDPLTHQ 209
Cdd:PTZ00266   92 LMEFCDAgDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNLKDgpngerVLHRDLKPQNIFlstgirhIGKITAQ 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   210 V---------KLCDFGSAKVLvkGEPNISYIC--SRYYRAPELIFGATE-YTASIDIWSAGCVLAELLLGQPLFPGENSV 277
Cdd:PTZ00266  172 AnnlngrpiaKIGDFGLSKNI--GIESMAHSCvgTPYYWSPELLLHETKsYDDKSDMWALGCIIYELCSGKTPFHKANNF 249

                  ....*...
gi 42571361   278 DQLVEIIK 285
Cdd:PTZ00266  250 SQLISELK 257
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
76-264 5.55e-14

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: 71.57  E-value: 5.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVA-----IKKVLQDRRYK-NRELQLMRPMDHPNVISLKHCFFSTTsRDELFLNLVMEYVP 149
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTVEVAwcelqTRKLSKGERQRfSEEVEMLKGLQHPNIVRFYDSWKSTV-RGHKCIILVTELMT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHT-VPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAkVLVKGEPNI 228
Cdd:cd14033  88 SG---TLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSrCPPILHRDLKCDNIFITGPTGSVKIGDLGLA-TLKRASFAK 163
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42571361 229 SYICSRYYRAPELIfgATEYTASIDIWSAGCVLAEL 264
Cdd:cd14033 164 SVIGTPEFMAPEMY--EEKYDEAVDVYAFGMCILEM 197
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
74-271 5.81e-14

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: 71.95  E-value: 5.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNR--------ELQLMRPMDHPNVISLKHCFfstTSRDELFLNLVM 145
Cdd:cd05631   6 RVLGKGGFGEVCACQVRATGKMYACKK-LEKKRIKKRkgeamalnEKRILEKVNSRFVVSLAYAY---ETKDALCLVLTI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVlrhYTSSN----QRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVL 221
Cdd:cd05631  82 MNGGDLKFHI---YNMGNpgfdEQRAIFYAA----ELCCGLEDLQR-ERIVYRDLKPENILLDDRGH-IRISDLGLAVQI 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLF 271
Cdd:cd05631 153 PEGETVRGRVGTVGYMAPEVI-NNEKYTFSPDWWGLGCLIYEMIQGQSPF 201
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
74-276 6.17e-14

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: 71.30  E-value: 6.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAK-CLETGE--SVAIKKVLQDRRYKNRE--LQ---LMRPMDHPNVISLkhcfFSTTSRDELFlnLVM 145
Cdd:cd05056  12 RCIGEGQFGDVYQGVyMSPENEkiAVAVKTCKNCTSPSVREkfLQeayIMRQFDHPHIVKL----IGVITENPVW--IVM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPetlYRVLRHYTSSNQ-RMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLV-DPltHQVKLCDFGSAKVLvk 223
Cdd:cd05056  86 ELAP---LGELRSYLQVNKySLDLASLILYAYQLSTALAYLESKRFV-HRDIAARNVLVsSP--DCVKLGDFGLSRYM-- 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 gEPNISYICSR-----YYRAPELIfGATEYTASIDIWSAG-CVLAELLLG-QPLFPGENS 276
Cdd:cd05056 158 -EDESYYKASKgklpiKWMAPESI-NFRRFTSASDVWMFGvCMWEILMLGvKPFQGVKNN 215
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
70-374 9.97e-14

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: 71.07  E-value: 9.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNR--------ELQLMRPMDHPNVISLKHCFFSTTSrdelfL 141
Cdd:cd05608   3 FLDFRVLGKGGFGEVSACQMRATGKLYACKK-LNKKRLKKRkgyegamvEKRILAKVHSRFIVSLAYAFQTKTD-----L 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 142 NLVMEYVPETLYRVlrHYTSSNQRMPIF---YVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSA 218
Cdd:cd05608  77 CLVMTIMNGGDLRY--HIYNVDEENPGFqepRACFYTAQIISGLEHLHQ-RRIIYRDLKPENVLLDDDGN-VRISDLGLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEPNI-SYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLF--PGEnsvdqlveiiKVLGTPTREEI 295
Cdd:cd05608 153 VELKDGQTKTkGYAGTPGFMAPELLLG-EEYDYSVDYFTLGVTLYEMIAARGPFraRGE----------KVENKELKQRI 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 296 RCMNPNYTDfrfpqikahpwhkvfhkRMPPEAIDLASRLLQYSPSLR-------CTALEacAHPFFNELrepNARLPNGR 368
Cdd:cd05608 222 LNDSVTYSE-----------------KFSPASKSICEALLAKDPEKRlgfrdgnCDGLR--THPFFRDI---NWRKLEAG 279

                ....*.
gi 42571361 369 PLPPLF 374
Cdd:cd05608 280 ILPPPF 285
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
167-354 1.19e-13

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: 71.59  E-value: 1.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 167 PIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQ------------------VKLCDFGSAKVlvKGEPNI 228
Cdd:cd14215 114 PIHQVRHMAFQVCQAVKFLHD-NKLTHTDLKPENILFVNSDYEltynlekkrdersvkstaIRVVDFGSATF--DHEHHS 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGTPTREEIRCM---------- 298
Cdd:cd14215 191 TIVSTRHYRAPEVIL-ELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPIPSRMIRKTrkqkyfyhgr 269
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 299 ---NPNYTDFRFPQIKAHPWHKVFHKRMPP--EAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14215 270 ldwDENTSAGRYVRENCKPLRRYLTSEAEEhhQLFDLIESMLEYEPSKRLTLAAALKHPFF 330
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
76-268 1.65e-13

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 70.36  E-value: 1.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQ--DRRYKN--RELQLMRPMDHPNVISlkhcFFSTTSRDELfLNLVMEYVP-E 150
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGKVMVMKELIRcdEETQKTflTEVKVMRSLDHPNVLK----FIGVLYKDKR-LNLLTEFIEgG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLVKGEP---- 226
Cdd:cd14222  76 TLKDFLRADDPFPWQQKVSFAK----GIASGMAYLHSM-SIIHRDLNSHNCLIK-LDKTVVVADFGLSRLIVEEKKkppp 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 227 -----------------NISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAElLLGQ 268
Cdd:cd14222 150 dkpttkkrtlrkndrkkRYTVVGNPYWMAPEMLNG-KSYDEKVDIFSFGIVLCE-IIGQ 206
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
97-265 1.77e-13

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: 70.51  E-value: 1.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  97 AIKKV----LQDRR--YKNR---ELQLMRPMDHPNVISLKHcfFSTTSRDELFLnlVMEYVPETLY-RVLRHYTSSNQRM 166
Cdd:cd14001  32 AVKKInskcDKGQRslYQERlkeEAKILKSLNHPNIVGFRA--FTKSEDGSLCL--AMEYGGKSLNdLIEERYEAGLGPF 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 167 PIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVL-----VKGEPNISYICSRYYRAPEL 241
Cdd:cd14001 108 PAATILKVALSIARALEYLHNEKKILHGDIKSGNVLIKGDFESVKLCDFGVSLPLtenleVDSDPKAQYVGTEPWKAKEA 187
                       170       180
                ....*....|....*....|....
gi 42571361 242 IFGATEYTASIDIWSAGCVLAELL 265
Cdd:cd14001 188 LEEGGVITDKADIFAYGLVLWEMM 211
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
103-355 1.86e-13

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: 70.35  E-value: 1.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 103 QDRRYKNRELQLMRPMDHPNVISL-----KHCFFSTTSRDeLFLNLVMEYVPETLYRvlrhytSSNQRMPIFYVKLYTYQ 177
Cdd:cd14020  46 GDYGFAKERAALEQLQGHRNIVTLygvftNHYSANVPSRC-LLLELLDVSVSELLLR------SSNQGCSMWMIQHCARD 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 178 IFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAkvLVKGEPNISYICSRYYRAPEL----------IFGATE 247
Cdd:cd14020 119 VLEALAFLHH-EGYVHADLKPRNILWSAEDECFKLIDFGLS--FKEGNQDVKYIQTDGYRAPEAelqnclaqagLQSETE 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 248 YTASIDIWSAGCVLAELLLGqplfpgensvdqlveiIKVLGTPTREEIRCMNPNYTDFRFP-QIKAHPWHKVFHKRmppe 326
Cdd:cd14020 196 CTSAVDLWSLGIVLLEMFSG----------------MKLKHTVRSQEWKDNSSAIIDHIFAsNAVVNPAIPAYHLR---- 255
                       250       260
                ....*....|....*....|....*....
gi 42571361 327 aiDLASRLLQYSPSLRCTALEACAHPFFN 355
Cdd:cd14020 256 --DLIKSMLHNDPGKRATAEAALCSPFFS 282
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
74-284 1.99e-13

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: 71.22  E-value: 1.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDH--------PNVISLKHCFfSTTSRdelfLNLVM 145
Cdd:cd05618  26 RVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHvfeqasnhPFLVGLHSCF-QTESR----LFFVI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVP--ETLYRVLRHytssnQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV-LV 222
Cdd:cd05618 101 EYVNggDLMFHMQRQ-----RKLPEEHARFYSAEISLALNYLHE-RGIIYRDLKLDNVLLDSEGH-IKLTDYGMCKEgLR 173
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELLLGQPLF--------PGENSVDQLVEII 284
Cdd:cd05618 174 PGDTTSTFCGTPNYIAPEILRG-EDYGFSVDWWALGVLMFEMMAGRSPFdivgssdnPDQNTEDYLFQVI 242
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
71-370 2.55e-13

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: 70.06  E-value: 2.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  71 MAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQL-MRPMDHPNVISLKHCFFSTTSRDELFLnLVMEYVP 149
Cdd:cd14170   5 VTSQVLGLGINGKVLQIFNKRTQEKFALK-MLQDCPKARREVELhWRASQCPHIVRIVDVYENLYAGRKCLL-IVMECLD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 --ETLYRVL-RHYTSSNQRMPIFYVKlytyQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQ--VKLCDFGSAKVLVKG 224
Cdd:cd14170  83 ggELFSRIQdRGDQAFTEREASEIMK----SIGEAIQYLHSI-NIAHRDVKPENLLYTSKRPNaiLKLTDFGFAKETTSH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVdqlveiikVLGTPTREEIRcmnpnYTD 304
Cdd:cd14170 158 NSLTTPCYTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGL--------AISPGMKTRIR-----MGQ 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 305 FRFPQIKahpWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPFFNE-LREPNARLPNGRPL 370
Cdd:cd14170 224 YEFPNPE---WSEV-----SEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQsTKVPQTPLHTSRVL 282
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
75-357 2.89e-13

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: 70.02  E-value: 2.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRE-----------LQLMRPMDHPNVISLKHCFfsTTSRDELFlnl 143
Cdd:cd05589   6 VLGRGHFGKVLLAEYKPTGELFAIK-ALKKGDIIARDeveslmcekriFETVNSARHPFLVNLFACF--QTPEHVCF--- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRVLRHYTSSNQRMPIFY---VKLytyqifrGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV 220
Cdd:cd05589  80 VMEYAAGGDLMMHIHEDVFSEPRAVFYaacVVL-------GLQFLHE-HKIVYRDLKLDNLLLDTEGY-VKIADFGLCKE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPG---ENSVDQLVEiikvlgtptrEEIR 296
Cdd:cd05589 151 GMGFGDRTSTFCgTPEFLAPE-VLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGddeEEVFDSIVN----------DEVR 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 297 cmnpnYTDFrfpqikahpwhkvfhkrMPPEAIDLASRLLQYSPSLRCTALEACA-----HPFFNEL 357
Cdd:cd05589 220 -----YPRF-----------------LSTEAISIMRRLLRKNPERRLGASERDAedvkkQPFFRNI 263
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
63-293 2.89e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 70.79  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   63 EPKQTISYMAERVVGTGSFGIV-----------FQAKCLE--TGESVAIKKvlQDRRYKNRELQLMRPMDHPNVISLKHC 129
Cdd:PHA03212  74 DADASLALCAEARAGIEKAGFSiletftpgaegFAFACIDnkTCEHVVIKA--GQRGGTATEAHILRAINHPSIIQLKGT 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  130 FFSTTsrdelFLNLVMEYVPETLYrvlrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpltHQ 209
Cdd:PHA03212 152 FTYNK-----FTCLILPRYKTDLY----CYLAAKRNIAICDILAIERSVLRAIQYLHE-NRIIHRDIKAENIFIN---HP 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  210 VKLC--DFGSAKVLVKGEPNisyicsRYY--------RAPELIfGATEYTASIDIWSAGCVLAELLLGQ-PLFPGE---- 274
Cdd:PHA03212 219 GDVClgDFGAACFPVDINAN------KYYgwagtiatNAPELL-ARDPYGPAVDIWSAGIVLFEMATCHdSLFEKDgldg 291
                        250       260
                 ....*....|....*....|.
gi 42571361  275 --NSVDQLVEIIKVLGTPTRE 293
Cdd:PHA03212 292 dcDSDRQIKLIIRRSGTHPNE 312
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
113-355 3.52e-13

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 69.11  E-value: 3.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  113 QLMRpmDHPNVISLKHCFfsTTSRDELflnLVMEYVPE-TLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHtVPGV 191
Cdd:PHA03390  63 QLMK--DNPNFIKLYYSV--TTLKGHV---LIMDYIKDgDLFDLLK----KEGKLSEAEVKKIIRQLVEALNDLH-KHNI 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  192 CHRDVKPQNLLVDPLTHQVKLCDFGSAKvlVKGEPnisyicSRY-----YRAPELIFGATeYTASIDIWSAGCVLAELLL 266
Cdd:PHA03390 131 IHNDIKLENVLYDRAKDRIYLCDYGLCK--IIGTP------SCYdgtldYFSPEKIKGHN-YDVSFDWWAVGVLTYELLT 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  267 GQplFPGENSVDQLVEIIKvlgtptreeircMNPNYTdfrfpqikahpWHKVFHKRMPPEAIDLASRLLQYSPSLRCTAL 346
Cdd:PHA03390 202 GK--HPFKEDEDEELDLES------------LLKRQQ-----------KKLPFIKNVSKNANDFVQSMLKYNINYRLTNY 256
                        250
                 ....*....|
gi 42571361  347 EACA-HPFFN 355
Cdd:PHA03390 257 NEIIkHPFLK 266
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
74-284 3.59e-13

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: 70.11  E-value: 3.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNREL-------QLMRPMDHPNVISLKHCFfSTTSRdelfLNLVME 146
Cdd:cd05593  21 KLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtltesRVLKNTRHPFLTSLKYSF-QTKDR----LCFVME 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKG 224
Cdd:cd05593  96 YVNggELFFHLSRERVFSEDR-----TRFYGAEIVSALDYLHS-GKIVYRDLKLENLMLDKDGH-IKITDFGLCKEGITD 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 225 EPNISYIC-SRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvDQLVEII 284
Cdd:cd05593 169 AATMKTFCgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDH-EKLFELI 227
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
75-264 3.62e-13

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: 69.39  E-value: 3.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCleTGESVAIKKV-LQDRRYKNRELQLMRP--MDHPNVISlkhcFFSTTSRD---ELFLNLVMEYV 148
Cdd:cd13998   2 VIGKGRFGEVWKASL--KNEPVAVKIFsSRDKQSWFREKEIYRTpmLKHENILQ----FIAADERDtalRTELWLVTAFH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PE-TLYRVLRHYTSSNQRMpifyVKLyTYQIFRGLAYIHT--------VPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAK 219
Cdd:cd13998  76 PNgSL*DYLSLHTIDWVSL----CRL-ALSVARGLAHLHSeipgctqgKPAIAHRDLKSKNILVKN-DGTCCIADFGLAV 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 220 VLVKGEP-----NISYICSRYYRAPELIFGA-----TEYTASIDIWSAGCVLAEL 264
Cdd:cd13998 150 RLSPSTGeednaNNGQVGTKRYMAPEVLEGAinlrdFESFKRVDIYAMGLVLWEM 204
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
75-357 3.93e-13

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: 69.39  E-value: 3.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQLM----RPM--------DHPNVISLKHCFfstTSRDELFLN 142
Cdd:cd05606   1 IIGRGGFGEVYGCRKADTGKMYAMK-CLDKKRIKMKQGETLalneRIMlslvstggDCPFIVCMTYAF---QTPDKLCFI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPETLYRVLRHYTSSNQRMpifyvKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLV 222
Cdd:cd05606  77 LDLMNGGDLHYHLSQHGVFSEAEM-----RFYAAEVILGLEHMH-NRFIVYRDLKPANILLDEHGH-VRISDLGLACDFS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISyICSRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLvEIIKVLGTptreeircMNPNY 302
Cdd:cd05606 150 KKKPHAS-VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKH-EIDRMTLT--------MNVEL 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 303 TDfrfpqikahpwhkvfhkRMPPEAIDLASRLLQYSPSLR--C---TALEACAHPFFNEL 357
Cdd:cd05606 220 PD-----------------SFSPELKSLLEGLLQRDVSKRlgClgrGATEVKEHPFFKGV 262
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
74-363 4.17e-13

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: 70.42  E-value: 4.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRpmDHPNVISLKHCFFSTT----SRDELFLNLVMEY-V 148
Cdd:cd05624  78 KVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFR--EERNVLVNGDCQWITTlhyaFQDENYLYLVMDYyV 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPLTHqVKLCDFGSA-KVLVKGEPN 227
Cdd:cd05624 156 GGDLLTLLSKF---EDKLPEDMARFYIGEMVLAIHSIHQLHYV-HRDIKPDNVLLDMNGH-IRLADFGSClKMNDDGTVQ 230
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 228 ISY-ICSRYYRAPELIF----GATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIkvlgtpTREEircmnpny 302
Cdd:cd05624 231 SSVaVGTPDYISPEILQamedGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM------NHEE-------- 296
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 303 tDFRFPqikAHPwhkvfhKRMPPEAIDLASRLL-QYSPSLRCTALEAC-AHPFFNELREPNAR 363
Cdd:cd05624 297 -RFQFP---SHV------TDVSEEAKDLIQRLIcSRERRLGQNGIEDFkKHAFFEGLNWENIR 349
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
104-315 4.27e-13

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: 68.93  E-value: 4.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 104 DRRYknRELQLMRPMDHPNVISLKHCFFSTtsrDELFLNLVMEYVPETlyRVLRHYT----SSNQrmpifyVKLYTYQIF 179
Cdd:cd14118  59 DRVY--REIAILKKLDHPNVVKLVEVLDDP---NEDNLYMVFELVDKG--AVMEVPTdnplSEET------ARSYFRDIV 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 180 RGLAYIHtVPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEPNISYIC-SRYYRAPE-LIFGATEYTA-SIDIWS 256
Cdd:cd14118 126 LGIEYLH-YQKIIHRDIKPSNLLLGDDGH-VKIADFGVSNEFEGDDALLSSTAgTPAFMAPEaLSESRKKFSGkALDIWA 203
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 257 AGCVLAELLLGQPLFPGENsVDQLVEIIK----------VLGTPTREEIRCM---NPNyTDFRFPQIKAHPW 315
Cdd:cd14118 204 MGVTLYCFVFGRCPFEDDH-ILGLHEKIKtdpvvfpddpVVSEQLKDLILRMldkNPS-ERITLPEIKEHPW 273
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
76-353 4.79e-13

