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Conserved domains on  [gi|23308722|ref|NP_003309|]
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dual specificity protein kinase TTK isoform 1 [Homo sapiens]

Protein Classification

Mps1 family protein kinase( domain architecture ID 18642190)

Mps1 (monopolar spindle 1) family protein kinase similar to dual-specificity mitotic checkpoint protein kinase Mps1/TTK that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates

CATH:  1.10.510.10
EC:  2.7.-.-
Gene Ontology:  GO:0006468|GO:0005524
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
523-791 8.66e-169

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: 489.80  E-value: 8.66e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDKIIRLYDYEITD--QYIYM 600
Cdd:cd14131   1 KPYEILKQLGKGGSSKVYKVLNPKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLK-GSDRIIQLYDYEVTDedDYLYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGNIDLNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSV 678
Cdd:cd14131  80 VMECGEIDLATILKKKrpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGRLKLIDFGIAKAIQNDTTSI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRENGkSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPD 758
Cdd:cd14131 160 VRDSQVGTLNYMSPEAIKDTSASGEGK-PKSKIGRPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQAIIDPNHEIEFPD 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14131 239 IPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
54-188 2.00e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 47.42  E-value: 2.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  54 QIMMMANNP---EDWLSLLLKLEKNSVPLSDALLN--KLIGRYSQAIEALppDKYGQ-NESFARIQVRFAELKAIQ-EPD 126
Cdd:COG2956  84 QDYLKAGLLdraEELLEKLLELDPDDAEALRLLAEiyEQEGDWEKAIEVL--ERLLKlGPENAHAYCELAELYLEQgDYD 161
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 127 DARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERG---AVPLEMLEIALRNLN 188
Cdd:COG2956 162 EAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDpdyLPALPRLAELYEKLG 226
 
Name Accession Description Interval E-value
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
523-791 8.66e-169

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: 489.80  E-value: 8.66e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDKIIRLYDYEITD--QYIYM 600
Cdd:cd14131   1 KPYEILKQLGKGGSSKVYKVLNPKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLK-GSDRIIQLYDYEVTDedDYLYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGNIDLNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSV 678
Cdd:cd14131  80 VMECGEIDLATILKKKrpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGRLKLIDFGIAKAIQNDTTSI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRENGkSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPD 758
Cdd:cd14131 160 VRDSQVGTLNYMSPEAIKDTSASGEGK-PKSKIGRPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQAIIDPNHEIEFPD 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14131 239 IPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
525-791 1.04e-79

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 257.84  E-value: 1.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQtLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME 603
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKtGKLVAIKVIKKKKIKKD-RERILREIKILKKL--KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSvvkD 681
Cdd:smart00220  78 yCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDeDGHVKLADFGLARQLDPGEKL---T 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    682 SQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIP- 760
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKA-----------VDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDi 223
                          250       260       270
                   ....*....|....*....|....*....|.
gi 23308722    761 EKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:smart00220 224 SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
525-791 5.30e-62

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 208.64  E-value: 5.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVME 603
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHrDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLN--HPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTihqhgivhsdlkpanflivdgmlklidfgianqmqpdttSVVKDS 682
Cdd:pfam00069  79 yVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES---------------------------------------GSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   683 QVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEK 762
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPK-----------VDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSE 188
                         250       260
                  ....*....|....*....|....*....
gi 23308722   763 DLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:pfam00069 189 EAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
522-787 3.00e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.97  E-value: 3.00e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 522 GRiYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQT-LDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIY 599
Cdd:COG0515   7 GR-YRILRLLGRGGMGVVYLARDLRlGRPVALKVLRPELAADPEaRERFRREARALARLNHPN--IVRVYDVGEEDGRPY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMqpDTTS 677
Cdd:COG0515  84 LVMEyVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTpDGRVKLIDFGIARAL--GGAT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQV-GTVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCILYYMTYGKTPFQ-----QIINQIskLHAI 747
Cdd:COG0515 162 LTQTGTVvGTPGYMAPEQARgepvDPRS---------------DVYSLGVTLYELLTGRPPFDgdspaELLRAH--LREP 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23308722 748 IDPNHEIEfPDIPEkDLQDVLKCCLKRDPKQRI-SIPELLA 787
Cdd:COG0515 225 PPPPSELR-PDLPP-ALDAIVLRALAKDPEERYqSAAELAA 263
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
522-779 2.70e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 98.71  E-value: 2.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  522 GRiYSILKQIGSGGSSKVFQ----VLNEKkqiYAIK-----YVNleeaDNQTLDSYRNE---IAYLNklqqHSDkIIRLY 589
Cdd:NF033483   7 GR-YEIGERIGRGGMAEVYLakdtRLDRD---VAVKvlrpdLAR----DPEFVARFRREaqsAASLS----HPN-IVSVY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  590 DYEITDQYIYMVMEC--GnIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFG 666
Cdd:NF033483  74 DVGEDGGIPYIVMEYvdG-RTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITkDGRVKVTDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  667 IANQMqpDTTSVVKDSQV-GTVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCILYYMTYGKTPF------- 734
Cdd:NF033483 153 IARAL--SSTTMTQTNSVlGTVHYLSPEQARggtvDARS---------------DIYSLGIVLYEMLTGRPPFdgdspvs 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 23308722  735 ------QQIINQISKLHaiidpnheiefPDIPEkDLQD-VLKcCLKRDPKQR 779
Cdd:NF033483 216 vaykhvQEDPPPPSELN-----------PGIPQ-SLDAvVLK-ATAKDPDDR 254
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
525-790 8.73e-20

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 90.65  E-value: 8.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  525 YSILKQIGSGGSSKVFQ----VLNEkkqIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYM 600
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKardrVTNE---TIALKKIRLEQEDEGVPSTAIREISLLKEMQH--GNIVRLQDVVHSEKRLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  601 VMECGNIDLNSWLKKKKSI--DPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGIANQMQPDTT 676
Cdd:PLN00009  79 VFEYLDLDLKKHMDSSPDFakNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIdrRTNALKLADFGLARAFGIPVR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  677 SVVKdsQVGTVNYMPPEAikdMSSSREngkskskISPKSDVWSLGCILYYMTYGKT--PFQQIINQISKLHAIID----- 749
Cdd:PLN00009 159 TFTH--EVVTLWYRAPEI---LLGSRH-------YSTPVDIWSVGCIFAEMVNQKPlfPGDSEIDELFKIFRILGtpnee 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  750 --------PNHEIEFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:PLN00009 227 twpgvtslPDYKSAFPKWPPKDLAtvvptlepagvDLLSKMLRLDPSKRITARAALEHEY 286
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
585-668 5.71e-06

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


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 47.98  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   585 IIRLYDYE---ITDQYIymvmecGNIDLNSWLKKKksidpweRKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLK 661
Cdd:TIGR03724  63 VIYDVDPDnktIVMEYI------EGKPLKDVIEEN-------GDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVY 129

                  ....*..
gi 23308722   662 LIDFGIA 668
Cdd:TIGR03724 130 LIDFGLG 136
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
54-188 2.00e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 47.42  E-value: 2.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  54 QIMMMANNP---EDWLSLLLKLEKNSVPLSDALLN--KLIGRYSQAIEALppDKYGQ-NESFARIQVRFAELKAIQ-EPD 126
Cdd:COG2956  84 QDYLKAGLLdraEELLEKLLELDPDDAEALRLLAEiyEQEGDWEKAIEVL--ERLLKlGPENAHAYCELAELYLEQgDYD 161
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 127 DARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERG---AVPLEMLEIALRNLN 188
Cdd:COG2956 162 EAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDpdyLPALPRLAELYEKLG 226
 
Name Accession Description Interval E-value
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
523-791 8.66e-169

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: 489.80  E-value: 8.66e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDKIIRLYDYEITD--QYIYM 600
Cdd:cd14131   1 KPYEILKQLGKGGSSKVYKVLNPKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLK-GSDRIIQLYDYEVTDedDYLYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGNIDLNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTSV 678
Cdd:cd14131  80 VMECGEIDLATILKKKrpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKGRLKLIDFGIAKAIQNDTTSI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRENGkSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPD 758
Cdd:cd14131 160 VRDSQVGTLNYMSPEAIKDTSASGEGK-PKSKIGRPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQAIIDPNHEIEFPD 238
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14131 239 IPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
524-791 3.75e-86

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: 274.85  E-value: 3.75e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEAdnQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKtGQIVAIKKINLESK--EKKESILNEIAILKKCK--HPNIVKYYGSYLKKDELWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLK-KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTsvv 679
Cdd:cd05122  77 EfCSGGSLKDLLKnTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTsDGEVKLIDFGLSAQLSDGKT--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQIInqISKLHAIIDPNHEIEFPDI 759
Cdd:cd05122 154 RNTFVGTPYWMAPEVIQGKPYG-----------FKADIWSLGITAIEMAEGKPPYSELP--PMKALFLIATNGPPGLRNP 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 760 P--EKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd05122 221 KkwSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
525-791 1.04e-79

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 257.84  E-value: 1.04e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQtLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME 603
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKtGKLVAIKVIKKKKIKKD-RERILREIKILKKL--KHPNIVRLYDVFEDEDKLYLVME 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSvvkD 681
Cdd:smart00220  78 yCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDeDGHVKLADFGLARQLDPGEKL---T 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    682 SQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIP- 760
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKA-----------VDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDi 223
                          250       260       270
                   ....*....|....*....|....*....|.
gi 23308722    761 EKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:smart00220 224 SPEAKDLIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
525-791 5.30e-62

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 208.64  E-value: 5.30e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVME 603
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHrDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLN--HPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTihqhgivhsdlkpanflivdgmlklidfgianqmqpdttSVVKDS 682
Cdd:pfam00069  79 yVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES---------------------------------------GSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   683 QVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEK 762
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPK-----------VDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELPSNLSE 188
                         250       260
                  ....*....|....*....|....*....
gi 23308722   763 DLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:pfam00069 189 EAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
529-791 4.42e-57

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: 196.59  E-value: 4.42e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVME-CGN 606
Cdd:cd06606   6 ELLGKGSFGSVYLALNLDtGELMAVKEVELSGDSEEELEALEREIRILSSLK--HPNIVRYLGTERTENTLNIFLEyVPG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVVKDSQVG 685
Cdd:cd06606  84 GSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVdSDGVVKLADFGCAKRLAEIATGEGTKSLRG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 686 TVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEKDLQ 765
Cdd:cd06606 164 TPYWMAPEVIRGEGYGRA-----------ADIWSLGCTVIEMATGKPPWSELGNPVAALFKIGSSGEPPPIPEHLSEEAK 232
                       250       260
                ....*....|....*....|....*.
gi 23308722 766 DVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06606 233 DFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
525-787 4.18e-53

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: 185.48  E-value: 4.18e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDS-YRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLlGRPVAIKVLRPELAEDEEFRErFLREARALARLS--HPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVVk 680
Cdd:cd14014  80 EyVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLtEDGRVKLTDFGIARALGDSGLTQT- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQ-QIINQISKLHAIIDPNHEIEF-PD 758
Cdd:cd14014 159 GSVLGTPAYMAPEQARGGPVDPR-----------SDIYSLGVVLYELLTGRPPFDgDSPAAVLAKHLQEAPPPPSPLnPD 227
                       250       260       270
                ....*....|....*....|....*....|
gi 23308722 759 IPeKDLQDVLKCCLKRDPKQRI-SIPELLA 787
Cdd:cd14014 228 VP-PALDAIILRALAKDPEERPqSAAELLA 256
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
531-789 1.08e-52

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: 182.86  E-value: 1.08e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQtLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME-CGNID 608
Cdd:cd00180   1 LGKGSFGKVYKARDkETGKKVAVKVIPKEKLKKL-LEELLREIEILKKL--NHPNIVKLYDVFETENFLYLVMEyCEGGS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWLKKK-KSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSVVKDSQVGT 686
Cdd:cd00180  78 LKDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDsDGTVKLADFGLAKDLDSDDSLLKTTGGTTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 687 VNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMtygktpfqqiinqisklhaiidpnheiefpdipeKDLQD 766
Cdd:cd00180 158 PYYAPPELLGGRYYGPK-----------VDIWSLGVILYEL----------------------------------EELKD 192
                       250       260
                ....*....|....*....|...
gi 23308722 767 VLKCCLKRDPKQRISIPELLAHP 789
Cdd:cd00180 193 LIRRMLQYDPKKRPSAKELLEHL 215
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
525-790 1.75e-50

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: 178.09  E-value: 1.75e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVME 603
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLtGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPN--IIKLYEVIETENKIYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSvvkD 681
Cdd:cd14003  80 yASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLdKNGNLKIIDFGLSNEFRGGSLL---K 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIKDmsssRE-NGkskskisPKSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDpNHEIEFPDIP 760
Cdd:cd14003 157 TFCGTPAYAAPEVLLG----RKyDG-------PKADVWSLGVILYAMLTGYLPFDD--DNDSKLFRKIL-KGKYPIPSHL 222
                       250       260       270
                ....*....|....*....|....*....|
gi 23308722 761 EKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14003 223 SPDARDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
531-791 1.19e-48

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: 173.51  E-value: 1.19e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEK-KQIYAIK------------YVNLEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYdyEITD-- 595
Cdd:cd14008   1 LGRGSFGKVKLALDTEtGQLYAIKifnksrlrkrreGKNDRGKIKNALDDVRREIAIMKKLDHPN--IVRLY--EVIDdp 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 --QYIYMVME-CGNIDLNSWLKKKKS--IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIAN 669
Cdd:cd14008  77 esDKLYLVLEyCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTaDGTVKISDFGVSE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMQPDTTSVVKdsQVGTVNYMPPEAIkdmsssreNGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQiiNQISKL-HAII 748
Cdd:cd14008 157 MFEDGNDTLQK--TAGTPAFLAPELC--------DGDSKTYSGKAADIWALGVTLYCLVFGRLPFNG--DNILELyEAIQ 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 749 DPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14008 225 NQNDEFPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
525-789 1.56e-48

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: 172.66  E-value: 1.56e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd05117   2 YELGKVLGRGSFGVVRLAVHKKtGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLD-HPN-IVKLYEVFEDDKNLYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIANQMQPDTTSV 678
Cdd:cd05117  80 lCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLAskdpDSPIKIIDFGLAKIFEEGEKLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKdsqVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPF-----QQIINQISKlhaiidpnHE 753
Cdd:cd05117 160 TV---CGTPYYVAPEVLKGKGYGKKC-----------DIWSLGVILYILLCGYPPFygeteQELFEKILK--------GK 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 754 IEFPDIPEKDL----QDVLKCCLKRDPKQRISIPELLAHP 789
Cdd:cd05117 218 YSFDSPEWKNVseeaKDLIKRLLVVDPKKRLTAAEALNHP 257
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
522-787 3.00e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 175.97  E-value: 3.00e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 522 GRiYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQT-LDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIY 599
Cdd:COG0515   7 GR-YRILRLLGRGGMGVVYLARDLRlGRPVALKVLRPELAADPEaRERFRREARALARLNHPN--IVRVYDVGEEDGRPY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMqpDTTS 677
Cdd:COG0515  84 LVMEyVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTpDGRVKLIDFGIARAL--GGAT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQV-GTVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCILYYMTYGKTPFQ-----QIINQIskLHAI 747
Cdd:COG0515 162 LTQTGTVvGTPGYMAPEQARgepvDPRS---------------DVYSLGVTLYELLTGRPPFDgdspaELLRAH--LREP 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23308722 748 IDPNHEIEfPDIPEkDLQDVLKCCLKRDPKQRI-SIPELLA 787
Cdd:COG0515 225 PPPPSELR-PDLPP-ALDAIVLRALAKDPEERYqSAAELAA 263
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
527-792 2.93e-46

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: 166.11  E-value: 2.93e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEE-ADNQTLDSYRNEIaylnKLQQHSD--KIIRLYDYEITDQYIYMVM 602
Cdd:cd14007   4 IGKPLGKGKFGNVYLAREKKsGFIVALKVISKSQlQKSGLEHQLRREI----EIQSHLRhpNILRLYGYFEDKKRIYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDttsvVK 680
Cdd:cd14007  80 EyAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLgSNGELKLADFGWSVHAPSN----RR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEaikdMSSSRENGKSKskispksDVWSLGCILYYMTYGKTPF-----QQIINQISKLhaiidpnhEIE 755
Cdd:cd14007 156 KTFCGTLDYLPPE----MVEGKEYDYKV-------DIWSLGVLCYELLVGKPPFeskshQETYKRIQNV--------DIK 216
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14007 217 FPSSVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
525-791 1.13e-45

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 164.56  E-value: 1.13e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd08215   2 YEKIRVIGKGSFGSAYLVRRkSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKL--KHPNIVKYYESFEENGKLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSI-DPWERKSYWK---NMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQpDTTS 677
Cdd:cd08215  80 yADGGDLAQKIKKQKKKgQPFPEEQILDwfvQICLALKYLHSRKILHRDLKTQNiFLTKDGVVKLGDFGISKVLE-STTD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKdSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQ-----QIINQISKLhaiidpnh 752
Cdd:cd08215 159 LAK-TVVGTPYYLSPELCENKPYN-----------YKSDIWALGCVLYELCTLKHPFEannlpALVYKIVKG-------- 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 753 eiEFPDIPE---KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd08215 219 --QYPPIPSqysSELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
525-790 1.04e-40

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: 151.10  E-value: 1.04e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADN---QTldSYRnEIAYLNKLQqHsDKIIRLYDYEITDQYIYM 600
Cdd:cd07829   1 YEKLEKLGEGTYGVVYKAKDKKtGEIVALKKIRLDNEEEgipST--ALR-EISLLKELK-H-PNIVKLLDVIHTENKLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGNIDLNSWLKKKKS-IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIA----NQMQPD 674
Cdd:cd07829  76 VFEYCDQDLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLInRDGVLKLADFGLArafgIPLRTY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVkdsqvgTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPFQ---QI--INQISKLHA 746
Cdd:cd07829 156 THEVV------TLWYRAPEILlgsKHYSTA-------------VDIWSVGCIFAELITGKPLFPgdsEIdqLFKIFQILG 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 747 IID----------PNHEIEFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07829 217 TPTeeswpgvtklPDYKPTFPKWPKNDLEkvlprldpegiDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
525-791 1.47e-40

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 150.07  E-value: 1.47e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd06627   2 YQLGDLIGRGAFGSVYKGLNLNTgEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLN-HPN-IVKYIGSVKTKDSLYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQ---PDTTSV 678
Cdd:cd06627  80 yVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTkDGLVKLADFGVATKLNeveKDENSV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VkdsqvGTVNYMPPEAIKdMSSSREngkskskispKSDVWSLGCILYYMTYGKTPFQQIiNQISKLHAIIDPNHeiefPD 758
Cdd:cd06627 160 V-----GTPYWMAPEVIE-MSGVTT----------ASDIWSVGCTVIELLTGNPPYYDL-QPMAALFRIVQDDH----PP 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 759 IPE---KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06627 219 LPEnisPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
531-790 1.51e-40

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: 149.59  E-value: 1.51e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQV-LNEKKQIYAIKYVNLEEA-DNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME-CGNI 607
Cdd:cd05123   1 LGKGSFGKVLLVrKKDTGKLYAMKVLRKKEIiKRKEVEHTLNERNILERV--NHPFIVKLHYAFQTEEKLYLVLDyVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVvkDSQVGT 686
Cdd:cd05123  79 ELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLdSDGHIKLTDFGLAKELSSDGDRT--YTFCGT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 687 VNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQISKLhaiidpnhEIEFPDIPE 761
Cdd:cd05123 157 PEYLAPEVLLGKGYGKA-----------VDWWSLGVLLYEMLTGKPPFyaenrKEIYEKILKS--------PLKFPEYVS 217
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 762 KDLQDVLKCCLKRDPKQRI---SIPELLAHPY 790
Cdd:cd05123 218 PEAKSLISGLLQKDPTKRLgsgGAEEIKAHPF 249
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
531-790 4.14e-39

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: 145.83  E-value: 4.14e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYMVME-CGNID 608
Cdd:cd14009   1 IGRGSFATVWKGRHKQtGEVVAIKEISRKKLNKKLQENLESEIAILKSIK-H-PNIVRLYDVQKTEDFIYLVLEyCAGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIANQMQPDTtsvVKDSQV 684
Cdd:cd14009  79 LSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLStsgdDPVLKIADFGFARSLQPAS---MAETLC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 685 GTVNYMPPEAIKdmsSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFPDIPE--K 762
Cdd:cd14009 156 GSPLYMAPEILQ---FQKYD--------AKADLWSVGAILFEMLVGKPPFRG-SNHVQLLRNIERSDAVIPFPIAAQlsP 223
                       250       260
                ....*....|....*....|....*...
gi 23308722 763 DLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14009 224 DCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
525-791 5.48e-38

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


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 143.07  E-value: 5.48e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIK---YVNLEEADNQTLdsyRNEIAYLNKLQqHsDKIIRLYDYEI--TDQYI 598
Cdd:cd08217   2 YEVLETIGKGSFGTVRKVRRKSdGKILVWKeidYGKMSEKEKQQL---VSEVNILRELK-H-PNIVRYYDRIVdrANTTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME-CGNIDLNSWLKKKKsidpwERKSY------WK---NMLEAVHTIH-----QHGIVHSDLKPAN-FLIVDGMLKL 662
Cdd:cd08217  77 YIVMEyCEGGDLAQLIKKCK-----KENQYipeefiWKiftQLLLALYECHnrsvgGGKILHRDLKPANiFLDSDNNVKL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 663 IDFGIANQMQpdTTSVVKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQiINQIS 742
Cdd:cd08217 152 GDFGLARVLS--HDSSFAKTYVGTPYYMSPELLNEQSYDE-----------KSDIWSLGCLIYELCALHPPFQA-ANQLE 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 23308722 743 kLHAIIdpnHEIEFPDIPE---KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd08217 218 -LAKKI---KEGKFPRIPSrysSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
525-791 5.69e-38

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: 142.39  E-value: 5.69e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQvlNEKK---QIYAIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMV 601
Cdd:cd14002   3 YHVLELIGEGSFGKVYK--GRRKytgQVVALKFIPKRGKSEKELRNLRQEIEILRKL--NHPNIIEMLDSFETKKEFVVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpDTTSVVK 680
Cdd:cd14002  79 TEYAQGELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIgKGGVVKLCDFGFARAM--SCNTLVL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQ-----QIINQISKlhaiiDPnheIE 755
Cdd:cd14002 157 TSIKGTPLYMAPELVQEQPYDH-----------TADLWSLGCILYELFVGQPPFYtnsiyQLVQMIVK-----DP---VK 217
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14002 218 WPSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
525-790 4.63e-37

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: 142.81  E-value: 4.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYVNLEEADNqtldsyRNEIAYLN-----KLQQHSDKIIRLYdYEITDQ-Y 597
Cdd:cd05573   3 FEVIKVIGRGAFGEVWLVRdKDTGQVYAMKILRKSDMLK------REQIAHVRaerdiLADADSPWIVRLH-YAFQDEdH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQM--QP 673
Cdd:cd05573  76 LYLVMEyMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLdADGHIKLADFGLCTKMnkSG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKDSQ-------------------------VGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMT 728
Cdd:cd05573 156 DRESYLNDSVntlfqdnvlarrrphkqrrvraysaVGTPDYIAPEVLRGTGYGPEC-----------DWWSLGVILYEML 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 729 YGKTPFQQIINQISKlHAIIDPNHEIEFPDIPE--KDLQDVLKCCLkRDPKQRI-SIPELLAHPY 790
Cdd:cd05573 225 YGFPPFYSDSLVETY-SKIMNWKESLVFPDDPDvsPEAIDLIRRLL-CDPEDRLgSAEEIKAHPF 287
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
531-791 5.02e-37

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: 140.13  E-value: 5.02e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVfQVLNEK----KQIYAIKYVN---LEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQY-IYMVM 602
Cdd:cd13994   1 IGKGATSVV-RIVTKKnprsGVLYAVKEYRrrdDESKRKDYVKRLTSEYIISSKL--HHPNIVKVLDLCQDLHGkWCLVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIAN--QMQPDTTSV 678
Cdd:cd13994  78 EYCPGgDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLdEDGVLKLTDFGTAEvfGMPAEKESP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAikdMSSSRENGkskskisPKSDVWSLGCILYYMTYGKTPF----------QQIINQISKLHAII 748
Cdd:cd13994 158 MSAGLCGSEPYMAPEV---FTSGSYDG-------RAVDVWSCGIVLFALFTGRFPWrsakksdsayKAYEKSGDFTNGPY 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 749 DPNheieFPDIPEkDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd13994 228 EPI----ENLLPS-ECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
525-791 6.31e-37

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: 139.68  E-value: 6.31e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEE-------ADNQTLDSyrnEIAYLNKLQQHSDK-IIRLYD-YEIT 594
Cdd:cd14005   2 YEVGDLLGKGGFGTVYSgVRIRDGLPVAVKFVPKSRvtewamiNGPVPVPL---EIALLLKASKPGVPgVIRLLDwYERP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 595 DQYIyMVMEC--GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGIAnq 670
Cdd:cd14005  79 DGFL-LIMERpePCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLInlRTGEVKLIDFGCG-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 mQPDTTSVVKDSQvGTVNYMPPEAIkdmSSSRENGKSKSkispksdVWSLGCILYYMTYGKTPFQQIINqisklhaIIDP 750
Cdd:cd14005 156 -ALLKDSVYTDFD-GTRVYSPPEWI---RHGRYHGRPAT-------VWSLGILLYDMLCGDIPFENDEQ-------ILRG 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23308722 751 NheIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14005 217 N--VLFRPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
523-790 1.45e-36

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: 138.46  E-value: 1.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEE-ADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYM 600
Cdd:cd14099   1 KRYRRGKFLGKGGFAKCYEVTDmSTGKVYAGKVVPKSSlTKPKQREKLKSEIKIHRSLK-HPN-IVKFHDCFEDEENVYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSv 678
Cdd:cd14099  79 LLElCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMnVKIGDFGLAARLEYDGER- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vKDSQVGTVNYMPPEAIKDMSS-SREngkskskispkSDVWSLGCILYYMTYGKTPFQQiinqiSKLHAI---IDPNhEI 754
Cdd:cd14099 158 -KKTLCGTPNYIAPEVLEKKKGhSFE-----------VDIWSLGVILYTLLVGKPPFET-----SDVKETykrIKKN-EY 219
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 755 EFPDIPE--KDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14099 220 SFPSHLSisDEAKDLIRSMLQPDPTKRPSLDEILSHPF 257
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
529-791 1.79e-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: 138.59  E-value: 1.79e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME-CGN 606
Cdd:cd06626   6 NKIGEGTFGKVYTAVNlDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGL--DHPNLVRYYGVEVHREEVYIFMEyCQE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSVVK---DS 682
Cdd:cd06626  84 GTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSnGLIKLGDFGSAVKLKNNTTTMAPgevNS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 QVGTVNYMPPEAIKdmsSSRENGkskskISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHeiefPDIPEK 762
Cdd:cd06626 164 LVGTPAYMAPEVIT---GNKGEG-----HGRAADIWSLGCVVLEMATGKRPWSELDNEWAIMYHVGMGHK----PPIPDS 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 763 DL-----QDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06626 232 LQlspegKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
531-790 2.17e-36

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: 138.50  E-value: 2.17e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFqvLNEKKQ---IYAIKYVNLEE--ADNQTlDSYRNEIAYLnkLQQHSDKIIRLYDYEITDQYIYMVME-C 604
Cdd:cd05579   1 ISRGAYGRVY--LAKKKStgdLYAIKVIKKRDmiRKNQV-DSVLAERNIL--SQAQNPFVVKLYYSFQGKKNLYLVMEyL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFG------------IANQM 671
Cdd:cd05579  76 PGGDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIdANGHLKLTDFGlskvglvrrqikLSIQK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QPDTTSVVKDSQ-VGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQISklh 745
Cdd:cd05579 156 KSNGAPEKEDRRiVGTPDYLAPEILLGQGHGKT-----------VDWWSLGVILYEFLVGIPPFhaetpEEIFQNIL--- 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 746 aiidpNHEIEFPDIPE--KDLQDVLKCCLKRDPKQRI---SIPELLAHPY 790
Cdd:cd05579 222 -----NGKIEWPEDPEvsDEAKDLISKLLTPDPEKRLgakGIEEIKNHPF 266
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
525-790 2.59e-36

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 137.37  E-value: 2.59e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEADNQTldSYRnEIAYLNKLQQHSDK--IIRLYD--YEITDQYIY 599
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLArDKVTGEKVAIKKIKNDFRHPKA--ALR-EIKLLKHLNDVEGHpnIVKLLDvfEHRGGNHLC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDLNSWLKKKKS-IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGIANQMQPDTt 676
Cdd:cd05118  78 LVFELMGMNLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILInlELGQLKLADFGLARSFTSPP- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 svvKDSQVGTVNYMPPEAIKDMsssRENGkskskisPKSDVWSLGCILYYMTYGKTPFQQI--INQISKLHAIIDPnhei 754
Cdd:cd05118 157 ---YTPYVATRWYRAPEVLLGA---KPYG-------SSIDIWSLGCILAELLTGRPLFPGDseVDQLAKIVRLLGT---- 219
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 755 efpdipeKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd05118 220 -------PEALDLLSKMLKYDPAKRITASQALAHPY 248
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
525-797 4.38e-36

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: 137.73  E-value: 4.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIK--------------YVNLEeadnqtldsyRNEIAYLNklqqhSDKIIRLY 589
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAkEKETGKEYAIKvldkrhiikekkvkYVTIE----------KEVLSRLA-----HPGIVKLY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 590 dYEITDQY-IYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFG 666
Cdd:cd05581  68 -YTFQDESkLYFVLEyAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMhIKITDFG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 667 IANQMQPD----TTSVVKDSQ-----------VGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGK 731
Cdd:cd05581 147 TAKVLGPDsspeSTKGDADSQiaynqaraasfVGTAEYVSPELLNEKPAGKSS-----------DLWALGCIIYQMLTGK 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 732 TPFQQiINQISKLHAIIdpNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELlaHPYVQIQTHP 797
Cdd:cd05581 216 PPFRG-SNEYLTFQKIV--KLEYEFPENFPPDAKDLIQKLLVLDPSKRLGVNEN--GGYDELKAHP 276
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
525-791 8.57e-36

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: 136.36  E-value: 8.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKV-FQVLNEKKQIYAIKYVNLEEADNQTLDSYRN------EIAYLNKLQQHSDK-IIRLYDYEITDQ 596
Cdd:cd14004   2 YTILKEMGEGAYGQVnLAIYKSKGKEVVIKFIFKERILVDTWVRDRKlgtvplEIHILDTLNKRSHPnIVKLLDFFEDDE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVMEC-GN-IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANfLIVD--GMLKLIDFGIANQMQ 672
Cdd:cd14004  82 FYYLVMEKhGSgMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDEN-VILDgnGTIKLIDFGSAAYIK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSVVkdsqVGTVNYMPPEAIK-DMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFqqiinqiSKLHAIIDPn 751
Cdd:cd14004 161 SGPFDTF----VGTIDYAAPEVLRgNPYGGKE-----------QDIWALGVLLYTLVFKENPF-------YNIEEILEA- 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 752 hEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14004 218 -DLRIPYAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
527-792 1.55e-35

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 135.80  E-value: 1.55e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLdSYRNEIAYLnkLQQHSDKIIRLYDYEITDQYIYMVME-- 603
Cdd:cd06623   5 RVKVLGQGSSGVVYKVRHKPtGKIYALKKIHVDGDEEFRK-QLLRELKTL--RSCESPYVVKCYGAFYKEGEISIVLEym 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNidLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQ-HGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpDTTSVVK 680
Cdd:cd06623  82 dGGS--LADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLInSKGEVKIADFGISKVL--ENTLDQC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQ--IINQISKLHAIIDpnheIEFPD 758
Cdd:cd06623 158 NTFVGTVTYMSPERIQGESYSY-----------AADIWSLGLTLLECALGKFPFLPpgQPSFFELMQAICD----GPPPS 222
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 759 IPEK----DLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06623 223 LPAEefspEFRDFISACLQKDPKKRPSAAELLQHPFIK 260
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
531-790 2.64e-35

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: 134.72  E-value: 2.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEK--KQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME-CGNI 607
Cdd:cd14121   3 LGSGTYATVYKAYRKSgaREVVAVKCVSKSSLNKASTENLLTEIELLKKL--KHPHIVELKDFQWDEEHIYLIMEyCSGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG---MLKLIDFGIANQMQPDttsVVKDSQV 684
Cdd:cd14121  81 DLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRynpVLKLADFGFAQHLKPN---DEAHSLR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 685 GTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDPNHEIEFPDIPE--K 762
Cdd:cd14121 158 GSPLYMAPEMILKKKYD-----------ARVDLWSVGVILYECLFGRAPFAS--RSFEELEEKIRSSKPIEIPTRPElsA 224
                       250       260
                ....*....|....*....|....*...
gi 23308722 763 DLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14121 225 DCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
531-791 8.35e-34

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: 130.45  E-value: 8.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVnleeaDNQTL-------DSYRNEIAYLNKLqqHSDKIIRLYD--YEITDQYIYM 600
Cdd:cd14119   1 LGEGSYGKVKEVLDtETLCRRAVKIL-----KKRKLrripngeANVKREIQILRRL--NHRNVIKLVDvlYNEEKQKLYM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGNIDLNSWLKK--KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTS 677
Cdd:cd14119  74 VMEYCVGGLQEMLDSapDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLtTDGTLKISDFGVAEALDLFAED 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPE--AIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDPNhEIE 755
Cdd:cd14119 154 DTCTTSQGSPAFQPPEiaNGQDSFSGFK-----------VDIWSAGVTLYNMTTGKYPFEG--DNIYKLFENIGKG-EYT 219
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14119 220 IPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
525-790 9.27e-34

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: 131.47  E-value: 9.27e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEeadnqtlDSYRN-EIAYLNKLQQHSdkIIRLYDYEIT------DQ 596
Cdd:cd14137   6 YTIEKVIGSGSFGVVYQAkLLETGEVVAIKKVLQD-------KRYKNrELQIMRRLKHPN--IVKLKYFFYSsgekkdEV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVMECGNIDLNSWLKK----KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGIANQ 670
Cdd:cd14137  77 YLNLVMEYMPETLYRVIRHysknKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVdpETGVLKLCDFGSAKR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MQPDTTSVvkdSQVGTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPFQQiINQISKLHAI 747
Cdd:cd14137 157 LVPGEPNV---SYICSRYYRAPELIfgaTDYTTA-------------IDIWSAGCVLAELLLGQPLFPG-ESSVDQLVEI 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 748 ID--------------PNH-EIEFPDIPEKDLQ------------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14137 220 IKvlgtptreqikamnPNYtEFKFPQIKPHPWEkvfpkrtppdaiDLLSKILVYNPSKRLTALEALAHPF 289
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
525-791 9.64e-34