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: 68.88  E-value: 4.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAiKKVLQDRRYKN-----------RELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLV 144
Cdd:cd14195  13 LGSGQFAIVRKCREKGTGKEYA-AKFIKKRRLSSsrrgvsreeieREVNILREIQHPNIITLHDIFENKTD-----VVLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVP-ETLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLLV---DPLTHQVKLCDFGSAKV 220
Cdd:cd14195  87 LELVSgGELFDFLAEKESLTEEEATQFLK----QILDGVHYLHS-KRIAHFDLKPENIMLldkNVPNPRIKLIDFGIAHK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 LVKGEPNISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeircmnp 300
Cdd:cd14195 162 IEAGNEFKNIFGTPEFVAPEIV-NYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAV-------------- 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 301 NYtDFrfpqikahpwHKVFHKRMPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14195 227 NY-DF----------DEEYFSNTSELAKDFIRRLLVKDPKKRMTIAQSLEHSW 268
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
70-354 6.14e-13

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: 68.49  E-value: 6.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYKN--RELQLMRPMDHPNVIslkHCFFSTTSRDELFLNLVM 145
Cdd:cd14191   4 YDIEERLGSGKFGQVFRLVEKKTKKVWAGKffKAYSAKEKENirQEISIMNCLHHPKLV---QCVDAFEEKANIVMVLEM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLL-VDPLTHQVKLCDFGSAKVLVKG 224
Cdd:cd14191  81 VSGGELFERIIDEDFELTERECIKYMR----QISEGVEYIHK-QGIVHLDLKPENIMcVNKTGTKIKLIDFGLARRLENA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRYYRAPELI-FGATEYtaSIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVlgtptreeircmNPNYT 303
Cdd:cd14191 156 GSLKVLFGTPEFVAPEVInYEPIGY--ATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSA------------TWDFD 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 304 DFRFPQIKahpwhkvfhkrmpPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14191 222 DEAFDEIS-------------DDAKDFISNLLKKDMKARLTCTQCLQHPWL 259
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
74-265 6.88e-13

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: 68.42  E-value: 6.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIV----FQAKCLETGESVAIKKVLQDRRYKN-----RELQLMRPMDHPNVISLKHCFFSTTSRDelfLNLV 144
Cdd:cd05079  10 RDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHiadlkKEIEILRNLYHENIVKYKGICTEDGGNG---IKLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPETlyrVLRHYTSSNQ-RMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvk 223
Cdd:cd05079  87 MEFLPSG---SLKEYLPRNKnKINLKQQLKYAVQICKGMDYLGSRQYV-HRDLAARNVLVES-EHQVKIGDFGLTKAI-- 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 224 gEPNISYICSR-------YYRAPELIFGATEYTASiDIWSAGCVLAELL 265
Cdd:cd05079 160 -ETDKEYYTVKddldspvFWYAPECLIQSKFYIAS-DVWSFGVTLYELL 206
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
74-363 7.57e-13

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: 68.91  E-value: 7.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPM-------DHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd05597   7 KVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREErdvlvngDRRWITKLHYAF-----QDENYLYLVMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 -YVPETLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGe 225
Cdd:cd05597  82 yYCGGDLLTLLSKF---EDRLPEEMARFYLAEMVLAIDSIHQL-GYVHRDIKPDNVLLDRNGH-IRLADFGSCLKLRED- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 pniSYICSRY------YRAPElIFGATE-----YTASIDIWSAGCVLAELLLGQPLFPGENsvdqLVEiikvlgtpTREE 294
Cdd:cd05597 156 ---GTVQSSVavgtpdYISPE-ILQAMEdgkgrYGPECDWWSLGVCMYEMLYGETPFYAES----LVE--------TYGK 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 295 IrcMNpNYTDFRFPQIKahpwhkvfhKRMPPEAIDLASRLLQySPSLRC--TALEAC-AHPFFNELREPNAR 363
Cdd:cd05597 220 I--MN-HKEHFSFPDDE---------DDVSEEAKDLIRRLIC-SRERRLgqNGIDDFkKHPFFEGIDWDNIR 278
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
74-271 8.25e-13

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 68.85  E-value: 8.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   74 RVVGTGSFGIVFQAKCL-ETGESVAIKKVLQDRRYKNR-------ELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVM 145
Cdd:PTZ00426  36 RTLGTGSFGRVILATYKnEDFPPVAIKRFEKSKIIKQKqvdhvfsERKILNYINHPFCVNLYGSF-----KDESYLYLVL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  146 EYV-PETLYRVLRHytssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvkg 224
Cdd:PTZ00426 111 EFViGGEFFTFLRR----NKRFPNDVGCFYAAQIVLIFEYLQSL-NIVYRDLKPENLLLDK-DGFIKMTDFGFAKVV--- 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 42571361  225 EPNISYIC-SRYYRAPELIFGATEYTASiDIWSAGCVLAELLLGQPLF 271
Cdd:PTZ00426 182 DTRTYTLCgTPEYIAPEILLNVGHGKAA-DWWTLGIFIYEILVGCPPF 228
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
76-295 1.20e-12

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: 67.53  E-value: 1.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESV-AIKKV----LQDRRYKNR----------ELQLMRP-MDHPNVISLKHCFfstTSRDEL 139
Cdd:cd08528   8 LGSGAFGCVYKVRKKSNGQTLlALKEInmtnPAFGRTEQErdksvgdiisEVNIIKEqLRHPNIVRYYKTF---LENDRL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 140 FLnlVMEYVPETLYRvlRHYTS---SNQRMP---IFYVKLytyQIFRGLAYIHTVPGVCHRDVKPQNLLVDPlTHQVKLC 213
Cdd:cd08528  85 YI--VMELIEGAPLG--EHFSSlkeKNEHFTedrIWNIFV---QMVLALRYLHKEKQIVHRDLKPNNIMLGE-DDKVTIT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 214 DFGSAKvlvKGEPNISYICSR----YYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKVLGT 289
Cdd:cd08528 157 DFGLAK---QKGPESSKMTSVvgtiLYSCPE-IVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYE 232

                ....*.
gi 42571361 290 PTREEI 295
Cdd:cd08528 233 PLPEGM 238
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
71-353 1.83e-12

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: 66.94  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  71 MAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQL-MRPMDHPNVISLKHcFFSTTSRDELFLNLVMEYVP 149
Cdd:cd14172   7 LSKQVLGLGVNGKVLECFHRRTGQKCALK-LLYDSPKARREVEHhWRASGGPHIVHILD-VYENMHHGKRCLLIIMECME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 --ETLYRVlrhytssNQRMPIFYVKLYTYQIFR----GLAYIHTVpGVCHRDVKPQNLLVDPL--THQVKLCDFGSAKVL 221
Cdd:cd14172  85 ggELFSRI-------QERGDQAFTEREASEIMRdigtAIQYLHSM-NIAHRDVKPENLLYTSKekDAVLKLTDFGFAKET 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 222 VKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvdqlveiiKVLGTPTREEIRcmnpn 301
Cdd:cd14172 157 TVQNALQTPCYTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTG--------QAISPGMKRRIR----- 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 302 YTDFRFPqikAHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14172 223 MGQYGFP---NPEWAEV-----SEEAKQLIRHLLKTDPTERMTITQFMNHPW 266
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
70-288 1.83e-12

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: 68.12  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELqlmrpmdhpNVISLKHCFFS---TTSRDELFLNLVME 146
Cdd:cd14218  12 YHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAV---------DEIKLLKCVRDsdpSDPKRETIVQLIDD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 Y------------VPETL-YRVLRHYTSSN-QRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQN------------ 200
Cdd:cd14218  83 FkisgvngvhvcmVLEVLgHQLLKWIIKSNyQGLPLPCVKSILRQVLQGLDYLHTKCKIIHTDIKPENilmcvdegyvrr 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 201 ---------------------------LLVDPLTHQ------VKLCDFGSAKVLVKGepNISYICSRYYRAPELIFGAtE 247
Cdd:cd14218 163 laaeatiwqqagapppsgssvsfgasdFLVNPLEPQnadkirVKIADLGNACWVHKH--FTEDIQTRQYRALEVLIGA-E 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 42571361 248 YTASIDIWSAGCVLAELLLGQPLF---PGENSV---DQLVEIIKVLG 288
Cdd:cd14218 240 YGTPADIWSTACMAFELATGDYLFephSGEDYTrdeDHIAHIVELLG 286
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
79-265 1.92e-12

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 67.35  E-value: 1.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  79 GSFGIVFQAKCLEtgESVAIKKV-LQDRRYKNRELQLMRP--MDHPNVISLkHCFFSTTSRDELFLNLVMEYVPE-TLYR 154
Cdd:cd14053   6 GRFGAVWKAQYLN--RLVAVKIFpLQEKQSWLTEREIYSLpgMKHENILQF-IGAEKHGESLEAEYWLITEFHERgSLCD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 155 VLRHYTSSNQRMpifyVKLYTyQIFRGLAYIHT---------VPGVCHRDVKPQNLLVDP-LThqVKLCDFGSAkvlVKG 224
Cdd:cd14053  83 YLKGNVISWNEL----CKIAE-SMARGLAYLHEdipatngghKPSIAHRDFKSKNVLLKSdLT--ACIADFGLA---LKF 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 225 EPNISY------ICSRYYRAPELIFGATEYTAS----IDIWSAGCVLAELL 265
Cdd:cd14053 153 EPGKSCgdthgqVGTRRYMAPEVLEGAINFTRDaflrIDMYAMGLVLWELL 203
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
177-354 2.31e-12

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: 67.46  E-value: 2.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 177 QIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKGepnISYICSRY-----YRAPELIFGATEYTAS 251
Cdd:cd14013 128 QILVALRKLHST-GIVHRDVKPQNIIVSEGDGQFKIIDLGAAADLRIG---INYIPKEFlldprYAPPEQYIMSTQTPSA 203
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 252 ---------------------IDIWSAGcvlaeLLLGQPLFPGENSVDQLVEIikvlgtptREEIRCMnpnytDFRFPQI 310
Cdd:cd14013 204 ppapvaaalspvlwqmnlpdrFDMYSAG-----VILLQMAFPNLRSDSNLIAF--------NRQLKQC-----DYDLNAW 265
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 311 KAHPWHKVFHKRMPPEAI---------DLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14013 266 RMLVEPRASADLREGFEIldlddgagwDLVTKLIRYKPRGRLSASAALAHPYF 318
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
63-354 2.37e-12

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: 66.88  E-value: 2.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  63 EP-KQTISYMAERVVGTGSFGIVfqAKCLE--TGESVAIKKVLQDRRYKNRELQLMRPM-------DHPNVISLkHCFFS 132
Cdd:cd14197   3 EPfQERYSLSPGRELGRGKFAVV--RKCVEkdSGKEFAAKFMRKRRKGQDCRMEIIHEIavlelaqANPWVINL-HEVYE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 133 TTSRdelfLNLVMEYVP--ETLYRVLRHYTSSNQRMPifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV---DPLT 207
Cdd:cd14197  80 TASE----MILVLEYAAggEIFNQCVADREEAFKEKD---VKRLMKQILEGVSFLHN-NNVVHLDLKPQNILLtseSPLG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 208 hQVKLCDFGSAKVLVKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvl 287
Cdd:cd14197 152 -DIKIVDFGLSRILKNSEELREIMGTPEYVAPE-ILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQ-- 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 288 gtptreeircMNPNYTDFRFPQIKAhpwhkvfhkrmppEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14197 228 ----------MNVSYSEEEFEHLSE-------------SAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
110-315 2.49e-12

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: 66.91  E-value: 2.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 110 RELQLMRPMDHPNVISLKHCFfSTTSRDELFLnlVMEYV---PETLYRVLRHYTSSNQRmpiFYVKlytyQIFRGLAYIH 186
Cdd:cd14199  74 QEIAILKKLDHPNVVKLVEVL-DDPSEDHLYM--VFELVkqgPVMEVPTLKPLSEDQAR---FYFQ----DLIKGIEYLH 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 187 tVPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLvKGEPNI--SYICSRYYRAPELIFGATEYTA--SIDIWSAGCVLA 262
Cdd:cd14199 144 -YQKIIHRDVKPSNLLVGEDGH-IKIADFGVSNEF-EGSDALltNTVGTPAFMAPETLSETRKIFSgkALDVWAMGVTLY 220
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 263 ELLLGQPLFPGENsVDQLVEIIKV--LGTPTREEI---------RCMNPN-YTDFRFPQIKAHPW 315
Cdd:cd14199 221 CFVFGQCPFMDER-ILSLHSKIKTqpLEFPDQPDIsddlkdllfRMLDKNpESRISVPEIKLHPW 284
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
64-271 3.32e-12

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 66.00  E-value: 3.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMAERvvGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNR---ELQLMRPMDHPNVISLKHCFFstTSRdelF 140
Cdd:cd14111   1 PQKPYTFLDEK--ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQGvlqEYEILKSLHHERIMALHEAYI--TPR---Y 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVPgVCHRDVKPQNLLVDPLtHQVKLCDFGSA 218
Cdd:cd14111  74 LVLIAEFCSgkELLHSLIDRFRYSEDD-----VVGYLVQILQGLEYLHGRR-VLHLDIKPDNIMVTNL-NAIKIVDFGSA 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 219 KVLvkgEPNISYICSRY-----YRAPELIFGATEYTASiDIWSAGCVLAELLLGQPLF 271
Cdd:cd14111 147 QSF---NPLSLRQLGRRtgtleYMAPEMVKGEPVGPPA-DIWSIGVLTYIMLSGRSPF 200
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
76-264 3.36e-12

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: 66.25  E-value: 3.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNRELQ-------LMRPMDHPNVISLkHCFFSTTSRDELFLNLVMEYV 148
Cdd:cd14032   9 LGRGSFKTVYKGLDTETWVEVAWCE-LQDRKLTKVERQrfkeeaeMLKGLQHPNIVRF-YDFWESCAKGKRCIVLVTELM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHT-VPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAkVLVKGEPN 227
Cdd:cd14032  87 TSG---TLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTrTPPIIHRDLKCDNIFITGPTGSVKIGDLGLA-TLKRASFA 162
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42571361 228 ISYICSRYYRAPELIfgATEYTASIDIWSAGCVLAEL 264
Cdd:cd14032 163 KSVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEM 197
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
63-354 3.40e-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: 3.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  63 EPKQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPM-------DHPNVISLkHCFFSTTS 135
Cdd:cd14198   3 DNFNNFYILTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIavlelakSNPRVVNL-HEVYETTS 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 136 RdelfLNLVMEY----------VPETLYRVlrhytSSNQrmpifyVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLL--- 202
Cdd:cd14198  82 E----IILILEYaaggeifnlcVPDLAEMV-----SEND------IIRLIRQILEGVYYLHQ-NNIVHLDLKPQNILlss 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 203 VDPLThQVKLCDFGSAKVLVKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVE 282
Cdd:cd14198 146 IYPLG-DIKIVDFGMSRKIGHACELREIMGTPEYLAPE-ILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLN 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 283 IIKVlgtptreeircmNPNYTDFRFpqikahpwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14198 224 ISQV------------NVDYSEETF-------------SSVSQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
75-363 3.78e-12

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 66.67  E-value: 3.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYK-NRELQLMRPMDHPNVISLKHCFFSTTS----RDELFlnLVMEY 147
Cdd:cd06637  13 LVGNGTYGQVYKGRHVKTGQLAAIKvmDVTGDEEEEiKQEINMLKKYSHHRNIATYYGAFIKKNppgmDDQLW--LVMEF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPETLYRVLRHYTSSNQrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK--GE 225
Cdd:cd06637  91 CGAGSVTDLIKNTKGNT-LKEEWIAYICREILRGLSHLHQ-HKVIHRDIKGQNVLLTE-NAEVKLVDFGVSAQLDRtvGR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 226 PNiSYICSRYYRAPELIF----GATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEIIKvlgtptreeircmNPN 301
Cdd:cd06637 168 RN-TFIGTPYWMAPEVIAcdenPDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPR-------------NPA 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 302 ytdfrfPQIKAHPWHKVFHKrmppeaidLASRLLQYSPSLRCTALEACAHPFFNElrEPNAR 363
Cdd:cd06637 234 ------PRLKSKKWSKKFQS--------FIESCLVKNHSQRPSTEQLMKHPFIRD--QPNER 279
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
76-265 5.22e-12

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 65.62  E-value: 5.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYKNRELQLMRPMDHPNVISlkhcFFSTTSRDElFLNLVMEYVP-ETL 152
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKiyKNDVDQHKIVREISLLQKLSHPNIVR----YLGICVKDE-KLHPILEYVSgGCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 153 YRVLrhytsSNQRMPIFY---VKLYTyQIFRGLAYIHTvPGVCHRDVKPQNLLV--DPLTHQVKLCDFGSAKVLVKGEPN 227
Cdd:cd14156  76 EELL-----AREELPLSWrekVELAC-DISRGMVYLHS-KNIYHRDLNSKNCLIrvTPRGREAVVTDFGLAREVGEMPAN 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 42571361 228 -----ISYICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELL 265
Cdd:cd14156 149 dperkLSLVGSAFWMAPEMLRG-EPYDRKVDVFSFGIVLCEIL 190
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
76-271 6.70e-12

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 65.24  E-value: 6.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCleTGESVAIKkvlqdrRYKN-------------RELQLMRPMDHPNVISlkhcFFSTTSRDELFLN 142
Cdd:cd14064   1 IGSGSFGKVYKGRC--RNKIVAIK------RYRAntycsksdvdmfcREVSILCRLNHPCVIQ----FVGACLDDPSQFA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVL---RHYTSSNQRMPIfyvklyTYQIFRGLAYIHTVPG-VCHRDVKPQNLLVDPLTHQVkLCDFGS 217
Cdd:cd14064  69 IVTQYVSGgSLFSLLheqKRVIDLQSKLII------AVDVAKGMEYLHNLTQpIIHRDLNSHNILLYEDGHAV-VADFGE 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 218 AKVL--------VKGEPNISYIcsryyrAPELIFGATEYTASIDIWSAGCVLAELLLGQPLF 271
Cdd:cd14064 142 SRFLqsldednmTKQPGNLRWM------APEVFTQCTRYSIKADVFSYALCLWELLTGEIPF 197
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
77-268 8.11e-12

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: 64.97  E-value: 8.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIK--KVLQDRRYKNRELQLMRPMDhpnviSLKH-CFFSTTSRDELFLNLVMEYVPETLY 153
Cdd:cd14017   9 GGGGFGEIYKVRDVVDGEEVAMKveSKSQPKQVLKMEVAVLKKLQ-----GKPHfCRLIGCGRTERYNYIVMTLLGPNLA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 154 RVLR-----HYTSSNQ-RMPIfyvklytyQIFRGLAYIHTVpGVCHRDVKPQNLL--VDPLT-HQVKLCDFGSAKVLVKG 224
Cdd:cd14017  84 ELRRsqprgKFSVSTTlRLGI--------QILKAIEDIHEV-GFLHRDVKPSNFAigRGPSDeRTVYILDFGLARQYTNK 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 225 EPNIsyicSRYYRAPELIFGATEYtASI------------DIWSAGCVLAELLLGQ 268
Cdd:cd14017 155 DGEV----ERPPRNAAGFRGTVRY-ASVnahrnkeqgrrdDLWSWFYMLIEFVTGQ 205
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
174-334 9.30e-12

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: 65.79  E-value: 9.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 174 YTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNISYICSRY---YRAPELIFGATeYTA 250
Cdd:cd14207 185 YSFQVARGMEFLSSRKCI-HRDLAARNILLSE-NNVVKICDFGLARDIYKNPDYVRKGDARLplkWMAPESIFDKI-YST 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 251 SIDIWSAGCVLAELL-LGQPLFPGensvdqlVEIIKVLGTPTREEIRCMNPNYTDFRFPQIKAHPWHKVFHKRmpPEAID 329
Cdd:cd14207 262 KSDVWSYGVLLWEIFsLGASPYPG-------VQIDEDFCSKLKEGIRMRAPEFATSEIYQIMLDCWQGDPNER--PRFSE 332

                ....*
gi 42571361 330 LASRL 334
Cdd:cd14207 333 LVERL 337
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
76-281 1.25e-11

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: 64.34  E-value: 1.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETgesVAIKKV-------LQDRRYKNrELQLMRPMDHPNVIslkhCFFSTTSRDELflNLVMEYV 148
Cdd:cd14062   1 IGSGSFGTVYKGRWHGD---VAVKKLnvtdptpSQLQAFKN-EVAVLRKTRHVNIL----LFMGYMTKPQL--AIVTQWC 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P-ETLYRvlrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNL-LVDPLThqVKLCDFGSAKVLVK--- 223
Cdd:cd14062  71 EgSSLYK---HLHVLETKFEMLQLIDIARQTAQGMDYLHA-KNIIHRDLKSNNIfLHEDLT--VKIGDFGLATVKTRwsg 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 224 GEPNISYICSRYYRAPELI--FGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLV 281
Cdd:cd14062 145 SQQFEQPTGSILWMAPEVIrmQDENPYSFQSDVYAFGIVLYELLTGQLPYSHINNRDQIL 204
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
76-264 1.71e-11

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: 64.30  E-value: 1.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNRELQ-------LMRPMDHPNVISLKHCFfSTTSRDELFLNLVMEYV 148
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTVEVAWCE-LQDRKLSKSERQrfkeeagMLKGLQHPNIVRFYDSW-ESTVKGKKCIVLVTELM 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHT-VPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAkVLVKGEPN 227
Cdd:cd14030 111 TSG---TLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTrTPPIIHRDLKCDNIFITGPTGSVKIGDLGLA-TLKRASFA 186
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42571361 228 ISYICSRYYRAPELIfgATEYTASIDIWSAGCVLAEL 264
Cdd:cd14030 187 KSVIGTPEFMAPEMY--EEKYDESVDVYAFGMCMLEM 221
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
70-284 2.59e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 65.04  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   70 YMAERVVGTGSFGIVFQA-KCLETGESVAIKKV-LQDRR---YKNRELQLMRPMDHPNVIslKHcFFSTTSRDELFLnlV 144
Cdd:PTZ00267  69 YVLTTLVGRNPTTAAFVAtRGSDPKEKVVAKFVmLNDERqaaYARSELHCLAACDHFGIV--KH-FDDFKSDDKLLL--I 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  145 MEY-----VPETLYRVLRhytssnQRMPI--FYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGS 217
Cdd:PTZ00267 144 MEYgsggdLNKQIKQRLK------EHLPFqeYEVGLLFYQIVLALDEVHS-RKMMHRDLKSANIFLMP-TGIIKLGDFGF 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  218 AKVL---VKGEPNISYICSRYYRAPELiFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEII 284
Cdd:PTZ00267 216 SKQYsdsVSLDVASSFCGTPYYLAPEL-WERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVL 284
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
65-265 3.16e-11

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: 63.89  E-value: 3.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  65 KQTiSYMAERVVGTGSFGIVFQAKCLETGES----VAIKKVLQDRRYK-NREL----QLMRPMDHPNVISLKH-CFFSTt 134
Cdd:cd05108   5 KET-EFKKIKVLGSGAFGTVYKGLWIPEGEKvkipVAIKELREATSPKaNKEIldeaYVMASVDNPHVCRLLGiCLTST- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 135 srdelfLNLVMEYVPetlYRVLRHYTSSNQ-RMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPLTHqVKLC 213
Cdd:cd05108  83 ------VQLITQLMP---FGCLLDYVREHKdNIGSQYLLNWCVQIAKGMNYLEDRRLV-HRDLAARNVLVKTPQH-VKIT 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 214 DFGSAKVLVKGEPNISYICSRY---YRAPELIFGATeYTASIDIWSAGCVLAELL 265
Cdd:cd05108 152 DFGLAKLLGAEEKEYHAEGGKVpikWMALESILHRI-YTHQSDVWSYGVTVWELM 205
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
71-353 3.84e-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: 63.51  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  71 MAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELqLMRPMDHPNVISLKHcFFSTTSRDEL-FLNL 143
Cdd:cd14173   5 LQEEVLGEGAYARVQTCINLITNKEYAVKIIekrpghSRSRVFREVEM-LYQCQGHRNVLELIE-FFEEEDKFYLvFEKM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPETLYRvLRHYtssNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQ---VKLCDF--GSA 218
Cdd:cd14173  83 RGGSILSHIHR-RRHF---NELEASVVVQ----DIASALDFLHN-KGIAHRDLKPENILCEH-PNQvspVKICDFdlGSG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVK-----GEPNISYIC-SRYYRAPELIFGATE----YTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEiiKVLG 288
Cdd:cd14173 153 IKLNSdcspiSTPELLTPCgSAEYMAPEVVEAFNEeasiYDKRCDLWSLGVILYIMLSGYPPFVGRCGSDCGWD--RGEA 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 289 TPTREEIRCMNPNYTDFRFPQikaHPWHKVfhkrmPPEAIDLASRLLQYSPSLRCTALEACAHPF 353
Cdd:cd14173 231 CPACQNMLFESIQEGKYEFPE---KDWAHI-----SCAAKDLISKLLVRDAKQRLSAAQVLQHPW 287
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
74-273 4.30e-11

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: 62.69  E-value: 4.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGEsVAIKKVLQDRRYKN---RELQLMRPMDHPNVISLkhcfFSTTSRDELFLnLVMEYVPE 150
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGTTK-VAVKTLKPGTMSPEaflQEAQIMKKLRHDKLVQL----YAVCSDEEPIY-IVTELMSK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 -TLYRVLRHYTSSNQRMPIFyVKLYTyQIFRGLAYIHtVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEpnis 229
Cdd:cd05034  75 gSLLDYLRTGEGRALRLPQL-IDMAA-QIASGMAYLE-SRNYIHRDLAARNILVGE-NNVCKVADFGLARLIEDDE---- 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 230 YICSRYYR------APELIFGATeYTASIDIWSAGCVLAELL-LGQPLFPG 273
Cdd:cd05034 147 YTAREGAKfpikwtAPEAALYGR-FTIKSDVWSFGILLYEIVtYGRVPYPG 196
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
76-265 5.13e-11

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: 62.49  E-value: 5.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYKNRELQLMRPMDHPNVISlkhcfFSTTSRDELFLNLVMEYVPetlY 153
Cdd:cd14155   1 IGSGFFSEVYKVRHRTSGQVMALKmnTLSSNRANMLREVQLMNRLSHPNILR-----FMGVCVHQGQLHALTEYIN---G 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 154 RVLRHYTSSNQRMP-IFYVKLyTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVK--LCDFGSA-KVLVKGEPN-- 227
Cdd:cd14155  73 GNLEQLLDSNEPLSwTVRVKL-ALDIARGLSYLHS-KGIFHRDLTSKNCLIKRDENGYTavVGDFGLAeKIPDYSDGKek 150
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 42571361 228 ISYICSRYYRAPELIFGATeYTASIDIWSAGCVLAELL 265
Cdd:cd14155 151 LAVVGSPYWMAPEVLRGEP-YNEKADVFSYGIILCEII 187
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
91-347 6.39e-11

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 64.48  E-value: 6.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361     91 ETGESVAIKKVLQD-----RRYK--NRELQLMRPMDHPNVISLkhcfFSTTSRDELFLNLVMEYVPEtlyRVLRHYTSSN 163
Cdd:TIGR03903    1 MTGHEVAIKLLRTDapeeeHQRArfRRETALCARLYHPNIVAL----LDSGEAPPGLLFAVFEYVPG---RTLREVLAAD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    164 QRMP-IFYVKLYTyQIFRGLAYIHTvPGVCHRDVKPQNLLVDP--LTHQVKLCDFGSAKVLVKGEPNI--------SYIC 232
Cdd:TIGR03903   74 GALPaGETGRLML-QVLDALACAHN-QGIVHRDLKPQNIMVSQtgVRPHAKVLDFGIGTLLPGVRDADvatltrttEVLG 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361    233 SRYYRAPELIFGATEyTASIDIWSAGCVLAELLLGQPLFPGENsvdqLVEIIKvlgtptreeiRCMNPnyTDFRFPQ-IK 311
Cdd:TIGR03903  152 TPTYCAPEQLRGEPV-TPNSDLYAWGLIFLECLTGQRVVQGAS----VAEILY----------QQLSP--VDVSLPPwIA 214
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 42571361    312 AHPWHKVFHKRM---PPEAIDLASRLLQYSPSLRCTALE 347
Cdd:TIGR03903  215 GHPLGQVLRKALnkdPRQRAASAPALAERFRALELCALV 253
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
76-264 6.57e-11

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 62.43  E-value: 6.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKvLQDRRYKNRELQ-------LMRPMDHPNVISLKHCFFSTTSRDELFLnLVMEYV 148
Cdd:cd14031  18 LGRGAFKTVYKGLDTETWVEVAWCE-LQDRKLTKAEQQrfkeeaeMLKGLQHPNIVRFYDSWESVLKGKKCIV-LVTELM 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHT-VPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAkVLVKGEPN 227
Cdd:cd14031  96 TSG---TLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTrTPPIIHRDLKCDNIFITGPTGSVKIGDLGLA-TLMRTSFA 171
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 42571361 228 ISYICSRYYRAPELIfgATEYTASIDIWSAGCVLAEL 264
Cdd:cd14031 172 KSVIGTPEFMAPEMY--EEHYDESVDVYAFGMCMLEM 206
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
74-284 6.92e-11

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: 63.50  E-value: 6.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRpmDHPNVISLKHCFFSTT----SRDELFLNLVMEY-V 148
Cdd:cd05623  78 KVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFR--EERDVLVNGDSQWITTlhyaFQDDNNLYLVMDYyV 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPLTHqVKLCDFGSA-KVLVKGEPN 227
Cdd:cd05623 156 GGDLLTLLSKF---EDRLPEDMARFYLAEMVLAIDSVHQLHYV-HRDIKPDNILMDMNGH-IRLADFGSClKLMEDGTVQ 230
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 228 ISY-ICSRYYRAPELIF----GATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEII 284
Cdd:cd05623 231 SSVaVGTPDYISPEILQamedGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIM 292
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
76-285 7.74e-11

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: 62.43  E-value: 7.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAK-----CLETGES-VAIKKVLQDRRYKN-----RELQLMRPM-DHPNVISLKHCffsTTSRDELFLnl 143
Cdd:cd05053  20 LGEGAFGQVVKAEavgldNKPNEVVtVAVKMLKDDATEKDlsdlvSEMEMMKMIgKHKNIINLLGA---CTQDGPLYV-- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLR-------HYTSSNQRMPIFYVKLY-----TYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQV 210
Cdd:cd05053  95 VVEYASKgNLREFLRarrppgeEASPDDPRVPEEQLTQKdlvsfAYQVARGMEYLASKKCI-HRDLAARNVLVTE-DNVM 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 211 KLCDFGSAKvlvkgepNISYIcsRYYR------------APELIFGATeYTASIDIWSAGCVLAELL-LGQPLFPGEnSV 277
Cdd:cd05053 173 KIADFGLAR-------DIHHI--DYYRkttngrlpvkwmAPEALFDRV-YTHQSDVWSFGVLLWEIFtLGGSPYPGI-PV 241

                ....*...
gi 42571361 278 DQLVEIIK 285
Cdd:cd05053 242 EELFKLLK 249
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
76-269 9.60e-11

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: 61.99  E-value: 9.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYK----NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVPE 150
Cdd:cd06640  12 IGKGSFGEVFKGIDNRTQQVVAIKIIdLEEAEDEiediQQEITVLSQCDSPYVTKYYGSYLKGTK-----LWIIMEYLGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQrmpiFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGE-PNIS 229
Cdd:cd06640  87 GSALDLLRAGPFDE----FQIATMLKEILKGLDYLHSEKKI-HRDIKAANVLLSE-QGDVKLADFGVAGQLTDTQiKRNT 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42571361 230 YICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQP 269
Cdd:cd06640 161 FVGTPFWMAPEVI-QQSAYDSKADIWSLGITAIELAKGEP 199
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
77-280 1.03e-10

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: 61.51  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAkcLETGESVAIKKVLQ--DRRYKNRELQLMRPMDHPNVISLKHCffSTTSRdelflNLVMEYVPE-TLY 153
Cdd:cd14068   3 GDGGFGSVYRA--VYRGEDVAVKIFNKhtSFRLLRQELVVLSHLHHPSLVALLAA--GTAPR-----MLVMELAPKgSLD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 154 RVLRHYTSSNQRMPIFYVKLytyQIFRGLAYIHTVPgVCHRDVKPQNLLVDPLTHQ----VKLCDFGSAKvlvkgepnis 229
Cdd:cd14068  74 ALLQQDNASLTRTLQHRIAL---HVADGLRYLHSAM-IIYRDLKPHNVLLFTLYPNcaiiAKIADYGIAQ---------- 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 230 YIC---------SRYYRAPELIFGATEYTASIDIWSAGCVLAELLLGqplfpGENSVDQL 280
Cdd:cd14068 140 YCCrmgiktsegTPGFRAPEVARGNVIYNQQADVYSFGLLLYDILTC-----GERIVEGL 194
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
76-281 1.16e-10

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: 61.57  E-value: 1.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKcLETGESVAIKKVL-----QDRRYKNrELQLMRPMDHPNVIslkhCFFSTTSRDElFLNLVMEYVPE 150
Cdd:cd14150   8 IGTGSFGTVFRGK-WHGDVAVKILKVTeptpeQLQAFKN-EMQVLRKTRHVNIL----LFMGFMTRPN-FAIITQWCEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYrvlRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV-DPLThqVKLCDFGSAKVLVK---GEP 226
Cdd:cd14150  81 SLY---RHLHVTETRFDTMQLIDVARQTAQGMDYLHA-KNIIHRDLKSNNIFLhEGLT--VKIGDFGLATVKTRwsgSQQ 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 227 NISYICSRYYRAPELIF--GATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLV 281
Cdd:cd14150 155 VEQPSGSILWMAPEVIRmqDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQII 211
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
64-269 1.21e-10

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: 61.95  E-value: 1.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMAERVVGTGSFGIVFQAKCLETGESVAIKkVLQDRRYKNRELQ----LMRPM-DHPNVISLKHCFFSTTSRDE 138
Cdd:cd06638  14 PDPSDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVK-ILDPIHDIDEEIEaeynILKALsDHPNVVKFYGMYYKKDVKNG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 139 LFLNLVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLvdpLTHQ--VKLCDF 215
Cdd:cd06638  93 DQLWLVLELCNGgSVTDLVKGFLKRGERMEEPIIAYILHEALMGLQHLH-VNKTIHRDVKGNNIL---LTTEggVKLVDF 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 216 G-SAKVLVKGEPNISYICSRYYRAPELIFGA----TEYTASIDIWSAGCVLAELLLGQP 269
Cdd:cd06638 169 GvSAQLTSTRLRRNTSVGTPFWMAPEVIACEqqldSTYDARCDVWSLGITAIELGDGDP 227
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
76-267 1.24e-10

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: 61.76  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVlQDRRYKNRELQLMRPMDHPNVISLkhcfFSTTsRDELFLNLVMEYVPE-TLYR 154
Cdd:cd13991  14 IGRGSFGEVHRMEDKQTGFQCAVKKV-RLEVFRAEELMACAGLTSPRVVPL----YGAV-REGPWVNIFMDLKEGgSLGQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 155 VLRHYTSSNQRMPIFYVklytYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKGEPNISYICSR 234
Cdd:cd13991  88 LIKEQGCLPEDRALHYL----GQALEGLEYLHS-RKILHGDVKADNVLLSSDGSDAFLCDFGHAECLDPDGLGKSLFTGD 162
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 42571361 235 Y------YRAPELIFGaTEYTASIDIWSAGCVLAELLLG 267
Cdd:cd13991 163 YipgtetHMAPEVVLG-KPCDAKVDVWSSCCMMLHMLNG 200
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
93-292 2.10e-10

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: 60.87  E-value: 2.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  93 GESVAIKKVLQDRRYKN---RELQLMRPMDHPNVISlkhcFFST-TSRDELFLnlVMEYVPE-TLYRVLRhytssNQRMP 167
Cdd:cd13992  25 GRTVAIKHITFSRTEKRtilQELNQLKELVHDNLNK----FIGIcINPPNIAV--VTEYCTRgSLQDVLL-----NREIK 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 168 I--FYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNISYICSRYYR----APEL 241
Cdd:cd13992  94 MdwMFKSSFIKDIVKGMNYLHSSSIGYHGRLKSSNCLVDS-RWVVKLTDFGLRNLLEEQTNHQLDEDAQHKKllwtAPEL 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 242 IFGATEY---TASIDIWSAGCVLAELLLGQPLFPGEnSVDQLVEIIKVLGTPTR 292
Cdd:cd13992 173 LRGSLLEvrgTQKGDVYSFAIILYEILFRSDPFALE-REVAIVEKVISGGNKPF 225
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
76-269 2.38e-10