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: 130.20  E-value: 9.64e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVME 603
Cdd:cd08530   2 FKVLKKLGKGSYGSVYKVKrLSDNQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPN--IIRYKEAFLDGNRLCIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNI-DLNSWLKK-KKSIDPWERKSYWK---NMLEAVHTIHQHGIVHSDLKPANFLIVDG-MLKLIDFGIANQMqpdtTS 677
Cdd:cd08530  80 YAPFgDLSKLISKrKKKRRLFPEDDIWRifiQMLRGLKALHDQKILHRDLKSANILLSAGdLVKIGDLGISKVL----KK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQisklhaiiDPNHEI--- 754
Cdd:cd08530 156 NLAKTQIGTPLYAAPEVWKGRPYD-----------YKSDIWSLGCLLYEMATFRPPFEARTMQ--------ELRYKVcrg 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 755 EFPDIPE---KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd08530 217 KFPPIPPvysQDLQQIIRSLLQVNPKKRPSCDKLLQSPAV 256
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
525-790 4.54e-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: 128.75  E-value: 4.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEE--ADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMV 601
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKaVEVETGKMRAIKQIVKRKvaGNDKNLQLFQREINILKSL--EHPGIVRLIDWYEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV---DGMLKLIDFGIANQMQPDTTS 677
Cdd:cd14098  80 MEyVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITqddPVIVKISDFGLAKVIHTGTFL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VvkdSQVGTVNYMPPEAIKDMSSSRENGkskskISPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIIDPNH 752
Cdd:cd14098 160 V---TFCGTMAYLAPEILMSKEQNLQGG-----YSNLVDMWSVGCLVYVMLTGALPFdgssqLPVEKRIRKGRYTQPPLV 231
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 753 EIEfpdIPEKDLqDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14098 232 DFN---ISEEAI-DFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
531-790 5.98e-33

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: 128.63  E-value: 5.98e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQ-VLNEKKQIYAIKYVNL------EEADNQTLDSYRNEIAYLNKLQQHsDKIIRLYDYEITDQYIYMVME 603
Cdd:cd14093  11 LGRGVSSTVRRcIEKETGQEFAVKIIDItgekssENEAEELREATRREIEILRQVSGH-PNIIELHDVFESPTFIFLVFE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTsvVKD 681
Cdd:cd14093  90 lCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLnVKISDFGFATRLDEGEK--LRE 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 sQVGTVNYMPPEAIKdmSSSRENgksKSKISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEI---EFPD 758
Cdd:cd14093 168 -LCGTPGYLAPEVLK--CSMYDN---APGYGKEVDMWACGVIMYTLLAGCPPFWH-RKQMVMLRNIMEGKYEFgspEWDD 240
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 759 IPEkDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14093 241 ISD-TAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
525-786 9.69e-33

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: 127.85  E-value: 9.69e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYV-----NLEEADNQTLDSYRNEIAYLNKLQQHsDKIIRLYDYEITDQYI 598
Cdd:cd13993   2 YQLISPIGEGAYGVVYLAVDlRTGRKYAIKCLyksgpNSKDGNDFQKLPQLREIDLHRRVSRH-PNIITLHDVFETEVAI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME-CGNIDLNSWLKKKKsIDPWERKSYWKNMLE---AVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGIANQmq 672
Cdd:cd13993  81 YIVLEyCPNGDLFEAITENR-IYVGKTELIKNVFLQlidAVKHCHSLGIYHRDIKPENILLsqDEGTVKLCDFGLATT-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 pDTTSvvKDSQVGTVNYMPPEAIKDMSSSREngkskSKISPKSDVWSLGCILYYMTYGKTPFqQIINQISKLHAIIDPNH 752
Cdd:cd13993 158 -EKIS--MDFGVGSEFYMAPECFDEVGRSLK-----GYPCAAGDIWSLGIILLNLTFGRNPW-KIASESDPIFYDYYLNS 228
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 753 EIEFPDIP--EKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd13993 229 PNLFDVILpmSDDFYNLLRQIFTVNPNNRILLPELQ 264
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
565-791 1.42e-32

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: 127.48  E-value: 1.42e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 565 LDSYRNEIAYLNKLQqHSDkIIRLYdyEITD----QYIYMVMEcgnidlnswLKKKKSI------DPWER---KSYWKNM 631
Cdd:cd14118  58 LDRVYREIAILKKLD-HPN-VVKLV--EVLDdpneDNLYMVFE---------LVDKGAVmevptdNPLSEetaRSYFRDI 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 632 LEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSVvkDSQVGTVNYMPPEAIKDmSSSRENGKSKsk 710
Cdd:cd14118 125 VLGIEYLHYQKIIHRDIKPSNLLLGdDGHVKIADFGVSNEFEGDDALL--SSTAGTPAFMAPEALSE-SRKKFSGKAL-- 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 711 ispksDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDpNHEIEFPDIPE--KDLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd14118 200 -----DIWAMGVTLYCFVFGRCPFED--DHILGLHEKIK-TDPVVFPDDPVvsEQLKDLILRMLDKNPSERITLPEIKEH 271

                ...
gi 23308722 789 PYV 791
Cdd:cd14118 272 PWV 274
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
525-789 2.48e-32

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: 126.37  E-value: 2.48e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVVRKvDGRVYALKQIDISRMSRKMREEAIDEARVLSKLN--SPYVIKYYDSFVDKGKLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSiDPWERKSYWK---NMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMqpDTTSV 678
Cdd:cd08529  80 yAENGDLHSLIKSQRG-RPLPEDQIWKffiQTLLGLSHLHSKKILHRDIKSMNiFLDKGDNVKIGDLGVAKIL--SDTTN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFqQIINQISKLHAIIDPnheiEFPD 758
Cdd:cd08529 157 FAQTIVGTPYYLSPELCEDKPYNEKS-----------DVWALGCVLYELCTGKHPF-EAQNQGALILKIVRG----KYPP 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 759 IPE---KDLQDVLKCCLKRDPKQRISIPELLAHP 789
Cdd:cd08529 221 ISAsysQDLSQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
531-786 2.80e-32

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: 125.73  E-value: 2.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNeKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVME-CGNIDL 609
Cdd:cd13999   1 IGSGSFGEVYKGKW-RGTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPN--IVQFIGACLSPPPLCIVTEyMPGGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 610 NSWLKKKKSIDPWERKSYW-KNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQpdTTSVVKDSQVGTV 687
Cdd:cd13999  78 YDLLHKKKIPLSWSLRLKIaLDIARGMNYLHSPPIIHRDLKSLNILLDENFtVKIADFGLSRIKN--STTEKMTGVVGTP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 688 NYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQqiinQISKLHAIIDPNHEIEFPDIPE---KDL 764
Cdd:cd13999 156 RWMAPEVLRGEPYTEK-----------ADVYSFGIVLWELLTGEVPFK----ELSPIQIAAAVVQKGLRPPIPPdcpPEL 220
                       250       260
                ....*....|....*....|..
gi 23308722 765 QDVLKCCLKRDPKQRISIPELL 786
Cdd:cd13999 221 SKLIKRCWNEDPEKRPSFSEIV 242
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
531-790 4.40e-31

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: 122.86  E-value: 4.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVF--QVLNEKKQIYAIKYVNLEE-ADNQTLDSyrNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME-CGN 606
Cdd:cd14120   1 IGHGAFAVVFkgRHRKKPDLPVAIKCITKKNlSKSQNLLG--KEIKILKEL--SHENVVALLDCQETSSSVYLVMEyCNG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI----------VDGMLKLIDFGIANQMQPDTT 676
Cdd:cd14120  77 GDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLshnsgrkpspNDIRLKIADFGFARFLQDGMM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVvkdSQVGTVNYMPPEAIkdMSSSREngkskskisPKSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDPNHEIeF 756
Cdd:cd14120 157 AA---TLCGSPMYMAPEVI--MSLQYD---------AKADLWSIGTIVYQCLTGKAPFQA--QTPQELKAFYEKNANL-R 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 757 PDIPE---KDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14120 220 PNIPSgtsPALKDLLLGLLKRNPKDRIDFEDFFSHPF 256
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
525-791 7.06e-31

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: 122.05  E-value: 7.06e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSYRNEIaYLNKLQQHsDKIIRLYDYEITDQYIYMVME 603
Cdd:cd14069   3 WDLVQTLGEGAFGEVFLAVNRNtEEAVAVKFVDMKRAPGDCPENIKKEV-CIQKMLSH-KNVVRFYGHRREGEFQYLFLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSVVKD 681
Cdd:cd14069  81 yASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDEnDNLKISDFGLATVFRYKGKERLLN 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAikdMSSSRENGkskskisPKSDVWSLGCILYYMTYGKTPFQQ-IINQISKLHAIIDPNHE------I 754
Cdd:cd14069 161 KMCGTLPYVAPEL---LAKKKYRA-------EPVDVWSCGIVLFAMLAGELPWDQpSDSCQEYSDWKENKKTYltpwkkI 230
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 755 EFPDIpekdlqDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14069 231 DTAAL------SLLRKILTENPNKRITIEDIKKHPWY 261
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
531-791 1.14e-30

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: 121.74  E-value: 1.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRN---EIAYLNKLQqHSDkIIRLYDYEITDQYIYMVMECgn 606
Cdd:cd06632   8 LGSGSFGSVYEGFNgDTGDFFAVKEVSLVDDDKKSRESVKQleqEIALLSKLR-HPN-IVQYYGTEREEDNLYIFLEY-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDPWER---KSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQPDTTSVVKd 681
Cdd:cd06632  84 VPGGSIHKLLQRYGAFEEpviRLYTRQILSGLAYLHSRNTVHRDIKGANILVdTNGVVKLADFGMAKHvEAFSFAKSFK- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 sqvGTVNYMPPEAIKDMSSSrengkskskISPKSDVWSLGCILYYMTYGKTPFqqiiNQISKLHAIIDPNHEIEFPDIPE 761
Cdd:cd06632 163 ---GSPYWMAPEVIMQKNSG---------YGLAVDIWSLGCTVLEMATGKPPW----SQYEGVAAIFKIGNSGELPPIPD 226
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 762 ---KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06632 227 hlsPDAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
525-791 6.34e-30

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: 119.28  E-value: 6.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADN-QTLDSYRNEIAYLnKLQQHSDkIIRLYD-YEiTDQYIYMV 601
Cdd:cd14081   3 YRLGKTLGKGQTGLVKLAKHCVtGQKVAIKIVNKEKLSKeSVLMKVEREIAIM-KLIEHPN-VLKLYDvYE-NKKYLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MEC---GniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDT-- 675
Cdd:cd14081  80 LEYvsgG--ELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLdEKNNIKIADFGMASLQPEGSll 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 -TSvvkdsqVGTVNYMPPEAIKdmsSSRENGkskskisPKSDVWSLGCILYYMTYGKTPF-----QQIINQISklhaiid 749
Cdd:cd14081 158 eTS------CGSPHYACPEVIK---GEKYDG-------RKADIWSCGVILYALLVGALPFdddnlRQLLEKVK------- 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 750 pNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14081 215 -RGVFHIPHFISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
528-789 2.06e-29

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: 117.87  E-value: 2.06e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVME-CG 605
Cdd:cd13997   5 LEQIGSGSFSEVFKVRSkVDGCLYAVKKSKKPFRGPKERARALREVEAHAALGQHPN-IVRYYSSWEEGGHLYIQMElCE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKKKSIDPWERKSYWKNMLE---AVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpdttSVVKD 681
Cdd:cd13997  84 NGSLQDALEELSPISKLSEAEVWDLLLQvalGLAFIHSKGIVHLDIKPDNIFIsNKGTCKIGDFGLATRL-----ETSGD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIKDmsssrengksKSKISPKSDVWSLGCILYYMTYGkTPFQQIINQISKLHaiidpnhEIEFPDIPE 761
Cdd:cd13997 159 VEEGDSRYLAPELLNE----------NYTHLPKADIFSLGVTVYEAATG-EPLPRNGQQWQQLR-------QGKLPLPPG 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 762 K----DLQDVLKCCLKRDPKQRISIPELLAHP 789
Cdd:cd13997 221 LvlsqELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
525-790 2.61e-29

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: 118.44  E-value: 2.61e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLE-EADNQTLDSYRnEIAYLNKLQQhsDKIIRLYDYEITDQY----- 597
Cdd:cd07840   1 YEKIAQIGEGTYGQVYKARNKKtGELVALKKIRMEnEKEGFPITAIR-EIKLLQKLDH--PNVVRLKEIVTSKGSakykg 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 -IYMVMECGNIDLNSWLKKKKS-IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPD 674
Cdd:cd07840  78 sIYMVFEYMDHDLTGLLDNPEVkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINnDGVLKLADFGLARPYTKE 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 -----TTSVVkdsqvgTVNYMPPEAIkdMSSSRENGkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIID 749
Cdd:cd07840 158 nnadyTNRVI------TLWYRPPELL--LGATRYGP--------EVDMWSVGCILAELFTGKPIFQG-KTELEQLEKIFE 220
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 750 ----------------PNHEIEFPDIPEKD-LQDVLKCC------------LKRDPKQRISIPELLAHPY 790
Cdd:cd07840 221 lcgspteenwpgvsdlPWFENLKPKKPYKRrLREVFKNVidpsaldlldklLTLDPKKRISADQALQHEY 290
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
524-797 3.63e-29

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: 117.73  E-value: 3.63e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEEADNQtLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd06609   2 LFTLLERIGKGSFGEVYKgIDKRTNQVVAIKVIDLEEAEDE-IEDIQQEIQFLSQC--DSPYITKYYGSFLKGSKLWIIM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKsIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQpdTTSVVK 680
Cdd:cd06609  79 EyCGGGSVLDLLKPGP-LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSeEGDVKLADFGVSGQLT--STMSKR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFqqiinqiSKLHA----IIDPNHEIef 756
Cdd:cd06609 156 NTFVGTPFWMAPEVIKQSGYD-----------EKADIWSLGITAIELAKGEPPL-------SDLHPmrvlFLIPKNNP-- 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 757 PDIPE----KDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHP 797
Cdd:cd06609 216 PSLEGnkfsKPFKDFVELCLNKDPKERPSAKELLKHKFIKKAKKT 260
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
531-793 4.16e-29

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: 116.94  E-value: 4.16e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQI-YAIKYVNleeadnqtldsyRNEIAYLNkLQQH------------SDKIIRLYDYEITDQY 597
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRtFALKCVK------------KRHIVQTR-QQEHifsekeileecnSPFIVKLYRTFKDKKY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDT 675
Cdd:cd05572  68 LYMLMEyCLGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLdSNGYVKLVDFGFAKKLGSGR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVvkdSQVGTVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCILYYMTYGKTPFQQI-INQISKLHAIIDP 750
Cdd:cd05572 148 KTW---TFCGTPEYVAPEIILnkgyDFSV---------------DYWSLGILLYELLTGRPPFGGDdEDPMKIYNIILKG 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 23308722 751 NHEIEFPDIPEKDLQDVLKCCLKRDPKQRI-----SIPELLAHPYVQI 793
Cdd:cd05572 210 IDKIEFPKYIDKNAKNLIKQLLRRNPEERLgylkgGIRDIKKHKWFEG 257
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
525-791 4.32e-29

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: 116.90  E-value: 4.32e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK---KQIYAIKYVNleeaDNQTLDSYRN-----EIAYLNKLQqHSDkIIRLYDYEITDQ 596
Cdd:cd14080   2 YRLGKTIGEGSYSKVKLAEYTKsglKEKVACKIID----KKKAPKDFLEkflprELEILRKLR-HPN-IIQVYSIFERGS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPD 674
Cdd:cd14080  76 KVFIFMEyAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNnVKLSDFGFARLCPDD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKDSQVGTVNYMPPEAIK----DMSSSrengkskskispksDVWSLGCILYYMTYGKTPF------QQIINQIskl 744
Cdd:cd14080 156 DGDVLSKTFCGSAAYAAPEILQgipyDPKKY--------------DIWSLGVILYIMLCGSMPFddsnikKMLKDQQ--- 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 745 haiidpNHEIEFPDIPEK---DLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14080 219 ------NRKVRFPSSVKKlspECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
525-790 4.57e-29

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: 116.74  E-value: 4.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSY-RNEIAYLnKLQQHSDkIIRLYDYEITDQYIYMVM 602
Cdd:cd14663   2 YELGRTLGEGTFAKVKFARNtKTGESVAIKIIDKEQVAREGMVEQiKREIAIM-KLLRHPN-IVELHEVMATKTKIFFVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVV 679
Cdd:cd14663  80 ElvTGG-ELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLdEDGNLKISDFGLSALSEQFRQDGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIkdmsssRENGksksKISPKSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDpNHEIEFPDI 759
Cdd:cd14663 159 LHTTCGTPNYVAPEVL------ARRG----YDGAKADIWSCGVILFVLLAGYLPFDD--ENLMALYRKIM-KGEFEYPRW 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 23308722 760 PEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14663 226 FSPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
571-792 8.04e-29

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: 116.99  E-value: 8.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 571 EIAYLNKLQqHSD--KIIRLYDyEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDL 648
Cdd:cd14199  75 EIAILKKLD-HPNvvKLVEVLD-DPSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDV 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 649 KPANFLI-VDGMLKLIDFGIANQMQpdTTSVVKDSQVGTVNYMPPEAikdMSSSRENgksksKISPKSDVWSLGCILYYM 727
Cdd:cd14199 153 KPSNLLVgEDGHIKIADFGVSNEFE--GSDALLTNTVGTPAFMAPET---LSETRKI-----FSGKALDVWAMGVTLYCF 222
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 728 TYGKTPFQQiiNQISKLHAIIDpNHEIEFPDIPE--KDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14199 223 VFGQCPFMD--ERILSLHSKIK-TQPLEFPDQPDisDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
531-790 1.31e-28

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: 115.06  E-value: 1.31e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLnEK--KQIYAIKYVNLEEADNqtlDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYMVME-CGNI 607
Cdd:cd14006   1 LGRGRFGVVKRCI-EKatGREFAAKFIPKRDKKK---EAVLREISILNQLQ-H-PRIIQLHEAYESPTELVLILElCSGG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM---LKLIDFGIANQMQPDttsVVKDSQV 684
Cdd:cd14006  75 ELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspqIKIIDFGLARKLNPG---EELKEIF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 685 GTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIIDPnheiEFPDI 759
Cdd:cd14006 152 GTPEFVAPEIVNGEPVS-----------LATDMWSIGVLTYVLLSGLSPFlgeddQETLANISACRVDFSE----EYFSS 216
                       250       260       270
                ....*....|....*....|....*....|.
gi 23308722 760 PEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14006 217 VSQEAKDFIRKLLVKEPRKRPTAQEALQHPW 247
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
525-791 1.61e-28

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: 116.22  E-value: 1.61e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQ-IYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSD-KIIRLYDYEITDQY----- 597
Cdd:cd07838   1 YEEVAEIGEGAYGTVYKARDLQDGrFVALKKVRVPLSEEGIPLSTIREIALLKQLESFEHpNVVRLLDVCHGPRTdrelk 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKK--KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIA----NQ 670
Cdd:cd07838  81 LTLVFEHVDQDLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTsDGQVKLADFGLAriysFE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MQpdTTSVVKdsqvgTVNYMPPEAIkdMSSSrengkskskISPKSDVWSLGCILYYMtYGKTPF---QQIINQISKLHAI 747
Cdd:cd07838 161 MA--LTSVVV-----TLWYRAPEVL--LQSS---------YATPVDMWSVGCIFAEL-FNRRPLfrgSSEADQLGKIFDV 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 748 I-------------------DPNHEIEFPD-IPEKDLQ--DVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd07838 222 IglpseeewprnsalprssfPSYTPRPFKSfVPEIDEEglDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
525-790 2.79e-28

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: 115.75  E-value: 2.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYVNLEE----ADNQTLDSYRnEIAYLNKLQqHsDKIIRLYDYEITDQYIY 599
Cdd:cd07841   2 YEKGKKLGEGTYAVVYKARdKETGRIVAIKKIKLGErkeaKDGINFTALR-EIKLLQELK-H-PNIIGLLDVFGHKSNIN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDLNSwLKKKKSID--PWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQM-QPDT 675
Cdd:cd07841  79 LVFEFMETDLEK-VIKDKSIVltPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIAsDGVLKLADFGLARSFgSPNR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 tsvVKDSQVGTVNYMPPEAikdMSSSRENGkskskisPKSDVWSLGCILYYMTYGKtPF---QQIINQISKLHAII-DPN 751
Cdd:cd07841 158 ---KMTHQVVTRWYRAPEL---LFGARHYG-------VGVDMWSVGCIFAELLLRV-PFlpgDSDIDQLGKIFEALgTPT 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 752 HE-----------IEFPDIPEK-----------DLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07841 224 EEnwpgvtslpdyVEFKPFPPTplkqifpaasdDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
525-790 4.21e-28

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: 113.89  E-value: 4.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEAD-NQTLDSYRNEIAYLNKLQqHSdKIIRLYdYEITD-QYIYMV 601
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVqKKDTKKMFAMKYMNKQKCIeKDSVRNVLNELEILQELE-HP-FLVNLW-YSFQDeEDMYMV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSvv 679
Cdd:cd05578  79 VDlLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLdEQGHVHITDFNIATKLTDGTLA-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 kDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDI 759
Cdd:cd05578 157 -TSTSGTKPYMAPEVFMRAGYSFA-----------VDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAG 224
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 760 PEKDLQDVLKCCLKRDPKQRISIPE-LLAHPY 790
Cdd:cd05578 225 WSEEAIDLINKLLERDPQKRLGDLSdLKNHPY 256
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
547-798 5.80e-28

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 115.09  E-value: 5.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 547 KQIYAIKYVNleeadnQTLDSYRnEIAYLNKLQQHSDkIIRLYDYeITDQY-IYMVMEC--GNiDLNSWLKKKKSIDPWE 623
Cdd:cd14092  31 GQEFAVKIVS------RRLDTSR-EVQLLRLCQGHPN-IVKLHEV-FQDELhTYLVMELlrGG-ELLERIRKKKRFTESE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 624 RKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD----GMLKLIDFGIAN---QMQPDTTSVVkdsqvgTVNYMPPEAIK 696
Cdd:cd14092 101 ASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDedddAEIKIVDFGFARlkpENQPLKTPCF------TLPYAAPEVLK 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 697 DMSSsrENGkskskISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFP-DIPE-----KDLQDVLKC 770
Cdd:cd14092 175 QALS--TQG-----YDESCDLWSLGVILYTMLSGQVPFQS-PSRNESAAEIMKRIKSGDFSfDGEEwknvsSEAKSLIQG 246
                       250       260
                ....*....|....*....|....*...
gi 23308722 771 CLKRDPKQRISIPELLAHPYVQIQTHPV 798
Cdd:cd14092 247 LLTVDPSKRLTMSELRNHPWLQGSSSPS 274
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
525-790 7.77e-28

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: 113.95  E-value: 7.77e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIYA---IKYVNLEEADNQTLDSYR---NEIAYLNKLQQHsdKIIRLYD-YEITDQY 597
Cdd:cd13990   2 YLLLNLLGKGGFSEVYKAFDLVEQRYVackIHQLNKDWSEEKKQNYIKhalREYEIHKSLDHP--RIVKLYDvFEIDTDS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQH--GIVHSDLKPANFLIVD----GMLKLIDFGIANQ 670
Cdd:cd13990  80 FCTVLEyCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIkpPIIHYDLKPGNILLHSgnvsGEIKITDFGLSKI 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MQPDTTSVVK---DSQ-VGTVNYMPPEAIkdmsssrENGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHA 746
Cdd:cd13990 160 MDDESYNSDGmelTSQgAGTYWYLPPECF-------VVGKTPPKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILEE 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23308722 747 -IIDPNHEIEFPDIP--EKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd13990 233 nTILKATEVEFPSKPvvSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
525-790 1.08e-27

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: 113.95  E-value: 1.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME 603
Cdd:cd07833   3 YEVLGVVGEGAYGVVLKCRNkATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRH--ENIVNLKEAFRRKGRLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSVVkD 681
Cdd:cd07833  81 yVERTLLELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSeSGVLKLCDFGFARALTARPASPL-T 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAikdMSSSRENGkskskisPKSDVWSLGCILYYMTYGKTPF------------QQIINQISKLH---- 745
Cdd:cd07833 160 DYVATRWYRAPEL---LVGDTNYG-------KPVDVWAIGCIMAELLDGEPLFpgdsdidqlyliQKCLGPLPPSHqelf 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 746 ---------AIIDPNH----EIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07833 230 ssnprfagvAFPEPSQpeslERRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
525-790 1.28e-27

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: 113.58  E-value: 1.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd07832   2 YKILGRIGEGAHGIVFKAKDrETGETVALKKVALRKLEGGIPNQALREIKALQACQGHPY-VVKLRDVFPHGTGFVLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLK-KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDtTSVVKD 681
Cdd:cd07832  81 YMLSSLSEVLRdEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISStGVLKIADFGLARLFSEE-DPRLYS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIkdmSSSRENGkskskisPKSDVWSLGCILYYMTYGK--------------------TPFQQIINQI 741
Cdd:cd07832 160 HQVATRWYRAPELL---YGSRKYD-------EGVDLWAVGCIFAELLNGSplfpgendieqlaivlrtlgTPNEKTWPEL 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 742 SKL---HAIIDPNH-----EIEFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07832 230 TSLpdyNKITFPESkgirlEEIFPDCSPEAI-DLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
525-790 1.42e-27

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: 112.77  E-value: 1.42e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVlNEKKQI--YAIKYVNleeadnqtlDSYRNEIAYLNKLQQ--HSDKIIRLYD-YEiTDQYIY 599
Cdd:cd14010   2 YVLYDEIGRGKHSVVYKG-RRKGTIefVAIKCVD---------KSKRPEVLNEVRLTHelKHPNVLKFYEwYE-TSNHLW 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLiVD--GMLKLIDFGIA-------- 668
Cdd:cd14010  71 LVVEyCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNIL-LDgnGTLKLSDFGLArregeilk 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 ----------NQMQPDttsvVKDSQVGTVNYMPPEAIKD----MSSsrengkskskispksDVWSLGCILYYMTYGKTPF 734
Cdd:cd14010 150 elfgqfsdegNVNKVS----KKQAKRGTPYYMAPELFQGgvhsFAS---------------DLWALGCVLYEMFTGKPPF 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23308722 735 Q-----QIINQIskLHAiiDPNH-EIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14010 211 VaesftELVEKI--LNE--DPPPpPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
525-786 1.53e-27

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: 112.81  E-value: 1.53e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIK--YVNleeaDNQTLDSYRNEIAYLNKLQQHSDkIIRLYDYEITD----QY 597
Cdd:cd13985   2 YQVTKQLGEGGFSYVYLAHDVnTGRRYALKrmYFN----DEEQLRVAIKEIEIMKRLCGHPN-IVQYYDSAILSsegrKE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNiDLNSWLKKKKSIDPWERK--SYWKNMLEAVHTIHQHG--IVHSDLKPANFLIVD-GMLKLIDFGIA-NQ 670
Cdd:cd13985  77 VLLLMEyCPG-SLVDILEKSPPSPLSEEEvlRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNtGRFKLCDFGSAtTE 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MQPDTTS---VVKDSQVG---TVNYMPPEAIkDMSSSRENGKSKskispksDVWSLGCILYYMTYGKTPFQQiinqiSKL 744
Cdd:cd13985 156 HYPLERAeevNIIEEEIQkntTPMYRAPEMI-DLYSKKPIGEKA-------DIWALGCLLYKLCFFKLPFDE-----SSK 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 745 HAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd13985 223 LAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVI 264
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
525-786 2.79e-27

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: 111.98  E-value: 2.79e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEE-ADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVM 602
Cdd:cd08224   2 YEIEKKIGKGQFSVVYRARCLLdGRLVALKKVQIFEmMDAKARQDCLKEIDLLQQLNHPN--IIKYLASFIENNELNIVL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKK-KKSIDPWERKSYWKNMLE---AVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQPDTT 676
Cdd:cd08224  80 ElADAGDLSRLIKHfKKQKRLIPERTIWKYFVQlcsALEHMHSKRIMHRDIKPANvFITANGVVKLGDLGLGRFFSSKTT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 svVKDSQVGTVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCILYYMTYGKTPFQQ-------IINQISKlh 745
Cdd:cd08224 160 --AAHSLVGTPYYMSPERIReqgyDFKS---------------DIWSLGCLLYEMAALQSPFYGekmnlysLCKKIEK-- 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 746 aiidpnheIEFPDIPEK----DLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd08224 221 --------CEYPPLPADlysqELRDLVAACIQPDPEKRPDISYVL 257
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
525-791 2.87e-27

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: 111.75  E-value: 2.87e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-------KQIYAIKYVNLEEadNQTLDSYRnEIAYLNKLQQHSdkIIRLYDYEITDQY 597
Cdd:cd08222   2 YRVVRKLGSGNFGTVYLVSDLKatadeelKVLKEISVGELQP--DETVDANR-EAKLLSKLDHPA--IVKFHDSFVEKES 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNIDL----NSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQ 672
Cdd:cd08222  77 FCIVTEyCEGGDLddkiSEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNVIKVGDFGISRILM 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 pdTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIdpnh 752
Cdd:cd08222 157 --GTSDLATTFTGTPYYMSPEVLKHEGYNSKS-----------DIWSLGCILYEMCCLKHAFDG-QNLLSVMYKIV---- 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 753 EIEFPDIPE---KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd08222 219 EGETPSLPDkysKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
565-791 3.30e-27

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: 112.35  E-value: 3.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 565 LDSYRNEIAYLNKLQqHSD--KIIRLYDYEITDQyIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHG 642
Cdd:cd14200  67 LERVYQEIAILKKLD-HVNivKLIEVLDDPAEDN-LYMVFDLLRKGPVMEVPSDKPFSEDQARLYFRDIVLGIEYLHYQK 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 643 IVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSVvkDSQVGTVNYMPPEAIKDMSSSRENgkskskisPKSDVWSLG 721
Cdd:cd14200 145 IVHRDIKPSNLLLGDdGHVKIADFGVSNQFEGNDALL--SSTAGTPAFMAPETLSDSGQSFSG--------KALDVWAMG 214
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23308722 722 CILYYMTYGKTPFqqIINQISKLHAIIDpNHEIEFPDIPE--KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14200 215 VTLYCFVYGKCPF--IDEFILALHNKIK-NKPVEFPEEPEisEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
525-801 5.08e-27

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: 111.96  E-value: 5.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNqtldsyRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd14091   2 YEIKEEIGKGSYSVCKRCIHKaTGKEYAVKIIDKSKRDP------SEEIEILLRYGQHPN-IITLRDVYDDGNSVYLVTE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-----GMLKLIDFGIANQMQPDTts 677
Cdd:cd14091  75 lLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADesgdpESLRICDFGFAKQLRAEN-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 vvkdsqvG-------TVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCILYYMTYGKTPF--------QQII 738
Cdd:cd14091 153 -------GllmtpcyTANFVAPEVLKkqgyDAAC---------------DIWSLGVLLYTMLAGYTPFasgpndtpEVIL 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 739 NQIS--KL-------HAIIDpnheiefpdiPEKDLqdvLKCCLKRDPKQRISIPELLAHPYVQIQTH-PVNQM 801
Cdd:cd14091 211 ARIGsgKIdlsggnwDHVSD----------SAKDL---VRKMLHVDPSQRPTAAQVLQHPWIRNRDSlPQRQL 270
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
528-792 7.30e-27

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: 110.90  E-value: 7.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVLNEKK-QIYAIKYVNL---EEADNQTLdsyrNEIAYLNKlqQHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd06605   6 LGELGEGNGGVVSKVRHRPSgQIMAVKVIRLeidEALQKQIL----RELDVLHK--CNSPYIVGFYGAFYSEGDISICME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDpwerKSYWKNMLEAV-----HTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpdTT 676
Cdd:cd06605  80 yMDGGSLDKILKEVGRIP----ERILGKIAVAVvkgliYLHEKHKIIHRDVKPSNILVnSRGQVKLCDFGVSGQL---VD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSqVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQI-----INQISKLHAIID-- 749
Cdd:cd06605 153 SLAKTF-VGTRSYMAPERISGGKYT-----------VKSDIWSLGLSLVELATGRFPYPPPnakpsMMIFELLSYIVDep 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23308722 750 ----PNHEieFPdipeKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06605 221 ppllPSGK--FS----PDFQDFVSQCLQKDPTERPSYKELMEHPFIK 261
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
523-792 1.14e-26

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: 111.88  E-value: 1.14e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVnleeadnqtLDSYRN---------EIAYLNKLQQHsDKIIRLYDY- 591
Cdd:cd07852   7 RRYEILKKLGKGAYGIVWKAIDKKtGEVVALKKI---------FDAFRNatdaqrtfrEIMFLQELNDH-PNIIKLLNVi 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 592 -EITDQYIYMVMECGNIDLNSWLKKkksidpwerksywkNMLEAVHT-------------IHQHGIVHSDLKPANFLI-V 656
Cdd:cd07852  77 rAENDKDIYLVFEYMETDLHAVIRA--------------NILEDIHKqyimyqllkalkyLHSGGVIHRDLKPSNILLnS 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 657 DGMLKLIDFGIA---NQMQPDTTSVVKDSQVGTVNYMPPEAIkdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTP 733
Cdd:cd07852 143 DCRVKLADFGLArslSQLEEDDENPVLTDYVATRWYRAPEIL--LGSTRYT--------KGVDMWSVGCILGEMLLGKPL 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 734 FQ--QIINQISKLHAIID-PNHE-IE-------------------------FPDIPeKDLQDVLKCCLKRDPKQRISIPE 784
Cdd:cd07852 213 FPgtSTLNQLEKIIEVIGrPSAEdIEsiqspfaatmleslppsrpksldelFPKAS-PDALDLLKKLLVFNPNKRLTAEE 291

                ....*...
gi 23308722 785 LLAHPYVQ 792
Cdd:cd07852 292 ALRHPYVA 299
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
524-792 1.24e-26