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 60.86  E-value: 2.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYK----NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVPE 150
Cdd:cd06641  12 IGKGSFGEVFKGIDNRTQKVVAIKIIdLEEAEDEiediQQEITVLSQCDSPYVTKYYGSYLKDTK-----LWIIMEYLGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRhytssnQRMPIFYVKLYTY--QIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNI 228
Cdd:cd06641  87 GSALDLL------EPGPLDETQIATIlrEILKGLDYLHSEKKI-HRDIKAANVLLSE-HGEVKLADFGVAGQLTDTQIKR 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42571361 229 S-YICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQP 269
Cdd:cd06641 159 N*FVGTPFWMAPEVI-KQSAYDSKADIWSLGITAIELARGEP 199
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
77-264 3.20e-10

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: 60.05  E-value: 3.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAK-CLETGE--SVAIKKVLQDRRYKN-------RELQLMRPMDHPNVISLKHCFFSTTsrdelfLNLVME 146
Cdd:cd05040   4 GDGSFGVVRRGEwTTPSGKviQVAVKCLKSDVLSQPnamddflKEVNAMHSLDHPNLIRLYGVVLSSP------LMMVTE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP-ETLYRVLRhytSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGE 225
Cdd:cd05040  78 LAPlGSLLDRLR---KDQGHFLISTLCDYAVQIANGMAYLESKRFI-HRDLAARNILLAS-KDKVKIGDFGLMRALPQNE 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 226 pnisyicsRYYR------------APELIFGATEYTASiDIWSAGCVLAEL 264
Cdd:cd05040 153 --------DHYVmqehrkvpfawcAPESLKTRKFSHAS-DVWMFGVTLWEM 194
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
98-287 3.29e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 61.40  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   98 IKKVLQDRRYKNRELQLMRPMDHPNVISLKHCFfsttsRDELFLNLVMEYVPETLYRvlrhYTSSNQRMPIFYVKLYTYQ 177
Cdd:PHA03207 123 IVKAVTGGKTPGREIDILKTISHRAIINLIHAY-----RWKSTVCMVMPKYKCDLFT----YVDRSGPLPLEQAITIQRR 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  178 IFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHQVkLCDFGSAKVLvkGEPNISYICSRY-----YRAPELIfGATEYTASI 252
Cdd:PHA03207 194 LLEALAYLHG-RGIIHRDVKTENIFLDEPENAV-LGDFGAACKL--DAHPDTPQCYGWsgtleTNSPELL-ALDPYCAKT 268
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 42571361  253 DIWSAGCVLAELLLGQ-PLFPGEN--SVDQLVEIIKVL 287
Cdd:PHA03207 269 DIWSAGLVLFEMSVKNvTLFGKQVksSSSQLRSIIRCM 306
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
74-261 3.43e-10

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 60.65  E-value: 3.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVlQDRRYKNRELQLMR-------PMDHPNVISLKHCFFSttsRDELFLNLVME 146
Cdd:cd13977   6 REVGRGSYGVVYEAVVRRTGARVAVKKI-RCNAPENVELALREfwalssiQRQHPNVIQLEECVLQ---RDGLAQRMSHG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETLYRVLRHYTSSNQRM-----PIF---------------YV----------KLYTYQIFRGLAYIHTvPGVCHRDV 196
Cdd:cd13977  82 SSKSDLYLLLVETSLKGERCfdprsACYlwfvmefcdggdmneYLlsrrpdrqtnTSFMLQLSSALAFLHR-NQIVHRDL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 197 KPQNLLV-----DPLthqVKLCDFGSAKVLVKGEPN-----------ISYIC-SRYYRAPELIFGatEYTASIDIWSAGC 259
Cdd:cd13977 161 KPDNILIshkrgEPI---LKVADFGLSKVCSGSGLNpeepanvnkhfLSSACgSDFYMAPEVWEG--HYTAKADIFALGI 235

                ..
gi 42571361 260 VL 261
Cdd:cd13977 236 II 237
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
46-275 3.86e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 61.42  E-value: 3.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   46 DAVTGHIIST---TIGGKNGEPK-QTISYMAERVVGTGSFGIVFQAKCLETGESVAIKKV------LQDRRYKNRELQLM 115
Cdd:PTZ00283   6 DAMIGRVCRTfpdTFAKDEATAKeQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVdmegmsEADKNRAQAEVCCL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  116 RPMDHPNVISLKHCFFSTTSRDE---LFLNLVMEYVPE-TLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGV 191
Cdd:PTZ00283  86 LNCDFFSIVKCHEDFAKKDPRNPenvLMIALVLDYANAgDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHS-KHM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  192 CHRDVKPQNLLV--DPLthqVKLCDFGSAKVL---VKGEPNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLL 266
Cdd:PTZ00283 165 IHRDIKSANILLcsNGL---VKLGDFGFSKMYaatVSDDVGRTFCGTPYYVAPE-IWRRKPYSKKADMFSLGVLLYELLT 240

                 ....*....
gi 42571361  267 GQPLFPGEN 275
Cdd:PTZ00283 241 LKRPFDGEN 249
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
174-316 4.70e-10

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: 60.76  E-value: 4.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 174 YTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNISYICSRY---YRAPELIFGATeYTA 250
Cdd:cd05103 184 YSFQVAKGMEFLASRKCI-HRDLAARNILLSE-NNVVKICDFGLARDIYKDPDYVRKGDARLplkWMAPETIFDRV-YTI 260
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 251 SIDIWSAGCVLAELL-LGQPLFPGensvdqlVEIIKVLGTPTREEIRCMNPNYTDFRFPQIKAHPWH 316
Cdd:cd05103 261 QSDVWSFGVLLWEIFsLGASPYPG-------VKIDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWH 320
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
74-265 5.43e-10

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 59.65  E-value: 5.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK---KVLQDRRY--KNREL----QLMRPMDHPNVISLKH-CFFSTtsrdelfLNL 143
Cdd:cd05109  13 KVLGSGAFGTVYKGIWIPDGENVKIPvaiKVLRENTSpkANKEIldeaYVMAGVGSPYVCRLLGiCLTST-------VQL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPetlYRVLRHYTSSNQ-RMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPLTHqVKLCDFGSAKVLV 222
Cdd:cd05109  86 VTQLMP---YGCLLDYVRENKdRIGSQDLLNWCVQIAKGMSYLEEVRLV-HRDLAARNVLVKSPNH-VKITDFGLARLLD 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42571361 223 KGEPNISYICSRY---YRAPELIFgATEYTASIDIWSAGCVLAELL 265
Cdd:cd05109 161 IDETEYHADGGKVpikWMALESIL-HRRFTHQSDVWSYGVTVWELM 205
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
73-285 6.61e-10

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: 59.66  E-value: 6.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQ--AKCLETGES---VAIKKV-----LQDRRYKNRELQLMRPMDHPNVISLkhcfFSTTSRDELFLn 142
Cdd:cd05032  11 IRELGQGSFGMVYEglAKGVVKGEPetrVAIKTVnenasMRERIEFLNEASVMKEFNCHHVVRL----LGVVSTGQPTL- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPE-TLYRVLRHYTSSNQ----RMPIFYVKLYTY--QIFRGLAYIHTVPgVCHRDVKPQNLLV-DPLThqVKLCD 214
Cdd:cd05032  86 VVMELMAKgDLKSYLRSRRPEAEnnpgLGPPTLQKFIQMaaEIADGMAYLAAKK-FVHRDLAARNCMVaEDLT--VKIGD 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 215 FGSAKvlvkgepNISYicSRYYR------------APELIFGATeYTASIDIWSAGCVLAELL-LGQPLFPGEnSVDQLV 281
Cdd:cd05032 163 FGMTR-------DIYE--TDYYRkggkgllpvrwmAPESLKDGV-FTTKSDVWSFGVVLWEMAtLAEQPYQGL-SNEEVL 231

                ....
gi 42571361 282 EIIK 285
Cdd:cd05032 232 KFVI 235
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
74-340 6.96e-10

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 60.45  E-value: 6.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQ-DRRYKNR------ELQLMRPMDHPNVISLkhcFFSTTSRDELFLnlVME 146
Cdd:cd05625   7 KTLGIGAFGEVCLARKVDTKALYATKTLRKkDVLLRNQvahvkaERDILAEADNEWVVRL---YYSFQDKDNLYF--VMD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPETlyrvlrHYTSSNQRMPIF---YVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFG------- 216
Cdd:cd05625  82 YIPGG------DMMSLLIRMGVFpedLARFYIAELTCAVESVHKM-GFIHRDIKPDNILIDRDGH-IKLTDFGlctgfrw 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 --------SAKVLVK---------GEPNI------------------------SYICSRYYRAPELIFgATEYTASIDIW 255
Cdd:cd05625 154 thdskyyqSGDHLRQdsmdfsnewGDPENcrcgdrlkplerraarqhqrclahSLVGTPNYIAPEVLL-RTGYTQLCDWW 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 256 SAGCVLAELLLGQPLFPGENSVDQLVEIIK---VLGTPTREEircMNPNYTDF-----RFP----------QIKAHPWHK 317
Cdd:cd05625 233 SVGVILFEMLVGQPPFLAQTPLETQMKVINwqtSLHIPPQAK---LSPEASDLiiklcRGPedrlgkngadEIKAHPFFK 309
                       330       340
                ....*....|....*....|...
gi 42571361 318 vfhkrmppeAIDLASRLLQYSPS 340
Cdd:cd05625 310 ---------TIDFSSDLRQQSAP 323
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
74-273 7.47e-10

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: 59.81  E-value: 7.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGES-----VAIKKVLQDRRYKNR-----ELQLMRPM-DHPNVISLkhcFFSTTSRDELFln 142
Cdd:cd05055  41 KTLGAGAFGKVVEATAYGLSKSdavmkVAVKMLKPTAHSSERealmsELKIMSHLgNHENIVNL---LGACTIGGPIL-- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVpetLYRVLRHYTSSNQRMPIFYVKL--YTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd05055 116 VITEYC---CYGDLLNFLRRKRESFLTLEDLlsFSYQVAKGMAFLASKNCI-HRDLAARNVLLTH-GKIVKICDFGLARD 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 221 LVKGEPNISYICSRY---YRAPELIFGATeYTASIDIWSAGCVLAELL-LGQPLFPG 273
Cdd:cd05055 191 IMNDSNYVVKGNARLpvkWMAPESIFNCV-YTFESDVWSYGILLWEIFsLGSNPYPG 246
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
74-336 9.51e-10

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 59.02  E-value: 9.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGES---VAIKKV-----LQDRRYKNRELQLMRPMDHPNVISLkhcfFSTTSRDElflNLVM 145
Cdd:cd05058   1 EVIGKGHFGCVYHGTLIDSDGQkihCAVKSLnritdIEEVEQFLKEGIIMKDFSHPNVLSL----LGICLPSE---GSPL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPETLYRVLRHYTSSNQRMPIfyVK---LYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLV 222
Cdd:cd05058  74 VVLPYMKHGDLRNFIRSETHNPT--VKdliGFGLQVAKGMEYLASKKFV-HRDLAARNCMLDE-SFTVKVADFGLARDIY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEpnisYICSRYYRAPEL--IFGATE------YTASIDIWSAGCVLAELLL-GQPLFPGENSVDQLVEIIKvlGTPTRE 293
Cdd:cd05058 150 DKE----YYSVHNHTGAKLpvKWMALEslqtqkFTTKSDVWSFGVLLWELMTrGAPPYPDVDSFDITVYLLQ--GRRLLQ 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42571361 294 EIRCMNPNYtdfrfpQIKAHPWHKVFHKRmpPEAIDLASRLLQ 336
Cdd:cd05058 224 PEYCPDPLY------EVMLSCWHPKPEMR--PTFSELVSRISQ 258
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
75-265 9.75e-10

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 59.21  E-value: 9.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCleTGESVAIKKV-LQDRRYKNRE-----LQLMRpmdHPNVIslkhCF-----FSTTSRDELFLnl 143
Cdd:cd14056   2 TIGKGRYGEVWLGKY--RGEKVAVKIFsSRDEDSWFREteiyqTVMLR---HENIL----GFiaadiKSTGSWTQLWL-- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLRHYTSSNQRMpifyVKLyTYQIFRGLAYIHTV-------PGVCHRDVKPQNLLV-DPLThqvklC- 213
Cdd:cd14056  71 ITEYHEHgSLYDYLQRNTLDTEEA----LRL-AYSAASGLAHLHTEivgtqgkPAIAHRDLKSKNILVkRDGT-----Cc 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 214 --DFG------SAKVLVKGEPNISyICSRYYRAPELI---FGATEYTASI--DIWSAGCVLAELL 265
Cdd:cd14056 141 iaDLGlavrydSDTNTIDIPPNPR-VGTKRYMAPEVLddsINPKSFESFKmaDIYSFGLVLWEIA 204
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
76-283 9.85e-10

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: 59.24  E-value: 9.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGeSVAIKKVLQDRRYKNRELQ----LMRPM-DHPNVISLKHCFFSTTSRDELFLNLVMEY--- 147
Cdd:cd06639  30 IGKGTYGKVYKVTNKKDG-SLAAVKILDPISDVDEEIEaeynILRSLpNHPNVVKFYGMFYKADQYVGGQLWLVLELcng 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 --VPETLYRVLRhytsSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLvdpLTHQ--VKLCDFGSAKVLVK 223
Cdd:cd06639 109 gsVTELVKGLLK----CGQRLDEAMISYILYGALLGLQHLHN-NRIIHRDVKGNNIL---LTTEggVKLVDFGVSAQLTS 180
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 224 GE--PNISyICSRYYRAPELIFGATEYTAS----IDIWSAGCVLAELLLGQPLFPGENSVDQLVEI 283
Cdd:cd06639 181 ARlrRNTS-VGTPFWMAPEVIACEQQYDYSydarCDVWSLGITAIELADGDPPLFDMHPVKALFKI 245
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
174-336 1.14e-09

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: 59.22  E-value: 1.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 174 YTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNISYICSRY---YRAPELIFGATeYTA 250
Cdd:cd05102 177 YSFQVARGMEFLASRKCI-HRDLAARNILLSE-NNVVKICDFGLARDIYKDPDYVRKGSARLplkWMAPESIFDKV-YTT 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 251 SIDIWSAGCVLAELL-LGQPLFPGensvdqlVEIIKVLGTPTREEIRCMNPNYTDFRFPQIKAHPWHKVFHKRMP-PEAI 328
Cdd:cd05102 254 QSDVWSFGVLLWEIFsLGASPYPG-------VQINEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPTfSDLV 326

                ....*...
gi 42571361 329 DLASRLLQ 336
Cdd:cd05102 327 EILGDLLQ 334
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
73-265 1.25e-09

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


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 58.72  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGE---SVAIKKVL-----QDRRYKNRELQLMRPMDHPNVISLKhcffSTTSRDELFLnLV 144
Cdd:cd05066   9 EKVIGAGEFGEVCSGRLKLPGKreiPVAIKTLKagyteKQRRDFLSEASIMGQFDHPNIIHLE----GVVTRSKPVM-IV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLRHYtssNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDplTHQV-KLCDFGSAKVLv 222
Cdd:cd05066  84 TEYMENgSLDAFLRKH---DGQFTVIQLVGMLRGIASGMKYLSDM-GYVHRDLAARNILVN--SNLVcKVSDFGLSRVL- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 223 KGEPNISYICSR-----YYRAPELIfGATEYTASIDIWSAGCVLAELL 265
Cdd:cd05066 157 EDDPEAAYTTRGgkipiRWTAPEAI-AYRKFTSASDVWSYGIVMWEVM 203
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
76-273 1.26e-09

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: 58.22  E-value: 1.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKK-----VLQDRRYKNRELQLMRPMDHPNVISLkhcFFSTTSRDELFlnLVMEYVPE 150
Cdd:cd05041   3 IGRGNFGDVYRGVLKPDNTEVAVKTcretlPPDLKRKFLQEARILKQYDHPNIVKL---IGVCVQKQPIM--IVMELVPG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TlyRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKLCDFGsakvLVKGEPNISY 230
Cdd:cd05041  78 G--SLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLES-KNCIHRDLAARNCLVG-ENNVLKISDFG----MSREEEDGEY 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 231 ICSRYYR-------APE-LIFGatEYTASIDIWSAGCVLAELL-LGQPLFPG 273
Cdd:cd05041 150 TVSDGLKqipikwtAPEaLNYG--RYTSESDVWSFGILLWEIFsLGATPYPG 199
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
74-273 1.28e-09

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: 58.82  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETG-----ESVAIKKVLQ-----DRRYKNRELQLMRPMDHPNVISLkhcfFSTTSRDELFLnL 143
Cdd:cd05045   6 KTLGEGEFGKVVKATAFRLKgragyTTVAVKMLKEnasssELRDLLSEFNLLKQVNHPHVIKL----YGACSQDGPLL-L 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPetlYRVLRHYTSSNQRMPIFYVKL------------------------YTYQIFRGLAYIHTVPGVcHRDVKPQ 199
Cdd:cd05045  81 IVEYAK---YGSLRSFLRESRKVGPSYLGSdgnrnssyldnpderaltmgdlisFAWQISRGMQYLAEMKLV-HRDLAAR 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 200 NLLVDPlTHQVKLCDFGSAKVLVKGEPNISYICSRY---YRAPELIFGATeYTASIDIWSAGCVLAELL-LGQPLFPG 273
Cdd:cd05045 157 NVLVAE-GRKMKISDFGLSRDVYEEDSYVKRSKGRIpvkWMAIESLFDHI-YTTQSDVWSFGVLLWEIVtLGGNPYPG 232
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
73-265 1.71e-09

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: 58.34  E-value: 1.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGES---VAIKKVL-----QDRRYKNRELQLMRPMDHPNVISLKHCFfsTTSRDELFLNLV 144
Cdd:cd05065   9 EEVIGAGEFGEVCRGRLKLPGKReifVAIKTLKsgyteKQRRDFLSEASIMGQFDHPNIIHLEGVV--TKSRPVMIITEF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEyvPETLYRVLRHytSSNQRMPIFYVKLYTyQIFRGLAYIHTVPGVcHRDVKPQNLLVDplTHQV-KLCDFGSAKVLVK 223
Cdd:cd05065  87 ME--NGALDSFLRQ--NDGQFTVIQLVGMLR-GIAAGMKYLSEMNYV-HRDLAARNILVN--SNLVcKVSDFGLSRFLED 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 42571361 224 GEPNISYICSR------YYRAPELIfGATEYTASIDIWSAGCVLAELL 265
Cdd:cd05065 159 DTSDPTYTSSLggkipiRWTAPEAI-AYRKFTSASDVWSYGIVMWEVM 205
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
74-274 1.73e-09

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 58.92  E-value: 1.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRP-------MDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd05627   8 KVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAerdilveADGAWVVKMFYSF-----QDKRNLYLIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFG-------- 216
Cdd:cd05627  83 FLPggDMMTLLMKKDTLSEEA-----TQFYIAETVLAIDAIHQL-GFIHRDIKPDNLLLDAKGH-VKLSDFGlctglkka 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 217 --------------------------SAKVLVKGEPNISY--ICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQ 268
Cdd:cd05627 156 hrtefyrnlthnppsdfsfqnmnskrKAETWKKNRRQLAYstVGTPDYIAPE-VFMQTGYNKLCDWWSLGVIMYEMLIGY 234

                ....*.
gi 42571361 269 PLFPGE 274
Cdd:cd05627 235 PPFCSE 240
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
73-316 1.85e-09

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: 58.27  E-value: 1.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGES-----VAIKKVLQDRRYKNR-----ELQLMRPM-DHPNVISL-KHCffsTTSRDELF 140
Cdd:cd05054  12 GKPLGRGAFGKVIQASAFGIDKSatcrtVAVKMLKEGATASEHkalmtELKILIHIgHHLNVVNLlGAC---TKPGGPLM 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LnlVMEYVP----ETLYRVLRHYTSSNQ-----------------RMPIFYVKL--YTYQIFRGLAYIHTVPGVcHRDVK 197
Cdd:cd05054  89 V--IVEFCKfgnlSNYLRSKREEFVPYRdkgardveeeedddelyKEPLTLEDLicYSFQVARGMEFLASRKCI-HRDLA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 198 PQNLLVDPlTHQVKLCDFGSAKVLVKgEPNisYICSRYYR------APELIFGATeYTASIDIWSAGCVLAELL-LGQPL 270
Cdd:cd05054 166 ARNILLSE-NNVVKICDFGLARDIYK-DPD--YVRKGDARlplkwmAPESIFDKV-YTTQSDVWSFGVLLWEIFsLGASP 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 42571361 271 FPGENsVDQlvEIIKVLgtptREEIRCMNPNYTDFRFPQIKAHPWH 316
Cdd:cd05054 241 YPGVQ-MDE--EFCRRL----KEGTRMRAPEYTTPEIYQIMLDCWH 279
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
73-265 2.84e-09

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: 57.38  E-value: 2.84e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGE---SVAIKKVL-----QDRRYKNRELQLMRPMDHPNVISLKhcffSTTSRDELFLnLV 144
Cdd:cd05033   9 EKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLKsgysdKQRLDFLTEASIMGQFDHPNVIRLE----GVVTKSRPVM-IV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLRHytSSNQRMPIFYVKLyTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDplTHQV-KLCDFGSAKVLv 222
Cdd:cd05033  84 TEYMENgSLDKFLRE--NDGKFTVTQLVGM-LRGIASGMKYLSEM-NYVHRDLAARNILVN--SDLVcKVSDFGLSRRL- 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 223 kGEPNISY------ICSRyYRAPELIfGATEYTASIDIWSAGCVLAELL 265
Cdd:cd05033 157 -EDSEATYttkggkIPIR-WTAPEAI-AYRKFTSASDVWSFGIVMWEVM 202
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
74-274 3.17e-09

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 58.13  E-value: 3.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRP-------MDHPNVISLKHCFfsttsRDELFLNLVME 146
Cdd:cd05628   7 KVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAerdilveADSLWVVKMFYSF-----QDKLNLYLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVP--ETLYRVLRHYTSSNQRmpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKG 224
Cdd:cd05628  82 FLPggDMMTLLMKKDTLTEEE-----TQFYIAETVLAIDSIHQL-GFIHRDIKPDNLLLDSKGH-VKLSDFGLCTGLKKA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPN------------------------------------ISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQ 268
Cdd:cd05628 155 HRTefyrnlnhslpsdftfqnmnskrkaetwkrnrrqlaFSTVGTPDYIAPE-VFMQTGYNKLCDWWSLGVIMYEMLIGY 233

                ....*.
gi 42571361 269 PLFPGE 274
Cdd:cd05628 234 PPFCSE 239
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
76-263 3.33e-09

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: 57.43  E-value: 3.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAK-CLETGESVAIKKVLQDR-RYKNRE--------LQLMRPMDHPNVISLkhcFFSTTSRDELFLNLvm 145
Cdd:cd14052   8 IGSGEFSQVYKVSeRVPTGKVYAVKKLKPNYaGAKDRLrrleevsiLRELTLDGHDNIVQL---IDSWEYHGHLYIQT-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLRHYtSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVL--- 221
Cdd:cd14052  83 ELCENgSLDVFLSEL-GLLGRLDEFRVWKILVELSLGLRFIHDH-HFVHLDLKPANVLIT-FEGTLKIGDFGMATVWpli 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 42571361 222 --VKGEPNISYICsryyraPELIFGATeYTASIDIWSAGCVLAE 263
Cdd:cd14052 160 rgIEREGDREYIA------PEILSEHM-YDKPADIFSLGLILLE 196
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
76-269 3.47e-09

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: 57.37  E-value: 3.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKV-LQDRRYK----NRELQLMRPMDHPNVISLKHCFFSTTSrdelfLNLVMEYVPE 150
Cdd:cd06642  12 IGKGSFGEVYKGIDNRTKEVVAIKIIdLEEAEDEiediQQEITVLSQCDSPYITRYYGSYLKGTK-----LWIIMEYLGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRmpifYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLvdpLTHQ--VKLCDFGSAKVLVKGE-PN 227
Cdd:cd06642  87 GSALDLLKPGPLEET----YIATILREILKGLDYLHSERKI-HRDIKAANVL---LSEQgdVKLADFGVAGQLTDTQiKR 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 42571361 228 ISYICSRYYRAPELIfGATEYTASIDIWSAGCVLAELLLGQP 269
Cdd:cd06642 159 NTFVGTPFWMAPEVI-KQSAYDFKADIWSLGITAIELAKGEP 199
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
64-279 3.51e-09

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: 57.76  E-value: 3.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMAERVVGTGSFGIVFQAKCLETGESVAIK-----KVLQDRRYKN------RELQLMRPMDHPNVISLKHCFfs 132
Cdd:cd14040   2 PTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYF-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 133 ttSRDELFLNLVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTV-PGVCHRDVKPQN-LLVDPLT-HQ 209
Cdd:cd14040  80 --SLDTDTFCTVLEYCEGN---DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIkPPIIHYDLKPGNiLLVDGTAcGE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 VKLCDFGSAKVL------VKGEPNISYICSRY-YRAPELIFGATE---YTASIDIWSAGCVLAELLLGQPLFpGENSVDQ 279
Cdd:cd14040 155 IKITDFGLSKIMdddsygVDGMDLTSQGAGTYwYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQ 233
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
79-274 3.63e-09

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: 57.97  E-value: 3.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  79 GSFGIVFQAKCLETGESVAIKKVLQ-DRRYKNRELQLMRPMD------HPNVISLkhcFFSTTSRDELFLnlVMEY-VPE 150
Cdd:cd05610  15 GAFGKVYLGRKKNNSKLYAVKVVKKaDMINKNMVHQVQAERDalalskSPFIVHL---YYSLQSANNVYL--VMEYlIGG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRMPIFYVKlytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEPNISY 230
Cdd:cd05610  90 DVKSLLHIYGYFDEEMAVKYIS----EVALALDYLHR-HGIIHRDLKPDNMLISNEGH-IKLTDFGLSKVTLNRELNMMD 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 231 ICSR---------YYRAP---------------------------------ELIFGATEYTA-----------SIDIWSA 257
Cdd:cd05610 164 ILTTpsmakpkndYSRTPgqvlslisslgfntptpyrtpksvrrgaarvegERILGTPDYLApelllgkphgpAVDWWAL 243
                       250
                ....*....|....*..
gi 42571361 258 GCVLAELLLGQPLFPGE 274
Cdd:cd05610 244 GVCLFEFLTGIPPFNDE 260
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
104-315 3.66e-09

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: 57.27  E-value: 3.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 104 DRRYKnrELQLMRPMDHPNVISLKHCFfSTTSRDELFLNL-------VMEyVPETlyrvlrHYTSSNQrmpifyVKLYTY 176
Cdd:cd14200  68 ERVYQ--EIAILKKLDHVNIVKLIEVL-DDPAEDNLYMVFdllrkgpVME-VPSD------KPFSEDQ------ARLYFR 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 177 QIFRGLAYIHtVPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEPNISYIC-SRYYRAPELIF--GATEYTASID 253
Cdd:cd14200 132 DIVLGIEYLH-YQKIVHRDIKPSNLLLGDDGH-VKIADFGVSNQFEGNDALLSSTAgTPAFMAPETLSdsGQSFSGKALD 209
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 254 IWSAGCVLAELLLGQPLFPGE------NSVDQlvEIIKVLGTPT-REEIRCM-------NPNyTDFRFPQIKAHPW 315
Cdd:cd14200 210 VWAMGVTLYCFVYGKCPFIDEfilalhNKIKN--KPVEFPEEPEiSEELKDLilkmldkNPE-TRITVPEIKVHPW 282
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
70-354 4.90e-09

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: 57.73  E-value: 4.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELqlmrpmdhpNVISLKHCFFSTTSRD---ELFLNLVME 146
Cdd:cd14217  14 YHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETAL---------DEIKLLRCVRESDPEDpnkDMVVQLIDD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE--------TLYRVLRHY------TSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVCHRDVKPQN------------ 200
Cdd:cd14217  85 FKISgmngihvcMVFEVLGHHllkwiiKSNYQGLPIRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENilmcvddayvrr 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 201 --------------------------LLVDPLTH------QVKLCDFGSAKVLVKGepNISYICSRYYRAPELIFGATeY 248
Cdd:cd14217 165 maaeatewqkagapppsgsavstapdLLVNPLDPrnadkiRVKIADLGNACWVHKH--FTEDIQTRQYRSIEVLIGAG-Y 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 249 TASIDIWSAGCVLAELLLGQPLF---PGEN---SVDQLVEIIKVLGTPTREeiRCMNPNYTDFRFPQ-------IKAHPW 315
Cdd:cd14217 242 STPADIWSTACMAFELATGDYLFephSGEDysrDEDHIAHIIELLGCIPRH--FALSGKYSREFFNRrgelrhiTKLKPW 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 42571361 316 --HKVFHKRM--PPEA----IDLASRLLQYSPSLRCTALEACAHPFF 354
Cdd:cd14217 320 slFDVLVEKYgwPHEDaaqfTDFLIPMLEMVPEKRASAGECLRHPWL 366
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
79-298 5.19e-09

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 56.90  E-value: 5.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  79 GSFGIVFQAKclETGESVAIKKvLQDRRYKNR--------------------------ELQLMRPMDHPNVISL------ 126
Cdd:cd14067   5 GSGTVIYRAR--YQGQPVAVKR-FHIKKCKKRtdgsadtmlkhlraadamknfsefrqEASMLHSLQHPCIVYLigisih 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 127 KHCFfsttsrdelflnlVMEYVP-ETLYRVLRHYTSSNQRMPIFYVKLY--TYQIFRGLAYIHTvPGVCHRDVKPQNLLV 203
Cdd:cd14067  82 PLCF-------------ALELAPlGSLNTVLEENHKGSSFMPLGHMLTFkiAYQIAAGLAYLHK-KNIIFCDLKSDNILV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 204 DPLTHQ----VKLCDFGSAK-------VLVKGEPNisyicsryYRAPELIFGATeYTASIDIWSAGCVLAELLLGQPLFP 272
Cdd:cd14067 148 WSLDVQehinIKLSDYGISRqsfhegaLGVEGTPG--------YQAPEIRPRIV-YDEKVDMFSYGMVLYELLSGQRPSL 218
                       250       260       270
                ....*....|....*....|....*....|
gi 42571361 273 GENSVDQLVEIIK----VLGTPTREEIRCM 298
Cdd:cd14067 219 GHHQLQIAKKLSKgirpVLGQPEEVQFFRL 248
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
64-279 5.55e-09

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


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 56.99  E-value: 5.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMAERVVGTGSFGIVFQAKCLETGESVAIK-----KVLQDRRYKN------RELQLMRPMDHPNVISLKHCFfs 132
Cdd:cd14041   2 PTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKihqlnKNWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYF-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 133 ttSRDELFLNLVMEYVPETlyrVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTV-PGVCHRDVKPQNLLVDPLTH--Q 209
Cdd:cd14041  80 --SLDTDSFCTVLEYCEGN---DLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIkPPIIHYDLKPGNILLVNGTAcgE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 VKLCDFGSAKVL-------VKGEPNISYICSRY-YRAPELIFGATE---YTASIDIWSAGCVLAELLLGQPLFpGENSVD 278
Cdd:cd14041 155 IKITDFGLSKIMdddsynsVDGMELTSQGAGTYwYLPPECFVVGKEppkISNKVDVWSVGVIFYQCLYGRKPF-GHNQSQ 233

                .
gi 42571361 279 Q 279
Cdd:cd14041 234 Q 234
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
84-356 9.97e-09

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 56.18  E-value: 9.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  84 VFQAKCLETGESVAI----KKVLQ--DRRYKNRELQLMRP-------MDHPNVISLKHCFfsTTSRDELflNLVMEYVPE 150
Cdd:cd14011  12 IYNGSKKSTKQEVSVfvfeKKQLEeySKRDREQILELLKRgvkqltrLRHPRILTVQHPL--EESRESL--AFATEPVFA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLRHYTSSNQRMP-IFYVKLYT-------YQIFRGLAYIHTVPGVCHRDVKPQNLLVDPLTHQvKLCDFGSAkVLV 222
Cdd:cd14011  88 SLANVLGERDNMPSPPPeLQDYKLYDveikyglLQISEALSFLHNDVKLVHGNICPESVVINSNGEW-KLAGFDFC-ISS 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 223 KGEPNISYICSRY-------------YRAPELIFGATEYTASiDIWSAGCVLAELLL-GQPLFpgensvdqlveiikvlg 288
Cdd:cd14011 166 EQATDQFPYFREYdpnlpplaqpnlnYLAPEYILSKTCDPAS-DMFSLGVLIYAIYNkGKPLF----------------- 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 289 tptreeiRCMNpNYTDF-RFPQIKAHPWHKVFHKrMPPEAIDLASRLLQYSPSLRCTALEACAHPFFNE 356
Cdd:cd14011 228 -------DCVN-NLLSYkKNSNQLRQLSLSLLEK-VPEELRDHVKTLLNVTPEVRPDAEQLSKIPFFDD 287
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
76-322 1.07e-08

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: 56.18  E-value: 1.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCL-------ETGESVAIKKVLQDRRYKN-----RELQLMRPM-DHPNVISLkhcFFSTTSRDELFLn 142
Cdd:cd05101  32 LGEGCFGQVVMAEAVgidkdkpKEAVTVAVKMLKDDATEKDlsdlvSEMEMMKMIgKHKNIINL---LGACTQDGPLYV- 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 lVMEYVPE-TLYRVLR-------HYTSSNQRMP---IFYVKLY--TYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQ 209
Cdd:cd05101 108 -IVEYASKgNLREYLRarrppgmEYSYDINRVPeeqMTFKDLVscTYQLARGMEYLASQKCI-HRDLAARNVLVTE-NNV 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 VKLCDFGsakvLVKGEPNISYICSRY-------YRAPELIFGATeYTASIDIWSAGCVLAELL-LGQPLFPGeNSVDQLV 281
Cdd:cd05101 185 MKIADFG----LARDINNIDYYKKTTngrlpvkWMAPEALFDRV-YTHQSDVWSFGVLMWEIFtLGGSPYPG-IPVEELF 258
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 42571361 282 EIIKVlGTPTREEIRCMNPNYTDFRfpqikaHPWHKVFHKR 322
Cdd:cd05101 259 KLLKE-GHRMDKPANCTNELYMMMR------DCWHAVPSQR 292
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
73-275 1.33e-08

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: 55.52  E-value: 1.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETgESVAIKKVLQDRRYKNR----ELQLMRPMDHPNVISLkhcfFSTTSRDELFlnlvmeYV 148
Cdd:cd05148  11 ERKLGSGYFGEVWEGLWKNR-VRVAIKILKSDDLLKQQdfqkEVQALKRLRHKHLISL----FAVCSVGEPV------YI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PETLYR--VLRHY--TSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV-DPLThqVKLCDFGSAKVL-- 221
Cdd:cd05148  80 ITELMEkgSLLAFlrSPEGQVLPVASLIDMACQVAEGMAYLEE-QNSIHRDLAARNILVgEDLV--CKVADFGLARLIke 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 222 ---VKGEPNISYicsrYYRAPELIfGATEYTASIDIWSAGCVLAELLL-GQPLFPGEN 275
Cdd:cd05148 157 dvyLSSDKKIPY----KWTAPEAA-SHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMN 209
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
73-272 1.43e-08

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: 55.19  E-value: 1.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGESVAIKKVL-QDRRYKNR---ELQLMRPM-DHPNVISLK-----HCFFSTTSRDELfln 142
Cdd:cd13975   5 GRELGRGQYGVVYACDSWGGHFPCALKSVVpPDDKHWNDlalEFHYTRSLpKHERIVSLHgsvidYSYGGGSSIAVL--- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 LVMEYVPETLYRVLRHYTSSNQRMPIfyvklyTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPlTHQVKLCDFGSAK--V 220
Cdd:cd13975  82 LIMERLHRDLYTGIKAGLSLEERLQI------ALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDK-KNRAKITDLGFCKpeA 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 221 LVKGepniSYICSRYYRAPELIFGatEYTASIDIWSAGCVLAELLLGQPLFP 272
Cdd:cd13975 154 MMSG----SIVGTPIHMAPELFSG--KYDNSVDVYAFGILFWYLCAGHVKLP 199
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
76-284 1.89e-08

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: 55.07  E-value: 1.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCletGESVAIKKV-------LQDRRYKNrELQLMRPMDHPNVIslkhCFFSTTSRDELflNLVMEYV 148
Cdd:cd14151  16 IGSGSFGTVYKGKW---HGDVAVKMLnvtaptpQQLQAFKN-EVGVLRKTRHVNIL----LFMGYSTKPQL--AIVTQWC 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 P-ETLYRvlrHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVK--GE 225
Cdd:cd14151  86 EgSSLYH---HLHIIETKFEMIKLIDIARQTAQGMDYLHA-KSIIHRDLKSNNIFLHE-DLTVKIGDFGLATVKSRwsGS 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 226 PNISYIC-SRYYRAPELIF--GATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEII 284
Cdd:cd14151 161 HQFEQLSgSILWMAPEVIRmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMV 222
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
73-265 2.52e-08