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: 109.61  E-value: 1.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEeadNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd06614   1 LYKNLEKIGEGASGEVYKATDRATgKEVAIKKMRLR---KQNKELIINEILIMKEC--KHPNIVDYYDSYLVGDELWVVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E---CGNidLNSWLKKKKSIDPWERKSY-WKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpdTTS 677
Cdd:cd06614  76 EymdGGS--LTDIITQNPVRMNESQIAYvCREVLQGLEYLHSQNVIHRDIKSDNILLsKDGSVKLADFGFAAQL---TKE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVK-DSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQISKLhaiidPN 751
Cdd:cd06614 151 KSKrNSVVGTPYWMAPEVIKRKDYGPK-----------VDIWSLGIMCIEMAEGEPPYleeppLRALFLITTK-----GI 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23308722 752 HEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06614 215 PPLKNPEKWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
529-791 1.27e-26

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: 109.75  E-value: 1.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQV--LNEKKQIyAIKYVNLEEADNQT---LDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME 603
Cdd:cd06625   6 KLLGQGAFGQVYLCydADTGREL-AVKQVEIDPINTEAskeVKALECEIQLLKNLQH--ERIVQYYGCLQDEKSLSIFME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 C---GNIdlNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVV 679
Cdd:cd06625  83 YmpgGSV--KDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRdSNGNVKLGDFGASKRLQTICSSTG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFPDI 759
Cdd:cd06625 161 MKSVTGTPYWMSPEVINGEGYGRK-----------ADIWSVGCTVVEMLTTKPPWAE-FEPMAAIFKIATQPTNPQLPPH 228
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 760 PEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06625 229 VSEDARDFLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
525-791 1.30e-26

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: 109.69  E-value: 1.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSY--RnEIAYLNKLQqHSDkIIRLYDYEITDQYIYMV 601
Cdd:cd14162   2 YIVGKTLGHGSYAVVKKAYSTKhKCKVAIKIVSKKKAPEDYLQKFlpR-EIEVIKGLK-HPN-LICFYEAIETTSRVYII 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECG-NIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIA-NQMQP-DTTS 677
Cdd:cd14162  79 MELAeNGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLdKNNNLKITDFGFArGVMKTkDGKP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPEAIKDMSssrengksksKISPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKlhaiidpnh 752
Cdd:cd14162 159 KLSETYCGSYAYASPEILRGIP----------YDPFLSDIWSMGVVLYTMVYGRLPFddsnlKVLLKQVQR--------- 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23308722 753 EIEFPDIPE--KDLQDVLKCCLkRDPKQRISIPELLAHPYV 791
Cdd:cd14162 220 RVVFPKNPTvsEECKDLILRML-SPVKKRITIEEIKRDPWF 259
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
525-788 2.40e-26

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: 108.96  E-value: 2.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKV----FQVLNEKkqiYAIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYM 600
Cdd:cd14075   4 YRIRGELGSGNFSQVklgiHQLTKEK---VAIKILDKTKLDQKTQRLLSREISSMEKL--HHPNIIRLYEVVETLSKLHL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME--CGNIDLNSWLKKKKSIDPwERKSYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQPDTTS 677
Cdd:cd14075  79 VMEyaSGGELYTKISTEGKLSES-EAKPLFAQIVSAVKHMHENNIIHRDLKAENvFYASNNCVKVGDFGFSTHAKRGETL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 vvkDSQVGTVNYMPPEAIKDMSSSREngkskskispKSDVWSLGCILYYMTYGKTPFQQiiNQISKLH-AIIDPNHEIef 756
Cdd:cd14075 158 ---NTFCGSPPYAAPELFKDEHYIGI----------YVDIWALGVLLYFMVTGVMPFRA--ETVAKLKkCILEGTYTI-- 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 757 PDIPEKDLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd14075 221 PSYVSEPCQELIRGILQPVPSDRYSIDEIKNS 252
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
525-793 2.70e-26

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: 110.69  E-value: 2.70e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIY-AIKYVNLEEADnqTLDSYR--NEIAYLNKLQqHsDKIIRLYDYEITDQY---- 597
Cdd:cd07834   2 YELLKPIGSGAYGVVCSAYDKRTGRKvAIKKISNVFDD--LIDAKRilREIKILRHLK-H-ENIIGLLDILRPPSPeefn 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 -IYMVMECGNIDLNSWLKKKKSIDPwERKSYWK-NMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPD 674
Cdd:cd07834  78 dVYIVTELMETDLHKVIKSPQPLTD-DHIQYFLyQILRGLKYLHSAGVIHRDLKPSNILVnSNCDLKICDFGLARGVDPD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKDSQVGTVNYMPPEAIkdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQ--QIINQiskLHAIID--- 749
Cdd:cd07834 157 EDKGFLTEYVVTRWYRAPELL--LSSKKYT--------KAIDIWSVGCIFAELLTRKPLFPgrDYIDQ---LNLIVEvlg 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 750 --PNHEIE-------------------------FPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPYVQI 793
Cdd:cd07834 224 tpSEEDLKfissekarnylkslpkkpkkplsevFPGASPEAI-DLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
577-791 3.40e-26

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: 108.65  E-value: 3.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 577 KLQQHSDkIIRLYDYEITDQYIYMVMECGNI-DLNSW-LKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPAN-- 652
Cdd:cd14074  57 KLVQHPN-VVRLYEVIDTQTKLYLILELGDGgDMYDYiMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENvv 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 653 FLIVDGMLKLIDFGIANQMQPDTTSvvkDSQVGTVNYMPPEAIkdMSSSREngkskskiSPKSDVWSLGCILYYMTYGKT 732
Cdd:cd14074 136 FFEKQGLVKLTDFGFSNKFQPGEKL---ETSCGSLAYSAPEIL--LGDEYD--------APAVDIWSLGVILYMLVCGQP 202
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 733 PFQQiINQISKLHAIIDPNHEIefPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14074 203 PFQE-ANDSETLTMIMDCKYTV--PAHVSPECKDLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
531-790 4.55e-26

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: 110.09  E-value: 4.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVfQVLNEKK--QIYAIKYVNLEEADNQTLDSYRNE---IAYLNKlqqhSDKIIRLYdYEITDQ-YIYMVME- 603
Cdd:cd05601   9 IGRGHFGEV-QVVKEKAtgDIYAMKVLKKSETLAQEEVSFFEEerdIMAKAN----SPWITKLQ-YAFQDSeNLYLVMEy 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNiDLNSWLKKKKSI-DPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIvD--GMLKLIDFGIANQMQPDTTsVV 679
Cdd:cd05601  83 hPGG-DLLSLLSRYDDIfEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI-DrtGHIKLADFGSAAKLSSDKT-VT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKDMsssreNGKSKSKISPKSDVWSLGCILYYMTYGKTPF--QQIINQISKlhaIIDPNHEIEFP 757
Cdd:cd05601 160 SKMPVGTPDYIAPEVLTSM-----NGGSKGTYGVECDWWSLGIVAYEMLYGKTPFteDTVIKTYSN---IMNFKKFLKFP 231
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 758 DIP--EKDLQDVLKCCLKrDPKQRISIPELLAHPY 790
Cdd:cd05601 232 EDPkvSESAVDLIKGLLT-DAKERLGYEGLCCHPF 265
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
525-791 4.66e-26

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: 108.63  E-value: 4.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEE------ADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQY 597
Cdd:cd14084   8 YIMSRTLGSGACGEVKLAYDKSTcKKVAIKIINKRKftigsrREINKPRNIETEIEILKKLSHPC--IIKIEDFFDAEDD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMV---MECGniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG----MLKLIDFGIANQ 670
Cdd:cd14084  86 YYIVlelMEGG--ELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQeeecLIKITDFGLSKI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MqpDTTSVVKdSQVGTVNYMPPEAIkdmsssRENGksKSKISPKSDVWSLGCILYYMTYGKTPFQQ------IINQISKL 744
Cdd:cd14084 164 L--GETSLMK-TLCGTPTYLAPEVL------RSFG--TEGYTRAVDCWSLGVILFICLSGYPPFSEeytqmsLKEQILSG 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23308722 745 HAIIDPNHeieFPDIPEKdLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14084 233 KYTFIPKA---WKNVSEE-AKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
523-791 7.15e-26

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 108.02  E-value: 7.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMV 601
Cdd:cd14097   1 KIYTFGRKLGQGSFGVVIEATHKETQTkWAIKKINREKAGSSAVKLLEREVDILKHVNH--AHIIHLEEVFETPKRMYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFL----IVDGMLKLI----DFGIANQMQ 672
Cdd:cd14097  79 MElCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILvkssIIDNNDKLNikvtDFGLSVQKY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSVVKDSqVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFqqIINQISKLHAIIDPNh 752
Cdd:cd14097 159 GLGEDMLQET-CGTPIYMAPEVISAHGYSQQ-----------CDIWSIGVIMYMLLCGEPPF--VAKSEEKLFEEIRKG- 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 753 EIEFPDIPEKDLQD----VLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14097 224 DLTFTQSVWQSVSDaaknVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
531-792 1.03e-25

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: 107.40  E-value: 1.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIY--AIKYVNLEE-ADNQTLdsYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME-CGN 606
Cdd:cd14202  10 IGHGAFAVVFKGRHKEKHDLevAVKCINKKNlAKSQTL--LGKEIKILKELKH--ENIVALYDFQEIANSVYLVMEyCNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM----------LKLIDFGIANQMQPDTT 676
Cdd:cd14202  86 GDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnnirIKIADFGFARYLQNNMM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVvkdSQVGTVNYMPPEAIkdMSSSREngkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQisKLHAIIDPNHEIEf 756
Cdd:cd14202 166 AA---TLCGSPMYMAPEVI--MSQHYD---------AKADLWSIGTIIYQCLTGKAPFQASSPQ--DLRLFYEKNKSLS- 228
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 757 PDIPEKD---LQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14202 229 PNIPRETsshLRQLLLGLLQRNQKDRMDFDEFFHHPFLD 267
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
525-790 1.20e-25

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: 107.76  E-value: 1.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd07835   1 YQKLEKIGEGTYGVVYKARDkLTGEIVALKKIRLETEDEGVPSTAIREISLLKEL--NHPNIVRLLDVVHSENKLYLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWL--KKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ----MQPDTT 676
Cdd:cd07835  79 FLDLDLKKYMdsSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIdTEGALKLADFGLARAfgvpVRTYTH 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVkdsqvgTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAII-DP 750
Cdd:cd07835 159 EVV------TLWYRAPEILlgsKHYSTP-------------VDIWSVGCIFAEMVTRRPLFpgDSEIDQLFRIFRTLgTP 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 751 NHEI------------EFPDIPEKDL-----------QDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07835 220 DEDVwpgvtslpdykpTFPKWARQDLskvvpsldedgLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
523-790 1.49e-25

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: 106.79  E-value: 1.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSY-RNEIAYLNKLQQHSdkIIRLYD-YEITDQYIY 599
Cdd:cd14165   1 RGYILGINLGEGSYAKVKSAYSERlKCNVAIKIIDKKKAPDDFVEKFlPRELEILARLNHKS--IIKTYEiFETSDGKVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECG-NIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTS 677
Cdd:cd14165  79 IVMELGvQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLdKDFNIKLTDFGFSKRCLRDENG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 --VVKDSQVGTVNYMPPEAIKDMSssrengksksKISPKSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAiIDPNHEIE 755
Cdd:cd14165 159 riVLSKTFCGSAAYAAPEVLQGIP----------YDPRIYDIWSLGVILYIMVCGSMPYDD--SNVKKMLK-IQKEHRVR 225
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 756 FPdiPEK----DLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14165 226 FP--RSKnltsECKDLIYRLLQPDVSQRLCIDEVLSHPW 262
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
525-790 1.64e-25

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: 107.36  E-value: 1.64e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIK-----YVNLEEADNQtldsyrNEIAYLNKLQQHSDkIIRLYD--YEITDQ 596
Cdd:cd07831   1 YKILGKIGEGTFSEVLKAQSRKTgKYYAIKcmkkhFKSLEQVNNL------REIQALRRLSPHPN-ILRLIEvlFDRKTG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVMECGNIDLNSWLKKKKSIDPWER-KSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIA---NQMQ 672
Cdd:cd07831  74 RLALVFELMDMNLYELIKGRKRPLPEKRvKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDILKLADFGSCrgiYSKP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTtsvvkdSQVGTVNYMPPEAIkdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQ--QIINQISKLHAII-D 749
Cdd:cd07831 154 PYT------EYISTRWYRAPECL--LTDGYYG--------PKMDIWAVGCVFFEILSLFPLFPgtNELDQIAKIHDVLgT 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 750 PNHEIEF---------PDIPEKDLQ--------------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07831 218 PDAEVLKkfrksrhmnYNFPSKKGTglrkllpnasaeglDLLKKLLAYDPDERITAKQALRHPY 281
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
525-791 2.16e-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: 106.31  E-value: 2.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKV----FQVLNEKkqiYAIKYVNlEEADNQTLDSYRNEIAYLNKLQ-QHsdkIIRLYDYEITDQYIY 599
Cdd:cd14078   5 YELHETIGSGGFAKVklatHILTGEK---VAIKIMD-KKALGDDLPRVKTEIEALKNLShQH---ICRLYHVIETDNKIF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTS 677
Cdd:cd14078  78 MVLEyCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLdEDQNLKLIDFGLCAKPKGGMDH 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSqVGTVNYMPPEAIKDMSssrengksksKISPKSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDpNHEIEFP 757
Cdd:cd14078 158 HLETC-CGSPAYAAPELIQGKP----------YIGSEADVWSMGVLLYALLCGFLPFDD--DNVMALYRKIQ-SGKYEEP 223
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 758 DIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14078 224 EWLSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
525-791 2.49e-25

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: 106.20  E-value: 2.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYV-NLEEADNQTLDsyrnEIAYLNKLQQHSDK----IIRLYDYEITDQYI 598
Cdd:cd14133   1 YEVLEVLGKGTFGQVVKCYDLLtGEEVALKIIkNNKDYLDQSLD----EIRLLELLNKKDKAdkyhIVRLKDVFYFKNHL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNIDLNSWLKKKK----SIdPWERKsYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD---GMLKLIDFGIANQM 671
Cdd:cd14133  77 CIVFELLSQNLYEFLKQNKfqylSL-PRIRK-IAQQILEALVFLHSLGLIHCDLKPENILLASysrCQIKIIDFGSSCFL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 qPDTTSvvkdSQVGTVNYMPPEAI----KDMSssrengkskskispkSDVWSLGCILYYMTYGKTPFQ--QIINQISKLH 745
Cdd:cd14133 155 -TQRLY----SYIQSRYYRAPEVIlglpYDEK---------------IDMWSLGCILAELYTGEPLFPgaSEVDQLARII 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 23308722 746 AIID--PNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14133 215 GTIGipPAHMLDQGKADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
525-787 2.50e-25

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: 106.43  E-value: 2.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE--KKQIYAIKYVNLEEA----DNQTLD-SYRNEIAYLN--KLQQHSDKIIRLYDYEITD 595
Cdd:cd08528   2 YAVLELLGSGAFGCVYKVRKKsnGQTLLALKEINMTNPafgrTEQERDkSVGDIISEVNiiKEQLRHPNIVRYYKTFLEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVME----CGNIDLNSWLKKKKSIDPWERksYWK---NMLEAVHTIH-QHGIVHSDLKPANFLIVDG-MLKLIDFG 666
Cdd:cd08528  82 DRLYIVMEliegAPLGEHFSSLKEKNEHFTEDR--IWNifvQMVLALRYLHkEKQIVHRDLKPNNIMLGEDdKVTITDFG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 667 IANQMQPDTTSVVkdSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQiINQISKLHA 746
Cdd:cd08528 160 LAKQKGPESSKMT--SVVGTILYSCPEIVQNEPYGEK-----------ADIWALGCILYQMCTLQPPFYS-TNMLTLATK 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 747 IIdpnhEIEFPDIPE----KDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd08528 226 IV----EAEYEPLPEgmysDDITFVIRSCLTPDPEARPDIVEVSS 266
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
531-790 2.87e-25

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 105.77  E-value: 2.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLnEKK--QIYAIKYVNLEEADNQtlDSYRNEIAYLNKLQQHsdKIIRLYD-YEITDQyIYMVMEC--G 605
Cdd:cd14103   1 LGRGKFGTVYRCV-EKAtgKELAAKFIKCRKAKDR--EDVRNEIEIMNQLRHP--RLLQLYDaFETPRE-MVLVMEYvaG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 N------IDLNSWLKKKKSIdpwerkSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD---GMLKLIDFGIANQMQPDtt 676
Cdd:cd14103  75 GelfervVDDDFELTERDCI------LFMRQICEGVQYMHKQGILHLDLKPENILCVSrtgNQIKIIDFGLARKYDPD-- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 svvKDSQV--GTVNYMPPEAIK-DMSSSrengkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHE 753
Cdd:cd14103 147 ---KKLKVlfGTPEFVAPEVVNyEPISY------------ATDMWSVGVICYVLLSGLSPFMG-DNDAETLANVTRAKWD 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 754 IE---FPDIPE--KDLQDVLkccLKRDPKQRISIPELLAHPY 790
Cdd:cd14103 211 FDdeaFDDISDeaKDFISKL---LVKDPRKRMSAAQCLQHPW 249
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
525-791 6.60e-25

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: 104.94  E-value: 6.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEADNQTL-DSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVM 602
Cdd:cd14186   3 FKVLNLLGKGSFACVYRARSLHTGLeVAIKMIDKKAMQKAGMvQRVRNEVEIHCQLKHPS--ILELYNYFEDSNYVYLVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLK-KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQ-PDTTSV 678
Cdd:cd14186  81 EmCHNGEMSRYLKnRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMnIKIADFGLATQLKmPHEKHF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vkdSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQIINQiSKLHAIIDPNHEIefPD 758
Cdd:cd14186 161 ---TMCGTPNYISPEIATRSAHGLES-----------DVWSLGCMFYTLLVGRPPFDTDTVK-NTLNKVVLADYEM--PA 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14186 224 FLSREAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
524-791 6.66e-25

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: 104.66  E-value: 6.66e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEadnqTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd06612   4 VFDILEKLGEGSYGSVYKAIHkETGQVVAIKVVPVEE----DLQEIIKEISILKQCD--SPYIVKYYGSYFKNTDLWIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLK-KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQpdTTSVV 679
Cdd:cd06612  78 EyCGAGSVSDIMKiTNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLnEEGQAKLADFGVSGQLT--DTMAK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKdmsssrENGKSKSKispksDVWSLGCILYYMTYGKTPFQQIiNQISKLHAIID-PNHEIEFPD 758
Cdd:cd06612 156 RNTVIGTPFWMAPEVIQ------EIGYNNKA-----DIWSLGITAIEMAEGKPPYSDI-HPMRAIFMIPNkPPPTLSDPE 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06612 224 KWSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
525-790 8.68e-25

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: 104.27  E-value: 8.68e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKV-FQVLNEKKQIYAIKYVNLEEADNQTLDS-YRNEIAYLnKLQQHSDkIIRLYDYEITDQYIYMVM 602
Cdd:cd14079   4 YILGKTLGVGSFGKVkLAEHELTGHKVAVKILNRQKIKSLDMEEkIRREIQIL-KLFRHPH-IIRLYEVIETPTDIFMVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E---CGniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQpD---- 674
Cdd:cd14079  82 EyvsGG--ELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMnVKIADFGLSNIMR-Dgefl 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSvvkdsqVGTVNYMPPEAIkdmSSSRENGkskskisPKSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAIIDPnh 752
Cdd:cd14079 159 KTS------CGSPNYAAPEVI---SGKLYAG-------PEVDVWSCGVILYALLCGSLPFddEHIPNLFKKIKSGIYT-- 220
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 753 eieFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14079 221 ---IPSHLSPGARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
531-791 1.08e-24

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: 104.44  E-value: 1.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIYAIKYVNLEEAD----NQTLDSYRNEIAYLNKLQQHsdKIIRLYDYEITDQYIYMVMEC-- 604
Cdd:cd06631   9 LGKGAYGTVYCGLTSTGQLIAVKQVELDTSDkekaEKEYEKLQEEVDLLKTLKHV--NIVGYLGTCLEDNVVSIFMEFvp 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 -GNIdlNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIAN----QMQPDTTSV 678
Cdd:cd06631  87 gGSI--ASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNiMLMPNGVIKLIDFGCAKrlciNLSSGSQSQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQIiNQISKLHAIidPNHEIEFPD 758
Cdd:cd06631 165 LLKSMRGTPYWMAPEVINETGHGRKS-----------DIWSIGCTVFEMATGKPPWADM-NPMAAIFAI--GSGRKPVPR 230
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 759 IPEK---DLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06631 231 LPDKfspEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
527-786 1.19e-24

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: 104.30  E-value: 1.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEAdNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME-C 604
Cdd:cd13996  10 EIELLGSGGFGSVYKVRNKVDGVtYAIKKIRLTEK-SSASEKVLREVKALAKL--NHPNIVRYYTAWVEEPPLYIQMElC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 GNIDLNSWLKKKKSIDPWERKSYW---KNMLEAVHTIHQHGIVHSDLKPANFLIV--DGMLKLIDFGIANQM---QPDTT 676
Cdd:cd13996  87 EGGTLRDWIDRRNSSSKNDRKLALelfKQILKGVSYIHSKGIVHRDLKPSNIFLDndDLQVKIGDFGLATSIgnqKRELN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKD---------SQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAI 747
Cdd:cd13996 167 NLNNNnngntsnnsVGIGTPLYASPEQLDGENYNEK-----------ADIYSLGIILFEMLHPFKTAMERSTILTDLRNG 235
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 748 IDPnHEIEFPDIPEKDLqdvLKCCLKRDPKQRISIPELL 786
Cdd:cd13996 236 ILP-ESFKAKHPKEADL---IQSLLSKNPEERPSAEQLL 270
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
527-788 1.36e-24

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 103.73  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   527 ILKQIGSGGSSKVFQ-----VLNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYMV 601
Cdd:pfam07714   3 LGEKLGEGAFGEVYKgtlkgEGENTKIKVAVKTLK-EGADEEEREDFLEEASIMKKLD-H-PNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   602 ME-CGNIDLNSWLKKKK-SIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGML-KLIDFGIANQMQPDTTSV 678
Cdd:pfam07714  80 TEyMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVvKISDFGLSRDIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   679 VKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILY-YMTYGKTPFQQIINQiSKLHAIIDpNHEIEFP 757
Cdd:pfam07714 160 KRGGGKLPIKWMAPESLKDGKFTSK-----------SDVWSFGVLLWeIFTLGEQPYPGMSNE-EVLEFLED-GYRLPQP 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 23308722   758 DIPEKDLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:pfam07714 227 ENCPDELYDLMKQCWAYDPEDRPTFSELVED 257
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
525-797 1.60e-24

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: 106.65  E-value: 1.60e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFqvLNEKK---QIYAIKYVN---LEEAD--NQTLDSyRNEIAYLNklqqhSDKIIRLYdYEITDQ 596
Cdd:cd05600  13 FQILTQVGQGGYGSVF--LARKKdtgEICALKIMKkkvLFKLNevNHVLTE-RDILTTTN-----SPWLVKLL-YAFQDP 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 -YIYMVME--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIA---- 668
Cdd:cd05600  84 eNVYLAMEyvPGG-DFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIdSSGHIKLTDFGLAsgtl 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 -----------------------------NQMQP--DTTSVVKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDV 717
Cdd:cd05600 163 spkkiesmkirleevkntafleltakerrNIYRAmrKEDQNYANSVVGSPDYMAPEVLRGEGYDL-----------TVDY 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 718 WSLGCILYYMTYGKTPF---------QQIINQISKLHAII--DPNHEIEFPDipekDLQDVLKCCLKrDPKQRISIPEll 786
Cdd:cd05600 232 WSLGCILFECLVGFPPFsgstpnetwANLYHWKKTLQRPVytDPDLEFNLSD----EAWDLITKLIT-DPQDRLQSPE-- 304
                       330
                ....*....|.
gi 23308722 787 ahpyvQIQTHP 797
Cdd:cd05600 305 -----QIKNHP 310
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
525-790 1.77e-24

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: 104.10  E-value: 1.77e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEeADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME 603
Cdd:cd07836   2 FKQLEKLGEGTYATVYKGRNrTTGEIVALKEIHLD-AEEGTPSTAIREISLMKELKH--ENIVRLHDVIHTENKLMLVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLK---KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQ-PDTTSv 678
Cdd:cd07836  79 YMDKDLKKYMDthgVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLInKRGELKLADFGLARAFGiPVNTF- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vkDSQVGTVNYMPPEAikdMSSSRengksksKISPKSDVWSLGCILYYMTYGK--------------------TPFQQII 738
Cdd:cd07836 158 --SNEVVTLWYRAPDV---LLGSR-------TYSTSIDIWSVGCIMAEMITGRplfpgtnnedqllkifrimgTPTESTW 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 739 NQISKLhaiidPNHEIEFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07836 226 PGISQL-----PEYKPTFPRYPPQDLQqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
526-779 1.92e-24

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 103.40  E-value: 1.92e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    526 SILKQIGSGGSSKVFQ-----VLNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYM 600
Cdd:smart00221   2 TLGKKLGEGAFGEVYKgtlkgKGDGKEVEVAVKTLK-EDASEQQIEEFLREARIMRKLD-H-PNIVKLLGVCTEEEPLMI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    601 VME-CGNIDLNSWLKKKKSID-PWERKSYW-----KNMleavHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQ 672
Cdd:smart00221  79 VMEyMPGGDLLDYLRKNRPKElSLSDLLSFalqiaRGM----EYLESKNFIHRDLAARNCLVgENLVVKISDFGLSRDLY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    673 PDTTSVVKDSQVgTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYM-TYGKTPFQQIINQisKLHAIIDPN 751
Cdd:smart00221 155 DDDYYKVKGGKL-PIRWMAPESLKEGKFT-----------SKSDVWSFGVLLWEIfTLGEEPYPGMSNA--EVLEYLKKG 220
                          250       260
                   ....*....|....*....|....*...
gi 23308722    752 HEIEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:smart00221 221 YRLPKPPNCPPELYKLMLQCWAEDPEDR 248
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
525-790 2.11e-24

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: 104.15  E-value: 2.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIK-----YVNLEEADNQtldsyrNEIAYLNKLQQHsDKIIRLYDYEITDQYI 598
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNkETGELVAIKkmkkkFYSWEECMNL------REVKSLRKLNEH-PNIVKLKEVFRENDEL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNIDLNSWLK--KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQM--QP 673
Cdd:cd07830  74 YFVFEYMEGNLYQLMKdrKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSgPEVVKIADFGLAREIrsRP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVvkdsqVGTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAII 748
Cdd:cd07830 154 PYTDY-----VSTRWYRAPEILlrsTSYSSP-------------VDIWALGCIMAELYTLRPLFpgSSEIDQLYKICSVL 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 749 -DPNHE-------------IEFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07830 216 gTPTKQdwpegyklasklgFRFPQFAPTSLHqlipnaspeaiDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
525-791 2.58e-24

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: 104.06  E-value: 2.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK--QIYAIKYVNLEE-ADNQTLDSYRNEIayLNKLQQHS----DKIIRLYDYEITDQY 597
Cdd:cd14096   3 YRLINKIGEGAFSNVYKAVPLRNtgKPVAIKVVRKADlSSDNLKGSSRANI--LKEVQIMKrlshPNIVKLLDFQESDEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMEC---GNIdlnswlkkkksIDPWERKSYW---------KNMLEAVHTIHQHGIVHSDLKPANFLI---------- 655
Cdd:cd14096  81 YYIVLELadgGEI-----------FHQIVRLTYFsedlsrhviTQVASAVKYLHEIGVVHRDIKPENLLFepipfipsiv 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 656 -----------VD-------------GMLKLIDFGIANQMQPDTTSvvkdSQVGTVNYMPPEAIKDMSSSRengkskski 711
Cdd:cd14096 150 klrkadddetkVDegefipgvggggiGIVKLADFGLSKQVWDSNTK----TPCGTVGYTAPEVVKDERYSK--------- 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 712 spKSDVWSLGCILYYMTYGKTPF-QQIINQISKlhAIIDPNHEIEFP--DIPEKDLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd14096 217 --KVDMWALGCVLYTLLCGFPPFyDESIETLTE--KISRGDYTFLSPwwDEISKSAKDLISHLLTVDPAKRYDIDEFLAH 292

                ...
gi 23308722 789 PYV 791
Cdd:cd14096 293 PWI 295
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
527-799 3.83e-24

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: 103.29  E-value: 3.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNqtldSYRNEIayLNKLQQ----HSDKIIRLYD---YEITDQYIY 599
Cdd:cd06620   9 TLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKS----SVRKQI--LRELQIlhecHSPYIVSFYGaflNENNNIIIC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 M-VMECGNIDlnSWLKKKKSIDPWERKSYWKNMLEAV-HTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMqpdtT 676
Cdd:cd06620  83 MeYMDCGSLD--KILKKKGPFPEEVLGKIAVAVLEGLtYLYNVHRIIHRDIKPSNILVNSkGQIKLCDFGVSGEL----I 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF---QQIINQISKLHAIIDPNHE 753
Cdd:cd06620 157 NSIADTFVGTSTYMSPERIQGGKYS-----------VKSDVWSLGLSIIELALGEFPFagsNDDDDGYNGPMGILDLLQR 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 23308722 754 I---EFPDIPE-----KDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVN 799
Cdd:cd06620 226 IvnePPPRLPKdrifpKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRASD 279
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
529-786 4.30e-24

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: 102.62  E-value: 4.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVF----QVLNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYMVME- 603
Cdd:cd00192   1 KKLGEGAFGEVYkgklKGGDGKTVDVAVKTLK-EDASESERKDFLKEARVMKKLG-H-PNVVRLLGVCTEEEPLYLVMEy 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWERKSY--WKNMLEAVHTI-------HQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQP 673
Cdd:cd00192  78 MEGGDLLDFLRKSRPVFPSPEPSTlsLKDLLSFAIQIakgmeylASKKFVHRDLAARNCLVgEDLVVKISDFGLSRDIYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIINQ-IskLHAIIDPN 751
Cdd:cd00192 158 DDYYRKKTGGKLPIRWMAPESLKDGIFTSKS-----------DVWSFGVLLWeIFTLGATPYPGLSNEeV--LEYLRKGY 224
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 752 HeIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd00192 225 R-LPKPENCPDELYELMLSCWQLDPEDRPTFSELV 258
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
531-790 5.63e-24

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 102.74  E-value: 5.63e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVNL--EEADNQTLD----SYRNEIAYLNKLQQHSdKIIRLYDYEITDQYIYMV-- 601
Cdd:cd14181  18 IGRGVSSVVRRCVHrHTGQEFAVKIIEVtaERLSPEQLEevrsSTLKEIHILRQVSGHP-SIITLIDSYESSTFIFLVfd 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 -MECGniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTsvv 679
Cdd:cd14181  97 lMRRG--ELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLhIKLSDFGFSCHLEPGEK--- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIK-DMSSSRENgkskskISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFPD 758
Cdd:cd14181 172 LRELCGTPGYLAPEILKcSMDETHPG------YGKEVDLWACGVILFTLLAGSPPFWH-RRQMLMLRMIMEGRYQFSSPE 244
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 759 IPEKD--LQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14181 245 WDDRSstVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
525-782 5.78e-24

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: 102.41  E-value: 5.78e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQ---VLNEKKqiYAIKYVNL-EEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYM 600
Cdd:cd08228   4 FQIEKKIGRGQFSEVYRatcLLDRKP--VALKKVQIfEMMDAKARQDCVKEIDLLKQLNHPN--VIKYLDSFIEDNELNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGNI-DLNS---WLKKKKSIDPweRKSYWK---NMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQ 672
Cdd:cd08228  80 VLELADAgDLSQmikYFKKQKRLIP--ERTVWKyfvQLCSAVEHMHSRRVMHRDIKPANvFITATGVVKLGDLGLGRFFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSVvkDSQVGTVNYMPPEAIkdmsssRENGKSKSKispksDVWSLGCILYYMTYGKTPF-QQIINQISKLHAIidpn 751
Cdd:cd08228 158 SKTTAA--HSLVGTPYYMSPERI------HENGYNFKS-----DIWSLGCLLYEMAALQSPFyGDKMNLFSLCQKI---- 220
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 752 HEIEFPDIP----EKDLQDVLKCCLKRDPKQRISI 782
Cdd:cd08228 221 EQCDYPPLPtehySEKLRELVSMCIYPDPDQRPDI 255
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
524-791 6.73e-24

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 102.38  E-value: 6.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEaDNQtlDSYRNEIAYLNKLQQHSDkIIRLY------DYEITDQ 596
Cdd:cd06608   7 IFELVEVIGEGTYGKVYKARHKKTgQLAAIKIMDIIE-DEE--EEIKLEINILRKFSNHPN-IATFYgafikkDPPGGDD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVME-CGN---IDLNSWLKKKKSIDPWERKSY-WKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQ 670
Cdd:cd06608  83 QLWLVMEyCGGgsvTDLVKGLRKKGKRLKEEWIAYiLRETLRGLAYLHENKVIHRDIKGQNILLTeEAEVKLVDFGVSAQ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MqpDTTSVVKDSQVGTVNYMPPEAIKDMSSsrengkSKSKISPKSDVWSLGCILYYMTYGKTPFqqiinqiSKLHA---- 746
Cdd:cd06608 163 L--DSTLGRRNTFIGTPYWMAPEVIACDQQ------PDASYDARCDVWSLGITAIELADGKPPL-------CDMHPmral 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 23308722 747 --II-DPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06608 228 fkIPrNPPPTLKSPEKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
525-791 6.77e-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: 101.70  E-value: 6.77e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVfQVLNEKK--QIYAIKYVNLEE-ADNQTLDSYRNEIAYLNKLQQhsDKIIRLYD-YEITDQyIYM 600
Cdd:cd14073   3 YELLETLGKGTYGKV-KLAIERAtgREVAIKSIKKDKiEDEQDMVRIRREIEIMSSLNH--PHIIRIYEvFENKDK-IVI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECG-NIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTtsv 678
Cdd:cd14073  79 VMEYAsGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLdQNGNAKIADFGLSNLYSKDK--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIkdmsssreNGksKSKISPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKlHAIIDPNHe 753
Cdd:cd14073 156 LLQTFCGSPLYASPEIV--------NG--TPYQGPEVDCWSLGVLLYTLVYGTMPFdgsdfKRLVKQISS-GDYREPTQ- 223
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 754 iefpdipEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14073 224 -------PSDASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
523-791 7.35e-24