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: 54.59  E-value: 2.52e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGES---VAIKKVLQDRRYKNR-----ELQLMRPMDHPNVISLKHCFfsTTSRDELFLNLV 144
Cdd:cd05063  10 QKVIGAGEFGEVFRGILKMPGRKevaVAIKTLKPGYTEKQRqdflsEASIMGQFSHHNIIRLEGVV--TKFKPAMIITEY 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEyvPETLYRVLRHYtsSNQRMPIFYVKLYTyQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLvKG 224
Cdd:cd05063  88 ME--NGALDKYLRDH--DGEFSSYQLVGMLR-GIAAGMKYLSDMNYV-HRDLAARNILVNS-NLECKVSDFGLSRVL-ED 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 42571361 225 EPNISYICSR-----YYRAPELIfGATEYTASIDIWSAGCVLAELL 265
Cdd:cd05063 160 DPEGTYTTSGgkipiRWTAPEAI-AYRKFTSASDVWSFGIVMWEVM 204
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
63-264 2.55e-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: 2.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  63 EPKQTISYMAErvVGTGSFGIVFQAKCLETGE-----SVAIK--------KVLQDRRyknRELQLMRPMDHPNVIslkhC 129
Cdd:cd05048   2 IPLSAVRFLEE--LGEGAFGKVYKGELLGPSSeesaiSVAIKtlkenaspKTQQDFR---REAELMSDLQHPNIV----C 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 130 FFSTTSRDELfLNLVMEYVPE-TLYRVLrhytssNQRMPIFYVKLYT------------------YQIFRGLAYI---Ht 187
Cdd:cd05048  73 LLGVCTKEQP-QCMLFEYMAHgDLHEFL------VRHSPHSDVGVSSdddgtassldqsdflhiaIQIAAGMEYLsshH- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 188 vpgVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEpnisyicsrYYR------------APELI-FGatEYTASIDI 254
Cdd:cd05048 145 ---YVHRDLAARNCLVGD-GLTVKISDFGLSRDIYSSD---------YYRvqsksllpvrwmPPEAIlYG--KFTTESDV 209
                       250
                ....*....|
gi 42571361 255 WSAGCVLAEL 264
Cdd:cd05048 210 WSFGVVLWEI 219
pknD PRK13184
serine/threonine-protein kinase PknD;
74-265 3.36e-08

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 55.55  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   74 RVVGTGSFGIVFQAKCLETGESVAIKKVLQD----RRYKNR---ELQLMRPMDHPNVISLkhcfFSTTSRDELfLNLVME 146
Cdd:PRK13184   8 RLIGKGGMGEVYLAYDPVCSRRVALKKIREDlsenPLLKKRflrEAKIAADLIHPGIVPV----YSICSDGDP-VYYTMP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  147 YVP-ETLYRVLRHY-------------TSSNQRMPIFYvklytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDpLTHQVKL 212
Cdd:PRK13184  83 YIEgYTLKSLLKSVwqkeslskelaekTSVGAFLSIFH------KICATIEYVHS-KGVLHRDLKPDNILLG-LFGEVVI 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361  213 CDFGSAKV----------LVKGEPNISY---------ICSRYYRAPELIFGaTEYTASIDIWSAGCVLAELL 265
Cdd:PRK13184 155 LDWGAAIFkkleeedlldIDVDERNICYssmtipgkiVGTPDYMAPERLLG-VPASESTDIYALGVILYQML 225
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
174-273 4.12e-08

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 54.65  E-value: 4.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 174 YTYQIFRGLAYIHTVPGVcHRDVKPQNLLvdpLTHQ--VKLCDFGSAKVLVKGEPNIS---YICSRYYRAPELIFGATeY 248
Cdd:cd05105 242 FTYQVARGMEFLASKNCV-HRDLAARNVL---LAQGkiVKICDFGLARDIMHDSNYVSkgsTFLPVKWMAPESIFDNL-Y 316
                        90       100
                ....*....|....*....|....*.
gi 42571361 249 TASIDIWSAGCVLAELL-LGQPLFPG 273
Cdd:cd05105 317 TTLSDVWSYGILLWEIFsLGGTPYPG 342
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
64-357 4.24e-08

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: 54.20  E-value: 4.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMAErvVGTGSFGIVFQ--AKCLETGES---VAIKKVLQDRRYKNR-----ELQLMRPMDHPNVISLkhcfFST 133
Cdd:cd05061   4 SREKITLLRE--LGQGSFGMVYEgnARDIIKGEAetrVAVKTVNESASLRERieflnEASVMKGFTCHHVVRL----LGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 134 TSRDELFLnLVMEYVP----ETLYRVLRHYTSSNQRMPIFYVK---LYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPl 206
Cdd:cd05061  78 VSKGQPTL-VVMELMAhgdlKSYLRSLRPEAENNPGRPPPTLQemiQMAAEIADGMAYLNAKKFV-HRDLAARNCMVAH- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 207 THQVKLCDFGSAKVLVKGEpnisyicsrYYR------------APELIFGATeYTASIDIWSAGCVLAEL--LLGQPlFP 272
Cdd:cd05061 155 DFTVKIGDFGMTRDIYETD---------YYRkggkgllpvrwmAPESLKDGV-FTTSSDMWSFGVVLWEItsLAEQP-YQ 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 273 GEnSVDQLVEIIkvlgtptreeircMNPNYTDfrfpqikaHPwhkvfhKRMPPEAIDLASRLLQYSPSLRCTALEACA-- 350
Cdd:cd05061 224 GL-SNEQVLKFV-------------MDGGYLD--------QP------DNCPERVTDLMRMCWQFNPKMRPTFLEIVNll 275
                       330
                ....*....|.
gi 42571361 351 ----HPFFNEL 357
Cdd:cd05061 276 kddlHPSFPEV 286
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
74-269 4.37e-08

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


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 54.30  E-value: 4.37e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK---KVLQDRRYKNRELQ------LMRPMDHPNVISLKHCFFSTTsrdelfLNLV 144
Cdd:cd05110  13 KVLGSGAFGTVYKGIWVPEGETVKIPvaiKILNETTGPKANVEfmdealIMASMDHPHLVRLLGVCLSPT------IQLV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPETLYRVLRHYTSSNQRMPIFYVklYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKG 224
Cdd:cd05110  87 TQLMPHGCLLDYVHEHKDNIGSQLLLN--WCVQIAKGMMYLEE-RRLVHRDLAARNVLVKSPNH-VKITDFGLARLLEGD 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 42571361 225 EPNISYICSRY---YRAPELIFgATEYTASIDIWSAGCVLAELLL--GQP 269
Cdd:cd05110 163 EKEYNADGGKMpikWMALECIH-YRKFTHQSDVWSYGVTIWELMTfgGKP 211
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
75-273 4.68e-08

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: 53.86  E-value: 4.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKcLETGESVAIKKVLQD--RRYKNR---ELQLMRPMDHPNVISLkhcFFSTTSRDELFlnLVMEYVP 149
Cdd:cd05085   3 LLGKGNFGEVYKGT-LKDKTPVAVKTCKEDlpQELKIKflsEARILKQYDHPNIVKL---IGVCTQRQPIY--IVMELVP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYrvLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGsakvLVKGEPNIS 229
Cdd:cd05085  77 GGDF--LSFLRKKKDELKTKQLVKFSLDAAAGMAYLES-KNCIHRDLAARNCLVGE-NNALKISDFG----MSRQEDDGV 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 230 YICSRY------YRAPE-LIFGatEYTASIDIWSAGCVLAELL-LGQPLFPG 273
Cdd:cd05085 149 YSSSGLkqipikWTAPEaLNYG--RYSSESDVWSFGILLWETFsLGVCPYPG 198
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
177-355 6.00e-08

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 54.80  E-value: 6.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  177 QIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLVKGepnISYICSRY-----YRAPELIFGATEyTAS 251
Cdd:PLN03225 263 QILFALDGLHST-GIVHRDVKPQNIIFSEGSGSFKIIDLGAAADLRVG---INYIPKEFlldprYAAPEQYIMSTQ-TPS 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  252 ----------------------IDIWSAGcvlaeLLLGQPLFPGENSVDQLVEIikvlgtpTREEIRCmnpnytDFRFPQ 309
Cdd:PLN03225 338 apsapvatalspvlwqlnlpdrFDIYSAG-----LIFLQMAFPNLRSDSNLIQF-------NRQLKRN------DYDLVA 399
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  310 ikahpWHKVFHKRMPP------EAIDLASR--------LLQYSPSLRCTALEACAHPFFN 355
Cdd:PLN03225 400 -----WRKLVEPRASPdlrrgfEVLDLDGGagwellksMMRFKGRQRISAKAALAHPYFD 454
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
111-263 8.06e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 54.13  E-value: 8.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  111 ELQLMRPMDHPNVISL--KHCFFSTTSrdelflnLVMEYVPETLYRVLRHYTSSNQRMPIFYVklyTYQIFRGLAYIHTv 188
Cdd:PHA03211 210 EARLLRRLSHPAVLALldVRVVGGLTC-------LVLPKYRSDLYTYLGARLRPLGLAQVTAV---ARQLLSAIDYIHG- 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  189 PGVCHRDVKPQNLLVDPlTHQVKLCDFGSAkVLVKGepniSYICSRYY--------RAPELIFGaTEYTASIDIWSAGCV 260
Cdd:PHA03211 279 EGIIHRDIKTENVLVNG-PEDICLGDFGAA-CFARG----SWSTPFHYgiagtvdtNAPEVLAG-DPYTPSVDIWSAGLV 351

                 ...
gi 42571361  261 LAE 263
Cdd:PHA03211 352 IFE 354
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
66-344 1.02e-07

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: 52.89  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  66 QTISYMAERVVGTGSFGIVFQAKCLETGesvaikkvlqdrryknrelQLMRPMDHPNVISLKHCFFsttsrDELFLNLVM 145
Cdd:cd14027  15 RTQGLVVLKTVYTGPNCIEHNEALLEEG-------------------KMMNRLRHSRVVKLLGVIL-----EEGKYSLVM 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLRHYTssnqrMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKV---- 220
Cdd:cd14027  71 EYMEKgNLMHVLKKVS-----VPLSVKGRIILEIIEGMAYLHG-KGVIHKDLKPENILVDNDFH-IKIADLGLASFkmws 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 221 -LVKGEPNI--SYICSRYYRAPELIFGATEYTASI--------DIWSAGCVLAELLLGQPlfPGENSV--DQLVEIIKVL 287
Cdd:cd14027 144 kLTKEEHNEqrEVDGTAKKNAGTLYYMAPEHLNDVnakpteksDVYSFAIVLWAIFANKE--PYENAIneDQIIMCIKSG 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 288 GTPTREEIrcmnPNYTdfrfpqikahpwhkvfhkrmPPEAIDLASRLLQYSPSLRCT 344
Cdd:cd14027 222 NRPDVDDI----TEYC--------------------PREIIDLMKLCWEANPEARPT 254
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
174-273 1.19e-07

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: 53.31  E-value: 1.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 174 YTYQIFRGLAYIhTVPGVCHRDVKPQNLLVDPLtHQVKLCDFGSAK-------VLVKGEPNISYicsrYYRAPELIFGAT 246
Cdd:cd05106 217 FSSQVAQGMDFL-ASKNCIHRDVAARNVLLTDG-RVAKICDFGLARdimndsnYVVKGNARLPV----KWMAPESIFDCV 290
                        90       100
                ....*....|....*....|....*...
gi 42571361 247 eYTASIDIWSAGCVLAELL-LGQPLFPG 273
Cdd:cd05106 291 -YTVQSDVWSYGILLWEIFsLGKSPYPG 317
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
174-315 1.27e-07

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: 53.37  E-value: 1.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 174 YTYQIFRGLAYIhTVPGVCHRDVKPQNLLvdpLTHQ--VKLCDFGSAK-------VLVKGEPNISYicsrYYRAPELIFG 244
Cdd:cd05104 219 FSYQVAKGMEFL-ASKNCIHRDLAARNIL---LTHGriTKICDFGLARdirndsnYVVKGNARLPV----KWMAPESIFE 290
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 245 ATeYTASIDIWSAGCVLAELL-LGQPLFPGENSVDQLVEIIKvlgtptrEEIRCMNPNYTDFRFPQIKAHPW 315
Cdd:cd05104 291 CV-YTFESDVWSYGILLWEIFsLGSSPYPGMPVDSKFYKMIK-------EGYRMDSPEFAPSEMYDIMRSCW 354
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
64-290 1.40e-07

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: 52.47  E-value: 1.40e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYMaeRVVGTGSFGIVFQAKC--LETGES---VAIkKVLQD------RRYKNRELQLMRPMDHPNVISlkhcFFS 132
Cdd:cd05049   3 KRDTIVLK--RELGEGAFGKVFLGECynLEPEQDkmlVAV-KTLKDasspdaRKDFEREAELLTNLQHENIVK----FYG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 133 TTSRDELFLnLVMEYVPE-TLYRVLRHY----------TSSNQRMPIFYVKLYTYQIFRGLAYI---HTVpgvcHRDVKP 198
Cdd:cd05049  76 VCTEGDPLL-MVFEYMEHgDLNKFLRSHgpdaaflaseDSAPGELTLSQLLHIAVQIASGMVYLasqHFV----HRDLAT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 199 QNLLV-DPLThqVKLCDFGSAKVLVKGEpnisyicsrYYR------------APELIFGATeYTASIDIWSAGCVLAELL 265
Cdd:cd05049 151 RNCLVgTNLV--VKIGDFGMSRDIYSTD---------YYRvgghtmlpirwmPPESILYRK-FTTESDVWSFGVVLWEIF 218
                       250       260       270
                ....*....|....*....|....*....|
gi 42571361 266 L--GQPLFpgENSVDQLVEIIK---VLGTP 290
Cdd:cd05049 219 TygKQPWF--QLSNTEVIECITqgrLLQRP 246
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
75-264 1.55e-07

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


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 52.47  E-value: 1.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAK----CLETGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLkhcffsttsrdelfLNLV 144
Cdd:cd05046  12 TLGRGEFGEVFLAKakgiEEEGGETLVLVKALQKTKDENlqsefrRELDMFRKLSHKNVVRL--------------LGLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPEtlYRVLRHY-----------------------TSSNQRMPIfyvklyTYQIFRGLAYIHTVPGVcHRDVKPQNL 201
Cdd:cd05046  78 REAEPH--YMILEYTdlgdlkqflratkskdeklkpppLSTKQKVAL------CTQIALGMDHLSNARFV-HRDLAARNC 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 42571361 202 LVDPlTHQVKLcdfgSAKVLVKGEPNisyicSRYYR-----------APELIFgATEYTASIDIWSAGCVLAEL 264
Cdd:cd05046 149 LVSS-QREVKV----SLLSLSKDVYN-----SEYYKlrnaliplrwlAPEAVQ-EDDFSTKSDVWSFGVLMWEV 211
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
76-284 1.80e-07

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 52.34  E-value: 1.80e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKcLETGESVAIKKVL-----QDRRYKNrELQLMRPMDHPNVIslkhCFFSTTSRDElfLNLVMEYVP- 149
Cdd:cd14149  20 IGSGSFGTVYKGK-WHGDVAVKILKVVdptpeQFQAFRN-EVAVLRKTRHVNIL----LFMGYMTKDN--LAIVTQWCEg 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 ETLYRVLrHYTSSNQRMpiFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLV-DPLThqVKLCDFGSAKVLVK--GEP 226
Cdd:cd14149  92 SSLYKHL-HVQETKFQM--FQLIDIARQTAQGMDYLHA-KNIIHRDMKSNNIFLhEGLT--VKIGDFGLATVKSRwsGSQ 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 227 NISYIC-SRYYRAPELIF--GATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQLVEII 284
Cdd:cd14149 166 QVEQPTgSILWMAPEVIRmqDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMV 226
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
64-264 1.92e-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: 52.14  E-value: 1.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  64 PKQTISYmaERVVGTGSFGIVFQAKCL-----ETGESVAIKKV-----LQDRRYKNRELQLMRPMDHPNVISLKH-CFFS 132
Cdd:cd05050   3 PRNNIEY--VRDIGQGAFGRVFQARAPgllpyEPFTMVAVKMLkeeasADMQADFQREAALMAEFDHPNIVKLLGvCAVG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 133 TTsrdelfLNLVMEYV-PETLYRVLRH---YTSSNQRMPIFYVKLYT---------------YQIFRGLAYIHTVPGVcH 193
Cdd:cd05050  81 KP------MCLLFEYMaYGDLNEFLRHrspRAQCSLSHSTSSARKCGlnplplscteqlciaKQVAAGMAYLSERKFV-H 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 194 RDVKPQNLLVDPlTHQVKLCDFGSAKvlvkgepNIsyICSRYYRA------------PELIFGAtEYTASIDIWSAGCVL 261
Cdd:cd05050 154 RDLATRNCLVGE-NMVVKIADFGLSR-------NI--YSADYYKAsendaipirwmpPESIFYN-RYTTESDVWAYGVVL 222

                ...
gi 42571361 262 AEL 264
Cdd:cd05050 223 WEI 225
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
76-264 3.36e-07

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 51.67  E-value: 3.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAkcLETGESVAIKkVLQDRRYKN--RELQ-----LMRpmdHPNVISlkhcFFST--TSR-DELFLNLVM 145
Cdd:cd14142  13 IGKGRYGEVWRG--QWQGESVAVK-IFSSRDEKSwfRETEiyntvLLR---HENILG----FIASdmTSRnSCTQLWLIT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLRHYTSSNQRMpifyVKLyTYQIFRGLAYIHT-------VPGVCHRDVKPQNLLVDPlTHQVKLCDFGS 217
Cdd:cd14142  83 HYHENgSLYDYLQRTTLDHQEM----LRL-ALSAASGLVHLHTeifgtqgKPAIAHRDLKSKNILVKS-NGQCCIADLGL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 218 AKVLVKGEPNISYIC-----SRYYRAPELIFGATEYTA-----SIDIWSAGCVLAEL 264
Cdd:cd14142 157 AVTHSQETNQLDVGNnprvgTKRYMAPEVLDETINTDCfesykRVDIYAFGLVLWEV 213
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
174-324 4.95e-07

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: 51.55  E-value: 4.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 174 YTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEPNI---SYICSRYYRAPELIFGATeYTA 250
Cdd:cd05107 244 FSYQVANGMEFLASKNCV-HRDLAARNVLICE-GKLVKICDFGLARDIMRDSNYIskgSTFLPLKWMAPESIFNNL-YTT 320
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 251 SIDIWSAGCVLAELL-LGQPLFPGENSVDQLVEIIKvlgtptrEEIRCMNPNYTDFRFPQIKAHPWHKVFHKRMP 324
Cdd:cd05107 321 LSDVWSFGILLWEIFtLGGTPYPELPMNEQFYNAIK-------RGYRMAKPAHASDEIYEIMQKCWEEKFEIRPD 388
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
76-340 5.83e-07