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: 102.38  E-value: 7.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTldSYRNEIAYLNKLQqHSDkIIRLYD-YEITDQYiYM 600
Cdd:cd14166   3 ETFIFMEVLGSGAFSEVYLVKQRSTgKLYALKCIKKSPLSRDS--SLENEIAVLKRIK-HEN-IVTLEDiYESTTHY-YL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGN--------IDLNSWLKKKKSIdpwerksYWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIA 668
Cdd:cd14166  78 VMQLVSggelfdriLERGVYTEKDASR-------VINQVLSAVKYLHENGIVHRDLKPENLLYLtpdeNSKIMITDFGLS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQMQPDTTSvvkdSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAII 748
Cdd:cd14166 151 KMEQNGIMS----TACGTPGYVAPEVLAQKPYSK-----------AVDCWSIGVITYILLCGYPPFYE-ETESRLFEKIK 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 749 DPNHEIEFP---DIPEKdLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14166 215 EGYYEFESPfwdDISES-AKDFIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
525-792 7.82e-24

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: 105.09  E-value: 7.82e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIKYVN----LEEADNQTLDSYRNEIAylnklqqHSD-KIIRLYDYEITDQ-Y 597
Cdd:cd05624  74 FEIIKVIGRGAFGEVAVVkMKNTERIYAMKILNkwemLKRAETACFREERNVLV-------NGDcQWITTLHYAFQDEnY 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME--CGNiDLNSWLKKKKSIDPWE-RKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQP 673
Cdd:cd05624 147 LYLVMDyyVGG-DLLTLLSKFEDKLPEDmARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLdMNGHIRLADFGSCLKMND 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTsVVKDSQVGTVNYMPPEAIKDMsssrENGKSKSKISPksDVWSLGCILYYMTYGKTPF--QQIINQISKLHaiidpN 751
Cdd:cd05624 226 DGT-VQSSVAVGTPDYISPEILQAM----EDGMGKYGPEC--DWWSLGVCMYEMLYGETPFyaESLVETYGKIM-----N 293
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 23308722 752 HE--IEFP----DIPE--KDLQDVLKCCLKRDPKQRiSIPELLAHPYVQ 792
Cdd:cd05624 294 HEerFQFPshvtDVSEeaKDLIQRLICSRERRLGQN-GIEDFKKHAFFE 341
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
524-791 1.36e-23

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: 100.84  E-value: 1.36e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNqtLDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYMVM 602
Cdd:cd06613   1 DYELIQRIGSGTYGDVYKARNIATgELAAVKVIKLEPGDD--FEIIQQEISMLKECR-H-PNIVAYFGSYLRRDKLWIVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKkksIDPWERK--SY-WKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMqpdTTS 677
Cdd:cd06613  77 EyCGGGSLQDIYQV---TGPLSELqiAYvCRETLKGLAYLHSTGKIHRDIKGANILLTEdGDVKLADFGVSAQL---TAT 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVK-DSQVGTVNYMPPEAIKDMSSSRENGKSkskispksDVWSLGCILYYMTYGKTPF-----QQIINQISKlhAIIDPn 751
Cdd:cd06613 151 IAKrKSFIGTPYWMAPEVAAVERKGGYDGKC--------DIWALGITAIELAELQPPMfdlhpMRALFLIPK--SNFDP- 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 752 heiefPDIPEK-----DLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06613 220 -----PKLKDKekwspDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
524-786 1.40e-23

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: 101.40  E-value: 1.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEEADNQTLDSYRnEIAYLNKLQQHSDK-IIRLYDYEITDQYIYMV 601
Cdd:cd06917   2 LYRRLELVGRGSYGAVYRgYHVKTGRVVALKVLNLDTDDDDVSDIQK-EVALLSQLKLGQPKnIIKYYGSYLKGPSLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME-CGNIDLNSwLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQpdTTSVV 679
Cdd:cd06917  81 MDyCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTnTGNVKLCDFGVAASLN--QNSSK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKDMSSsrengkskskISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHeiefPDI 759
Cdd:cd06917 158 RSTFVGTPYWMAPEVITEGKY----------YDTKADIWSLGITTYEMATGNPPYSD-VDALRAVMLIPKSKP----PRL 222
                       250       260       270
                ....*....|....*....|....*....|.
gi 23308722 760 PE----KDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd06917 223 EGngysPLLKEFVAACLDEEPKDRLSADELL 253
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
525-788 2.01e-23

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: 101.22  E-value: 2.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLdsYRNEIAYLNKLqqHSDKIIRLYDYEI-----TDQYI 598
Cdd:cd13986   2 YRIQRLLGEGGFSFVYLVEDLStGRLYALKKILCHSKEDVKE--AMREIENYRLF--NHPNILRLLDSQIvkeagGKKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVM---ECGNI-DLNSWLKKKKSIDPWERKSYW-KNMLEAVHTIHQHGIV---HSDLKPANFLIVDGMLKLI-DFGIAN 669
Cdd:cd13986  78 YLLLpyyKRGSLqDEIERRLVKGTFFPEDRILHIfLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILmDLGSMN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 Q--MQPDTTSV-----VKDSQVGTVNYMPPE-------AIKDmsssrengkskskisPKSDVWSLGCILYYMTYGKTPFQ 735
Cdd:cd13986 158 ParIEIEGRREalalqDWAAEHCTMPYRAPElfdvkshCTID---------------EKTDIWSLGCTLYALMYGESPFE 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 736 QIINQISKLH-AIIDPNheIEFPDIP--EKDLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd13986 223 RIFQKGDSLAlAVLSGN--YSFPDNSrySEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
525-792 2.29e-23

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: 102.46  E-value: 2.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVfQVLNEK--KQIYAIKYVN----LEEADNQTLDSYRNEIAYLNklqqhSDKIIRLYDYEITDQYI 598
Cdd:cd05596  28 FDVIKVIGRGAFGEV-QLVRHKstKKVYAMKLLSkfemIKRSDSAFFWEERDIMAHAN-----SEWIVQLHYAFQDDKYL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMEC--GNiDLNSWLKKKKSIDPWERkSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDT 675
Cdd:cd05596 102 YMVMDYmpGG-DLVNLMSNYDVPEKWAR-FYTAEVVLALDAIHSMGFVHRDVKPDNMLLdASGHLKLADFGTCMKMDKDG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TsVVKDSQVGTVNYMPPEAIKDMSSSRENGkskskisPKSDVWSLGCILYYMTYGKTPF--QQIINQISKlhaIIDPNHE 753
Cdd:cd05596 180 L-VRSDTAVGTPDYISPEVLKSQGGDGVYG-------RECDWWSVGVFLYEMLVGDTPFyaDSLVGTYGK---IMNHKNS 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 754 IEFPDIPE--KDLQDVLkCCLKRDPKQRI---SIPELLAHPYVQ 792
Cdd:cd05596 249 LQFPDDVEisKDAKSLI-CAFLTDREVRLgrnGIEEIKAHPFFK 291
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
526-779 2.89e-23

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 99.91  E-value: 2.89e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    526 SILKQIGSGGSSKVF-----QVLNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYM 600
Cdd:smart00219   2 TLGKKLGEGAFGEVYkgklkGKGGKKKVEVAVKTLK-EDASEQQIEEFLREARIMRKLD-H-PNVVKLLGVCTEEEPLYI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    601 VME-CGNIDLNSWLKKKKSIDPWERKSYW-KNMLEAVHTIHQHGIVHSDLKPANFLIVDG-MLKLIDFGIANQMQPDTTS 677
Cdd:smart00219  79 VMEyMEGGDLLSYLRKNRPKLSLSDLLSFaLQIARGMEYLESKNFIHRDLAARNCLVGENlVVKISDFGLSRDLYDDDYY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    678 VVKDSQVgTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYM-TYGKTPFQQIINQisKLHAIIDPNHEIEF 756
Cdd:smart00219 159 RKRGGKL-PIRWMAPESLKEGKFT-----------SKSDVWSFGVLLWEIfTLGEQPYPGMSNE--EVLEYLKNGYRLPQ 224
                          250       260
                   ....*....|....*....|...
gi 23308722    757 PDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:smart00219 225 PPNCPPELYDLMLQCWAEDPEDR 247
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
525-790 3.26e-23

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: 100.59  E-value: 3.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd07839   2 YEKLEKIGEGTYGTVFKAKNrETHEIVALKRVRLDDDDEGVPSSALREICLLKEL--KHKNIVRLYDVLHSDKKLTLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKK-KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVvkD 681
Cdd:cd07839  80 YCDQDLKKYFDScNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLInKNGELKLADFGLARAFGIPVRCY--S 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPF---QQIINQISKLHAII-DPNHEI 754
Cdd:cd07839 158 AEVVTLWYRPPDVLfgaKLYSTS-------------IDMWSAGCIFAELANAGRPLfpgNDVDDQLKRIFRLLgTPTEES 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 755 -----EFPDIPEKDLQ------------------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07839 225 wpgvsKLPDYKPYPMYpattslvnvvpklnstgrDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
525-792 3.54e-23

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: 100.08  E-value: 3.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIY--AIKYVNLEE-ADNQTLdsYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMV 601
Cdd:cd14201   8 YSRKDLVGHGAFAVVFKGRHRKKTDWevAIKSINKKNlSKSQIL--LGKEIKILKELQH--ENIVALYDVQEMPNSVFLV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI---------VDGM-LKLIDFGIANQ 670
Cdd:cd14201  84 MEyCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLsyasrkkssVSGIrIKIADFGFARY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MQpdtTSVVKDSQVGTVNYMPPEAIkdMSSSREngkskskisPKSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDP 750
Cdd:cd14201 164 LQ---SNMMAATLCGSPMYMAPEVI--MSQHYD---------AKADLWSIGTVIYQCLVGKPPFQA--NSPQDLRMFYEK 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 751 NHEIEfPDIPEKD---LQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14201 228 NKNLQ-PSIPRETspyLADLLLGLLQRNQKDRMDFEAFFSHPFLE 271
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
528-788 4.25e-23

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: 100.14  E-value: 4.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRnEIAYLNKLQ-QHsdkIIRLYDYEITDQYIYMVME-C 604
Cdd:cd14046  11 LQVLGKGAFGQVVKVRNKlDGRYYAIKKIKLRSESKNNSRILR-EVMLLSRLNhQH---VVRYYQAWIERANLYIQMEyC 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIA----------NQMQP 673
Cdd:cd14046  87 EKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNiFLDSNGNVKIGDFGLAtsnklnvelaTQDIN 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKDS------QVGTVNYMPPEaIKDMSSSRENgkskskisPKSDVWSLGCILYYMTYgktPFQQIINQISKLHAI 747
Cdd:cd14046 167 KSTSAALGSsgdltgNVGTALYVAPE-VQSGTKSTYN--------EKVDMYSLGIIFFEMCY---PFSTGMERVQILTAL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 748 IDPNheIEFPDI---PEKDLQ-DVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd14046 235 RSVS--IEFPPDfddNKHSKQaKLIRWLLNHDPAKRPSAQELLKS 277
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
528-803 5.18e-23

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: 100.19  E-value: 5.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEADNQTLDSYRnEIAYLNKLqqHSDKIIRLYD--YEITDQYIYMVME- 603
Cdd:cd06621   6 LSSLGEGAGGSVTKCrLRNTKTIFALKTITTDPNPDVQKQILR-ELEINKSC--ASPYIVKYYGafLDEQDSSIGIAMEy 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKK--KKSIDPWER--KSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMqpdTTSV 678
Cdd:cd06621  83 CEGGSLDSIYKKvkKKGGRIGEKvlGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTrKGQVKLCDFGVSGEL---VNSL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKdSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF----QQIINQISKLHAIID-PNHE 753
Cdd:cd06621 160 AG-TFTGTSYYMAPERIQGGPYS-----------ITSDVWSLGLTLLEVAQNRFPFppegEPPLGPIELLSYIVNmPNPE 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 754 IefPDIPE------KDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAK 803
Cdd:cd06621 228 L--KDEPEngikwsESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKVNMAK 281
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
525-790 6.29e-23

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: 100.88  E-value: 6.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIKYVN----LEEADNQTLDSYRNEIAYLNklqqhSDKIIRLYdYEITDQ-YI 598
Cdd:cd05597   3 FEILKVIGRGAFGEVAVVkLKSTEKVYAMKILNkwemLKRAETACFREERDVLVNGD-----RRWITKLH-YAFQDEnYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME--CGNiDLNSWLKKKKSIDPWE-RKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPD 674
Cdd:cd05597  77 YLVMDyyCGG-DLLTLLSKFEDRLPEEmARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLdRNGHIRLADFGSCLKLRED 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTsVVKDSQVGTVNYMPPEAIKDMsssrENGksKSKISPKSDVWSLGCILYYMTYGKTPF--QQIINQISKLHaiidpNH 752
Cdd:cd05597 156 GT-VQSSVAVGTPDYISPEILQAM----EDG--KGRYGPECDWWSLGVCMYEMLYGETPFyaESLVETYGKIM-----NH 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 23308722 753 E--IEFP----DIPE--KDLQDVLKCclkrDPKQRI---SIPELLAHPY 790
Cdd:cd05597 224 KehFSFPddedDVSEeaKDLIRRLIC----SRERRLgqnGIDDFKKHPF 268
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
525-790 8.95e-23

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: 98.90  E-value: 8.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQI-GSGGSSKVFQVLNEK-KQIYAIKYVNleeaDNQtldSYRNEIAYLNKLQQHSDkIIRLYD-YEITDQ---YI 598
Cdd:cd14089   2 YTISKQVlGLGINGKVLECFHKKtGEKFALKVLR----DNP---KARREVELHWRASGCPH-IVRIIDvYENTYQgrkCL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMEC--GNiDLNSWLKKKKSIDPWERK--SYWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIANQ 670
Cdd:cd14089  74 LVVMECmeGG-ELFSRIQERADSAFTEREaaEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSskgpNAILKLTDFGFAKE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 mqpDTTSVVKDSQVGTVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCILYYMTYGKTPFqqiinqISKLHA 746
Cdd:cd14089 153 ---TTTKKSLQTPCYTPYYVAPEVLGpekyDKSC---------------DMWSLGVIMYILLCGYPPF------YSNHGL 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 747 IIDP-------NHEIEFPDiPE-----KDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14089 209 AISPgmkkrirNGQYEFPN-PEwsnvsEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
523-790 1.03e-22

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 98.46  E-value: 1.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEE-ADNQTLDSYRNEIAyLNKLQQHSdKIIRLYDYEITDQYIYM 600
Cdd:cd14189   1 RSYCKGRLLGKGGFARCYEMTDlATNKTYAVKVIPHSRvAKPHQREKIVNEIE-LHRDLHHK-HVVKFSHHFEDAENIYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME-CGNIDL-NSWLKKKKSIDPwERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTS 677
Cdd:cd14189  79 FLElCSRKSLaHIWKARHTLLEP-EVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMeLKVGDFGLAARLEPPEQR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 vvKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQIinQISKLHAIIDPNHEIeFP 757
Cdd:cd14189 158 --KKTICGTPNYLAPEVLLRQGHGPES-----------DVWSLGCVMYTLLCGNPPFETL--DLKETYRCIKQVKYT-LP 221
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 758 DIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14189 222 ASLSLPARHLLAGILKRNPGDRLTLDQILEHEF 254
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
525-793 1.25e-22

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: 99.79  E-value: 1.25e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN---EKKQIYAIKYVNleEADNQTLDSYR--NEIAYLNKLQQHsDKIIRLYDYEITDQ--- 596
Cdd:cd07857   2 YELIKELGQGAYGIVCSARNaetSEEETVAIKKIT--NVFSKKILAKRalRELKLLRHFRGH-KNITCLYDMDIVFPgnf 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 ---YIYM-VMECgniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQM 671
Cdd:cd07857  79 nelYLYEeLMEA---DLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVnADCELKICDFGLARGF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QPDTtsvVKDSQ-----VGTVNYMPPEAikdMSSSREngkskskISPKSDVWSLGCILYYMtYGKTPF---QQIINQISK 743
Cdd:cd07857 156 SENP---GENAGfmteyVATRWYRAPEI---MLSFQS-------YTKAIDVWSVGCILAEL-LGRKPVfkgKDYVDQLNQ 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 744 -LHAIIDPNHEI--------------EFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPYVQI 793
Cdd:cd07857 222 iLQVLGTPDEETlsrigspkaqnyirSLPNIPKKPFEsifpnanplalDLLEKLLAFDPTKRISVEEALEHPYLAI 297
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
525-791 1.72e-22

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: 97.57  E-value: 1.72e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK--KQiYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVM 602
Cdd:cd08218   2 YVRIKKIGEGSFGKALLVKSKEdgKQ-YVIKEINISKMSPKEREESRKEVAVLSKMK-HPN-IVQYQESFEENGNLYIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKSIDPWERK--SYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMqpDTTSV 678
Cdd:cd08218  79 DyCDGGDLYKRINAQRGVLFPEDQilDWFVQLCLALKHVHDRKILHRDIKSQNiFLTKDGIIKLGDFGIARVL--NSTVE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQ--QIINQISKlhaIIDPNheieF 756
Cdd:cd08218 157 LARTCIGTPYYLSPEICENKPYNNKS-----------DIWALGCVLYEMCTLKHAFEagNMKNLVLK---IIRGS----Y 218
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 757 PDIP---EKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd08218 219 PPVPsrySYDLRSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
531-792 2.09e-22

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: 98.06  E-value: 2.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEK-KQIYAIKYVNLEEAD---NQTLDSYRN----EIAYLNKLQQHSDkIIRLYDYEITDQYIYMV- 601
Cdd:cd14182  11 LGRGVSSVVRRCIHKPtRQEYAVKIIDITGGGsfsPEEVQELREatlkEIDILRKVSGHPN-IIQLKDTYETNTFFFLVf 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 --MECGniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTtsv 678
Cdd:cd14182  90 dlMKKG--ELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMnIKLTDFGFSCQLDPGE--- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vKDSQV-GTVNYMPPEAIKDMSSSRENGkskskISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFP 757
Cdd:cd14182 165 -KLREVcGTPGYLAPEIIECSMDDNHPG-----YGKEVDMWSTGVIMYTLLAGSPPFWH-RKQMLMLRMIMSGNYQFGSP 237
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 758 DIPEKD--LQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14182 238 EWDDRSdtVKDLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
525-790 2.20e-22

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: 98.26  E-value: 2.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd07861   2 YTKIEKIGEGTYGVVYKGRNKKTgQIVAMKKIRLESEEEGVPSTAIREISLLKELQ-HPN-IVCLEDVLMQENRLYLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWL---KKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMqpDTTSVV 679
Cdd:cd07861  80 FLSMDLKKYLdslPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNkGVIKLADFGLARAF--GIPVRV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIkdMSSSRengkskskISPKSDVWSLGCILYYMTYGKTPFQ--QIINQISKLHAII-DPNHEI-- 754
Cdd:cd07861 158 YTHEVVTLWYRAPEVL--LGSPR--------YSTPVDIWSIGTIFAEMATKKPLFHgdSEIDQLFRIFRILgTPTEDIwp 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 755 ----------EFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07861 228 gvtslpdyknTFPKWKKGSLRtavknldedglDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
528-790 2.33e-22

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: 97.55  E-value: 2.33e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFqvLNEKK---QIYAIKYvnLEEADNQTLDSYRNEIAYLNKL--QQHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd05611   1 LKPISKGAFGSVY--LAKKRstgDYFAIKV--LKKSDMIAKNQVTNVKAERAIMmiQGESPYVAKLYYSFQSKDYLYLVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECGNI-DLNSWLKKKKSI-DPWERKsYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA-----NQMQPD 674
Cdd:cd05611  77 EYLNGgDCASLIKTLGGLpEDWAKQ-YIAEVVLGVEDLHQRGIIHRDIKPENLLIDQtGHLKLTDFGLSrngleKRHNKK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TtsvvkdsqVGTVNYMPPEAIkdmsssreNGkskSKISPKSDVWSLGCILYYMTYGKTPFQ-----QIINQIskLHAIID 749
Cdd:cd05611 156 F--------VGTPDYLAPETI--------LG---VGDDKMSDWWSLGCVIFEFLFGYPPFHaetpdAVFDNI--LSRRIN 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 750 -PNHEIEFPDIPEKDLQDVLKCClkrDPKQRIS---IPELLAHPY 790
Cdd:cd05611 215 wPEEVKEFCSPEAVDLINRLLCM---DPAKRLGangYQEIKSHPF 256
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
531-788 4.22e-22

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: 96.96  E-value: 4.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQY---IYMVMECGNi 607
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVKRLN-EMNCAASKKEFLTELEMLGRLR-H-PNLVRLLGYCLESDEkllVYEYMPNGS- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 dLNSWLKKKKSIDP--WE-RKSYWKNMLEAVHTIHQHG---IVHSDLKPANFLIVDGML-KLIDFGIANQMQPDTTSVVK 680
Cdd:cd14066  77 -LEDRLHCHKGSPPlpWPqRLKIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEpKLTDFGLARLIPPSESVSKT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQISK--LHAIIDPNHEIEFPD 758
Cdd:cd14066 156 SAVKGTIGYLAPEYIRTGRVS-----------TKSDVYSFGVVLLELLTGKPAVDENRENASRkdLVEWVESKGKEELED 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 759 IPEKDLQ-------DVLKC-------CLKRDPKQRISIPELLAH 788
Cdd:cd14066 225 ILDKRLVdddgveeEEVEAllrlallCTRSDPSLRPSMKEVVQM 268
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
531-786 5.20e-22

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: 96.68  E-value: 5.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIyAIKYVNLEEADNQTLDSYRNEiayLNKLQQHSDKIIRLYDYE---ITDQYIYMVME-CGN 606
Cdd:cd13979  11 LGSGGFGSVYKATYKGETV-AVKIVRRRRKNRASRQSFWAE---LNAARLRHENIVRVLAAEtgtDFASLGLIIMEyCGN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDP-WERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQM-QPDTTSVVKDSQ 683
Cdd:cd13979  87 GTLQQLIYEGSEPLPlAHRILISLDIARALRFCHSHGIVHLDVKPANILIsEQGVCKLCDFGCSVKLgEGNEVGTPRSHI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 684 VGTVNYMPPEAIKdmsssrengksKSKISPKSDVWSLGCILYYMTYGKTPF----QQIINQISK--LHAIIDPNHEIEFP 757
Cdd:cd13979 167 GGTYTYRAPELLK-----------GERVTPKADIYSFGITLWQMLTRELPYaglrQHVLYAVVAkdLRPDLSGLEDSEFG 235
                       250       260
                ....*....|....*....|....*....
gi 23308722 758 DIpekdLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd13979 236 QR----LRSLISRCWSAQPAERPNADESL 260
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
522-792 6.18e-22

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: 97.02  E-value: 6.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 522 GRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVnLEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMV 601
Cdd:cd06644  11 NEVWEIIGELGDGAFGKVYKAKNKETGALAAAKV-IETKSEEELEDYMVEIEILATCNHPY--IVKLLGAFYWDGKLWIM 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME-C--GNIDLnSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQpdTTS 677
Cdd:cd06644  88 IEfCpgGAVDA-IMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLtLDGDIKLADFGVSAKNV--KTL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPEAIkdMSSSRENgkskSKISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAII--DPNhEIE 755
Cdd:cd06644 165 QRRDSFIGTPYWMAPEVV--MCETMKD----TPYDYKADIWSLGITLIEMAQIEPPHHE-LNPMRVLLKIAksEPP-TLS 236
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06644 237 QPSKWSMEFRDFLKTALDKHPETRPSAAQLLEHPFVS 273
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
525-790 8.13e-22

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: 95.89  E-value: 8.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEAdNQTLDSYRNEIAYLNklQQHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd06610   3 YELIEVIGSGATAVVYAAYCLpKKEKVAIKRIDLEKC-QTSMDELRKEIQAMS--QCNHPNVVSYYTSFVVGDELWLVMP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 ---CGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGI-ANQMQP-DTT 676
Cdd:cd06610  80 llsGGSLlDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLgEDGSVKIADFGVsASLATGgDRT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSQVGTVNYMPPEAikdMSSSRENGKSKskispksDVWSLGCILYYMTYGKTPFQQIinQISKLHAIIDPNHeieF 756
Cdd:cd06610 160 RKVRKTFVGTPCWMAPEV---MEQVRGYDFKA-------DIWSFGITAIELATGAAPYSKY--PPMKVLMLTLQND---P 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 757 PDIPE--------KDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd06610 225 PSLETgadykkysKSFRKMISLCLQKDPSKRPTAEELLKHKF 266
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
524-791 8.53e-22

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 95.84  E-value: 8.53e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQtlDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd14191   3 FYDIEERLGSGKFGQVFRLVEKKtKKVWAGKFFKAYSAKEK--ENIRQEISIMNCL--HHPKLVQCVDAFEEKANIVMVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECGN--------IDLNSWLKKKKSIdpwerkSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM---LKLIDFGIANQM 671
Cdd:cd14191  79 EMVSggelferiIDEDFELTERECI------KYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtkIKLIDFGLARRL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QPDTTSVVkdsQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPN 751
Cdd:cd14191 153 ENAGSLKV---LFGTPEFVAPEVINYEPIGYAT-----------DMWSIGVICYILVSGLSPFMG-DNDNETLANVTSAT 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 752 HEIE---FPDIPEkDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14191 218 WDFDdeaFDEISD-DAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
524-791 1.19e-21

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 95.79  E-value: 1.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEADNQTLDSYRNEIAY-LNKLQQ-HSDKIIRLYD-YE-ITDQYI 598
Cdd:cd14196   6 FYDIGEELGSGQFAIVKKCREKSTGLeYAAKFIKKRQSRASRRGVSREEIEReVSILRQvLHPNIITLHDvYEnRTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG-----MLKLIDFGIANQMQp 673
Cdd:cd14196  86 ILELVSGG-ELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKnipipHIKLIDFGLAHEIE- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 dtTSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAII 748
Cdd:cd14196 164 --DGVEFKNIFGTPEFVAPEIVNYEPLGLE-----------ADMWSIGVITYILLSGASPFlgdtkQETLANITAVSYDF 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 749 DPnheiEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14196 231 DE----EFFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
524-795 1.22e-21

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: 95.97  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNqtLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVM 602
Cdd:cd06611   6 IWEIIGELGDGAFGKVYKAQHkETGLFAAAKIIQIESEEE--LEDFMVEIDILSECKH--PNIVGLYEAYFYENKLWILI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNS-WLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQpdTTSVV 679
Cdd:cd06611  82 EfCDGGALDSiMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTlDGDVKLADFGVSAKNK--STLQK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAI--KDMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAII-DPNHEIEF 756
Cdd:cd06611 160 RDTFIGTPYWMAPEVVacETFKDNPYD--------YKADIWSLGITLIELAQMEPPHHE-LNPMRVLLKILkSEPPTLDQ 230
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 757 PDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQT 795
Cdd:cd06611 231 PSKWSSSFNDFLKSCLVKDPDDRPTAAELLKHPFVSDQS 269
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
525-791 1.48e-21

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: 95.21  E-value: 1.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVN-------LEEADNQTLDSYRNEI-----AYLNKLQQHSdKIIRLYDY 591
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRtGEKCAIKIIPrasnaglKKEREKRLEKEISRDIrtireAALSSLLNHP-HICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 592 EITDQYIYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIAN 669
Cdd:cd14077  82 LRTPNHYYMLFEyVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKsGNIKIIDFGLSN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMQPDTtsvVKDSQVGTVNYMPPEAIKdmsSSRENGKSKskispksDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIID 749
Cdd:cd14077 162 LYDPRR---LLRTFCGSLYFAAPELLQ---AQPYTGPEV-------DVWSFGVVLYVLVCGKVPFDD--ENMPALHAKIK 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 750 pNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14077 227 -KGKVEYPSYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
525-791 1.76e-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: 95.02  E-value: 1.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYV---NLEEADNQtlDSYRNEIaylnKLQQH--SDKIIRLYDYEITDQYI 598
Cdd:cd14116   7 FEIGRPLGKGKFGNVYLAReKQSKFILALKVLfkaQLEKAGVE--HQLRREV----EIQSHlrHPNILRLYGYFHDATRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQmqpdTT 676
Cdd:cd14116  81 YLILEYAPLgTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLgSAGELKIADFGWSVH----AP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQISKLhaiidpn 751
Cdd:cd14116 157 SSRRTTLCGTLDYLPPEMIEGRMHDEK-----------VDLWSLGVLCYEFLVGKPPFeantyQETYKRISRV------- 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 752 hEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14116 219 -EFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWI 257
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
525-791 2.29e-21

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: 95.69  E-value: 2.29e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYV-NLEEADNQTLdsyrNEIAYLNKLQQH--SDK--IIRLYDYEITDQYI 598
Cdd:cd14210  15 YEVLSVLGKGSFGQVVKCLDHKtGQLVAIKIIrNKKRFHQQAL----VEVKILKHLNDNdpDDKhnIVRYKDSFIFRGHL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNIDLNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM---LKLIDFGianqmqp 673
Cdd:cd14210  91 CIVFELLSINLYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSkssIKVIDFG------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 dtTSVVKDSQVGTV----NYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGK------------------ 731
Cdd:cd14210 164 --SSCFEGEKVYTYiqsrFYRAPEVILGLPYDTA-----------IDMWSLGCILAELYTGYplfpgeneeeqlacimev 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 732 --TPFQQIINQISKLHAIIDPNHEI-EFPDIP-------EKDLQDVLKC-----------CLKRDPKQRISIPELLAHPY 790
Cdd:cd14210 231 lgVPPKSLIDKASRRKKFFDSNGKPrPTTNSKgkkrrpgSKSLAQVLKCddpsfldflkkCLRWDPSERMTPEEALQHPW 310

                .
gi 23308722 791 V 791
Cdd:cd14210 311 I 311
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
618-792 2.57e-21

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: 94.80  E-value: 2.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 618 SIDPWERKSYWKNM--------------LEAVHTIH-QHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpdTTSVVKD 681
Cdd:cd06617  85 SLDKFYKKVYDKGLtipedilgkiavsiVKALEYLHsKLSVIHRDVKPSNVLInRNGQVKLCDFGISGYL---VDSVAKT 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIK-DMSSSRENgkskskisPKSDVWSLGCILYYMTYG-------KTPFQQIiNQISKlhaiiDPNhe 753
Cdd:cd06617 162 IDAGCKPYMAPERINpELNQKGYD--------VKSDVWSLGITMIELATGrfpydswKTPFQQL-KQVVE-----EPS-- 225
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 23308722 754 iefPDIPEK----DLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06617 226 ---PQLPAEkfspEFQDFVNKCLKKNYKERPNYPELLQHPFFE 265
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
522-779 2.70e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 98.71  E-value: 2.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  522 GRiYSILKQIGSGGSSKVFQ----VLNEKkqiYAIK-----YVNleeaDNQTLDSYRNE---IAYLNklqqHSDkIIRLY 589
Cdd:NF033483   7 GR-YEIGERIGRGGMAEVYLakdtRLDRD---VAVKvlrpdLAR----DPEFVARFRREaqsAASLS----HPN-IVSVY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  590 DYEITDQYIYMVMEC--GnIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFG 666
Cdd:NF033483  74 DVGEDGGIPYIVMEYvdG-RTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITkDGRVKVTDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  667 IANQMqpDTTSVVKDSQV-GTVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCILYYMTYGKTPF------- 734
Cdd:NF033483 153 IARAL--SSTTMTQTNSVlGTVHYLSPEQARggtvDARS---------------DIYSLGIVLYEMLTGRPPFdgdspvs 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 23308722  735 ------QQIINQISKLHaiidpnheiefPDIPEkDLQD-VLKcCLKRDPKQR 779
Cdd:NF033483 216 vaykhvQEDPPPPSELN-----------PGIPQ-SLDAvVLK-ATAKDPDDR 254
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
525-738 2.77e-21

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: 94.16  E-value: 2.77e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSY-RNEIAYLNKLQQhsDKIIRLYD-YEITDQYIYMV 601
Cdd:cd14164   2 YTLGTTIGEGSFSKVKLATSQKyCCKVAIKIVDRRRASPDFVQKFlPRELSILRRVNH--PNIVQMFEcIEVANGRLYIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV--DGMLKLIDFGIANQMQ--PDTTS 677
Cdd:cd14164  80 MEAAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSadDRKIKIADFGFARFVEdyPELST 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 678 VVkdsqVGTVNYMPPEAIKDMSSSRENgkskskispkSDVWSLGCILYYMTYGKTPFQQII 738
Cdd:cd14164 160 TF----CGSRAYTPPEVILGTPYDPKK----------YDVWSLGVVLYVMVTGTMPFDETN 206
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
528-790 3.03e-21

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: 94.88  E-value: 3.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVMECGN 606
Cdd:cd07860   5 VEKIGEGTYGVVYKARNKLTgEVVALKKIRLDTETEGVPSTAIREISLLKELN-HPN-IVKLLDVIHTENKLYLVFEFLH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLnswlKKKKSIDPWER------KSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ----MQPDT 675
Cdd:cd07860  83 QDL----KKFMDASALTGiplpliKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLInTEGAIKLADFGLARAfgvpVRTYT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVVkdsqvgTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKT--PFQQIINQISKLHAIID- 749
Cdd:cd07860 159 HEVV------TLWYRAPEILlgcKYYSTA-------------VDIWSLGCIFAEMVTRRAlfPGDSEIDQLFRIFRTLGt 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 750 ------------PNHEIEFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07860 220 pdevvwpgvtsmPDYKPSFPKWARQDFSkvvppldedgrDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
525-791 3.07e-21

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: 3.07e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQYIYMVMe 603
Cdd:cd14086   3 YDLKEELGKGAFSVVRRCVQkSTGQEFAAKIINTKKLSARDHQKLERE-ARICRLLKHPN-IVRLHDSISEEGFHYLVF- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 cgniDLNSWLKKKKSIdpWERKSY--------WKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIANQM 671
Cdd:cd14086  80 ----DLVTGGELFEDI--VAREFYseadashcIQQILESVNHCHQNGIVHRDLKPENLLLAskskGAAVKLADFGLAIEV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QPDTTSVVkdSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF----QQiinqisKLHAI 747
Cdd:cd14086 154 QGDQQAWF--GFAGTPGYLSPEVLRKDPYGK-----------PVDIWACGVILYILLVGYPPFwdedQH------RLYAQ 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 23308722 748 IDpNHEIEFPDiPEKDL-----QDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14086 215 IK-AGAYDYPS-PEWDTvtpeaKDLINQMLTVNPAKRITAAEALKHPWI 261
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
577-790 3.25e-21

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: 94.26  E-value: 3.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 577 KLQQHSDK---IIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYwkNMLEAVHTI-----HQH--GIVHS 646
Cdd:cd13982  46 QLLRESDEhpnVIRYFCTEKDRQFLYIALELCAASLQDLVESPRESKLFLRPGL--EPVRLLRQIasglaHLHslNIVHR 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 647 DLKPANFLIV------DGMLKLIDFGIANQMQPDTTSVVKDSQV-GTVNYMPPEAIKDMSSSRENgkskskisPKSDVWS 719
Cdd:cd13982 124 DLKPQNILIStpnahgNVRAMISDFGLCKKLDVGRSSFSRRSGVaGTSGWIAPEMLSGSTKRRQT--------RAVDIFS 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 720 LGCILYY-MTYGKTPF----QQIINQISKLHAIIDPNHEIEFpdIPEkdLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd13982 196 LGCVFYYvLSGGSHPFgdklEREANILKGKYSLDKLLSLGEH--GPE--AQDLIERMIDFDPEKRPSAEEVLNHPF 267
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
525-790 3.61e-21