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: 51.17  E-value: 5.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGE-------SVAIKKVLQDRRYKN-----RELQLMRPM-DHPNVISLkhcFFSTTSRDELFLn 142
Cdd:cd05100  20 LGEGCFGQVVMAEAIGIDKdkpnkpvTVAVKMLKDDATDKDlsdlvSEMEMMKMIgKHKNIINL---LGACTQDGPLYV- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 143 lVMEYVPE-TLYRVLR-------HYTSSNQRMP---IFYVKLYT--YQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQ 209
Cdd:cd05100  96 -LVEYASKgNLREYLRarrppgmDYSFDTCKLPeeqLTFKDLVScaYQVARGMEYLASQKCI-HRDLAARNVLVTE-DNV 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 210 VKLCDFGsakvLVKGEPNISYICSRY-------YRAPELIFGATeYTASIDIWSAGCVLAELL-LGQPLFPGEnSVDQLV 281
Cdd:cd05100 173 MKIADFG----LARDVHNIDYYKKTTngrlpvkWMAPEALFDRV-YTHQSDVWSFGVLLWEIFtLGGSPYPGI-PVEELF 246
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 282 EIIKvlgtptrEEIRCMNPNYTDFRFPQIKAHPWHKVFHKR-----------------MPPEAIDLASRLLQYSPS 340
Cdd:cd05100 247 KLLK-------EGHRMDKPANCTHELYMIMRECWHAVPSQRptfkqlvedldrvltvtSTDEYLDLSVPFEQYSPG 315
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
77-216 8.17e-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: 47.82  E-value: 8.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  77 GTGSFGIVFQAKCLETGESVAIKkvLQDRRYKNRELQLMRPMD--------HPNVISLKHcffstTSRDELFLNLVMEYV 148
Cdd:cd13968   2 GEGASAKVFWAEGECTTIGVAVK--IGDDVNNEEGEDLESEMDilrrlkglELNIPKVLV-----TEDVDGPNILLMELV 74
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 149 PE-TLYRVLRHYTSSNQRMPIFYvklytYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPlTHQVKLCDFG 216
Cdd:cd13968  75 KGgTLIAYTQEEELDEKDVESIM-----YQLAECMRLLH-SFHLIHRDLNNDNILLSE-DGNVKLIDFG 136
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
74-265 9.13e-07

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 49.95  E-value: 9.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK---KVLQDRRYKNR------ELQLMRPMDHPNVISLKH-CFFSTtsrdelfLNL 143
Cdd:cd05111  13 KVLGSGVFGTVHKGIWIPEGDSIKIPvaiKVIQDRSGRQSfqavtdHMLAIGSLDHAYIVRLLGiCPGAS-------LQL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYVPE-TLYRVLRHYTSS--NQRMPIFYVklytyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd05111  86 VTQLLPLgSLLDHVRQHRGSlgPQLLLNWCV-----QIAKGMYYLEE-HRMVHRNLAARNVLLKS-PSQVQVADFGVADL 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 221 LVKGEPNISY----ICSRYYRAPELIFGatEYTASIDIWSAGCVLAELL 265
Cdd:cd05111 159 LYPDDKKYFYseakTPIKWMALESIHFG--KYTHQSDVWSYGVTVWEMM 205
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
161-354 9.66e-07

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: 49.85  E-value: 9.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 161 SSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVChRDVKPQNLLVDPLTHqVKLCDFGSakvLVKGEPNI-SYICSRYYRAP 239
Cdd:cd05576 105 ASRFYIPEECIQRWAAEMVVALDALHREGIVC-RDLNPNNILLNDRGH-IQLTYFSR---WSEVEDSCdSDAIENMYCAP 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 240 ElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSvdqlveiikvlGTPTreeircmnpnYTDFRFPQIkahpwhkvf 319
Cdd:cd05576 180 E-VGGISEETEACDWWSLGALLFELLTGKALVECHPA-----------GINT----------HTTLNIPEW--------- 228
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42571361 320 hkrMPPEAIDLASRLLQYSPSLRCTALEAC-----AHPFF 354
Cdd:cd05576 229 ---VSEEARSLLQQLLQFNPTERLGAGVAGvedikSHPFF 265
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
76-273 1.05e-06

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: 49.73  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKN---RELQLMRPMDHPNVISLkhcfFSTTSRDELFLnLVMEYVPetl 152
Cdd:cd05052  14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTMEVEeflKEAAVMKEIKHPNLVQL----LGVCTREPPFY-IITEFMP--- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 153 YRVLRHYTSSNQRMPIFYVKL--YTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKvLVKGEPNISY 230
Cdd:cd05052  86 YGNLLDYLRECNREELNAVVLlyMATQIASAMEYLEKKNFI-HRDLAARNCLVGE-NHLVKVADFGLSR-LMTGDTYTAH 162
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42571361 231 ICSRY---YRAPElifGATEYTASI--DIWSAGCVLAEL-LLGQPLFPG 273
Cdd:cd05052 163 AGAKFpikWTAPE---SLAYNKFSIksDVWAFGVLLWEIaTYGMSPYPG 208
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
76-283 1.20e-06

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 49.53  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETgESVAIKKVLQDRRYKN---RELQLMRPMDHPNVISLkhcfFSTTSRDELFLnlVMEYVPE-T 151
Cdd:cd14203   3 LGQGCFGEVWMGTWNGT-TKVAIKTLKPGTMSPEaflEEAQIMKKLRHDKLVQL----YAVVSEEPIYI--VTEFMSKgS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 152 LYRVLRHYTSSNQRMPIFyVKLYTyQIFRGLAYIHTVPGVcHRDVKPQNLLV-DPLThqVKLCDFGSAKVLVKGEPNISY 230
Cdd:cd14203  76 LLDFLKDGEGKYLKLPQL-VDMAA-QIASGMAYIERMNYI-HRDLRAANILVgDNLV--CKIADFGLARLIEDNEYTARQ 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 231 iCSRY---YRAPEL-IFGatEYTASIDIWSAGCVLAELLL-GQPLFPGENSVDQLVEI 283
Cdd:cd14203 151 -GAKFpikWTAPEAaLYG--RFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQV 205
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
76-276 1.46e-06

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: 49.58  E-value: 1.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCL----ETGESVAIKKVLQD-----RRYKNRELQLMRPMDHPNVISlkhcFFSTTSRDELFLnLVME 146
Cdd:cd05092  13 LGEGAFGKVFLAECHnllpEQDKMLVAVKALKEatesaRQDFQREAELLTVLQHQHIVR----FYGVCTEGEPLI-MVFE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE-TLYRVLR------HYTSSNQRMPIFYVKL-----YTYQIFRGLAYIHTVPGVcHRDVKPQNLLV-DPLThqVKLC 213
Cdd:cd05092  88 YMRHgDLNRFLRshgpdaKILDGGEGQAPGQLTLgqmlqIASQIASGMVYLASLHFV-HRDLATRNCLVgQGLV--VKIG 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 214 DFGSAKVLVKGEpnisyicsrYYRA------------PELIFgATEYTASIDIWSAGCVLAELLL--GQPLFPGENS 276
Cdd:cd05092 165 DFGMSRDIYSTD---------YYRVggrtmlpirwmpPESIL-YRKFTTESDIWSFGVVLWEIFTygKQPWYQLSNT 231
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
74-268 2.29e-06

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: 48.51  E-value: 2.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYKNRELQLMRPMDHPNVIslkhCFFSTTSRDELFLNLVMEYVPET 151
Cdd:cd14129   6 RKIGGGGFGEIYDALDLLTRENVALKveSAQQPKQVLKMEVAVLKKLQGKDHV----CRFIGCGRNDRFNYVVMQLQGRN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 152 LYRVLRhyTSSNQRMPIFYVKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLC---DFGSAKVLVKGEPNI 228
Cdd:cd14129  82 LADLRR--SQSRGTFTISTTLRLGRQILESIESIHSV-GFLHRDIKPSNFAMGRFPSTCRKCymlDFGLARQFTNSCGDV 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 42571361 229 syicsryyRAPELI--FGATEYTASI------------DIWSAGCVLAELLLGQ 268
Cdd:cd14129 159 --------RPPRAVagFRGTVRYASInahrnremgrhdDLWSLFYMLVEFVVGQ 204
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
74-334 2.66e-06

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 48.76  E-value: 2.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLE---TGESVAIKKVLQDRRYKN------RELQLMRPMDHPNVISLkhCFFSTTSRDELFLNLV 144
Cdd:cd05074  15 RMLGKGEFGSVREAQLKSedgSFQKVAVKMLKADIFSSSdieeflREAACMKEFDHPNVIKL--IGVSLRSRAKGRLPIP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPETLYRVLRHYTSSNQ------RMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSA 218
Cdd:cd05074  93 MVILPFMKHGDLHTFLLMSRigeepfTLPLQTLVRFMIDIASGMEYLSS-KNFIHRDLAARNCMLNE-NMTVCVADFGLS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEpnisyicsrYYR---APELIFG--ATE------YTASIDIWSAGCVLAELL-LGQPLFPG-ENSvdqlvEIIK 285
Cdd:cd05074 171 KKIYSGD---------YYRqgcASKLPVKwlALEsladnvYTTHSDVWAFGVTMWEIMtRGQTPYAGvENS-----EIYN 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42571361 286 VL--GTPTREEIRCMNPNYtdfrfpQIKAHPWHKVFHKRmpPEAIDLASRL 334
Cdd:cd05074 237 YLikGNRLKQPPDCLEDVY------ELMCQCWSPEPKCR--PSFQHLRDQL 279
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
79-269 3.06e-06

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 48.08  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  79 GSFGIVFQAKCLETGESVAIKKVLQDRrYKNRELQLMRPMDHPNVISLkhcfFSTTSRDELfLNLVME-----YVPETLy 153
Cdd:cd13995  15 GAFGKVYLAQDTKTKKRMACKLIPVEQ-FKPSDVEIQACFRHENIAEL----YGALLWEET-VHLFMEageggSVLEKL- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 154 rvlrhytSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVdpLTHQVKLCDFGsakVLVKGEPNISYI-- 231
Cdd:cd13995  88 -------ESCGPMREFEIIWVTKHVLKGLDFLHS-KNIIHHDIKPSNIVF--MSTKAVLVDFG---LSVQMTEDVYVPkd 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 42571361 232 --CSRYYRAPELIFgATEYTASIDIWSAGCVLAELLLGQP 269
Cdd:cd13995 155 lrGTEIYMSPEVIL-CRGHNTKADIYSLGATIIHMQTGSP 193
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
75-264 4.13e-06

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 48.11  E-value: 4.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLEtgESVAIKKV-LQDRRYKNRELQL--MRPMDHPNVISLKHCFFSTTSRD-ELFLnLVMEYVPE 150
Cdd:cd14141   2 IKARGRFGCVWKAQLLN--EYVAVKIFpIQDKLSWQNEYEIysLPGMKHENILQFIGAEKRGTNLDvDLWL-ITAFHEKG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 TLYRVLR-HYTSSNQRMPIfyvklyTYQIFRGLAYIHT---------VPGVCHRDVKPQNLLvdpLTHQVKLC--DFGSA 218
Cdd:cd14141  79 SLTDYLKaNVVSWNELCHI------AQTMARGLAYLHEdipglkdghKPAIAHRDIKSKNVL---LKNNLTACiaDFGLA 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 219 KVLVKGEP---NISYICSRYYRAPELIFGATEYTAS----IDIWSAGCVLAEL 264
Cdd:cd14141 150 LKFEAGKSagdTHGQVGTRRYMAPEVLEGAINFQRDaflrIDMYAMGLVLWEL 202
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
76-268 6.06e-06

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 47.51  E-value: 6.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETgeSVAIKKVLQDRRY-----KNR---ELQLMRPMDHPNVISlkhcfFSTTSRDELFLNLVMEY 147
Cdd:cd14159   1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSELdwsvvKNSfltEVEKLSRFRHPNIVD-----LAGYSAQQGNYCLIYVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 148 VPE-TLYRVLRHYTSS-----NQRMPIFyvkLYTYqifRGLAYIHT-VPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKV 220
Cdd:cd14159  74 LPNgSLEDRLHCQVSCpclswSQRLHVL---LGTA---RAIQYLHSdSPSLIHGDVKSSNILLDA-ALNPKLGDFGLARF 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 221 -----------------LVKGepNISYICSRYYRAPELifgateyTASIDIWSAGCVLAELLLGQ 268
Cdd:cd14159 147 srrpkqpgmsstlartqTVRG--TLAYLPEEYVKTGTL-------SVEIDVYSFGVVLLELLTGR 202
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
74-359 6.33e-06

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: 47.31  E-value: 6.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGE--SVAIK--KVLQDRRYKN----RELQLMRPMDHPNVISLKHCFFSTTSRDELFLNLVM 145
Cdd:cd05075   6 KTLGEGEFGSVMEGQLNQDDSvlKVAVKtmKIAICTRSEMedflSEAVCMKEFDHPNVMRLIGVCLQNTESEGYPSPVVI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 eyVPETLYRVLRHYT--SSNQRMPIF-----YVKLYTyQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSA 218
Cdd:cd05075  86 --LPFMKHGDLHSFLlySRLGDCPVYlptqmLVKFMT-DIASGMEYLSS-KNFIHRDLAARNCMLNE-NMNVCVADFGLS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 219 KVLVKGEpniSYICSRYYRAPeLIFGATE------YTASIDIWSAGCVLAELLL-GQPLFPG-ENSvdqlvEIIKVLGTP 290
Cdd:cd05075 161 KKIYNGD---YYRQGRISKMP-VKWIAIEsladrvYTTKSDVWSFGVTMWEIATrGQTPYPGvENS-----EIYDYLRQG 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42571361 291 TReeircmnpnytdfrfpqikahpwhkvfhKRMPPEAIDLAsrllqYSPSLRCTALEACAHPFFNELRE 359
Cdd:cd05075 232 NR----------------------------LKQPPDCLDGL-----YELMSSCWLLNPKDRPSFETLRC 267
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
74-284 8.88e-06

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 47.24  E-value: 8.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLE---TGESVAIKKVLQDRrYKNRELQ-------LMRPMDHPNVISLKHCFFSTTSR---DELF 140
Cdd:cd14204  13 KVLGEGEFGSVMEGELQQpdgTNHKVAVKTMKLDN-FSQREIEeflseaaCMKDFNHPNVIRLLGVCLEVGSQripKPMV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 141 LNLVMEYVPETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQN-LLVDPLThqVKLCDFGSAK 219
Cdd:cd14204  92 ILPFMKYGDLHSFLLRSRLGSGPQHVPLQTLLKFMIDIALGMEYLSS-RNFLHRDLAARNcMLRDDMT--VCVADFGLSK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 220 VLVKGEpnisyicsrYYRAPELI-----FGATE------YTASIDIWSAGCVLAE--------------------LLLGQ 268
Cdd:cd14204 169 KIYSGD---------YYRQGRIAkmpvkWIAVEsladrvYTVKSDVWAFGVTMWEiatrgmtpypgvqnheiydyLLHGH 239
                       250
                ....*....|....*.
gi 42571361 269 PLFPGENSVDQLVEII 284
Cdd:cd14204 240 RLKQPEDCLDELYDIM 255
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
75-203 2.92e-05

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 45.51  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCleTGESVAIKK-VLQDRRYKNRELQLMRP--MDHPNVISlkhcFFSTTSRD-----ELFLnlVME 146
Cdd:cd14143   2 SIGKGRFGEVWRGRW--RGEDVAVKIfSSREERSWFREAEIYQTvmLRHENILG----FIAADNKDngtwtQLWL--VSD 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 147 YVPE-TLYRVLRHYTSSNQRMpifyVKLyTYQIFRGLAYIHT-------VPGVCHRDVKPQNLLV 203
Cdd:cd14143  74 YHEHgSLFDYLNRYTVTVEGM----IKL-ALSIASGLAHLHMeivgtqgKPAIAHRDLKSKNILV 133
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
74-276 3.60e-05

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 45.22  E-value: 3.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGES---VAIKKVLQDRRYKN------RELQLMRPMDHPNVISLKHCFFSTTSRDELFLNLV 144
Cdd:cd05035   5 KILGEGEFGSVMEAQLKQDDGSqlkVAVKTMKVDIHTYSeieeflSEAACMKDFDHPNVMRLIGVCFTASDLNKPPSPMV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MeyVPETLYRVLRHYTSSNQ------RMPIFYVKLYTYQIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGSA 218
Cdd:cd05035  85 I--LPFMKHGDLHSYLLYSRlgglpeKLPLQTLLKFMVDIAKGMEYLSN-RNFIHRDLAARNCMLDE-NMTVCVADFGLS 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 219 KVLVKGEpnisyicsrYYRAPELI-----FGATE------YTASIDIWSAGCVLAELL-LGQPLFPG-ENS 276
Cdd:cd05035 161 RKIYSGD---------YYRQGRISkmpvkWIALEsladnvYTSKSDVWSFGVTMWEIAtRGQTPYPGvENH 222
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
74-219 3.79e-05

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 45.29  E-value: 3.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIKKVL-------QDRRYKNRELQLMRPMDHPNVISLkhcfFSTTSRDElFLNLVME 146
Cdd:cd14026   3 RYLSRGAFGTVSRARHADWRVTVAIKCLKldspvgdSERNCLLKEAEILHKARFSYILPI----LGICNEPE-FLGIVTE 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 147 YVPETLYRVLRHYTSSNQRM--PIFYVKLYtyQIFRGLAYIHTV-PGVCHRDVKPQNLLVDPLTHqVKLCDFGSAK 219
Cdd:cd14026  78 YMTNGSLNELLHEKDIYPDVawPLRLRILY--EIALGVNYLHNMsPPLLHHDLKTQNILLDGEFH-VKIADFGLSK 150
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
76-268 3.85e-05

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: 45.02  E-value: 3.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKCLETGESVAIK--KVLQDRRYKNRELQLMRPMDHPNVIslkhCFFSTTSRDELFLNLVMEYVPETLY 153
Cdd:cd14130   8 IGGGGFGEIYEAMDLLTRENVALKveSAQQPKQVLKMEVAVLKKLQGKDHV----CRFIGCGRNEKFNYVVMQLQGRNLA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 154 RVLRHYTSSNQRMPIfYVKLyTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPLTHQVKLC---DFGSAKVLVKGEPNIsy 230
Cdd:cd14130  84 DLRRSQPRGTFTLST-TLRL-GKQILESIEAIHSV-GFLHRDIKPSNFAMGRLPSTYRKCymlDFGLARQYTNTTGEV-- 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 42571361 231 icsryyRAPELI--FGATEYTASI------------DIWSAGCVLAELLLGQ 268
Cdd:cd14130 159 ------RPPRNVagFRGTVRYASVnahknremgrhdDLWSLFYMLVEFAVGQ 204
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
75-269 4.72e-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: 44.65  E-value: 4.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAKCLETGE--SVAIKKVLQ-----DRRYKNRELQLMRPM-DHPNVISLkhcffSTTSRDELFLNLVME 146
Cdd:cd05047   2 VIGEGNFGQVLKARIKKDGLrmDAAIKRMKEyaskdDHRDFAGELEVLCKLgHHPNIINL-----LGACEHRGYLYLAIE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 147 YVPE-TLYRVLR--------------HYTSS---NQRMPIFYVklytyQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTH 208
Cdd:cd05047  77 YAPHgNLLDFLRksrvletdpafaiaNSTAStlsSQQLLHFAA-----DVARGMDYLSQKQFI-HRDLAARNILVGE-NY 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 209 QVKLCDFGSAK---VLVKgePNISYICSRYYRAPELIFGAteYTASIDIWSAGCVLAEL--LLGQP 269
Cdd:cd05047 150 VAKIADFGLSRgqeVYVK--KTMGRLPVRWMAIESLNYSV--YTTNSDVWSYGVLLWEIvsLGGTP 211
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
74-264 5.18e-05