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: 93.93  E-value: 3.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTlDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVME 603
Cdd:cd14095   2 YDIGRVIGDGNFAVVKECRDKAtDKEYALKIIDKAKCKGKE-HMIENEVAILRRVKHPN--IVQLIEEYDTDTELYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 C---GniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV---DGM--LKLIDFGIANQMQPDT 675
Cdd:cd14095  79 LvkgG--DLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVeheDGSksLKLADFGLATEVKEPL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVvkdsqVGTVNYMPPEAIKdmsssrENGkskskISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNhEIE 755
Cdd:cd14095 157 FTV-----CGTPTYVAPEILA------ETG-----YGLKVDIWAAGVITYILLCGFPPFRSPDRDQEELFDLILAG-EFE 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 756 FP-----DIPEkDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14095 220 FLspywdNISD-SAKDLISRMLVVDPEKRYSAGQVLDHPW 258
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
525-787 3.63e-21

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: 93.89  E-value: 3.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSyRNEIAYLNKLQqHSDKIIRLYDYEiTDQYIYMVME 603
Cdd:cd08219   2 YNVLRVVGEGSFGRALLVQHVnSDQKYAMKEIRLPKSSSAVEDS-RKEAVLLAKMK-HPNIVAFKESFE-ADGHLYIVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKS-IDPWERKSYW-KNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQPDTTSVV 679
Cdd:cd08219  79 yCDGGDLMQKIKLQRGkLFPEDTILQWfVQMCLGVQHIHEKRVLHRDIKSKNiFLTQNGKVKLGDFGSARLLTSPGAYAC 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 kdSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQ-----QIINQISKlhAIIDPnhei 754
Cdd:cd08219 159 --TYVGTPYYVPPEIWENMPYNNKS-----------DIWSLGCILYELCTLKHPFQanswkNLILKVCQ--GSYKP---- 219
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 755 eFPDIPEKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd08219 220 -LPSHYSYELRSLIKQMFKRNPRSRPSATTILS 251
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
525-791 3.85e-21

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: 94.74  E-value: 3.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIYA-IKYVNLEEA-DNQTLDSYRNEIAYLNKLQQHSD--KIIRLYDYEI--TDQYI 598
Cdd:cd14040   8 YLLLHLLGRGGFSEVYKAFDLYEQRYAaVKIHQLNKSwRDEKKENYHKHACREYRIHKELDhpRIVKLYDYFSldTDTFC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQ--HGIVHSDLKPANFLIVDGM----LKLIDFGIANQMQ 672
Cdd:cd14040  88 TVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTacgeIKITDFGLSKIMD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSV----VKDSQVGTVNYMPPEAIKdmsssreNGKSKSKISPKSDVWSLGCILYYMTYGKTPF------QQIINQIS 742
Cdd:cd14040 168 DDSYGVdgmdLTSQGAGTYWYLPPECFV-------VGKEPPKISNKVDVWSVGVIFFQCLYGRKPFghnqsqQDILQENT 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 23308722 743 KLHAIidpnhEIEFPDIP--EKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14040 241 ILKAT-----EVQFPVKPvvSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
525-791 4.05e-21

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: 4.05e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVF--QVLNEKKQIyAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVM 602
Cdd:cd08225   2 YEIIKKIGEGSFGKIYlaKAKSDSEHC-VIKEIDLTKMPVKEKEASKKEVILLAKMK-HPN-IVTFFASFQENGRLFIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKSIDPWERK--SYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGML-KLIDFGIANQMQpDTTS 677
Cdd:cd08225  79 EyCDGGDLMKRINRQRGVLFSEDQilSWFVQISLGLKHIHDRKILHRDIKSQNiFLSKNGMVaKLGDFGIARQLN-DSME 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKdSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPF-----QQIINQISKLH-AIIDPN 751
Cdd:cd08225 158 LAY-TCVGTPYYLSPEICQNRPYNNKT-----------DIWSLGCVLYELCTLKHPFegnnlHQLVLKICQGYfAPISPN 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 752 HeiefpdipEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd08225 226 F--------SRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
524-790 4.24e-21

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: 93.80  E-value: 4.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKlqqhsDKIIRLYDYEITDQYIYMVM 602
Cdd:cd14107   3 VYEVKEEIGRGTFGFVKRVTHKgNGECCAAKFIPLRSSTRARAFQERDILARLSH-----RRLTCLLDQFETRKTLILIL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM---LKLIDFGIANQMQPdttSV 678
Cdd:cd14107  78 ElCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTredIKICDFGFAQEITP---SE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFPD 758
Cdd:cd14107 155 HQFSKYGSPEFVAPEIVHQEPVSA-----------ATDIWALGVIAYLSLTCHSPFAG-ENDRATLLNVAEGVVSWDTPE 222
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 759 IPEK--DLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14107 223 ITHLseDAKDFIKRVLQPDPEKRPSASECLSHEW 256
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
525-791 5.06e-21

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: 93.52  E-value: 5.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQ-IYAIKYVNLEEADNQTLDSY-RNEIAYLNKLQQHSdkIIRLYDY-EITDQYIYMV 601
Cdd:cd14163   2 YQLGKTIGEGTYSKVKEAFSKKHQrKVAIKIIDKSGGPEEFIQRFlPRELQIVERLDHKN--IIHVYEMlESADGKIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECG-NIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMqPDTTSVVK 680
Cdd:cd14163  80 MELAeDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGFTLKLTDFGFAKQL-PKGGRELS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDMSSSRENGkskskispksDVWSLGCILYYMTYGKTPFQQiiNQISKLhaIIDPNHEIEFPD-- 758
Cdd:cd14163 159 QTFCGSTAYAAPEVLQGVPHDSRKG----------DIWSMGVVLYVMLCAQLPFDD--TDIPKM--LCQQQKGVSLPGhl 224
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14163 225 GVSRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
520-791 6.06e-21

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 93.37  E-value: 6.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 520 VKGRIysilkqIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQT-------LDSYRNEIAYLNKLQQhsDKIIRLYDY 591
Cdd:cd06628   3 IKGAL------IGSGSFGSVYLGMNASSgELMAVKQVELPSVSAENkdrkksmLDALQREIALLRELQH--ENIVQYLGS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 592 EITDQYIYMVMEC---GNID--LNSWLKKKKSIdpweRKSYWKNMLEAVHTIHQHGIVHSDLKPANFLiVD--GMLKLID 664
Cdd:cd06628  75 SSDANHLNIFLEYvpgGSVAtlLNNYGAFEESL----VRNFVRQILKGLNYLHNRGIIHRDIKGANIL-VDnkGGIKISD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 665 FGIANQMQPDTTSVVKDSQ----VGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQqiinQ 740
Cdd:cd06628 150 FGISKKLEANSLSTKNNGArpslQGSVFWMAPEVVKQTSYTRK-----------ADIWSLGCLVVEMLTGTHPFP----D 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 23308722 741 ISKLHAI--IDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06628 215 CTQMQAIfkIGENASPTIPSNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
525-791 6.39e-21

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: 94.36  E-value: 6.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIY-AIKYVNLEEA-DNQTLDSYRNEIAYLNKLQQHSD--KIIRLYDYEI--TDQYI 598
Cdd:cd14041   8 YLLLHLLGRGGFSEVYKAFDLTEQRYvAVKIHQLNKNwRDEKKENYHKHACREYRIHKELDhpRIVKLYDYFSldTDSFC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQ--HGIVHSDLKPANFLIVDGM----LKLIDFGIANQMQ 672
Cdd:cd14041  88 TVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGTacgeIKITDFGLSKIMD 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSVVKDSQV-----GTVNYMPPEAIKdmsssreNGKSKSKISPKSDVWSLGCILYYMTYGKTPF------QQIINQI 741
Cdd:cd14041 168 DDSYNSVDGMELtsqgaGTYWYLPPECFV-------VGKEPPKISNKVDVWSVGVIFYQCLYGRKPFghnqsqQDILQEN 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 23308722 742 SKLHAIidpnhEIEFPDIP--EKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14041 241 TILKAT-----EVQFPPKPvvTPEAKAFIRRCLAYRKEDRIDVQQLACDPYL 287
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
529-792 7.31e-21

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: 94.34  E-value: 7.31e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLNEK-KQIYAIKYVNLE-EADNQtldsyrNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVMEC-G 605
Cdd:cd14179  13 KPLGEGSFSICRKCLHKKtNQEYAVKIVSKRmEANTQ------REIAALKLCEGHPN-IVKLHEVYHDQLHTFLVMELlK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD----GMLKLIDFGIANQMQPDTTSVvkD 681
Cdd:cd14179  86 GGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDesdnSEIKIIDFGFARLKPPDNQPL--K 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIKdmsssrENGkskskISPKSDVWSLGCILYYMTYGKTPFQ------------QIINQISKLhaiiD 749
Cdd:cd14179 164 TPCFTLHYAAPELLN------YNG-----YDESCDLWSLGVILYTMLSGQVPFQchdksltctsaeEIMKKIKQG----D 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 750 PNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14179 229 FSFEGEAWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQ 271
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
553-789 7.36e-21

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: 92.88  E-value: 7.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 553 KYVNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME-C--GNIDLNSWLKKKKSIDPWERKSYWK 629
Cdd:cd08221  31 KEVNLSRLSEKERRDALNEIDILSLLNH--DNIITYYNHFLDGESLFIEMEyCngGNLHDKIAQQKNQLFPEEVVLWYLY 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 630 NMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMqpDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgksk 708
Cdd:cd08221 109 QIVSAVSHIHKAGILHRDIKTLNiFLTKADLVKLGDFGISKVL--DSESSMAESIVGTPYYMSPELVQGVKYNFKS---- 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 709 skispksDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFPDIPEkDLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd08221 183 -------DIWAVGCVLYELLTLKRTFDA-TNPLRLAVKIVQGEYEDIDEQYSE-EIIQLVHDCLHQDPEDRPTAEELLER 253

                .
gi 23308722 789 P 789
Cdd:cd08221 254 P 254
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
529-789 7.51e-21

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: 93.26  E-value: 7.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLNEKK-QIYAIKYV----NLEEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd06630   6 PLLGTGAFSSCYQARDVKTgTLMAVKQVsfcrNSSSEQEEVVEAIREEIRMMARLN-HPN-IVRMLGATQHKSHFNIFVE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 C---GNIdlNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANfLIVDGM---LKLIDFGIANQMQPDTTS 677
Cdd:cd06630  84 WmagGSV--ASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGAN-LLVDSTgqrLRIADFGAAARLASKGTG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 V--VKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAIIDPNhe 753
Cdd:cd06630 161 AgeFQGQLLGTIAFMAPEVLRGEQYGR-----------SCDVWSVGCVIIEMATAKPPWnaEKISNHLALIFKIASAT-- 227
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 754 iEFPDIPE---KDLQDVLKCCLKRDPKQRISIPELLAHP 789
Cdd:cd06630 228 -TPPPIPEhlsPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
518-792 1.25e-20

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: 95.07  E-value: 1.25e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 518 ISVKGRIYSILKQIGSGGSSKVFQVLNEKKQ-IYAIKYVN----LEEADNQTLDSYRNEIAYLNklqqhSDKIIRLYDYE 592
Cdd:cd05621  47 LQMKAEDYDVVKVIGRGAFGEVQLVRHKASQkVYAMKLLSkfemIKRSDSAFFWEERDIMAFAN-----SPWVVQLFCAF 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 593 ITDQYIYMVME-CGNIDLNSWLKKKKSIDPWErKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQ 670
Cdd:cd05621 122 QDDKYLYMVMEyMPGGDLVNLMSNYDVPEKWA-KFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKyGHLKLADFGTCMK 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MqpDTTSVVK-DSQVGTVNYMPPEAIKDMSSSRENGkskskisPKSDVWSLGCILYYMTYGKTPF--QQIINQISKlhaI 747
Cdd:cd05621 201 M--DETGMVHcDTAVGTPDYISPEVLKSQGGDGYYG-------RECDWWSVGVFLFEMLVGDTPFyaDSLVGTYSK---I 268
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 748 IDPNHEIEFPDIPE--KDLQDVLkCCLKRDPKQRI---SIPELLAHPYVQ 792
Cdd:cd05621 269 MDHKNSLNFPDDVEisKHAKNLI-CAFLTDREVRLgrnGVEEIKQHPFFR 317
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
524-810 1.38e-20

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: 93.38  E-value: 1.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLE---EADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIY 599
Cdd:cd14094   4 VYELCEVIGKGPFSVVRRCIHrETGQQFAVKIVDVAkftSSPGLSTEDLKREASICHMLKH--PHIVELLETYSSDGMLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMEC--GNiDLNSWLKKKKS----IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIAN 669
Cdd:cd14094  82 MVFEFmdGA-DLCFEIVKRADagfvYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLAskenSAPVKLGGFGVAI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMqPDTTSVVKdSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF----QQIINQISKLH 745
Cdd:cd14094 161 QL-GESGLVAG-GRVGTPHFMAPEVVKREPYGK-----------PVDVWGCGVILFILLSGCLPFygtkERLFEGIIKGK 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 746 AIIDPNheiEFPDIPEKDlQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQM-AKGTTEEMK 810
Cdd:cd14094 228 YKMNPR---QWSHISESA-KDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRIhLPETVEQLR 289
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
523-790 1.66e-20

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: 92.00  E-value: 1.66e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLN-EKKQIYAIKYV-NLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYM 600
Cdd:cd14188   1 KRYCRGKVLGKGGFAKCYEMTDlTTNKVYAAKIIpHSRVSKPHQREKIDKEIELHRIL--HHKHVVQFYHYFEDKENIYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSv 678
Cdd:cd14188  79 LLEyCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMeLKVGDFGLAARLEPLEHR- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIefPD 758
Cdd:cd14188 158 -RRTICGTPNYLSPEVLNKQGHGCES-----------DIWALGCVMYTMLLGRPPFET-TNLKETYRCIREARYSL--PS 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14188 223 SLLAPAKHLIASMLSKNPEDRPSLDEIIRHDF 254
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
527-810 2.03e-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: 92.60  E-value: 2.03e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKKQ-IYAIKYVNLEeADNQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVMEcg 605
Cdd:cd06622   5 VLDELGKGNYGSVYKVLHRPTGvTMAMKEIRLE-LDESKFNQIIMELDILHKAV--SPYIVDFYGAFFIEGAVYMCME-- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKKKSIDPWERKSywKNMLE--AVHTIH-------QHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpdT 675
Cdd:cd06622  80 YMDAGSLDKLYAGGVATEGIP--EDVLRriTYAVVKglkflkeEHNIIHRDVKPTNVLVnGNGQVKLCDFGVSGNL---V 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVVKdSQVGTVNYMPPEAIKDmsssrENGKSKSKISPKSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAIID---P 750
Cdd:cd06622 155 ASLAK-TNIGCQSYMAPERIKS-----GGPNQNPTYTVQSDVWSLGLSILEMALGRYPYppETYANIFAQLSAIVDgdpP 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 751 NHEIEFPDipekDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMK 810
Cdd:cd06622 229 TLPSGYSD----DAQDFVAKCLNKIPNRRPTYAQLLEHPWLVKYKNADVDMAEWVTGALK 284
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
525-795 2.05e-20

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 92.40  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIYAIKYVnLEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVME- 603
Cdd:cd06643   7 WEIVGELGDGAFGKVYKAQNKETGILAAAKV-IDTKSEEELEDYMVEIDILASCDHPN--IVKLLDAFYYENNLWILIEf 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 C--GNIDLnSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQmqpDTTSVV- 679
Cdd:cd06643  84 CagGAVDA-VMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFtLDGDIKLADFGVSAK---NTRTLQr 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIK-DMSSSREngkskskISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPnheiEFPD 758
Cdd:cd06643 160 RDSFIGTPYWMAPEVVMcETSKDRP-------YDYKADVWSLGVTLIEMAQIEPPHHE-LNPMRVLLKIAKS----EPPT 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 759 I--PEK---DLQDVLKCCLKRDPKQRISIPELLAHPYVQIQT 795
Cdd:cd06643 228 LaqPSRwspEFKDFLRKCLEKNVDARWTTSQLLQHPFVSVLV 269
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
524-791 2.32e-20

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 92.06  E-value: 2.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKKQ-IYAIKYVNLEEADNQtLDSYRNEIAYLNklQQHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd06641   5 LFTKLEKIGKGSFGEVFKGIDNRTQkVVAIKIIDLEEAEDE-IEDIQQEITVLS--QCDSPYVTKYYGSYLKDTKLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 EC--GNIDLNswLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQpdTTSVV 679
Cdd:cd06641  82 EYlgGGSALD--LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEhGEVKLADFGVAGQLT--DTQIK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIinQISKLHAIIDPNHEIEFPDI 759
Cdd:cd06641 158 RN*FVGTPFWMAPEVIKQSAYDSK-----------ADIWSLGITAIELARGEPPHSEL--HPMKVLFLIPKNNPPTLEGN 224
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 760 PEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06641 225 YSKPLKEFVEACLNKEPSFRPTAKELLKHKFI 256
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
523-791 2.44e-20

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 92.04  E-value: 2.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEEADNQtLDSYRNEIAYLNklQQHSDKIIRLYDYEITDQYIYMV 601
Cdd:cd06642   4 ELFTKLERIGKGSFGEVYKgIDNRTKEVVAIKIIDLEEAEDE-IEDIQQEITVLS--QCDSPYITRYYGSYLKGTKLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MEC--GNIDLNswLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQpdTTSV 678
Cdd:cd06642  81 MEYlgGGSALD--LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEqGDVKLADFGVAGQLT--DTQI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIinQISKLHAIIDPNHEIEFPD 758
Cdd:cd06642 157 KRNTFVGTPFWMAPEVIKQSAYDFK-----------ADIWSLGITAIELAKGEPPNSDL--HPMRVLFLIPKNSPPTLEG 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06642 224 QHSKPFKEFVEACLNKDPRFRPTAKELLKHKFI 256
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
525-821 3.05e-20

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: 92.01  E-value: 3.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEADNQtldsyrNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd14175   3 YVVKETIGVGSYSVCKRCVHKATNMeYAVKVIDKSKRDPS------EEIEILLRYGQHPN-IITLKDVYDDGKHVYLVTE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 C--GNIDLNSWLKKKkSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-----GMLKLIDFGIANQMQPDTT 676
Cdd:cd14175  76 LmrGGELLDKILRQK-FFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDesgnpESLRICDFGFAKQLRAENG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVkdSQVGTVNYMPPEAIKdmSSSRENGkskskispkSDVWSLGCILYYMTYGKTPF--------QQIINQISKLHAII 748
Cdd:cd14175 155 LLM--TPCYTANFVAPEVLK--RQGYDEG---------CDIWSLGILLYTMLAGYTPFangpsdtpEEILTRIGSGKFTL 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 749 DPNHEIEFPDIPekdlQDVLKCCLKRDPKQRISIPELLAHPYV-QIQTHPVNQMAKgttEEMKYVLGQLVGLNS 821
Cdd:cd14175 222 SGGNWNTVSDAA----KDLVSKMLHVDPHQRLTAKQVLQHPWItQKDKLPQSQLNH---QDVQLVKGAMAATYS 288
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
518-792 3.27e-20

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: 93.92  E-value: 3.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 518 ISVKGRIYSILKQIGSGGSSKVfQVLNEK--KQIYAIKYVN----LEEADNQTLDSYRNEIAYLNklqqhSDKIIRLYDY 591
Cdd:cd05622  68 LRMKAEDYEVVKVIGRGAFGEV-QLVRHKstRKVYAMKLLSkfemIKRSDSAFFWEERDIMAFAN-----SPWVVQLFYA 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 592 EITDQYIYMVME-CGNIDLNSWLKKKKSIDPWERkSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIAN 669
Cdd:cd05622 142 FQDDRYLYMVMEyMPGGDLVNLMSNYDVPEKWAR-FYTAEVVLALDAIHSMGFIHRDVKPDNMLLdKSGHLKLADFGTCM 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMQPDTTsVVKDSQVGTVNYMPPEAIKDMSSSRENGKSKskispksDVWSLGCILYYMTYGKTPF--QQIINQISKlhaI 747
Cdd:cd05622 221 KMNKEGM-VRCDTAVGTPDYISPEVLKSQGGDGYYGREC-------DWWSVGVFLYEMLVGDTPFyaDSLVGTYSK---I 289
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 748 IDPNHEIEFPDIPE--KDLQDVLkCCLKRDPKQRI---SIPELLAHPYVQ 792
Cdd:cd05622 290 MNHKNSLTFPDDNDisKEAKNLI-CAFLTDREVRLgrnGVEEIKRHLFFK 338
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
525-791 3.44e-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: 92.00  E-value: 3.44e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEADNQtldsyrNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd14178   5 YEIKEDIGIGSYSVCKRCVHKATSTeYAVKIIDKSKRDPS------EEIEILLRYGQHPN-IITLKDVYDDGKFVYLVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 C--GNIDLNSWLKKKkSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-----LKLIDFGIANQMQPDTT 676
Cdd:cd14178  78 LmrGGELLDRILRQK-CFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESgnpesIRICDFGFAKQLRAENG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVkdSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF--------QQIINQI-SKLHAI 747
Cdd:cd14178 157 LLM--TPCYTANFVAPEVLKRQGYD-----------AACDIWSLGILLYTMLAGFTPFangpddtpEEILARIgSGKYAL 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 748 IDPNHeiefpDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14178 224 SGGNW-----DSISDAAKDIVSKMLHVDPHQRLTAPQVLRHPWI 262
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
524-791 3.75e-20

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: 90.78  E-value: 3.75e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEEADN-QTLDSYRN--EIAYLNKLQQHSDKIIRLYD-YEITDQYI 598
Cdd:cd14102   1 VYQVGSVLGSGGFGTVYAgSRIADGLPVAVKHVVKERVTEwGTLNGVMVplEIVLLKKVGSGFRGVIKLLDwYERPDGFL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 yMVMECGNI--DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANfLIVD---GMLKLIDFGiANQMQP 673
Cdd:cd14102  81 -IVMERPEPvkDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDEN-LLVDlrtGELKLIDFG-SGALLK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKDsqvGTVNYMPPEAIKdmsSSRENGKSKSkispksdVWSLGCILYYMTYGKTPFQQiinqisklhaiidpNHE 753
Cdd:cd14102 158 DTVYTDFD---GTRVYSPPEWIR---YHRYHGRSAT-------VWSLGVLLYDMVCGDIPFEQ--------------DEE 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 754 I-----EFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14102 211 IlrgrlYFRRRVSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
529-797 3.90e-20

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: 92.28  E-value: 3.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFqvLNEKK---QIYAIKYVNLEEA-DNQTLDSYRNEIAYLNKLQQHSdKIIRLYDYEITDQYIYMVME- 603
Cdd:cd05570   1 KVLGKGSFGKVM--LAERKktdELYAIKVLKKEVIiEDDDVECTMTEKRVLALANRHP-FLTGLHACFQTEDRLYFVMEy 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQPD-TTSVVk 680
Cdd:cd05570  78 VNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLdAEGHIKIADFGMCKEgIWGGnTTSTF- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 dsqVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQISklhaiidpNHEIE 755
Cdd:cd05570 157 ---CGTPDYIAPEILREQDYGFS-----------VDWWALGVLLYEMLAGQSPFegddeDELFEAIL--------NDEVL 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQRisipeLLAHPYVQ--IQTHP 797
Cdd:cd05570 215 YPRWLSREAVSILKGLLTKDPARR-----LGCGPKGEadIKAHP 253
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
524-791 4.18e-20

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: 90.86  E-value: 4.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVfqVLNEKK---QIYAIKYVNLEEADNQTlDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYM 600
Cdd:cd14167   4 IYDFREVLGTGAFSEV--VLAEEKrtqKLVAIKCIAKKALEGKE-TSIENEIAVLHKIK-HPN-IVALDDIYESGGHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIANQMQPDT 675
Cdd:cd14167  79 IMQlVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYYsldeDSKIMISDFGLSKIEGSGS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 tsvVKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIE 755
Cdd:cd14167 159 ---VMSTACGTPGYVAPEVLAQKPYSK-----------AVDCWSIGVIAYILLCGYPPFYD-ENDAKLFEQILKAEYEFD 223
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 756 FP---DIPEKdLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14167 224 SPywdDISDS-AKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
520-786 4.77e-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: 90.76  E-value: 4.77e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 520 VKGRIysilkqIGSGGSSKVFQVLN-EKKQIYAIKYV--NLEEADNQTlDSYRNEIAYLNKL-QQHsdkIIRLYDYEITD 595
Cdd:cd14187  10 VRGRF------LGKGGFAKCYEITDaDTKEVFAGKIVpkSLLLKPHQK-EKMSMEIAIHRSLaHQH---VVGFHGFFEDN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQP 673
Cdd:cd14187  80 DFVYVVLElCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMeVKIGDFGLATKVEY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSvvKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIDPNhE 753
Cdd:cd14187 160 DGER--KKTLCGTPNYIAPEVLSKKGHSFE-----------VDIWSIGCIMYTLLVGKPPFET--SCLKETYLRIKKN-E 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 754 IEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14187 224 YSIPKHINPVAASLIQKMLQTDPTARPTINELL 256
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
543-791 5.76e-20

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: 90.55  E-value: 5.76e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 543 LNEKKQIyAIKYVnlEEADNQTLDSYRNEIAyLNKLQQHSDkIIRLYDYEITDQYIYMVME---CGNidLNSWLKKKksi 619
Cdd:cd06624  30 LSTQVRI-AIKEI--PERDSREVQPLHEEIA-LHSRLSHKN-IVQYLGSVSEDGFFKIFMEqvpGGS--LSALLRSK--- 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 620 dpW--------ERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGIANQ---MQPDTTSVVkdsqvGT 686
Cdd:cd06624 100 --WgplkdnenTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVntYSGVVKISDFGTSKRlagINPCTETFT-----GT 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 687 VNYMPPEAIKdmSSSRENGKSKskispksDVWSLGCILYYMTYGKTPFQQIINQIS--------KLHaiidpnheiefPD 758
Cdd:cd06624 173 LQYMAPEVID--KGQRGYGPPA-------DIWSLGCTIIEMATGKPPFIELGEPQAamfkvgmfKIH-----------PE 232
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 759 IPE---KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06624 233 IPEslsEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
531-789 7.07e-20

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: 90.56  E-value: 7.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQV--LNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQH-SDKIIRLYD-YEITDQYIYMVMECGN 606
Cdd:cd14052   8 IGSGEFSQVYKVseRVPTGKVYAVKKLKPNYAGAKDRLRRLEEVSILRELTLDgHDNIVQLIDsWEYHGHLYIQTELCEN 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKK---KKSIDPWErksYWKNMLE---AVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMqPDTTSVV 679
Cdd:cd14052  88 GSLDVFLSElglLGRLDEFR---VWKILVElslGLRFIHDHHFVHLDLKPANVLITfEGTLKIGDFGMATVW-PLIRGIE 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDsqvGTVNYMPPEAIkdmsSSRENGkskskisPKSDVWSLGCILY------YMTYGKTPFQQIIN---------QISKL 744
Cdd:cd14052 164 RE---GDREYIAPEIL----SEHMYD-------KPADIFSLGLILLeaaanvVLPDNGDAWQKLRSgdlsdaprlSSTDL 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 23308722 745 HAIIDPNHEIEFPDIPEKDLQDVLKCCLKR----DPKQRISIPELLAHP 789
Cdd:cd14052 230 HSASSPSSNPPPDPPNMPILSGSLDRVVRWmlspEPDRRPTADDVLATP 278
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
527-779 7.88e-20

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: 90.72  E-value: 7.88e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKKQ-IYAIKYVNLEE-ADNQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVME- 603
Cdd:cd05580   5 FLKTLGTGSFGRVRLVKHKDSGkYYALKILKKAKiIKLKQVEHVLNEKRILSEVR--HPFIVNLLGSFQDDRNLYMVMEy 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVvkds 682
Cdd:cd05580  83 VPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLdSDGHIKITDFGFAKRVKDRTYTL---- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 qVGTVNYMPPEAIkdmsSSRENGkskskisPKSDVWSLGCILYYMTYGKTPF---------QQIINQisklhaiidpnhE 753
Cdd:cd05580 159 -CGTPEYLAPEII----LSKGHG-------KAVDWWALGILIYEMLAGYPPFfdenpmkiyEKILEG------------K 214
                       250       260
                ....*....|....*....|....*.
gi 23308722 754 IEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05580 215 IRFPSFFDPDAKDLIKRLLVVDLTKR 240
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
525-791 7.91e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 89.80  E-value: 7.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd08223   2 YQFLRVIGKGSYGEVWLVRHKRdRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLK-HPNIVSYKESFEGEDGFLYIVMG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERK--SYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMqpDTTSVV 679
Cdd:cd08223  81 fCEGGDLYTRLKEQKGVLLEERQvvEWFVQIAMALQYMHERNILHRDLKTQNiFLTKSNIIKVGDLGIARVL--ESSSDM 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQ-QIINqiSKLHAIIdpnhEIEFPD 758
Cdd:cd08223 159 ATTLIGTPYYMSPELFSNKPYNHKS-----------DVWALGCCVYEMATLKHAFNaKDMN--SLVYKIL----EGKLPP 221
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 759 IPEK---DLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd08223 222 MPKQyspELGELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
544-791 8.19e-20

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: 90.10  E-value: 8.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 544 NEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLnKLQQHSDKIIRLYD-YEITDQYIYMVMECGNIDLNSWLKKKKSIDPW 622
Cdd:cd14106  30 KETGKEYAAKFLRKRRRGQDCRNEILHEIAVL-ELCKDCPRVVNLHEvYETRSELILILELAAGGELQTLLDEEECLTEA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 623 ERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI----VDGMLKLIDFGIANQMQPDTTsvVKDSqVGTVNYMPPEAIkdm 698
Cdd:cd14106 109 DVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtsefPLGDIKLCDFGISRVIGEGEE--IREI-LGTPDYVAPEIL--- 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 699 ssSREngksksKISPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIIDPNHeieFPDIPEkDLQDVLKCCLK 773
Cdd:cd14106 183 --SYE------PISLATDMWSIGVLTYVLLTGHSPFggddkQETFLNISQCNLDFPEEL---FKDVSP-LAIDFIKRLLV 250
                       250
                ....*....|....*...
gi 23308722 774 RDPKQRISIPELLAHPYV 791
Cdd:cd14106 251 KDPEKRLTAKECLEHPWL 268
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
548-792 8.54e-20

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 91.09  E-value: 8.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 548 QIYAIKYVNLE-EADNQtldsyrNEIAYLNKLQQHSDkIIRLYDYeITDQY-IYMVMEC--GNiDLNSWLKKKKSIDPWE 623
Cdd:cd14180  32 QEYAVKIISRRmEANTQ------REVAALRLCQSHPN-IVALHEV-LHDQYhTYLVMELlrGG-ELLDRIKKKARFSESE 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 624 RKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD----GMLKLIDFGIAnQMQPDTTSVVKdSQVGTVNYMPPEAIKDMS 699
Cdd:cd14180 103 ASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADesdgAVLKVIDFGFA-RLRPQGSRPLQ-TPCFTLQYAAPELFSNQG 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 700 SSRengkskskispKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAiIDPNHEIEFPDIP---------EKDLQDVLKC 770
Cdd:cd14180 181 YDE-----------SCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHA-ADIMHKIKEGDFSlegeawkgvSEEAKDLVRG 248
                       250       260
                ....*....|....*....|..
gi 23308722 771 CLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14180 249 LLTVDPAKRLKLSELRESDWLQ 270
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
525-790 8.73e-20

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 90.65  E-value: 8.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  525 YSILKQIGSGGSSKVFQ----VLNEkkqIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYM 600
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKardrVTNE---TIALKKIRLEQEDEGVPSTAIREISLLKEMQH--GNIVRLQDVVHSEKRLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  601 VMECGNIDLNSWLKKKKSI--DPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGIANQMQPDTT 676
Cdd:PLN00009  79 VFEYLDLDLKKHMDSSPDFakNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIdrRTNALKLADFGLARAFGIPVR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  677 SVVKdsQVGTVNYMPPEAikdMSSSREngkskskISPKSDVWSLGCILYYMTYGKT--PFQQIINQISKLHAIID----- 749
Cdd:PLN00009 159 TFTH--EVVTLWYRAPEI---LLGSRH-------YSTPVDIWSVGCIFAEMVNQKPlfPGDSEIDELFKIFRILGtpnee 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  750 --------PNHEIEFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:PLN00009 227 twpgvtslPDYKSAFPKWPPKDLAtvvptlepagvDLLSKMLRLDPSKRITARAALEHEY 286
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
525-791 1.02e-19

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


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 90.08  E-value: 1.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSkVFQVLNEKK--QIYAIKYVNLEEADNQ----TLDSYRNEIAYLNKLQQHSdkIIRLYD-YEITDQY 597
Cdd:cd14194   7 YDTGEELGSGQFA-VVKKCREKStgLQYAAKFIKKRRTKSSrrgvSREDIEREVSILKEIQHPN--VITLHEvYENKTDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG-----MLKLIDFGIANQMq 672
Cdd:cd14194  84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRnvpkpRIKIIDFGLAHKI- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 pDTTSVVKDSqVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQISKlhai 747
Cdd:cd14194 163 -DFGNEFKNI-FGTPEFVAPEIVNYEPLGLE-----------ADMWSIGVITYILLSGASPFlgdtkQETLANVSA---- 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 748 IDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14194 226 VNYEFEDEYFSNTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
531-792 1.03e-19

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: 89.52  E-value: 1.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVF--QVLNEKKQIyAIKYVN----LEEADNQTLDSYRNEIAYLNKLQQHSDK--IIRLYDYEITDQYIYMVM 602
Cdd:cd14101   8 LGKGGFGTVYagHRISDGLQV-AIKQISrnrvQQWSKLPGVNPVPNEVALLQSVGGGPGHrgVIRLLDWFEIPEGFLLVL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E----CGniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGianqmqpdTT 676
Cdd:cd14101  87 ErpqhCQ--DLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVdlRTGDIKLIDFG--------SG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSQV----GTVNYMPPEAIkdmsssrengKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKlhaiidpnh 752
Cdd:cd14101 157 ATLKDSMYtdfdGTRVYSPPEWI----------LYHQYHALPATVWSLGILLYDMVCGDIPFERDTDILKA--------- 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 753 EIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14101 218 KPSFNKRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
528-792 1.21e-19

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: 90.75  E-value: 1.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVLN-EKKQIYAIKyvNLEEAD----NQT--LDSYRNEIAylnklQQHSDKIIRLYdYEITD-QYIY 599
Cdd:cd05599   6 LKVIGRGAFGEVRLVRKkDTGHVYAMK--KLRKSEmlekEQVahVRAERDILA-----EADNPWVVKLY-YSFQDeENLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQpdtTS 677
Cdd:cd05599  78 LIMEfLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLdARGHIKLSDFGLCTGLK---KS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFP 757
Cdd:cd05599 155 HLAYSTVGTPDYIAPEVFLQKGYGKE-----------CDWWSLGVIMYEMLIGYPPFCS-DDPQETCRKIMNWRETLVFP 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 758 DIPE--KDLQDVLK--CClkrDPKQRI---SIPELLAHPYVQ 792
Cdd:cd05599 223 PEVPisPEAKDLIErlLC---DAEHRLganGVEEIKSHPFFK 261
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
524-797 1.30e-19

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: 91.20  E-value: 1.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKKQIY-AIK-----YVNLEEADNqtldSYRnEIAYLnKLQQHsDKIIRLYDYEITD-- 595
Cdd:cd07851  16 RYQNLSPVGSGAYGQVCSAFDTKTGRKvAIKklsrpFQSAIHAKR----TYR-ELRLL-KHMKH-ENVIGLLDVFTPAss 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 ----QYIYMVMECGNIDLNSWLKKKKSIDpwERKSYW-KNMLEAVHTIHQHGIVHSDLKPANfLIV--DGMLKLIDFGIA 668
Cdd:cd07851  89 ledfQDVYLVTHLMGADLNNIVKCQKLSD--DHIQFLvYQILRGLKYIHSAGIIHRDLKPSN-LAVneDCELKILDFGLA 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQMQPDTTsvvkdSQVGTVNYMPPEAIKD-MSSSRengkskskispKSDVWSLGCILYYMTYGKTPF--QQIINQISKLH 745
Cdd:cd07851 166 RHTDDEMT-----GYVATRWYRAPEIMLNwMHYNQ-----------TVDIWSVGCIMAELLTGKTLFpgSDHIDQLKRIM 229
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 746 AII-DPNHEI--------------EFPDIPEKDLQDV-----------LKCCLKRDPKQRISIPELLAHPYVQIQTHP 797
Cdd:cd07851 230 NLVgTPDEELlkkissesarnyiqSLPQMPKKDFKEVfsganplaidlLEKMLVLDPDKRITAAEALAHPYLAEYHDP 307
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
524-791 1.43e-19

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: 89.26  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLE------EADNQTldSYRNEIAYLNKLQQHSDKIIRLYD-YEITD 595
Cdd:cd14100   1 QYQVGPLLGSGGFGSVYSGIRVADGApVAIKHVEKDrvsewgELPNGT--RVPMEIVLLKKVGSGFRGVIRLLDwFERPD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIyMVMECGNI--DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGiANQM 671
Cdd:cd14100  79 SFV-LVLERPEPvqDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIdlNTGELKLIDFG-SGAL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QPDTTSVVKDsqvGTVNYMPPEAIKdmsSSRENGKSKSkispksdVWSLGCILYYMTYGKTPFQQIINQISKlhaiidpn 751
Cdd:cd14100 157 LKDTVYTDFD---GTRVYSPPEWIR---FHRYHGRSAA-------VWSLGILLYDMVCGDIPFEHDEEIIRG-------- 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 752 hEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14100 216 -QVFFRQRVSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
523-792 1.46e-19

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: 89.22  E-value: 1.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLdsYRNEIAYLNKLQqHSDKIIRLYDYEITDQyIYMV 601
Cdd:cd06647   7 KKYTRFEKIGQGASGTVYTAIDvATGQEVAIKQMNLQQQPKKEL--IINEILVMRENK-NPNIVNYLDSYLVGDE-LWVV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSvvK 680
Cdd:cd06647  83 MEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLgMDGSVKLTDFGFCAQITPEQSK--R 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIkdmsSSRENGKSKskispksDVWSLGCILYYMTYGKTPFqqiINQiSKLHAI--IDPNHEIEFPD 758
Cdd:cd06647 161 STMVGTPYWMAPEVV----TRKAYGPKV-------DIWSLGIMAIEMVEGEPPY---LNE-NPLRALylIATNGTPELQN 225
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 759 iPEKD---LQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06647 226 -PEKLsaiFRDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
525-791 1.74e-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: 88.86  E-value: 1.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEE-ADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME 603
Cdd:cd14161   5 YEFLETLGKGTYGRVKKARDSSGRLVAIKSIRKDRiKDEQDLLHIRREIEIMSSLNH--PHIISVYEVFENSSKIVIVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTtsvVKD 681
Cdd:cd14161  83 YASRgDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLdANGNIKIADFGLSNLYNQDK---FLQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIkdmsssreNGksKSKISPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKlHAIIDPNHeief 756
Cdd:cd14161 160 TYCGSPLYASPEIV--------NG--RPYIGPEVDSWSLGVLLYILVHGTMPFdghdyKILVKQISS-GAYREPTK---- 224
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 757 pdipEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14161 225 ----PSDACGLIRWLLMVNPERRATLEDVASHWWV 255
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
524-790 1.90e-19

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: 1.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVfqVLNEKKQ---IYAIKYVNLEEADNQTlDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYM 600
Cdd:cd14083   4 KYEFKEVLGTGAFSEV--VLAEDKAtgkLVAIKCIDKKALKGKE-DSLENEIAVLRKIK-HPN-IVQLLDIYESKSHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI----VDGMLKLIDFGIAnQMQpd 674
Cdd:cd14083  79 VMElvTGG-ELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspdEDSKIMISDFGLS-KME-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 tTSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQiiNQISKLHA-IIDPNHE 753
Cdd:cd14083 155 -DSGVMSTACGTPGYVAPEVLAQKPYGKA-----------VDCWSIGVISYILLCGYPPFYD--ENDSKLFAqILKAEYE 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 754 IEFP---DIPE--KDLQDVLKCClkrDPKQRISIPELLAHPY 790
Cdd:cd14083 221 FDSPywdDISDsaKDFIRHLMEK---DPNKRYTCEQALEHPW 259
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
524-789 1.98e-19

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: 88.52  E-value: 1.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLN-EKKQIYAIKyvnleeadnQTLDSYRNEIAYLNKLQ---------QHsDKIIRLYDYEI 593
Cdd:cd14050   2 CFTILSKLGEGSFGEVFKVRSrEDGKLYAVK---------RSRSRFRGEKDRKRKLEeverheklgEH-PNCVRFIKAWE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQ 672
Cdd:cd14050  72 EKGILYIQTELCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANiFLSKDGVCKLGDFGLVVELD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 pdtTSVVKDSQVGTVNYMPPEAIkdmsssreNGksksKISPKSDVWSLG-CILYYMTYGKTP-----FQQIINQisklha 746
Cdd:cd14050 152 ---KEDIHDAQEGDPRYMAPELL--------QG----SFTKAADIFSLGiTILELACNLELPsggdgWHQLRQG------ 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 747 IIDPnheiEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHP 789
Cdd:cd14050 211 YLPE----EFTAGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
527-802 2.90e-19

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: 89.36  E-value: 2.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKK-QIYAIKYVnleeadnqtldsYRNEIAYLNK---------LQQH-SDKIIRLYDYEITD 595
Cdd:cd06618  19 NLGEIGSGTCGQVYKMRHKKTgHVMAVKQM------------RRSGNKEENKrilmdldvvLKSHdCPYIVKCYGYFITD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVMECGNIDLNSWLKKKKSidPWERKSYWKNMLEAVHTIH----QHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ 670
Cdd:cd06618  87 SDVFICMELMSTCLDKLLKRIQG--PIPEDILGKMTVSIVKALHylkeKHGVIHRDVKPSNILLdESGNVKLCDFGISGR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MqpdTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIID- 749
Cdd:cd06618 165 L---VDSKAKTRSAGCAAYMAPERIDPPDNPKYD--------IRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNe 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 750 ----PNHEIEFpdipEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMA 802
Cdd:cd06618 234 eppsLPPNEGF----SPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYETAEVDVA 286
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
524-790 3.38e-19

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: 88.05  E-value: 3.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVF--------QVLNEKKQIYAIKYVNleeadnQTLDSYR--NEIAYLNKLQQHSDKIIRLYDYEI 593
Cdd:cd14019   2 KYRIIEKIGEGTFSSVYkaedklhdLYDRNKGRLVALKHIY------PTSSPSRilNELECLERLGGSNNVSGLITAFRN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQyIYMVME-CGNIDLNSWLKKkksIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFL--IVDGMLKLIDFGIAnQ 670
Cdd:cd14019  76 EDQ-VVAVLPyIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLynRETGKGVLVDFGLA-Q 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MQPDTTSvVKDSQVGTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPFqqiINQISKLHAI 747
Cdd:cd14019 151 REEDRPE-QRAPRAGTRGFRAPEVLfkcPHQTTA-------------IDIWSAGVILLSILSGRFPF---FFSSDDIDAL 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 748 IdpnhEIE--FPDipeKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14019 214 A----EIAtiFGS---DEAYDLLDKLLELDPSKRITAEEALKHPF 251
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
524-791 3.79e-19

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: 88.57  E-value: 3.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEEADNQtLDSYRNEIAYLNklQQHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd06640   5 LFTKLERIGKGSFGEVFKgIDNRTQQVVAIKIIDLEEAEDE-IEDIQQEITVLS--QCDSPYVTKYYGSYLKGTKLWIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 EC--GNIDLNswLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQpdTTSVV 679
Cdd:cd06640  82 EYlgGGSALD--LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEqGDVKLADFGVAGQLT--DTQIK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQ-----QIINQISKLHAiidPNHEI 754
Cdd:cd06640 158 RNTFVGTPFWMAPEVIQQSAYDSK-----------ADIWSLGITAIELAKGEPPNSdmhpmRVLFLIPKNNP---PTLVG 223
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 755 EFpdipEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06640 224 DF----SKPFKEFIDACLNKDPSFRPTAKELLKHKFI 256
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
525-791 4.13e-19

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: 87.95  E-value: 4.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN----EKkqiYAIKYVNLEEA--DNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQYI 598
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHavtgEK---VAIKVIDKKKAkkDSYVTKNLRRE-GRIQQMIRHPN-ITQLLDILETENSY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTT 676
Cdd:cd14070  79 YLVMElCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDnIKLIDFGLSNCAGILGY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSQVGTVNYMPPEAIkdmsSSRENGkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEF 756
Cdd:cd14070 159 SDPFSTQCGSPAYAAPELL----ARKKYG-------PKVDVWSIGVNMYAMLTGTLPFTVEPFSLRALHQKMVDKEMNPL 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 757 PDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14070 228 PTDLSPGAISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
525-791 4.39e-19

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: 87.93  E-value: 4.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGsskvFQVLNEKKQ-----IYAIKYVNLEEADNQTLDSYRNEI----AYLNKLQQHSdkIIRLYD-YEI- 593
Cdd:cd14105   7 YDIGEELGSGQ----FAVVKKCREkstglEYAAKFIKKRRSKASRRGVSREDIerevSILRQVLHPN--IITLHDvFENk 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQYIYMVMECGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG-----MLKLIDFGIA 668
Cdd:cd14105  81 TDVVLILELVAGG-ELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKnvpipRIKLIDFGLA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQMQPdttSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQiSKLHAII 748
Cdd:cd14105 160 HKIED---GNEFKNIFGTPEFVAPEIVNYEPLGLE-----------ADMWSIGVITYILLSGASPFLGDTKQ-ETLANIT 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 749 DPNHEI--EFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14105 225 AVNYDFddEYFSNTSELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
525-790 4.54e-19

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: 88.74  E-value: 4.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQhSDKIIRLYDYEITDQ----YIY 599
Cdd:cd07837   3 YEKLEKIGEGTYGKVYKARDKNTgKLVALKKTRLEMEEEGVPSTALREVSLLQMLSQ-SIYIVRLLDVEHVEEngkpLLY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDLNSWLK--KKKSIDPWER---KSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD--GMLKLIDFGIANQMQ 672
Cdd:cd07837  82 LVFEYLDTDLKKFIDsyGRGPHNPLPAktiQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKqkGLLKIADLGLGRAFT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSVVKdsQVGTVNYMPPEAIkdMSSSRengkskskISPKSDVWSLGCILYYMTY------GKTPFQQIInQISKLha 746
Cdd:cd07837 162 IPIKSYTH--EIVTLWYRAPEVL--LGSTH--------YSTPVDMWSVGCIFAEMSRkqplfpGDSELQQLL-HIFRL-- 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 747 IIDPNHEI-----------EFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07837 227 LGTPNEEVwpgvsklrdwhEYPQWKPQDLSravpdlepegvDLLTKMLAYDPAKRISAKAALQHPY 292
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
517-790 4.78e-19

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: 88.44  E-value: 4.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 517 CISVKGriYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLE-EADNQTLDSYRnEIAYLNKLQqHsDKIIRLYdyEI- 593
Cdd:cd07843   1 CRSVDE--YEKLNRIEEGTYGVVYRARDKKtGEIVALKKLKMEkEKEGFPITSLR-EINILLKLQ-H-PNIVTVK--EVv 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 ---TDQYIYMVMECGNIDLNSWLK-KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA 668
Cdd:cd07843  74 vgsNLDKIYMVMEYVEHDLKSLMEtMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNrGILKICDFGLA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQ----MQPDTTSVVkdsqvgTVNYMPPE---AIKDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPF--QQIIN 739
Cdd:cd07843 154 REygspLKPYTQLVV------TLWYRAPElllGAKEYSTA-------------IDMWSVGCIFAELLTKKPLFpgKSEID 214
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 740 QISKLHAII-DPNHEI-----EFPDIPEKDLQ---------------------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07843 215 QLNKIFKLLgTPTEKIwpgfsELPGAKKKTFTkypynqlrkkfpalslsdngfDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
525-798 4.82e-19

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: 88.00  E-value: 4.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEADNQTLD-SYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVM 602
Cdd:cd14117   8 FDIGRPLGKGKFGNVYLArEKQSKFIVALKVLFKSQIEKEGVEhQLRREIEIQSHLRHPN--ILRLYNYFHDRKRIYLIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECG-NIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQmqpdTTSVVK 680
Cdd:cd14117  86 EYApRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMgYKGELKIADFGWSVH----APSLRR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINqiSKLHAIIdPNHEIEFPDIP 760
Cdd:cd14117 162 RTMCGTLDYLPPEMIEGRTHDEK-----------VDLWCIGVLCYELLVGMPPFESASH--TETYRRI-VKVDLKFPPFL 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 761 EKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPV 798
Cdd:cd14117 228 SDGSRDLISKLLRYHPSERLPLKGVMEHPWVKANSRRV 265
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
525-793 7.21e-19

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: 87.37  E-value: 7.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEADNQTLDSYRNEIAY-LNKLQ--QHSDkIIRLYD-YEITDQYIY 599
Cdd:cd14195   7 YEMGEELGSGQFAIVRKCREKGTGKeYAAKFIKKRRLSSSRRGVSREEIEReVNILReiQHPN-IITLHDiFENKTDVVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG-----MLKLIDFGIANQMQPD 674
Cdd:cd14195  86 ILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKnvpnpRIKLIDFGIAHKIEAG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSvvkDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIID 749
Cdd:cd14195 166 NEF---KNIFGTPEFVAPEIVNYEPLGLE-----------ADMWSIGVITYILLSGASPFlgetkQETLTNISAVNYDFD 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 750 PNHeieFPDIPEKdLQDVLKCCLKRDPKQRISIPELLAHPYVQI 793
Cdd:cd14195 232 EEY---FSNTSEL-AKDFIRRLLVKDPKKRMTIAQSLEHSWIKA 271
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
520-791 8.16e-19

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: 87.44  E-value: 8.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 520 VKGRIysilkqIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQ--------TLDSYRNEIAYLNKLQQhsDKIIRLYD 590
Cdd:cd06629   4 VKGEL------IGKGTYGRVYLAMNaTTGEMLAVKQVELPKTSSDradsrqktVVDALKSEIDTLKDLDH--PNIVQYLG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 591 YEITDQYIYMVMEC---GNIdlNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFG 666
Cdd:cd06629  76 FEETEDYFSIFLEYvpgGSI--GSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVdLEGICKISDFG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 667 IANQMQPDTTSVVKDSQVGTVNYMPPEAIkdMSSSRENGKSKskispksDVWSLGCILYYMTYGKTPFqqiiNQISKLHA 746
Cdd:cd06629 154 ISKKSDDIYGNNGATSMQGSVFWMAPEVI--HSQGQGYSAKV-------DIWSLGCVVLEMLAGRRPW----SDDEAIAA 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 747 IIDPNHEIEFPDIPE-----KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06629 221 MFKLGNKRSAPPVPEdvnlsPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
525-793 1.18e-18

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: 87.47  E-value: 1.18e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLdsYRNEIAYLNklQQHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd06656  21 YTRFEKIGQGASGTVYTAIDiATGQEVAIKQMNLQQQPKKEL--IINEILVMR--ENKNPNIVNYLDSYLVGDELWVVME 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSvvKDS 682
Cdd:cd06656  97 YLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMDGSVKLTDFGFCAQITPEQSK--RST 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 QVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIiNQISKLHAI-IDPNHEIEFPDIPE 761
Cdd:cd06656 175 MVGTPYWMAPEVVTRKAYGPK-----------VDIWSLGIMAIEMVEGEPPYLNE-NPLRALYLIaTNGTPELQNPERLS 242
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 762 KDLQDVLKCCLKRDPKQRISIPELLAHPYVQI 793
Cdd:cd06656 243 AVFRDFLNRCLEMDVDRRGSAKELLQHPFLKL 274
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
525-793 1.27e-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: 87.47  E-value: 1.27e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLdsYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd06655  21 YTRYEKIGQGASGTVFTAIDVAtGQEVAIKQINLQKQPKKEL--IINEILVMKELK--NPNIVNFLDSFLVGDELFVVME 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSvvKDS 682
Cdd:cd06655  97 YLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLgMDGSVKLTDFGFCAQITPEQSK--RST 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 QVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIiNQISKLHAI-IDPNHEIEFPDIPE 761
Cdd:cd06655 175 MVGTPYWMAPEVVTRKAYGPK-----------VDIWSLGIMAIEMVEGEPPYLNE-NPLRALYLIaTNGTPELQNPEKLS 242
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 762 KDLQDVLKCCLKRDPKQRISIPELLAHPYVQI 793
Cdd:cd06655 243 PIFRDFLNRCLEMDVEKRGSAKELLQHPFLKL 274
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
525-790 1.40e-18

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: 86.94  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRNeiAYLNKLQQHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd07870   2 YLNLEKLGEGSYATVYKGISRiNGQLVALKVISMKTEEGVPFTAIRE--ASLLKGLKHAN-IVLLHDIIHTKETLTFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKS-IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQ-PDTTSvvk 680
Cdd:cd07870  79 YMHTDLAQYMIQHPGgLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYlGELKLADFGLARAKSiPSQTY--- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPF---QQIINQISKLHAIID----- 749
Cdd:cd07870 156 SSEVVTLWYRPPDVLlgaTDYSSA-------------LDIWGAGCIFIEMLQGQPAFpgvSDVFEQLEKIWTVLGvpted 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 750 --------PNHEIE-FPDIPEKDLQDVLK-------------CCLKRDPKQRISIPELLAHPY 790
Cdd:cd07870 223 twpgvsklPNYKPEwFLPCKPQQLRVVWKrlsrppkaedlasQMLMMFPKDRISAQDALLHPY 285
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
510-791 1.83e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 87.96  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  510 ASSSANECISVKGRIYSIL---KQIGSGGSSKVFQVLNEKK-QIYAIK--YVNLEeadnqtlDSYRN----EIAYLNKLQ 579
Cdd:PLN00034  58 SSSSASGSAPSAAKSLSELervNRIGSGAGGTVYKVIHRPTgRLYALKviYGNHE-------DTVRRqicrEIEILRDVN 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  580 qHSD--KIIRLYDYEITDQYIYMVMECGNIDlNSWLKKKKSIDPWERKsywknMLEAVHTIHQHGIVHSDLKPANFLIVD 657
Cdd:PLN00034 131 -HPNvvKCHDMFDHNGEIQVLLEFMDGGSLE-GTHIADEQFLADVARQ-----ILSGIAYLHRRHIVHRDIKPSNLLINS 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  658 GM-LKLIDFGI----ANQMQPdttsvvKDSQVGTVNYMPPEAIK-DMSSSRENGKSKskispksDVWSLG-CIL-YYMty 729
Cdd:PLN00034 204 AKnVKIADFGVsrilAQTMDP------CNSSVGTIAYMSPERINtDLNHGAYDGYAG-------DIWSLGvSILeFYL-- 268
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722  730 GKTPF---QQiiNQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:PLN00034 269 GRFPFgvgRQ--GDWASLMCAICMSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFI 331
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
525-734 1.98e-18

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: 85.72  E-value: 1.98e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQtldSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME 603
Cdd:cd14108   4 YDIHKEIGRGAFSYLRRVKEKSsDLSFAAKFIPVRAKKKT---SARRELALLAELDH--KSIVRFHDAFEKRRVVIIVTE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG---MLKLIDFGIANQMQPDTTSVVK 680
Cdd:cd14108  79 LCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQktdQVRICDFGNAQELTPNEPQYCK 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23308722 681 dsqVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF 734
Cdd:cd14108 159 ---YGTPEFVAPEIVNQSPVSK-----------VTDIWPVGVIAYLCLTGISPF 198
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
527-786 2.02e-18

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: 86.18  E-value: 2.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQV-LNEKKQIYAIK--YVNleeaDNQTLDSYRNEIAYLNKLQQHSDkIIRLYDYEIT----DQY-I 598
Cdd:cd14037   7 IEKYLAEGGFAHVYLVkTSNGGNRAALKrvYVN----DEHDLNVCKREIEIMKRLSGHKN-IVGYIDSSANrsgnGVYeV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMEC----GNIDL-NSWLKKKKSIDpwERKSYWKNMLEAVHTIH--QHGIVHSDLKPANFLIVD-GMLKLIDFG---- 666
Cdd:cd14037  82 LLLMEYckggGVIDLmNQRLQTGLTES--EILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDsGNYKLCDFGsatt 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 667 -IANQMQPDTTSVVKD--SQVGTVNYMPPEAIKDMSSsrengkskSKISPKSDVWSLGCILYYMTYGKTPFQQiinqiSK 743
Cdd:cd14037 160 kILPPQTKQGVTYVEEdiKKYTTLQYRAPEMIDLYRG--------KPITEKSDIWALGCLLYKLCFYTTPFEE-----SG 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 744 LHAIIDPNHeiEFPDIPE--KDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14037 227 QLAILNGNF--TFPDNSRysKRLHKLIRYMLEEDPEKRPNIYQVS 269
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
525-788 3.41e-18

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: 85.39  E-value: 3.41e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKyVNLEEADNQTLdsyRNEIAYLNKLQQhSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd14017   2 WKVVKKIGGGGFGEIYKVRDVvDGEEVAMK-VESKSQPKQVL---KMEVAVLKKLQG-KPHFCRLIGCGRTERYNYIVMT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CG-NI-DLNSWLKKKK-SIDPWERKSywKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLK-----LIDFGIANQMQPD 674
Cdd:cd14017  77 lLGpNLaELRRSQPRGKfSVSTTLRLG--IQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDertvyILDFGLARQYTNK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKDSQ-----VGTVNYMPPEAikdmSSSRENGkskskisPKSDVWSlgciLYYMTygktpfqqiinqisklhaiid 749
Cdd:cd14017 155 DGEVERPPRnaagfRGTVRYASVNA----HRNKEQG-------RRDDLWS----WFYML--------------------- 198
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 750 pnheIEF-----PDIPEKDLQDVLKCclkrdpKQRISIPELLAH 788
Cdd:cd14017 199 ----IEFvtgqlPWRKLKDKEEVGKM------KEKIDHEELLKG 232
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
523-792 4.20e-18

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: 84.81  E-value: 4.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLeeADNQTLDSYRN---EIAYLNKLQqHSDkIIRLYDYEITDQYI 598
Cdd:cd06607   1 KIFEDLREIGHGSFGAVYYARNKRtSEVVAIKKMSY--SGKQSTEKWQDiikEVKFLRQLR-HPN-TIEYKGCYLREHTA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME-C-GN----IDLNswlkkKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQM 671
Cdd:cd06607  77 WLVMEyClGSasdiVEVH-----KKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEpGTVKLADFGSASLV 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QPDTtsvvkdSQVGTVNYMPPEAIKDMSSSRENGKSkskispksDVWSLGCILYYMTYGKTPFQQIiNQISKLHAII--D 749
Cdd:cd06607 152 CPAN------SFVGTPYWMAPEVILAMDEGQYDGKV--------DVWSLGITCIELAERKPPLFNM-NAMSALYHIAqnD 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23308722 750 PnheiefPDIPEKDLQDVLK----CCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06607 217 S------PTLSSGEWSDDFRnfvdSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
525-791 4.97e-18

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: 84.89  E-value: 4.97e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVnleEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd14087   3 YDIKALIGRGSFSRVVRVEHRvTRQPYAIKMI---ETKCRGREVCESELNVLRRVR-HTN-IIQLIEVFETKERVYMVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI----VDGMLKLIDFGIANQMQPDTTSV 678
Cdd:cd14087  78 LATGgELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpgPDSKIMITDFGLASTRKKGPNCL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSqVGTVNYMPPEAIkdmsssrengkSKSKISPKSDVWSLGCILYYMTYGKTPFQ-----QIINQISKLHAIIDPNHe 753
Cdd:cd14087 158 MKTT-CGTPEYIAPEIL-----------LRKPYTQSVDMWAVGVIAYILLSGTMPFDddnrtRLYRQILRAKYSYSGEP- 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 754 ieFPDIPE--KDLQDVLkccLKRDPKQRISIPELLAHPYV 791
Cdd:cd14087 225 --WPSVSNlaKDFIDRL---LTVNPGERLSATQALKHPWI 259
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
523-790 5.10e-18

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: 86.49  E-value: 5.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLE-EADNQTLDSYRnEIAYLNKLQQhsDKIIRLYDYEITD----- 595
Cdd:cd07879  15 ERYTSLKQVGSGAYGSVCSAIDKRtGEKVAIKKLSRPfQSEIFAKRAYR-ELTLLKHMQH--ENVIGLLDVFTSAvsgde 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 -QYIYMVMECGNIDLNSWLKKKKSIDPWERKSYwkNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQP 673
Cdd:cd07879  92 fQDFYLVMPYMQTDLQKIMGHPLSEDKVQYLVY--QMLCGLKYIHSAGIIHRDLKPGNLAVnEDCELKILDFGLARHADA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKdsqvgTVNYMPPEAIKDMSSSRENgkskskispkSDVWSLGCILYYMTYGKTPFQ---------QIINQ---- 740
Cdd:cd07879 170 EMTGYVV-----TRWYRAPEVILNWMHYNQT----------VDIWSVGCIMAEMLTGKTLFKgkdyldqltQILKVtgvp 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 741 ----ISKLHAIIDPNHEIEFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07879 235 gpefVQKLEDKAAKSYIKSLPKYPRKDFStlfpkaspqavDLLEKMLELDVDKRLTATEALEHPY 299
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
525-788 5.14e-18

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: 85.31  E-value: 5.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLeeADNqtlDSYRN----EIAYLNKLQQHSdkIIRLYDY-------- 591
Cdd:cd14048   8 FEPIQCLGRGGFGVVFEAKNKVDDCnYAVKRIRL--PNN---ELAREkvlrEVRALAKLDHPG--IVRYFNAwlerppeg 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 592 ---EITDQYIYMVME-CGNIDLNSWLKKKKSIDPWER---KSYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLI 663
Cdd:cd14048  81 wqeKMDEVYLYIQMQlCRKENLKDWMNRRCTMESRELfvcLNIFKQIASAVEYLHSKGLIHRDLKPSNvFFSLDDVVKVG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 664 DFGIANQM----------QPDTTSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYgktP 733
Cdd:cd14048 161 DFGLVTAMdqgepeqtvlTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEK-----------VDIFALGLILFELIY---S 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 734 FQqiiNQISKLHAIIDPnHEIEFPDI-----PEKdlQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd14048 227 FS---TQMERIRTLTDV-RKLKFPALftnkyPEE--RDMVQQMLSPSPSERPEAHEVIEH 280
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
525-790 5.97e-18

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: 85.67  E-value: 5.97e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQ----VLNEKKQIYAIKYVNLEEadnqtldsYRNEIAYLNKLQQHSDkIIRLYD---YEITDQY 597
Cdd:cd14132  20 YEIIRKIGRGKYSEVFEginiGNNEKVVIKVLKPVKKKK--------IKREIKILQNLRGGPN-IVKLLDvvkDPQSKTP 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IyMVMEcgNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIvD---GMLKLIDFGIANQMQPD 674
Cdd:cd14132  91 S-LIFE--YVNNTDFKTLYPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI-DhekRKLRLIDWGLAEFYHPG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKdsqVGTVNYMPPEAIKDMsssrengkskSKISPKSDVWSLGCILYYMTYGKTPF-------------------Q 735
Cdd:cd14132 167 QEYNVR---VASRYYKGPELLVDY----------QYYDYSLDMWSLGCMLASMIFRKEPFfhghdnydqlvkiakvlgtD 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 736 QIINQISKLHAIIDPNHEIEFPDIPEKDLQ----------------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14132 234 DLYAYLDKYGIELPPRLNDILGRHSKKPWErfvnsenqhlvtpealDLLDKLLRYDHQERITAKEAMQHPY 304
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
525-791 6.80e-18

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: 84.56  E-value: 6.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNL-EEADNQTLdsyRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd14114   4 YDILEELGTGAFGVVHRCTERATgNNFAAKFIMTpHESDKETV---RKEIQIMNQL--HHPKLINLHDAFEDDNEMVLIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E--CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV---DGMLKLIDFGIANQMQPDttS 677
Cdd:cd14114  79 EflSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkrSNEVKLIDFGLATHLDPK--E 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSqVGTVNYMPPEAIkdmssSREngksksKISPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIIDpnh 752
Cdd:cd14114 157 SVKVT-TGTAEFAAPEIV-----ERE------PVGFYTDMWAVGVLSYVLLSGLSPFagendDETLRNVKSCDWNFD--- 221
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 753 EIEFPDIPEkDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14114 222 DSAFSGISE-EAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
525-790 7.84e-18

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: 85.08  E-value: 7.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK--QIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQ--QHSDkIIRLYDY---EITDQ- 596
Cdd:cd07862   3 YECVAEIGEGAYGKVFKARDLKNggRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfEHPN-VVRLFDVctvSRTDRe 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 -YIYMVMECGNIDLNSWLKK--KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIAN--Q 670
Cdd:cd07862  82 tKLTLVFEHVDQDLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSsGQIKLADFGLARiyS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MQPDTTSVVKdsqvgTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQ--QIINQISKLHAII 748
Cdd:cd07862 162 FQMALTSVVV-----TLWYRAPEVLLQSSYA-----------TPVDLWSVGCIFAEMFRRKPLFRgsSDVDQLGKILDVI 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 749 D---------------------PNHEIE--FPDIPEKDlQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07862 226 GlpgeedwprdvalprqafhskSAQPIEkfVTDIDELG-KDLLLKCLTFNPAKRISAYSALSHPY 289
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
520-790 8.67e-18

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 85.77  E-value: 8.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 520 VKGRiYSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLE-EADNQTLDSYRnEIAYLNKLQQhsDKIIRLYDYEITDQY 597
Cdd:cd07880  13 VPDR-YRDLKQVGSGAYGTVCSALDRRTGAkVAIKKLYRPfQSELFAKRAYR-ELRLLKHMKH--ENVIGLLDVFTPDLS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 I------YMVMECGNIDLNSWLKKKKSIDpwERKSYW-KNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIAN 669
Cdd:cd07880  89 LdrfhdfYLVMPFMGTDLGKLMKHEKLSE--DRIQFLvYQMLKGLKYIHAAGIIHRDLKPGNLAVnEDCELKILDFGLAR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMQPDTTSVVKdsqvgTVNYMPPEAIKDMSSSRENgkskskispkSDVWSLGCILYYMTYGKTPFQ--QIINQ------- 740
Cdd:cd07880 167 QTDSEMTGYVV-----TRWYRAPEVILNWMHYTQT----------VDIWSVGCIMAEMLTGKPLFKghDHLDQlmeimkv 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 741 --------ISKLHAIIDPNHEIEFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07880 232 tgtpskefVQKLQSEDAKNYVKKLPRFRKKDFRsllpnanplavNVLEKMLVLDAESRITAAEALAHPY 300
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
519-797 1.26e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 85.20  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  519 SVKGRIYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEADNQTLDSYRN------------EIAYLNKLqqHSDKI 585
Cdd:PTZ00024   5 SISERYIQKGAHLGEGTYGKVEKAYDTLtGKIVAIKKVKIIEISNDVTKDRQLvgmcgihfttlrELKIMNEI--KHENI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  586 IRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLID 664
Cdd:PTZ00024  83 MGLVDVYVEGDFINLVMDIMASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSkGICKIAD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  665 FGIA----NQMQPDTTSVVKDSQ--------VGTVNYMPPEAIkdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKT 732
Cdd:PTZ00024 163 FGLArrygYPPYSDTLSKDETMQrreemtskVVTLWYRAPELL--MGAEKYH--------FAVDMWSVGCIFAELLTGKP 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  733 --PFQQIINQISKLHAIIDPNHEIEFPDIPE------------KDLQDVLKCC-----------LKRDPKQRISIPELLA 787
Cdd:PTZ00024 233 lfPGENEIDQLGRIFELLGTPNEDNWPQAKKlplyteftprkpKDLKTIFPNAsddaidllqslLKLNPLERISAKEALK 312
                        330
                 ....*....|
gi 23308722  788 HPYVQIQTHP 797
Cdd:PTZ00024 313 HEYFKSDPLP 322
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
525-793 1.30e-17