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 44.77  E-value: 5.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCleTGESVAIKKVLQDRR---YKNRELQLMRPMDHPNVISlkhcFFS-----TTSRDELFLnlVM 145
Cdd:cd14144   1 RSVGKGRYGEVWKGKW--RGEKVAVKIFFTTEEaswFRETEIYQTVLMRHENILG----FIAadikgTGSWTQLYL--IT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 146 EYVPE-TLYRVLRHYTSSNQRMpifyVKLyTYQIFRGLAYIHT-------VPGVCHRDVKPQNLLVDPlTHQVKLCDFGS 217
Cdd:cd14144  73 DYHENgSLYDFLRGNTLDTQSM----LKL-AYSAACGLAHLHTeifgtqgKPAIAHRDIKSKNILVKK-NGTCCIADLGL 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 42571361 218 A-KVLVKGE----PNISYICSRYYRAPELIFGATE---YTASI--DIWSAGCVLAEL 264
Cdd:cd14144 147 AvKFISETNevdlPPNTRVGTKRYMAPEVLDESLNrnhFDAYKmaDMYSFGLVLWEI 203
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
171-242 6.62e-05

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 45.06  E-value: 6.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361  171 VKLYTYQIFRGLAYIHTVpGVCHRDVKPQNLLVDpLTHQVKLCDFGSAKVLVKG---EPNISYICSRYYRAPELI 242
Cdd:PLN03224 311 IKGVMRQVLTGLRKLHRI-GIVHRDIKPENLLVT-VDGQVKIIDFGAAVDMCTGinfNPLYGMLDPRYSPPEELV 383
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
74-288 6.81e-05

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 44.02  E-value: 6.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCLETGESVAIK---KVLQDRRYKNRELQLMRPMDhpnVISLKHCF--FSTTSRDelfLNLVMEYV 148
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKHWKTWLAIKcppSLHVDDSERMELLEEAKKME---MAKFRHILpvYGICSEP---VGLVMEYM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 149 PE-TLYRVL-RHYTSSNQRMPIFYvklytyQIFRGLAYIHTV-PGVCHRDVKPQNLLVDPLTHqVKLCDFGSAKVL---- 221
Cdd:cd14025  76 ETgSLEKLLaSEPLPWELRFRIIH------ETAVGMNFLHCMkPPLLHLDLKPANILLDAHYH-VKISDFGLAKWNglsh 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42571361 222 --------VKGepNISYICSRYYRAPELIFGaTEYtasiDIWSAGCVLAELLLGQPLFPGENSVdqLVEIIKVLG 288
Cdd:cd14025 149 shdlsrdgLRG--TIAYLPPERFKEKNRCPD-TKH----DVYSFAIVIWGILTQKKPFAGENNI--LHIMVKVVK 214
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
70-219 6.85e-05

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. CK1alpha plays a role in cell cycle progression, spindle dynamics, and chromosome segregation. It is also involved in regulating apoptosis mediated by Fas or the retinoid X receptor (RXR), and is a positive regulator of Wnt signaling. CK1alpha phosphorylates the NS5A protein of flaviviruses such as the Hepatitis C virus (HCV) and yellow fever virus (YFV), and influences flaviviral replication. The CK1 alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 44.03  E-value: 6.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  70 YMAERVVGTGSFGIVFQAKCLETGESVAIKkvLQDRRYKNRELQ----LMRPMDhpNVISLKHCFFSTTSRDelFLNLVM 145
Cdd:cd14128   2 YRLVRKIGSGSFGDIYLGINITNGEEVAVK--LESQKARHPQLLyeskLYKILQ--GGVGIPHIRWYGQEKD--YNVLVM 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42571361 146 EYVPETLYRVlrhYTSSNQRMPIFYVKLYTYQIFRGLAYIHtVPGVCHRDVKPQNLLVDPLTH--QVKLCDFGSAK 219
Cdd:cd14128  76 DLLGPSLEDL---FNFCSRRFTMKTVLMLADQMIGRIEYVH-NKNFIHRDIKPDNFLMGIGRHcnKLFLIDFGLAK 147
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
76-322 1.96e-04

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: 42.56  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  76 VGTGSFGIVFQAKcLETGESVAIKKVLQDRRYKN---RELQLMRPMDHPNVISLkhcFFSTTSRDELFLnlVMEYVPE-- 150
Cdd:cd05113  12 LGTGQFGVVKYGK-WRGQYDVAIKMIKEGSMSEDefiEEAKVMMNLSHEKLVQL---YGVCTKQRPIFI--ITEYMANgc 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 151 --TLYRVLRHYTSSNQRMPIfyvklyTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEpNI 228
Cdd:cd05113  86 llNYLREMRKRFQTQQLLEM------CKDVCEAMEYLESKQFL-HRDLAARNCLVND-QGVVKVSDFGLSRYVLDDE-YT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 229 SYICSRY---YRAPElIFGATEYTASIDIWSAGCVLAELL-LG-QPLFPGENSvdQLVEIIKvlgtptrEEIRCMNPNYT 303
Cdd:cd05113 157 SSVGSKFpvrWSPPE-VLMYSKFSSKSDVWAFGVLMWEVYsLGkMPYERFTNS--ETVEHVS-------QGLRLYRPHLA 226
                       250
                ....*....|....*....
gi 42571361 304 DFRFPQIKAHPWHKVFHKR 322
Cdd:cd05113 227 SEKVYTIMYSCWHEKADER 245
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
96-265 1.96e-04

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 43.04  E-value: 1.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  96 VAIKKVLQD--RRYKN---RELQLMRPMDHPNVISLkhcfFSTTSRDELfLNLVMEYVPE-------TLYRVLRHYTSSN 163
Cdd:cd05097  47 VAVKMLRADvtKTARNdflKEIKIMSRLKNPNIIRL----LGVCVSDDP-LCMITEYMENgdlnqflSQREIESTFTHAN 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 164 QRMPIFYVKL--YTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQVKLCDFGSAKVLVKGEpnisyicsrYYR---- 237
Cdd:cd05097 122 NIPSVSIANLlyMAVQIASGMKYLASLNFV-HRDLATRNCLVGN-HYTIKIADFGMSRNLYSGD---------YYRiqgr 190
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 42571361 238 --------APELIFGATEYTASiDIWSAGCVLAELL 265
Cdd:cd05097 191 avlpirwmAWESILLGKFTTAS-DVWAFGVTLWEMF 225
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
143-219 3.16e-04

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: 41.10  E-value: 3.16e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 143 LVMEYVP-ETLYRVLRHYTSSNQRMpifyvklytYQIFRGLAYIHTVpGVCHRDVKPQNLLVDPltHQVKLCDFGSAK 219
Cdd:COG3642  33 LVMEYIEgETLADLLEEGELPPELL---------RELGRLLARLHRA-GIVHGDLTTSNILVDD--GGVYLIDFGLAR 98
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
191-348 4.60e-04

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 41.62  E-value: 4.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 191 VCHRDVKPQNLLVDPLTHQVKLCDFGSAKVLV---------KGEPniSYIcsryyrAPELIFGATEYTASIDIWSAGCVL 261
Cdd:cd13974 153 IVHRDLKLGNMVLNKRTRKITITNFCLGKHLVseddllkdqRGSP--AYI------SPDVLSGKPYLGKPSDMWALGVVL 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 262 AELLLGQplFPGENSVDQLVeiikvlgtptreeircmnpnytdfrFPQIKAHPWHKVFHKRMPPEAIDLASRLLQYSPSL 341
Cdd:cd13974 225 FTMLYGQ--FPFYDSIPQEL-------------------------FRKIKAAEYTIPEDGRVSENTVCLIRKLLVLNPQK 277

                ....*..
gi 42571361 342 RCTALEA 348
Cdd:cd13974 278 RLTASEV 284
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
75-265 5.22e-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: 41.59  E-value: 5.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  75 VVGTGSFGIVFQAK----CLETGESVAIKKVLQDRR--YKN-RELQLMRPMDHPNVISlkhcFFST---TSRDELFLNLV 144
Cdd:cd14055   2 LVGKGRFAEVWKAKlkqnASGQYETVAVKIFPYEEYasWKNeKDIFTDASLKHENILQ----FLTAeerGVGLDRQYWLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPEtlyRVLRHYTSSNqrmPIFYVKLYTY--QIFRGLAYIHT---------VPgVCHRDVKPQNLLV-DPLThqVKL 212
Cdd:cd14055  78 TAYHEN---GSLQDYLTRH---ILSWEDLCKMagSLARGLAHLHSdrtpcgrpkIP-IAHRDLKSSNILVkNDGT--CVL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 42571361 213 CDFGSAKVL-----VKGEPNISYICSRYYRAPELI-----FGATEYTASIDIWSAGCVLAELL 265
Cdd:cd14055 149 ADFGLALRLdpslsVDELANSGQVGTARYMAPEALesrvnLEDLESFKQIDVYSMALVLWEMA 211
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
61-260 5.90e-04

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 41.48  E-value: 5.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   61 NGEPKQTIS---YMAERVVGTGSFGIVFQAKC----------------LETGESVAIKKVLQDRRYKNRELQLMR--PMD 119
Cdd:PHA02882   2 EGIPLIDITgkeWKIDKLIGCGGFGCVYETQCasdhcinnqavakienLENETIVMETLVYNNIYDIDKIALWKNihNID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  120 HPNVISLKHCffSTTSRDELFLNLVM-EYVPETLYRVLRHYTSSNQRMpifyVKLYTYQIFRGLAYIHTVpGVCHRDVKP 198
Cdd:PHA02882  82 HLGIPKYYGC--GSFKRCRMYYRFILlEKLVENTKEIFKRIKCKNKKL----IKNIMKDMLTTLEYIHEH-GISHGDIKP 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361  199 QNLLVDPlTHQVKLCDFGSAKVLVKGEPNIsyicsRYYRAPELIFGATEYTASIDIWSAGCV 260
Cdd:PHA02882 155 ENIMVDG-NNRGYIIDYGIASHFIIHGKHI-----EYSKEQKDLHRGTLYYAGLDAHNGACV 210
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
73-276 6.86e-04

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 41.15  E-value: 6.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGES-----VAIKKV----LQDRRYKNRELQLMRPMDHPNVISlkhcfFSTTSRDELFLNL 143
Cdd:cd05094  10 KRELGEGAFGKVFLAECYNLSPTkdkmlVAVKTLkdptLAARKDFQREAELLTNLQHDHIVK-----FYGVCGDGDPLIM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 144 VMEYV-------------PETLYRVLRHYTSSNQRMPIFYVKLYTYQIFRGLAYIHTVPGVcHRDVKPQNLLVDPlTHQV 210
Cdd:cd05094  85 VFEYMkhgdlnkflrahgPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFV-HRDLATRNCLVGA-NLLV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 211 KLCDFGSAKVLVKgepnisyicSRYYRA------------PELIFgATEYTASIDIWSAGCVLAELLL--GQPLFPGENS 276
Cdd:cd05094 163 KIGDFGMSRDVYS---------TDYYRVgghtmlpirwmpPESIM-YRKFTTESDVWSFGVILWEIFTygKQPWFQLSNT 232
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
93-264 7.38e-04

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: 41.00  E-value: 7.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  93 GESVAIKKVLQ-----DRRYKnRELQLMRPMDHPNVislkhCFFSTTSRDELFLNLVMEYVPE-TLYRVLRhytssNQRM 166
Cdd:cd14045  30 GRTVAIKKIAKksftlSKRIR-KEVKQVRELDHPNL-----CKFIGGCIEVPNVAIITEYCPKgSLNDVLL-----NEDI 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 167 PIFYVKLYTY--QIFRGLAYIHTvPGVCHRDVKPQNLLVDPlTHQVKLCDFGsAKVLVK--GEPNISYICSR---YYRAP 239
Cdd:cd14045  99 PLNWGFRFSFatDIARGMAYLHQ-HKIYHGRLKSSNCVIDD-RWVCKIADYG-LTTYRKedGSENASGYQQRlmqVYLPP 175
                       170       180
                ....*....|....*....|....*.
gi 42571361 240 EL-IFGATEYTASIDIWSAGCVLAEL 264
Cdd:cd14045 176 ENhSNTDTEPTQATDVYSYAIILLEI 201
CotS COG0510
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
148-218 1.59e-03

Thiamine kinase or a related kinase [Coenzyme transport and metabolism];


Pssm-ID: 440276 [Multi-domain]  Cd Length: 156  Bit Score: 38.99  E-value: 1.59e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 42571361 148 VPETLYRVLRHYTSSNQRMPIFYVKLYtYQIFRGLAYIHTVPGVCHRDVKPQNLLVDPlTHQVKLCDFGSA 218
Cdd:COG0510   9 LRFDLFARLERYLALGPRDLPELLRRL-EELERALAARPLPLVLCHGDLHPGNFLVTD-DGRLYLIDWEYA 77
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
73-357 2.29e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 40.22  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361   73 ERVVGTGSFGIVFQAKCLETGESVAIKKVLQDRRYKNRELQLMRPMDHPNVISLkhcffSTTSRDELFLNLVMEYVP-ET 151
Cdd:PLN00113 695 ENVISRGKKGASYKGKSIKNGMQFVVKEINDVNSIPSSEIADMGKLQHPNIVKL-----IGLCRSEKGAYLIHEYIEgKN 769
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  152 LYRVLRHYTSSNQRmpifyvklytyQIFRGLA------YIHTVPGVCHRDVKPQNLLVDpLTHQVKLCdFGSAKVLVKge 225
Cdd:PLN00113 770 LSEVLRNLSWERRR-----------KIAIGIAkalrflHCRCSPAVVVGNLSPEKIIID-GKDEPHLR-LSLPGLLCT-- 834
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  226 pNISYICSRYYRAPElIFGATEYTASIDIWSAGCVLAELLLGQPLFPGENSVDQ-LVEIIKVlgtptreeirCMNPNYTD 304
Cdd:PLN00113 835 -DTKCFISSAYVAPE-TRETKDITEKSDIYGFGLILIELLTGKSPADAEFGVHGsIVEWARY----------CYSDCHLD 902
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 42571361  305 FRF-PQIKAhpwHKVFHKRMPPEAIDLAsrllqyspsLRCTALEACAHPFFNEL 357
Cdd:PLN00113 903 MWIdPSIRG---DVSVNQNEIVEVMNLA---------LHCTATDPTARPCANDV 944
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
143-218 2.39e-03

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: 38.44  E-value: 2.39e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42571361 143 LVMEYVPETLYRVLRHYTSSNQRmpifyVKLYTyQIFRGLAYIHTVP--GVCHRDVKPQNLLVDPLTHQVKLCDFGSA 218
Cdd:cd05120  69 LLMERIEGETLSEVWPRLSEEEK-----EKIAD-QLAEILAALHRIDssVLTHGDLHPGNILVKPDGKLSGIIDWEFA 140
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
177-282 2.77e-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: 39.53  E-value: 2.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 177 QIFRGLAYIHTVPGVcHRDVKPQNLLVDPLTHqVKLCDFGSAKVLVKGEpnisyicsrYYR------------APELIFG 244
Cdd:cd05096 146 QIASGMKYLSSLNFV-HRDLATRNCLVGENLT-IKIADFGMSRNLYAGD---------YYRiqgravlpirwmAWECILM 214
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 42571361 245 ATEYTASiDIWSAGCVLAELLL---GQPLfpGENSVDQLVE 282
Cdd:cd05096 215 GKFTTAS-DVWAFGVTLWEILMlckEQPY--GELTDEQVIE 252
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
73-265 2.81e-03

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: 39.21  E-value: 2.81e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  73 ERVVGTGSFGIVFQAKCLETGE--SVAIKKVLQ-----DRRYKNRELQLMRPM-DHPNVISLkhcffSTTSRDELFLNLV 144
Cdd:cd05089   7 EDVIGEGNFGQVIKAMIKKDGLkmNAAIKMLKEfasenDHRDFAGELEVLCKLgHHPNIINL-----LGACENRGYLYIA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 145 MEYVPE-TLYRVLRHyTSSNQRMPIFYVK------LYTYQIFR-------GLAYIHTVPGVcHRDVKPQNLLV-DPLThq 209
Cdd:cd05089  82 IEYAPYgNLLDFLRK-SRVLETDPAFAKEhgtastLTSQQLLQfasdvakGMQYLSEKQFI-HRDLAARNVLVgENLV-- 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42571361 210 VKLCDFGsakvLVKGEPniSYICSRYYRAPeLIFGATE------YTASIDIWSAGCVLAELL 265
Cdd:cd05089 158 SKIADFG----LSRGEE--VYVKKTMGRLP-VRWMAIEslnysvYTTKSDVWSFGVLLWEIV 212
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
74-264 3.69e-03

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 38.87  E-value: 3.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361  74 RVVGTGSFGIVFQAKCleTGESVAIKKVLQDRR---YKNRELQLMRPMDHPNVIS-LKHCFFSTTSRDELFLnlVMEYVP 149
Cdd:cd14220   1 RQIGKGRYGEVWMGKW--RGEKVAVKVFFTTEEaswFRETEIYQTVLMRHENILGfIAADIKGTGSWTQLYL--ITDYHE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42571361 150 E-TLYRVLRHYTSSNQRMpifyVKLyTYQIFRGLAYIHT-------VPGVCHRDVKPQNLLVDPlTHQVKLCDFGSAKVL 221
Cdd:cd14220  77 NgSLYDFLKCTTLDTRAL----LKL-AYSAACGLCHLHTeiygtqgKPAIAHRDLKSKNILIKK-NGTCCIADLGLAVKF 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42571361 222 VKGE-----PNISYICSRYYRAPELI---FGATEYTASI--DIWSAGCVLAEL 264
Cdd:cd14220 151 NSDTnevdvPLNTRVGTKRYMAPEVLdesLNKNHFQAYImaDIYSFGLIIWEM 203
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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