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: 85.16  E-value: 1.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIK-----YVNLEEADNqtldSYRNEIayLNKLQQHSDkIIRLYDYEITD--- 595
Cdd:cd07850   2 YQNLKPIGSGAQGIVCAAYDTVtGQNVAIKklsrpFQNVTHAKR----AYRELV--LMKLVNHKN-IIGLLNVFTPQksl 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 ---QYIYMVME------CG--NIDLNSwlkkkksidpwERKSYW-KNMLEAVHTIHQHGIVHSDLKPANflIV---DGML 660
Cdd:cd07850  75 eefQDVYLVMElmdanlCQviQMDLDH-----------ERMSYLlYQMLCGIKHLHSAGIIHRDLKPSN--IVvksDCTL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 661 KLIDFGIAnqmQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSrENgkskskispkSDVWSLGCILYYMTYGKTPFQ----- 735
Cdd:cd07850 142 KILDFGLA---RTAGTSFMMTPYVVTRYYRAPEVILGMGYK-EN----------VDIWSVGCIMGEMIRGTVLFPgtdhi 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 736 ----QIINQ--------ISKLHAIID------PNH-----EIEFPDI---PEKDL---------QDVLKCCLKRDPKQRI 780
Cdd:cd07850 208 dqwnKIIEQlgtpsdefMSRLQPTVRnyvenrPKYagysfEELFPDVlfpPDSEEhnklkasqaRDLLSKMLVIDPEKRI 287
                       330
                ....*....|...
gi 23308722 781 SIPELLAHPYVQI 793
Cdd:cd07850 288 SVDDALQHPYINV 300
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
531-790 1.35e-17

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 84.12  E-value: 1.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVF--QVLNEKKqIYAIKYVN---LEEADNQTLDsyRNEIAYLNKLqqHSDKIIRL-YDYEITDQ--YIYMVM 602
Cdd:cd05577   1 LGRGGFGEVCacQVKATGK-MYACKKLDkkrIKKKKGETMA--LNEKIILEKV--SSPFIVSLaYAFETKDKlcLVLTLM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSvvkD 681
Cdd:cd05577  76 NGGDLKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDhGHVRISDLGLAVEFKGGKKI---K 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIKDmsssrengksKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKlHAI--IDPNHEIEFPDI 759
Cdd:cd05577 153 GRVGTHGYMAPEVLQK----------EVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDK-EELkrRTLEMAVEYPDS 221
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 760 PEKDLQDVLKCCLKRDPKQRI-----SIPELLAHPY 790
Cdd:cd05577 222 FSPEARSLCEGLLQKDPERRLgcrggSADEVKEHPF 257
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
523-789 1.61e-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: 83.92  E-value: 1.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILkqiGSGGSSKVF--QVLNEKKqIYAIKyvnleEADNQTLDSYRNEIAYLNKLQ----QHSDKIIRL-YDYEITD 595
Cdd:cd05630   3 RQYRVL---GKGGFGEVCacQVRATGK-MYACK-----KLEKKRIKKRKGEAMALNEKQilekVNSRFVVSLaYAYETKD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QY--IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQ 672
Cdd:cd05630  74 ALclVLTLMNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDhGHIRISDLGLAVHVP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTsvVKdSQVGTVNYMPPEAIKDmsssrengkskSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISK--LHAIIDP 750
Cdd:cd05630 154 EGQT--IK-GRVGTVGYMAPEVVKN-----------ERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKReeVERLVKE 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 751 NHEiEFPDIPEKDLQDVLKCCLKRDPKQRI-----SIPELLAHP 789
Cdd:cd05630 220 VPE-EYSEKFSPQARSLCSMLLCKDPAERLgcrggGAREVKEHP 262
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
525-791 1.70e-17

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: 84.69  E-value: 1.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEADNQtldsyrNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd14176  21 YEVKEDIGVGSYSVCKRCIHKATNMeFAVKIIDKSKRDPT------EEIEILLRYGQHPN-IITLKDVYDDGKYVYVVTE 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 C--GNIDLNSWLKKKkSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-----GMLKLIDFGIANQMQPDTT 676
Cdd:cd14176  94 LmkGGELLDKILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDesgnpESIRICDFGFAKQLRAENG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVkdSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF--------QQIINQISKLHAII 748
Cdd:cd14176 173 LLM--TPCYTANFVAPEVLERQGYD-----------AACDIWSLGVLLYTMLTGYTPFangpddtpEEILARIGSGKFSL 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 749 DPNHEIEFPDipekDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14176 240 SGGYWNSVSD----TAKDLVSKMLHVDPHQRLTAALVLRHPWI 278
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
525-791 1.76e-17

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: 83.30  E-value: 1.76e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVF------QVLNEKKQIYAIKYV---NLEEADnQTLDSYRnEIAYLNKLQqHSDkIIRLYDYEITD 595
Cdd:cd14076   3 YILGRTLGEGEFGKVKlgwplpKANHRSGVQVAIKLIrrdTQQENC-QTSKIMR-EINILKGLT-HPN-IVRLLDVLKTK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIvDGMLKLI--DFGIANQMQ 672
Cdd:cd14076  79 KYIGIVLEfVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLL-DKNRNLVitDFGFANTFD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSVVKDSqVGTVNYMPPEAIkdMSSSRENGKSKskispksDVWSLGCILYYMTYGKTPFQQ-----IINQISKLHAI 747
Cdd:cd14076 158 HFNGDLMSTS-CGSPCYAAPELV--VSDSMYAGRKA-------DIWSCGVILYAMLAGYLPFDDdphnpNGDNVPRLYRY 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 748 IdPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14076 228 I-CNTPLIFPEYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
525-790 2.31e-17

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: 83.96  E-value: 2.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLE-EADNQTLDSYRnEIAYLNKLQQhsDKIIRLYdyEI-------TD 595
Cdd:cd07865  14 YEKLAKIGQGTFGEVFKARHRKtGQIVALKKVLMEnEKEGFPITALR-EIKILQLLKH--ENVVNLI--EIcrtkatpYN 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QY---IYMVMECGNIDLNSWLKKKK-SIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANq 670
Cdd:cd07865  89 RYkgsIYLVFEFCEHDLAGLLSNKNvKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITkDGVLKLADFGLAR- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 mqpdTTSVVKDSQ-------VGTVNYMPPEAikdMSSSRENGkskskisPKSDVWSLGCILYYMtYGKTPF------QQI 737
Cdd:cd07865 168 ----AFSLAKNSQpnrytnrVVTLWYRPPEL---LLGERDYG-------PPIDMWGAGCIMAEM-WTRSPImqgnteQHQ 232
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 738 INQISKLHAIIDPN-----------HEIEFPDIPEKDLQDVLKCCLKR-------------DPKQRISIPELLAHPY 790
Cdd:cd07865 233 LTLISQLCGSITPEvwpgvdklelfKKMELPQGQKRKVKERLKPYVKDpyaldlidkllvlDPAKRIDADTALNHDF 309
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
531-788 2.69e-17

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: 82.16  E-value: 2.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIyAIKYVNlEEADNqtldsyrnEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVME-CGNIDL 609
Cdd:cd14059   1 LGSGAQGAVFLGKFRGEEV-AVKKVR-DEKET--------DIKHLRKLN-HPN-IIKFKGVCTQAPCYCILMEyCPYGQL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 610 NSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTsvvKDSQVGTVN 688
Cdd:cd14059  69 YEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVtYNDVLKISDFGTSKELSEKST---KMSFAGTVA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 689 YMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQisklhAII----DPNHEIEFPDIPEKDL 764
Cdd:cd14059 146 WMAPEVIRNEPCSEK-----------VDIWSFGVVLWELLTGEIPYKDVDSS-----AIIwgvgSNSLQLPVPSTCPDGF 209
                       250       260
                ....*....|....*....|....
gi 23308722 765 QDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd14059 210 KLLMKQCWNSKPRNRPSFRQILMH 233
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
525-793 3.34e-17

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 83.24  E-value: 3.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLdsYRNEIAYLNklQQHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd06654  22 YTRFEKIGQGASGTVYTAMDvATGQEVAIRQMNLQQQPKKEL--IINEILVMR--ENKNPNIVNYLDSYLVGDELWVVME 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSvvKDS 682
Cdd:cd06654  98 YLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLgMDGSVKLTDFGFCAQITPEQSK--RST 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 QVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIiNQISKLHAI-IDPNHEIEFPDIPE 761
Cdd:cd06654 176 MVGTPYWMAPEVVTRKAYGPK-----------VDIWSLGIMAIEMIEGEPPYLNE-NPLRALYLIaTNGTPELQNPEKLS 243
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 762 KDLQDVLKCCLKRDPKQRISIPELLAHPYVQI 793
Cdd:cd06654 244 AIFRDFLNRCLEMDVEKRGSAKELLQHQFLKI 275
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
598-796 3.37e-17

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: 83.95  E-value: 3.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKnMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTT 676
Cdd:cd07878  95 VYLVTNLMGADLNNIVKCQKLSDEHVQFLIYQ-LLRGLKYIHSAGIIHRDLKPSNVAVnEDCELRILDFGLARQADDEMT 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVvkdsqVGTVNYMPPEAIKDMSSSRENgkskskispkSDVWSLGCILYYMTYGKT--PFQQIINQISKLHAII-DPNHE 753
Cdd:cd07878 174 GY-----VATRWYRAPEIMLNWMHYNQT----------VDIWSVGCIMAELLKGKAlfPGNDYIDQLKRIMEVVgTPSPE 238
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 754 I--------------EFPDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPYVqIQTH 796
Cdd:cd07878 239 VlkkisseharkyiqSLPHMPQQDLKkifrganplaiDLLEKMLVLDSDKRISASEALAHPYF-SQYH 305
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
525-792 3.90e-17

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: 82.45  E-value: 3.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNleeadNQTLdSYRNEI--AYLNK-LQQHSDK--IIRLYDYEITDQYI 598
Cdd:cd05609   2 FETIKLISNGAYGAVYLVRHrETRQRFAMKKIN-----KQNL-ILRNQIqqVFVERdILTFAENpfVVSMYCSFETKRHL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA-------- 668
Cdd:cd05609  76 CMVMEyVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSmGHIKLTDFGLSkiglmslt 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 -----NQMQPDTTSVVkDSQV-GTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQI 737
Cdd:cd05609 156 tnlyeGHIEKDTREFL-DKQVcGTPEYIAPEVILRQGYGKP-----------VDWWAMGIILYEFLVGCVPFfgdtpEEL 223
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 738 INQISklhaiidpNHEIEFP---DIPEKDLQDVLKCCLKRDPKQRI---SIPELLAHPYVQ 792
Cdd:cd05609 224 FGQVI--------SDEIEWPegdDALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQ 276
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
525-790 4.04e-17

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: 83.38  E-value: 4.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYVnleeadnQTLDSYRN----EIAYLNKLQQHsDK-----IIRLYDYEIT 594
Cdd:cd14134  14 YKILRLLGEGTFGKVLECWdRKRKRYVAVKII-------RNVEKYREaakiEIDVLETLAEK-DPngkshCVQLRDWFDY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 595 DQYIYMVME-CGnIDLNSWLKKKKSIdPWERK---SYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG------------ 658
Cdd:cd14134  86 RGHMCIVFElLG-PSLYDFLKKNNYG-PFPLEhvqHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSdyvkvynpkkkr 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 659 --------MLKLIDFGIANQMQPDTTSVVKdsqvgTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYG 730
Cdd:cd14134 164 qirvpkstDIKLIDFGSATFDDEYHSSIVS-----TRHYRAPEVILGLGWSY-----------PCDVWSIGCILVELYTG 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 731 KTPFQ------------QIINQISKL-------------------------------HAIIDPNHEIEFPDIPEKD-LQD 766
Cdd:cd14134 228 ELLFQthdnlehlammeRILGPLPKRmirrakkgakyfyfyhgrldwpegsssgrsiKRVCKPLKRLMLLVDPEHRlLFD 307
                       330       340
                ....*....|....*....|....
gi 23308722 767 VLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14134 308 LIRKMLEYDPSKRITAKEALKHPF 331
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
523-798 4.83e-17

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: 82.35  E-value: 4.83e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILkqiGSGGSSKVF--QVLNEKKqIYAIKYVNLEEADNQTLDSYR-NEIAYLNKLQqhSDKIIRL-YDYEITDQY- 597
Cdd:cd05631   3 RHYRVL---GKGGFGEVCacQVRATGK-MYACKKLEKKRIKKRKGEAMAlNEKRILEKVN--SRFVVSLaYAYETKDALc 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 -IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMqPDT 675
Cdd:cd05631  77 lVLTIMNGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDrGHIRISDLGLAVQI-PEG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVvkDSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHaiID---PNH 752
Cdd:cd05631 156 ETV--RGRVGTVGYMAPEVINNEKYT-----------FSPDWWGLGCLIYEMIQGQSPFRKRKERVKREE--VDrrvKED 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 753 EIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAhpyVQIQTHPV 798
Cdd:cd05631 221 QEEYSEKFSEDAKSICRMLLTKNPKERLGCRGNGA---AGVKQHPI 263
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
516-798 4.93e-17

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: 82.80  E-value: 4.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 516 ECISVKGriYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLE-EADNQTLDSYRnEIAYLnkLQQHSDKIIRLYDYEI 593
Cdd:cd07845   2 RCRSVTE--FEKLNRIGEGTYGIVYRARDTTsGEIVALKKVRMDnERDGIPISSLR-EITLL--LNLRHPNIVELKEVVV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQY--IYMVMECGNIDLNSWLKKKKSidPW---ERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGI 667
Cdd:cd07845  77 GKHLdsIFLVMEYCEQDLASLLDNMPT--PFsesQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDkGCLKIADFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 668 A----NQMQPDTTSVVkdsqvgTVNYMPPEAIKDMSSSREngkskskispKSDVWSLGCILYYMTYGKtPFQQIINQISK 743
Cdd:cd07845 155 ArtygLPAKPMTPKVV------TLWYRAPELLLGCTTYTT----------AIDMWAVGCILAELLAHK-PLLPGKSEIEQ 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 744 LHAIID----PNHEI-------------------------EFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPYVQIQ 794
Cdd:cd07845 218 LDLIIQllgtPNESIwpgfsdlplvgkftlpkqpynnlkhKFPWLSEAGL-RLLNFLLMYDPKKRATAEEALESSYFKEK 296

                ....
gi 23308722 795 THPV 798
Cdd:cd07845 297 PLPC 300
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
523-792 5.93e-17

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: 82.78  E-value: 5.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNE-KKQIYAIKyvNLEEADNQTLDSYRNEIAYLNKLQQ--HSDKIirlyDYE---ITDQ 596
Cdd:cd06633  21 EIFVDLHEIGHGSFGAVYFATNShTNEVVAIK--KMSYSGKQTNEKWQDIIKEVKFLQQlkHPNTI----EYKgcyLKDH 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPd 674
Cdd:cd06633  95 TAWLVMEyCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEpGQVKLADFGSASIASP- 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 ttsvvKDSQVGTVNYMPPEAIKDMSSSRENGkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIdpnhEI 754
Cdd:cd06633 174 -----ANSFVGTPYWMAPEVILAMDEGQYDG--------KVDIWSLGITCIELAERKPPLFN-MNAMSALYHIA----QN 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 755 EFPDIPEKDLQDVLKC----CLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06633 236 DSPTLQSNEWTDSFRGfvdyCLQKIPQERPSSAELLRHDFVR 277
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
525-734 6.02e-17

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: 81.41  E-value: 6.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKV---FQVLNEKKqiYAIKYVNLEEADNQTLDSYRNEIAYLnKLQQHSDkIIRLYDYEITDQYIYMV 601
Cdd:cd14072   2 YRLLKTIGKGNFAKVklaRHVLTGRE--VAIKIIDKTQLNPSSLQKLFREVRIM-KILNHPN-IVKLFEVIETEKTLYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSvv 679
Cdd:cd14072  78 MEYASGgEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMnIKIADFGFSNEFTPGNKL-- 155
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 680 kDSQVGTVNYMPPEAIKdmsSSRENGKSKskispksDVWSLGCILYYMTYGKTPF 734
Cdd:cd14072 156 -DTFCGSPPYAAPELFQ---GKKYDGPEV-------DVWSLGVILYTLVSGSLPF 199
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
581-791 6.80e-17

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: 81.41  E-value: 6.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 581 HSDKIIRLYDYEITDQYIYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DG 658
Cdd:cd14111  57 HHERIMALHEAYITPRYLVLIAEfCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTnLN 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 659 MLKLIDFGIANQMQPDTTSVvKDSQVGTVNYMPPEAIK-DMSSSrengkskskispKSDVWSLGCILYYMTYGKTPF--- 734
Cdd:cd14111 137 AIKIVDFGSAQSFNPLSLRQ-LGRRTGTLEYMAPEMVKgEPVGP------------PADIWSIGVLTYIMLSGRSPFedq 203
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 735 --QQIINQIskLHAIIDPNHeiEFPDIpEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14111 204 dpQETEAKI--LVAKFDAFK--LYPNV-SQSASLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
525-791 7.31e-17

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 81.98  E-value: 7.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVN-LEEADNQTLDSYRneiaYLNKLQQHSDkIIRLY------DYEITDQ 596
Cdd:cd06638  20 WEIIETIGKGTYGKVFKVLNKKNgSKAAVKILDpIHDIDEEIEAEYN----ILKALSDHPN-VVKFYgmyykkDVKNGDQ 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 yIYMVMECGN----IDL-NSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ 670
Cdd:cd06638  95 -LWLVLELCNggsvTDLvKGFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLtTEGGVKLVDFGVSAQ 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 MQpdTTSVVKDSQVGTVNYMPPEAI---KDMSSSREngkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAI 747
Cdd:cd06638 174 LT--STRLRRNTSVGTPFWMAPEVIaceQQLDSTYD---------ARCDVWSLGITAIELGDGDPPLADLHPMRALFKIP 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 748 IDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06638 243 RNPPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
525-790 7.93e-17

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: 83.53  E-value: 7.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSG--GSSKVFQVLNEKKqIYAIKYVN----LEEADNQTLDSYRNEIaylnkLQQHSDKIIRLYDYEITDQYI 598
Cdd:cd05623  74 FEILKVIGRGafGEVAVVKLKNADK-VFAMKILNkwemLKRAETACFREERDVL-----VNGDSQWITTLHYAFQDDNNL 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME--CGNiDLNSWLKKKKSIDPWE-RKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPD 674
Cdd:cd05623 148 YLVMDyyVGG-DLLTLLSKFEDRLPEDmARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMdMNGHIRLADFGSCLKLMED 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTsVVKDSQVGTVNYMPPEAIKDMSSSRengkskSKISPKSDVWSLGCILYYMTYGKTPF--QQIINQISKlhaIIDPNH 752
Cdd:cd05623 227 GT-VQSSVAVGTPDYISPEILQAMEDGK------GKYGPECDWWSLGVCMYEMLYGETPFyaESLVETYGK---IMNHKE 296
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 753 EIEFP----DIPE--KDLQDVLKCCLKRDPKQRiSIPELLAHPY 790
Cdd:cd05623 297 RFQFPtqvtDVSEnaKDLIRRLICSREHRLGQN-GIEDFKNHPF 339
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
521-790 8.28e-17

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: 81.98  E-value: 8.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 521 KGRIYSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRnEIAYLNKLQqHSDkIIRLYDYEITDQYIY 599
Cdd:cd07871   3 KLETYVKLDKLGEGTYATVFKGRSKlTENLVALKEIRLEHEEGAPCTAIR-EVSLLKNLK-HAN-IVTLHDIIHTERCLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDLNSWLKKKKSIDPWER-KSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTS 677
Cdd:cd07871  80 LVFEYLDSDLKQYLDNCGNLMSMHNvKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEkGELKLADFGLARAKSVPTKT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VvkDSQVGTVNYMPPEAIkdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQiSKLHAI---------- 747
Cdd:cd07871 160 Y--SNEVVTLWYRPPDVL--LGSTEYS--------TPIDMWGVGCILYEMATGRPMFPGSTVK-EELHLIfrllgtptee 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 748 ----IDPNHEIE---FPD---------IPEKDLQ--DVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07871 227 twpgVTSNEEFRsylFPQyraqplinhAPRLDTDgiDLLSSLLLYETKSRISAEAALRHSY 287
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
523-810 8.60e-17

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: 82.02  E-value: 8.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVfqVLNEKK---QIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIY 599
Cdd:cd14168  10 KIFEFKEVLGTGAFSEV--VLAEERatgKLFAVKCIP-KKALKGKESSIENEIAVLRKIKH--ENIVALEDIYESPNHLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD----GMLKLIDFGIANQmqpD 674
Cdd:cd14168  85 LVMQlVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSqdeeSKIMISDFGLSKM---E 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEI 754
Cdd:cd14168 162 GKGDVMSTACGTPGYVAPEVLAQKPYSK-----------AVDCWSIGVIAYILLCGYPPFYD-ENDSKLFEQILKADYEF 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 755 EFP--DIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMK 810
Cdd:cd14168 230 DSPywDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAGDTALCKNIHESVSAQIR 287
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
525-780 1.02e-16

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: 81.71  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLEEA-DNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVM 602
Cdd:cd05612   3 FERIKTIGTGTFGRVHLVRDRIsEHYYALKVMAIPEViRLKQEQHVHNEKRVLKEVSHPF--IIRLFWTEHDQRFLYMLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVv 679
Cdd:cd05612  81 EyvPGG-ELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLdKEGHIKLTDFGFAKKLRDRTWTL- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 kdsqVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDpnHEIEFP-- 757
Cdd:cd05612 159 ----CGTPEYLAPEVIQSKGHNK-----------AVDWWALGILIYEMLVGYPPFFD-DNPFGIYEKILA--GKLEFPrh 220
                       250       260
                ....*....|....*....|....
gi 23308722 758 -DIPEKDLqdvLKCCLKRDPKQRI 780
Cdd:cd05612 221 lDLYAKDL---IKKLLVVDRTRRL 241
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
529-791 1.13e-16

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: 80.95  E-value: 1.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGgSSKVFQVLNEKK--QIYAIKYVNLEEADNQTLdsYRNEIAYLNklQQHSDKIIRLYDYEITDQYIYMVMECGN 606
Cdd:cd06648  13 VKIGEG-STGIVCIATDKStgRQVAVKKMDLRKQQRREL--LFNEVVIMR--DYQHPNIVEMYSSYLVGDELWVVMEFLE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSvvKDSQVG 685
Cdd:cd06648  88 GGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTsDGRVKLSDFGFCAQVSKEVPR--RKSLVG 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 686 TVNYMPPEAIkdmssSREngksksKISPKSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAIIDPNheIEFPDIPEKD 763
Cdd:cd06648 166 TPYWMAPEVI-----SRL------PYGTEVDIWSLGIMVIEMVDGEPPYfnEPPLQAMKRIRDNEPPK--LKNLHKVSPR 232
                       250       260
                ....*....|....*....|....*...
gi 23308722 764 LQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06648 233 LRSFLDRMLVRDPAQRATAAELLNHPFL 260
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
525-792 1.14e-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: 81.59  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL----NEKKQIYAIKYVN----LEEAdnQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEiTDQ 596
Cdd:cd05613   2 FELLKVLGTGAYGKVFLVRkvsgHDAGKLYAMKVLKkatiVQKA--KTAEHTRTERQVLEHIRQSPFLVTLHYAFQ-TDT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVMECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPD 674
Cdd:cd05613  79 KLHLILDYINGgELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLdSSGHVVLTDFGLSKEFLLD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKdSQVGTVNYMPPEAIKDMSSSRENGKskskispksDVWSLGCILYYMTYGKTPFQqiINQISKLHAIIDP---N 751
Cdd:cd05613 159 ENERAY-SFCGTIEYMAPEIVRGGDSGHDKAV---------DWWSLGVLMYELLTGASPFT--VDGEKNSQAEISRrilK 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 752 HEIEFPDIPEKDLQDVLKCCLKRDPKQRI-----SIPELLAHPYVQ 792
Cdd:cd05613 227 SEPPYPQEMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQ 272
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
641-793 1.14e-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: 81.26  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 641 HGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQpdtTSVVKDSQVGTVNYMPPEAIkDMSSSREngksksKISPKSDVWS 719
Cdd:cd06616 129 LKIIHRDVKPSNILLDRnGNIKLCDFGISGQLV---DSIAKTRDAGCRPYMAPERI-DPSASRD------GYDVRSDVWS 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 720 LGCILYYMTYGKTPFQQ---IINQISKL----HAIIDPNHEIEFpdipEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06616 199 LGITLYEVATGKFPYPKwnsVFDQLTQVvkgdPPILSNSEEREF----SPSFVNFVNLCLIKDESKRPKYKELLKHPFIK 274

                .
gi 23308722 793 I 793
Cdd:cd06616 275 M 275
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
525-791 1.24e-16

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: 81.41  E-value: 1.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNleeadnQTLDS--YRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMV 601
Cdd:cd14085   5 FEIESELGRGATSVVYRCRQKgTQKPYAVKKLK------KTVDKkiVRTEIGVLLRLSH--PNIIKLKEIFETPTEISLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECgnidlnswLKKKKSIDPWERKSYW---------KNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIA 668
Cdd:cd14085  77 LEL--------VTGGELFDRIVEKGYYserdaadavKQILEAVAYLHENGIVHRDLKPENLLYAtpapDAPLKIADFGLS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQMQPDttsVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF------QQIINQIS 742
Cdd:cd14085 149 KIVDQQ---VTMKTVCGTPGYCAPEILRGCAYGPE-----------VDMWSVGVITYILLCGFEPFydergdQYMFKRIL 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 743 KL-HAIIDPnheieFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14085 215 NCdYDFVSP-----WWDDVSLNAKDLVKKLIVLDPKKRLTTQQALQHPWV 259
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
532-788 1.58e-16

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: 80.44  E-value: 1.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 532 GSGGSSKVFQVLNEKKQIyAIKYVNLEE---ADNQTLDSYRNEiaylnklqqhsdKIIRLYDYEITDQYIYMVMECGniD 608
Cdd:cd13995  15 GAFGKVYLAQDTKTKKRM-ACKLIPVEQfkpSDVEIQACFRHE------------NIAELYGALLWEETVHLFMEAG--E 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWLKKKKSIDPW-ERKSYW--KNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIANQMQPDTTsVVKDSQvG 685
Cdd:cd13995  80 GGSVLEKLESCGPMrEFEIIWvtKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLVDFGLSVQMTEDVY-VPKDLR-G 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 686 TVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQI---SKLHAIIDPNHEIEfpDIPEK 762
Cdd:cd13995 158 TEIYMSPEVILCRGHNTK-----------ADIYSLGATIIHMQTGSPPWVRRYPRSaypSYLYIIHKQAPPLE--DIAQD 224
                       250       260
                ....*....|....*....|....*....
gi 23308722 763 ---DLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd13995 225 cspAMRELLEAALERNPNHRSSAAELLKH 253
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
573-790 1.81e-16

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 79.78  E-value: 1.81e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 573 AYLnKLQQHSdKIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPAN 652
Cdd:cd13976  37 AYF-RLPSHP-NISGVHEVIAGETKAYVFFERDHGDLHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRK 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 653 FLIVDG---MLKLIDFGIANQMQPDTTSVvkDSQVGTVNYMPPEAIKdmSSSRENGkskskisPKSDVWSLGCILYYMTY 729
Cdd:cd13976 115 FVFADEertKLRLESLEDAVILEGEDDSL--SDKHGCPAYVSPEILN--SGATYSG-------KAADVWSLGVILYTMLV 183
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 730 GKTPFQQIINqiSKLHAIIDPNHeIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd13976 184 GRYPFHDSEP--ASLFAKIRRGQ-FAIPETLSPRARCLIRSLLRREPSERLTAEDILLHPW 241
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
525-792 2.24e-16

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: 80.82  E-value: 2.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRnEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd07873   4 YIKLDKLGEGTYATVYKGRSKlTDNLVALKEIRLEHEEGAPCTAIR-EVSLLKDLK-HAN-IVTLHDIIHTEKSLTLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKK-KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSVvkD 681
Cdd:cd07873  81 YLDKDLKQYLDDcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINErGELKLADFGLARAKSIPTKTY--S 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIkdMSSSrengksksKISPKSDVWSLGCILYYMTYGKT--PFQQIINQISKLHAIIDPNHEIEFPDI 759
Cdd:cd07873 159 NEVVTLWYRPPDIL--LGST--------DYSTQIDMWGVGCIFYEMSTGRPlfPGSTVEEQLHFIFRILGTPTEETWPGI 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 760 ---------------PE----------KDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd07873 229 lsneefksynypkyrADalhnhaprldSDGADLLSKLLQFEGRKRISAEEAMKHPYFH 286
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
570-791 2.27e-16

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: 79.98  E-value: 2.27e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 570 NEIAYLnKLQQHSDKIIRLYD-YEITDQYIyMVMEC---GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVH 645
Cdd:cd14197  57 HEIAVL-ELAQANPWVINLHEvYETASEMI-LVLEYaagGEIFNQCVADREEAFKEKDVKRLMKQILEGVSFLHNNNVVH 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 646 SDLKPANFLIVD----GMLKLIDFGIANqmqpdttsVVKDSQ-----VGTVNYMPPEAIKDMSSSrengkskskisPKSD 716
Cdd:cd14197 135 LDLKPQNILLTSesplGDIKIVDFGLSR--------ILKNSEelreiMGTPEYVAPEILSYEPIS-----------TATD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 717 VWSLGCILYYMTYGKTPF-----QQIINQISKLHaiIDPNHEiEFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14197 196 MWSIGVLAYVMLTGISPFlgddkQETFLNISQMN--VSYSEE-EFEHLSESAI-DFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
525-789 2.36e-16

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: 80.43  E-value: 2.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME 603
Cdd:cd07848   3 FEVLGVVGEGAYGVVLKCRHkETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQ--ENIVELKEAFRRRGKLYLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWER-KSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVVKD 681
Cdd:cd07848  81 YVEKNMLELLEEMPNGVPPEKvRSYIYQLIKAIHWCHKNDIVHRDIKPENLLIsHNDVLKLCDFGFARNLSEGSNANYTE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 sQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKT--PFQQIINQISKLHAIIDP--------- 750
Cdd:cd07848 161 -YVATRWYRSPELLLGAPYGK-----------AVDMWSVGCILGELSDGQPlfPGESEIDQLFTIQKVLGPlpaeqmklf 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 751 -----NHEIEFPDIPEKD-------------LQDVLKCCLKRDPKQRISIPELLAHP 789
Cdd:cd07848 229 ysnprFHGLRFPAVNHPQslerrylgilsgvLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
522-804 2.37e-16

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 80.44  E-value: 2.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 522 GRIYSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNLEEADNQtldsyrNEIAYLNKLQQHSDkIIRLYDYEITDQYIYM 600
Cdd:cd14177   3 TDVYELKEDIGVGSYSVCKRCIHRATNMeFAVKIIDKSKRDPS------EEIEILMRYGQHPN-IITLKDVYDDGRYVYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMEC--GNIDLNSWLKKKkSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-----GMLKLIDFGIANQMQP 673
Cdd:cd14177  76 VTELmkGGELLDRILRQK-FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDdsanaDSIRICDFGFAKQLRG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVkdSQVGTVNYMPPEAIkdMSSSREngkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQISK--LHAIIDPN 751
Cdd:cd14177 155 ENGLLL--TPCYTANFVAPEVL--MRQGYD---------AACDIWSLGVLLYTMLAGYTPFANGPNDTPEeiLLRIGSGK 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 752 HEIEFP--DIPEKDLQDVLKCCLKRDPKQRISIPELLAH---------PYVQIQTHPVNQMAKG 804
Cdd:cd14177 222 FSLSGGnwDTVSDAAKDLLSHMLHVDPHQRYTAEQVLKHswiacrdqlPHYQLNRQDAPHLVKG 285
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
525-811 2.78e-16

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 79.90  E-value: 2.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLdsyRNEIAYLNKLQQHsdKIIRLYD-YEITDQYIyMVM 602
Cdd:cd14104   2 YMIAEELGRGQFGIVHRCVEtSSKKTYMAKFVKVKGADQVLV---KKEISILNIARHR--NILRLHEsFESHEELV-MIF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKK-SIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI---VDGMLKLIDFGIANQMQPDTTS 677
Cdd:cd14104  76 EfISGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYctrRGSYIKIIEFGQSRQLKPGDKF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVkdsQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIIDpnh 752
Cdd:cd14104 156 RL---QYTSAEFYAPEVHQHESVS-----------TATDMWSLGCLVYVLLSGINPFeaetnQQTIENIRNAEYAFD--- 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 753 EIEFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKGTTEEMKY 811
Cdd:cd14104 219 DEAFKNISIEAL-DFVDRLLVKERKSRMTAQEALNHPWLKQGMETVSSKDIKTTRHRRY 276
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
525-800 3.26e-16

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 80.98  E-value: 3.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYVNLeeADNQTLDSYRNEIAYLNKLQQhsDKIIRLYD----------YEI 593
Cdd:cd07854   7 YMDLRPLGCGSNGLVFSAVdSDCDKRVAVKKIVL--TDPQSVKHALREIKIIRRLDH--DNIVKVYEvlgpsgsdltEDV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQY----IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKnMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGI 667
Cdd:cd07854  83 GSLTelnsVYIVQEYMETDLANVLEQGPLSEEHARLFMYQ-LLRGLKYIHSANVLHRDLKPANVFIntEDLVLKIGDFGL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 668 ANQMQPDTTSVVKDSQvGTVN--YMPPEAIkdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQ-----QIINQ 740
Cdd:cd07854 162 ARIVDPHYSHKGYLSE-GLVTkwYRSPRLL--LSPNNYT--------KAIDMWAAGCIFAEMLTGKPLFAgahelEQMQL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 741 ISKLHAIIDPNHEIE--------------FPDIPEKDLQ--------DVLKCCLKRDPKQRISIPELLAHPYVQIQTHPV 798
Cdd:cd07854 231 ILESVPVVREEDRNEllnvipsfvrndggEPRRPLRDLLpgvnpealDFLEQILTFNPMDRLTAEEALMHPYMSCYSCPF 310

                ..
gi 23308722 799 NQ 800
Cdd:cd07854 311 DE 312
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
525-790 3.38e-16

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: 80.12  E-value: 3.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQ---VLNEkkQIYAIKYVNLEEADNQTLDSYRnEIAYLNKLQqHSDkIIRLYDYEITDQYIYMV 601
Cdd:cd07844   2 YKKLDKLGEGSYATVYKgrsKLTG--QLVALKEIRLEHEEGAPFTAIR-EASLLKDLK-HAN-IVTLHDIIHTKKTLTLV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNIDLNSWLKKKKS-IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQ-PDTTSv 678
Cdd:cd07844  77 FEYLDTDLKQYMDDCGGgLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISErGELKLADFGLARAKSvPSKTY- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vkDSQVGTVNYMPPEAI---KDMSSSrengkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAI-------- 747
Cdd:cd07844 156 --SNEVVTLWYRPPDVLlgsTEYSTS-------------LDMWGVGCIFYEMATGRPLFPGSTDVEDQLHKIfrvlgtpt 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 748 ------IDPNHEIE---FPDIPEKDL-------------QDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07844 221 eetwpgVSSNPEFKpysFPFYPPRPLinhaprldriphgEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
524-791 3.93e-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: 79.55  E-value: 3.93e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVfqVLNEKK---QIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYM 600
Cdd:cd14169   4 VYELKEKLGEGAFSEV--VLAQERgsqRLVALKCIP-KKALRGKEAMVENEIAVLRRINH--ENIVSLEDIYESPTHLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME--CGNIDLNSWLkkkksidpwERKSYWK--------NMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFG 666
Cdd:cd14169  79 AMElvTGGELFDRII---------ERGSYTEkdasqligQVLQAVKYLHQLGIVHRDLKPENLLYAtpfeDSKIMISDFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 667 IAnQMQPDTtsvVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQI 741
Cdd:cd14169 150 LS-KIEAQG---MLSTACGTPGYVAPELLEQKPYGKA-----------VDVWAIGVISYILLCGYPPFydendSELFNQI 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 23308722 742 SKlhaiidPNHEIEFP---DIPEKdLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14169 215 LK------AEYEFDSPywdDISES-AKDFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
531-791 4.74e-16

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: 79.38  E-value: 4.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTldSYRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMV---MECGN 606
Cdd:cd14090  10 LGEGAYASVQTCINlYTGKEYAVKIIEKHPGHSRS--RVFREVETLHQCQGHPN-ILQLIEYFEDDERFYLVfekMRGGP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 idLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD----GMLKLIDFGIA-------NQMQPDT 675
Cdd:cd14090  87 --LLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESmdkvSPVKICDFDLGsgiklssTSMTPVT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVVKdSQVGTVNYMPPE---AIKDMSSSRENgkskskispKSDVWSLGCILYYMTYGKTPF----------------QQ 736
Cdd:cd14090 165 TPELL-TPVGSAEYMAPEvvdAFVGEALSYDK---------RCDLWSLGVILYIMLCGYPPFygrcgedcgwdrgeacQD 234
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 737 IINQIskLHAIIDpnHEIEFPDIPEKDL----QDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14090 235 CQELL--FHSIQE--GEYEFPEKEWSHIsaeaKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
524-793 4.82e-16

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: 79.59  E-value: 4.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDS-----YRNEIAYLNKLQQHSDkIIRLYDYeITDQYI 598
Cdd:cd14020   1 LWEVQSRLGQGSSASVYRVSSGRGADQPTSALKEFQLDHQGSQEsgdygFAKERAALEQLQGHRN-IVTLYGV-FTNHYS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 Y------MVMECGNIDLNSWL--KKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFL--IVDGMLKLIDFGIA 668
Cdd:cd14020  79 AnvpsrcLLLELLDVSVSELLlrSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILwsAEDECFKLIDFGLS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQmqpDTTSVVKDSQvgTVNYMPPEAIKDMSSSRENGKSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLH--A 746
Cdd:cd14020 159 FK---EGNQDVKYIQ--TDGYRAPEAELQNCLAQAGLQSETECTSAVDLWSLGIVLLEMFSGMKLKHTVRSQEWKDNssA 233
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 747 IID---PNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQI 793
Cdd:cd14020 234 IIDhifASNAVVNPAIPAYHLRDLIKSMLHNDPGKRATAEAALCSPFFSI 283
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
525-782 5.23e-16

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 79.69  E-value: 5.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQ---VLNEKkqIYAIKYVNL-EEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYM 600
Cdd:cd08229  26 FRIEKKIGRGQFSEVYRatcLLDGV--PVALKKVQIfDLMDAKARADCIKEIDLLKQLNHPN--VIKYYASFIEDNELNI 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGNI-DLNSWL---KKKKSIDPweRKSYWKNMLE---AVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQ 672
Cdd:cd08229 102 VLELADAgDLSRMIkhfKKQKRLIP--EKTVWKYFVQlcsALEHMHSRRVMHRDIKPANvFITATGVVKLGDLGLGRFFS 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSVvkDSQVGTVNYMPPEAIkdmsssRENGKSKSKispksDVWSLGCILYYMTYGKTPFqqiINQISKLHAIIDPNH 752
Cdd:cd08229 180 SKTTAA--HSLVGTPYYMSPERI------HENGYNFKS-----DIWSLGCLLYEMAALQSPF---YGDKMNLYSLCKKIE 243
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 753 EIEFPDIP----EKDLQDVLKCCLKRDPKQRISI 782
Cdd:cd08229 244 QCDYPPLPsdhySEELRQLVNMCINPDPEKRPDI 277
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
525-790 5.43e-16

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: 78.59  E-value: 5.43e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGsskvFQVLN------EKKQIyAIKYVNLEEADNQTLDSYRNEIAYLnKLQQHsDKIIRLYDYEITDQYI 598
Cdd:cd14071   2 YDIERTIGKGN----FAVVKlarhriTKTEV-AIKIIDKSQLDEENLKKIYREVQIM-KMLNH-PHIIKLYQVMETKDML 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME-CGNIDLNSWLKKKKSI-DPWERKSYWKnMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDT 675
Cdd:cd14071  75 YLVTEyASNGEIFDYLAQHGRMsEKEARKKFWQ-ILSAVEYCHKRHIVHRDLKAENLLLDANMnIKIADFGFSNFFKPGE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSvvkDSQVGTVNYMPPEAIKdmsSSRENGKSKskispksDVWSLGCILYYMTYGKTPFQQiiNQISKLHA-IIDPNHEI 754
Cdd:cd14071 154 LL---KTWCGSPPYAAPEVFE---GKEYEGPQL-------DIWSLGVVLYVLVCGALPFDG--STLQTLRDrVLSGRFRI 218
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 23308722 755 EFpdIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14071 219 PF--FMSTDCEHLIRRMLVLDPSKRLTIEQIKKHKW 252
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
547-791 5.54e-16

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: 78.62  E-value: 5.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 547 KQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVMEC---GNIDlnSWLKKKKS--IDP 621
Cdd:cd08220  25 NKLVIIKQIPVEQMTKEERQAALNEVKVLSML--HHPNIIEYYESFLEDKALMIVMEYapgGTLF--EYIQQRKGslLSE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 622 WERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG--MLKLIDFGIANQMqpdTTSVVKDSQVGTVNYMPPEAIKDMS 699
Cdd:cd08220 101 EEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKrtVVKIGDFGISKIL---SSKSKAYTVVGTPCYISPELCEGKP 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 700 SSRENgkskskispksDVWSLGCILYYMTYGKTPFQ-----QIINQISKlhAIIDPnheieFPDIPEKDLQDVLKCCLKR 774
Cdd:cd08220 178 YNQKS-----------DIWALGCVLYELASLKRAFEaanlpALVLKIMR--GTFAP-----ISDRYSEELRHLILSMLHL 239
                       250
                ....*....|....*..
gi 23308722 775 DPKQRISIPELLAHPYV 791
Cdd:cd08220 240 DPNKRPTLSEIMAQPII 256
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
528-780 5.73e-16

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: 79.59  E-value: 5.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEADNqtldsyRNEIAYLNKLQQhsdkIIRLYDYEI---------TDQY 597
Cdd:cd05574   6 IKLLGKGDVGRVYLVrLKGTGKLFAMKVLDKEEMIK------RNKVKRVLTERE----ILATLDHPFlptlyasfqTSTH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNIDLNSWLKK--KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQP 673
Cdd:cd05574  76 LCFVMDyCPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLhESGHIMLTDFDLSKQSSV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKD---------------------------SQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYY 726
Cdd:cd05574 156 TPPPVRKSlrkgsrrssvksieketfvaepsarsnSFVGTEEYIAPEVIKGDGHG-----------SAVDWWTLGILLYE 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 727 MTYGKTPF-----QQIINQIskLHAiidpnhEIEFPDIPE--KDLQDVLKCCLKRDPKQRI 780
Cdd:cd05574 225 MLYGTTPFkgsnrDETFSNI--LKK------ELTFPESPPvsSEAKDLIRKLLVKDPSKRL 277
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
525-790 6.37e-16

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: 78.45  E-value: 6.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGsskvFQVLNE-----KKQIYAIKYVNLEEADNQTlDSYRNEIAYLNKLQQHSdkIIRLY-DYEiTDQYI 598
Cdd:cd14185   2 YEIGRTIGDGN----FAVVKEcrhwnENQEYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPN--IVKLFeVYE-TEKEI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMEC--GNIDLNSWLKKKKSIDPwERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI---VDG--MLKLIDFGIANQM 671
Cdd:cd14185  74 YLILEYvrGGDLFDAIIESVKFTEH-DAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnPDKstTLKLADFGLAKYV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QPDTTSVvkdsqVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPN 751
Cdd:cd14185 153 TGPIFTV-----CGTPTYVAPEILSEKGYGLE-----------VDMWAAGVILYILLCGFPPFRSPERDQEELFQIIQLG 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 752 HEIEFP---DIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14185 217 HYEFLPpywDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
521-790 6.67e-16

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: 79.35  E-value: 6.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 521 KGRIYSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRNeiAYLNKLQQHSDkIIRLYDYEITDQYIY 599
Cdd:cd07869   3 KADSYEKLEKLGEGSYATVYKGKSKvNGKLVALKVIRLQEEEGTPFTAIRE--ASLLKGLKHAN-IVLLHDIIHTKETLT 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDLNSWLKKKKS-IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANqmQPDTTS 677
Cdd:cd07869  80 LVFEYVHTDLCQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDtGELKLADFGLAR--AKSVPS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPEAIkdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPF---QQIINQISKLHAIIDPNHEI 754
Cdd:cd07869 158 HTYSNEVVTLWYRPPDVL--LGSTEYS--------TCLDMWGVGCIFVEMIQGVAAFpgmKDIQDQLERIFLVLGTPNED 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 755 EFPDI-------PEK--------------------DLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07869 228 TWPGVhslphfkPERftlyspknlrqawnklsyvnHAEDLASKLLQCFPKNRLSAQAALSHEY 290
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
547-790 6.83e-16

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: 78.17  E-value: 6.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 547 KQIYAIKYVNLE--EADNQTL--------DSYRNEIAY----LNKLQQ--HsDKIIRLYDY---EITDQY---IYMVMEC 604
Cdd:cd14012   7 GTFYLVYEVVLDnsKKPGKFLtsqeyfktSNGKKQIQLlekeLESLKKlrH-PNLVSYLAFsieRRGRSDgwkVYLLTEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 GN-IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIANQMQPDTTSVV 679
Cdd:cd14012  86 APgGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDrdagTGIVKLTDYSLGKTLLDMCSRGS 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVnYMPPEAIK-DMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQqiinQISKLHAIIDPnheiefPD 758
Cdd:cd14012 166 LDEFKQTY-WLPPELAQgSKSPTRKT-----------DVWDLGLLFLQMLFGLDVLE----KYTSPNPVLVS------LD 223
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 759 IPEkDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14012 224 LSA-SLQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
530-790 7.10e-16

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 78.42  E-value: 7.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 530 QIGSGGSSKVFQVLNEKKQIY----AIKYVNLEEADNQTLdsyRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYMV---- 601
Cdd:cd13983   8 VLGRGSFKTVYRAFDTEEGIEvawnEIKLRKLPKAERQRF---KQEIEILKSLK-H-PNIIKFYDSWESKSKKEVIfite 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 -MECGNidLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHG--IVHSDLKPANFLI--VDGMLKLIDFGIANQMQPDTT 676
Cdd:cd13983  83 lMTSGT--LKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFIngNTGEVKIGDLGLATLLRQSFA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVkdsqVGTVNYMPPEaikdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQQIIN--QISK----------L 744
Cdd:cd13983 161 KSV----IGTPEFMAPE----MYEEHYD--------EKVDIYAFGMCLLEMATGEYPYSECTNaaQIYKkvtsgikpesL 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 745 HAIIDPNheiefpdipEKDLqdVLKCCLKRDpkQRISIPELLAHPY 790
Cdd:cd13983 225 SKVKDPE---------LKDF--IEKCLKPPD--ERPSARELLEHPF 257
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
525-790 8.48e-16

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: 78.85  E-value: 8.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQ--HSDkIIRLYDY---EITDQ-- 596
Cdd:cd07863   2 YEPVAEIGVGAYGTVYKARDpHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEAfdHPN-IVRLMDVcatSRTDRet 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVMECGNIDLNSWLKKKKSID-PWER-KSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIAN---- 669
Cdd:cd07863  81 KVTLVFEHVDQDLRTYLDKVPPPGlPAETiKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSgGQVKLADFGLARiysc 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMQPDTTSVvkdsqvgTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAI 747
Cdd:cd07863 161 QMALTPVVV-------TLWYRAPEVLLQSTYA-----------TPVDMWSVGCIFAEMFRRKPLFcgNSEADQLGKIFDL 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 748 IDPNHEIEF-----------------------PDIPEKDLQDVLKcCLKRDPKQRISIPELLAHPY 790
Cdd:cd07863 223 IGLPPEDDWprdvtlprgafsprgprpvqsvvPEIEESGAQLLLE-MLTFNPHKRISAFRALQHPF 287
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
524-791 9.24e-16

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: 78.53  E-value: 9.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQI-GSGGSSKVFQVLNE-KKQIYAIKYVnlEEADNQTLDSYRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMV 601
Cdd:cd14173   2 VYQLQEEVlGEGAYARVQTCINLiTNKEYAVKII--EKRPGHSRSRVFREVEMLYQCQGHRN-VLELIEFFEEEDKFYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME--CGNIDLNSwLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD----GMLKLIDFGIAN--QMQP 673
Cdd:cd14173  79 FEkmRGGSILSH-IHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHpnqvSPVKICDFDLGSgiKLNS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKD---SQVGTVNYMPPEAIKDMSSSrengksKSKISPKSDVWSLGCILYYMTYGKTPF---------------- 734
Cdd:cd14173 158 DCSPISTPellTPCGSAEYMAPEVVEAFNEE------ASIYDKRCDLWSLGVILYIMLSGYPPFvgrcgsdcgwdrgeac 231
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 735 QQIINQIskLHAIIDPNHEiefpdIPEKD-------LQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14173 232 PACQNML--FESIQEGKYE-----FPEKDwahiscaAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
531-792 1.40e-15

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: 77.82  E-value: 1.40e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVL----NEKKQIYAIKYvnLEEA----DNQTLDSYRNEIAYLNKLQQhSDKIIRL-YDYEiTDQYIYMV 601
Cdd:cd05583   2 LGTGAYGKVFLVRkvggHDAGKLYAMKV--LKKAtivqKAKTAEHTMTERQVLEAVRQ-SPFLVTLhYAFQ-TDAKLHLI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSV 678
Cdd:cd05583  78 LDyvNGG-ELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLdSEGHVVLTDFGLSKEFLPGENDR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKdSQVGTVNYMPPEAIKDMSSSREngkskskisPKSDVWSLGCILYYMTYGKTPF---------QQIINQISKLHAIId 749
Cdd:cd05583 157 AY-SFCGTIEYMAPEVVRGGSDGHD---------KAVDWWSLGVLTYELLTGASPFtvdgernsqSEISKRILKSHPPI- 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 23308722 750 pnheiefPDIPEKDLQDVLKCCLKRDPKQRI-----SIPELLAHPYVQ 792
Cdd:cd05583 226 -------PKTFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPFFK 266
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
525-790 2.02e-15

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: 77.80  E-value: 2.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVME 603
Cdd:cd07847   3 YEKLSKIGEGSYGVVFKCRNrETGQIVAIKKFVESEDDPVIKKIALREIRMLKQLK-HPN-LVNLIEVFRRKRKLHLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQP---DTTSV 678
Cdd:cd07847  81 yCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITkQGQIKLCDFGFARILTGpgdDYTDY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VK-------DSQVGTVNYMPPeaikdmsssrengkskskispkSDVWSLGCI-------------------LYYM--TYG 730
Cdd:cd07847 161 VAtrwyrapELLVGDTQYGPP----------------------VDVWAIGCVfaelltgqplwpgksdvdqLYLIrkTLG 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 731 KTPF--QQII--NQISKLHAIIDPNH----EIEFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07847 219 DLIPrhQQIFstNQFFKGLSIPEPETreplESKFPNISSPAL-SFLKGCLQMDPTERLSCEELLEHPY 285
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
527-786 2.04e-15

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: 77.55  E-value: 2.04e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVF--QVLNEKKQiYAIKyvNLEEADNQTLDSYRNEIAYLNKLQQHSDkIIRLYDYEIT---------D 595
Cdd:cd14036   4 IKRVIAEGGFAFVYeaQDVGTGKE-YALK--RLLSNEEEKNKAIIQEINFMKKLSGHPN-IVQFCSAASIgkeesdqgqA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVMEC--GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHG--IVHSDLKPANFLIV-DGMLKLIDFGIANQ 670
Cdd:cd14036  80 EYLLLTELCkgQLVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGnQGQIKLCDFGSATT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 --MQPDTT------SVVKD--SQVGTVNYMPPEAIkDMSSSRENGKSKskispksDVWSLGCILYYMTYGKTPFQqiinQ 740
Cdd:cd14036 160 eaHYPDYSwsaqkrSLVEDeiTRNTTPMYRTPEMI-DLYSNYPIGEKQ-------DIWALGCILYLLCFRKHPFE----D 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 741 ISKLhAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14036 228 GAKL-RIINAKYTIPPNDTQYTVFHDLIRSTLKVNPEERLSITEIV 272
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
531-790 2.35e-15

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: 78.03  E-value: 2.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQV-LNEKKQIYAIKY----VNLEEADnqtLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQyIYMVMECG 605
Cdd:cd05590   3 LGKGSFGKVMLArLKESGRLYAVKVlkkdVILQDDD---VECTMTEKRILSLARNHPFLTQLYCCFQTPDR-LFFVMEFV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPD--TTSVVkd 681
Cdd:cd05590  79 NGgDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLdHEGHCKLADFGMCKEGIFNgkTTSTF-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 sqVGTVNYMPPEAIKDMsssrengksksKISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIdpNHEIEFPDIPE 761
Cdd:cd05590 157 --CGTPDYIAPEILQEM-----------LYGPSVDWWAMGVLLYEMLCGHAPFEA-ENEDDLFEAIL--NDEVVYPTWLS 220
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 762 KDLQDVLKCCLKRDPKQRISIPEL------LAHPY 790
Cdd:cd05590 221 QDAVDILKAFMTKNPTMRLGSLTLggeeaiLRHPF 255
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
529-797 3.44e-15

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: 77.43  E-value: 3.44e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQV-LNEKKQIYAIKY----VNLEEADNQTLDSYRNEIAylnkLQQHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd05592   1 KVLGKGSFGKVMLAeLKGTNQYFAIKAlkkdVVLEDDDVECTMIERRVLA----LASQHPFLTHLFCTFQTESHLFFVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIAN-QMQPDTTSvvk 680
Cdd:cd05592  77 YLNGgDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLdREGHIKIADFGMCKeNIYGENKA--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDmsssrengkskSKISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIdpNHEIEFPDIP 760
Cdd:cd05592 154 STFCGTPDYIAPEILKG-----------QKYNQSVDWWSFGVLLYEMLIGQSPFHG-EDEDELFWSIC--NDTPHYPRWL 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 761 EKDLQDVLKCCLKRDPKQRISIPELLAHPyvqIQTHP 797
Cdd:cd05592 220 TKEAASCLSLLLERNPEKRLGVPECPAGD---IRDHP 253
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
525-740 3.58e-15

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: 76.34  E-value: 3.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKyvnLEEAD--NQTLdsyRNEIAYLNKLQQHsDKIIRLYDYEITDQYIYMV 601
Cdd:cd14016   2 YKLVKKIGSGSFGEVYLGIDlKTGEEVAIK---IEKKDskHPQL---EYEAKVYKLLQGG-PGIPRLYWFGQEGDYNVMV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME-CGNiDLNSWLKKKKsidpweRKSYWKN-------MLEAVHTIHQHGIVHSDLKPANFLIVDG----MLKLIDFGIA- 668
Cdd:cd14016  75 MDlLGP-SLEDLFNKCG------RKFSLKTvlmladqMISRLEYLHSKGYIHRDIKPENFLMGLGknsnKVYLIDFGLAk 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 669 -------NQMQPDTTsvvKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQIINQ 740
Cdd:cd14016 148 kyrdprtGKHIPYRE---GKSLTGTARYASINAHLGIEQSRRD-----------DLESLGYVLIYFLKGSLPWQGLKAQ 212
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
523-797 3.66e-15

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: 77.32  E-value: 3.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILkqiGSGGSSKVFQV-LNEKKQIYAIKYVNLEEADNQTLDSYR-NEIAYLNKLqqHSDKIIRL-YDYEITDQY-- 597
Cdd:cd05632   5 RQYRVL---GKGGFGEVCACqVRATGKMYACKRLEKKRIKKRKGESMAlNEKQILEKV--NSQFVVNLaYAYETKDALcl 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMqPDTT 676
Cdd:cd05632  80 VLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDyGHIRISDLGLAVKI-PEGE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVvkDSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQISK--LHAIIDPNHEI 754
Cdd:cd05632 159 SI--RGRVGTVGYMAPEVLNNQRYT-----------LSPDYWGLGCLIYEMIEGQSPFRGRKEKVKReeVDRRVLETEEV 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 755 EFPDIPEkDLQDVLKCCLKRDPKQRISIPEllaHPYVQIQTHP 797
Cdd:cd05632 226 YSAKFSE-EAKSICKMLLTKDPKQRLGCQE---EGAGEVKRHP 264
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
531-792 4.63e-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: 76.61  E-value: 4.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVNlEEADNQTLDSYRnEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVME---CGN 606
Cdd:cd14174  10 LGEGAYAKVQGCVSlQNGKEYAVKIIE-KNAGHSRSRVFR-EVETLYQCQGNKN-ILELIEFFEDDTRFYLVFEklrGGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IdlNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD----GMLKLIDFGIANQMQ------PDTT 676
Cdd:cd14174  87 I--LAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESpdkvSPVKICDFDLGSGVKlnsactPITT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKdSQVGTVNYMPPEAIKDMSSSrengksKSKISPKSDVWSLGCILYYMTYGKTPF-------------QQIINQISK 743
Cdd:cd14174 165 PELT-TPCGSAEYMAPEVVEVFTDE------ATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgwdrgEVCRVCQNK 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 23308722 744 LHAIIDPNhEIEFPDIP----EKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14174 238 LFESIQEG-KYEFPDKDwshiSSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
546-796 4.67e-15

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: 75.94  E-value: 4.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 546 KKQIYAIKyvnleeadnqTLDSYRNEIAYLNKLQQHSD----KIIRLYDYEITDQYIYMVME---CGNidLNSWLKKKKS 618
Cdd:cd14058  15 RNQIVAVK----------IIESESEKKAFEVEVRQLSRvdhpNIIKLYGACSNQKPVCLVMEyaeGGS--LYNVLHGKEP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 619 iDP---------WERKSywKNMLEAVHTIHQHGIVHSDLKPANFLIVDG--MLKLIDFGIANQMQPDTTsvvkDSQvGTV 687
Cdd:cd14058  83 -KPiytaahamsWALQC--AKGVAYLHSMKPKALIHRDLKPPNLLLTNGgtVLKICDFGTACDISTHMT----NNK-GSA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 688 NYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIdpnHEIEFPD----IPeKD 763
Cdd:cd14058 155 AWMAPEVFEGSKYSEK-----------CDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAV---HNGERPPliknCP-KP 219
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 764 LQDVLKCCLKRDPKQRISIPELlahpyVQIQTH 796
Cdd:cd14058 220 IESLMTRCWSKDPEKRPSMKEI-----VKIMSH 247
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
525-780 4.71e-15

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: 77.75  E-value: 4.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEA-DNQTLDSYRNEiAYLNKLQQHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd05617  17 FDLIRVIGRGSYAKVLLVrLKKNDQIYAMKVVKKELVhDDEDIDWVQTE-KHVFEQASSNPFLVGLHSCFQTTSRLFLVI 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQP-DTTSV 678
Cdd:cd05617  96 EYVNGgDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLdADGHIKLTDYGMCKEgLGPgDTTST 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VkdsqVGTVNYMPPEAIKdmssSRENGKSKskispksDVWSLGCILYYMTYGKTPFQQI-----INQISKLHAIIdPNHE 753
Cdd:cd05617 176 F----CGTPNYIAPEILR----GEEYGFSV-------DWWALGVLMFEMMAGRSPFDIItdnpdMNTEDYLFQVI-LEKP 239
                       250       260
                ....*....|....*....|....*..
gi 23308722 754 IEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05617 240 IRIPRFLSVKASHVLKGFLNKDPKERL 266
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
527-779 5.35e-15

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 76.23  E-value: 5.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKKQIYAIKYVnleEADNQTLDSYRNEiAYLNKLQQHsDKIIRLYDYEITDQYIYMVME-CG 605
Cdd:cd05072  11 LVKKLGAGQFGEVWMGYYNNSTKVAVKTL---KPGTMSVQAFLEE-ANLMKTLQH-DKLVRLYAVVTKEEPIYIITEyMA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKK--------KSIDpwerksYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGML-KLIDFGIANQMQpDTT 676
Cdd:cd05072  86 KGSLLDFLKSDeggkvllpKLID------FSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMcKIADFGLARVIE-DNE 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIINqiSKLHAIIDPNHEIE 755
Cdd:cd05072 159 YTAREGAKFPIKWTAPEAINFGSFTIKS-----------DVWSFGILLYeIVTYGKIPYPGMSN--SDVMSALQRGYRMP 225
                       250       260
                ....*....|....*....|....
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05072 226 RMENCPDELYDIMKTCWKEKAEER 249
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
529-790 5.86e-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: 76.67  E-value: 5.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLN----EKKQIYAIKYvnLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMEC 604
Cdd:cd05582   1 KVLGQGSFGKVFLVRKitgpDAGTLYAMKV--LKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 --GNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVVkd 681
Cdd:cd05582  79 lrGG-DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLdEDGHIKLTDFGLSKESIDHEKKAY-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIkdmssSRENgkskskISPKSDVWSLGCILYYMTYGKTPFQ-----QIINQISKLhaiidpnhEIEF 756
Cdd:cd05582 156 SFCGTVEYMAPEVV-----NRRG------HTQSADWWSFGVLMFEMLTGSLPFQgkdrkETMTMILKA--------KLGM 216
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 757 PDIPEKDLQDVLKCCLKRDPKQRI-----SIPELLAHPY 790
Cdd:cd05582 217 PQFLSPEAQSLLRALFKRNPANRLgagpdGVEEIKRHPF 255
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
525-790 5.92e-15

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: 75.79  E-value: 5.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSkVFQVLNEK--KQIYAIKYVnleEADNQTLDSYRNEIayLNKLQQHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd14665   2 YELVKDIGSGNFG-VARLMRDKqtKELVAVKYI---ERGEKIDENVQREI--INHRSLRHPNIVRFKEVILTPTHLAIVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIvDG----MLKLIDFGIAN----QMQP 673
Cdd:cd14665  76 EyAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL-DGspapRLKICDFGYSKssvlHSQP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTsvvkdsqVGTVNYMPPEAikdMSSSRENGKSKskispksDVWSLGCILYYMTYGKTPF---QQIINQISKLHAIIDP 750
Cdd:cd14665 155 KST-------VGTPAYIAPEV---LLKKEYDGKIA-------DVWSCGVTLYVMLVGAYPFedpEEPRNFRKTIQRILSV 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 751 NHEIefPDipekDLQDVLKCC--LKR----DPKQRISIPELLAHPY 790
Cdd:cd14665 218 QYSI--PD----YVHISPECRhlISRifvaDPATRITIPEIRNHEW 257
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
531-786 6.80e-15

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: 75.51  E-value: 6.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLnEKKQIYAIK--YVNLEEADNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQYIYMVME-CGNI 607
Cdd:cd14061   2 IGVGGFGKVYRGI-WRGEEVAVKaaRQDPDEDISVTLENVRQE-ARLFWMLRHPN-IIALRGVCLQPPNLCLVMEyARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 DLNSWLKKKKsIDPwERKSYWK-NMLEAVHTIHQHG---IVHSDLKPANFLIV---------DGMLKLIDFGIANQMQPD 674
Cdd:cd14061  79 ALNRVLAGRK-IPP-HVLVDWAiQIARGMNYLHNEApvpIIHRDLKSSNILILeaienedleNKTLKITDFGLAREWHKT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TtsvvKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQI----------INqisKL 744
Cdd:cd14061 157 T----RMSAAGTYAWMAPEVIKSSTFSK-----------ASDVWSYGVLLWELLTGEVPYKGIdglavaygvaVN---KL 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 745 HAIIdPNheiEFPDiPEKDLqdvLKCCLKRDPKQRISIPELL 786
Cdd:cd14061 219 TLPI-PS---TCPE-PFAQL---MKDCWQPDPHDRPSFADIL 252
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
525-792 7.22e-15

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: 76.88  E-value: 7.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL----NEKKQIYAIKYVNLEE--ADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEiTDQYI 598
Cdd:cd05614   2 FELLKVLGTGAYGKVFLVRkvsgHDANKLYAMKVLRKAAlvQKAKTVEHTRTERNVLEHVRQSPFLVTLHYAFQ-TDAKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTT 676
Cdd:cd05614  81 HLILDyVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLdSEGHVVLTDFGLSKEFLTEEK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKdSQVGTVNYMPPEAIKDMSSSREngkskskispKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIIDPn 751
Cdd:cd05614 161 ERTY-SFCGTIEYMAPEIIRGKSGHGK----------AVDWWSLGILMFELLTGASPFtlegeKNTQSEVSRRILKCDP- 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 752 heiEFPDIPEKDLQDVLKCCLKRDPKQRI-SIP----ELLAHPYVQ 792
Cdd:cd05614 229 ---PFPSFIGPVARDLLQKLLCKDPKKRLgAGPqgaqEIKEHPFFK 271
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
525-790 7.35e-15

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: 76.20  E-value: 7.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYV-NLEEADNQTLDSYRnEIAYLNKLQQHSdkIIRLYD--YEITDQY--- 597
Cdd:cd07866  10 YEILGKLGEGTFGEVYKARQIKtGRVVALKKIlMHNEKDGFPITALR-EIKILKKLKHPN--VVPLIDmaVERPDKSkrk 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 ---IYMVMECGNIDLNSWLKKKK-SIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA---- 668
Cdd:cd07866  87 rgsVYMVTPYMDHDLSGLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNqGILKIADFGLArpyd 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 ----NQMQPDTTSVVK-DSQVGTVNYMPPEAIkdMSSSRENGkskskispKSDVWSLGCILYYMTYGKTPFQ--QIINQI 741
Cdd:cd07866 167 gpppNPKGGGGGGTRKyTNLVVTRWYRPPELL--LGERRYTT--------AVDIWGIGCVFAEMFTRRPILQgkSDIDQL 236
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 742 SKLHAIIDPNHEIEFP---DIP----------------------EKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07866 237 HLIFKLCGTPTEETWPgwrSLPgcegvhsftnyprtleerfgklGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
524-794 7.84e-15

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: 75.91  E-value: 7.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTLdsyRNEIAYLNKLQQHSDkIIRLYDYEIT------DQ 596
Cdd:cd06637   7 IFELVELVGNGTYGQVYKGRHVKTgQLAAIKVMDVTGDEEEEI---KQEINMLKKYSHHRN-IATYYGAFIKknppgmDD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVME-CGNIDLNSWLKKKKSIdpwERKSYW-----KNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIAN 669
Cdd:cd06637  83 QLWLVMEfCGAGSVTDLIKNTKGN---TLKEEWiayicREILRGLSHLHQHKVIHRDIKGQNVLLTENAeVKLVDFGVSA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMqpDTTSVVKDSQVGTVNYMPPEAIkdmsSSRENgkSKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIID 749
Cdd:cd06637 160 QL--DRTVGRRNTFIGTPYWMAPEVI----ACDEN--PDATYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRN 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 750 PNHEIEFPDIPEKdLQDVLKCCLKRDPKQRISIPELLAHPYVQIQ 794
Cdd:cd06637 232 PAPRLKSKKWSKK-FQSFIESCLVKNHSQRPSTEQLMKHPFIRDQ 275
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
525-797 8.95e-15

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: 76.59  E-value: 8.95e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYVN-------------------LEEADNqtldsyrneiaylnklqqhsDK 584
Cdd:cd05598   3 FEKIKTIGVGAFGEVSLVRkKDTNALYAMKTLRkkdvlkrnqvahvkaerdiLAEADN--------------------EW 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 585 IIRLYdYEITDQ-YIYMVMEC--GNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGML 660
Cdd:cd05598  63 VVKLY-YSFQDKeNLYFVMDYipGG-DLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIdRDGHI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 661 KLIDFGIANQMQ--PDTTSVVKDSQVGTVNYMPPEAIkdmssSRENgkskskISPKSDVWSLGCILYYMTYGKTPF---- 734
Cdd:cd05598 141 KLTDFGLCTGFRwtHDSKYYLAHSLVGTPNYIAPEVL-----LRTG------YTQLCDWWSVGVILYEMLVGQPPFlaqt 209
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23308722 735 ----QqiinqisklHAIIDPNHEIEFPDIPE-----KDLqdVLKCClkRDPKQRISipellAHPYVQIQTHP 797
Cdd:cd05598 210 paetQ---------LKVINWRTTLKIPHEANlspeaKDL--ILRLC--CDAEDRLG-----RNGADEIKAHP 263
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
528-803 9.50e-15

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: 75.94  E-value: 9.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVLNEKKQ-IYAIKYVNLE---EADNQTLdsyrNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd06615   6 LGELGAGNGGVVTKVLHRPSGlIMARKLIHLEikpAIRNQII----RELKVLHEC--NSPYIVGFYGAFYSDGEISICME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 cgNID---LNSWLKKKKSI-DPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpdtTSV 678
Cdd:cd06615  80 --HMDggsLDQVLKKAGRIpENILGKISIAVLRGLTYLREKHKIMHRDVKPSNILVnSRGEIKLCDFGVSGQL----IDS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTP--------FQQIINQISKLHAIIDP 750
Cdd:cd06615 154 MANSFVGTRSYMSPERLQGTHYTVQS-----------DIWSLGLSLVEMAIGRYPipppdakeLEAMFGRPVSEGEAKES 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 751 NHEIE--FPDIP-------------------------EKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAK 803
Cdd:cd06615 223 HRPVSghPPDSPrpmaifelldyivnepppklpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAELEEVDFAG 302
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
528-790 1.13e-14

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: 75.90  E-value: 1.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVL----NEKKQIYAIKYvnLEEA-------DNQTLDSYRNeiaYLNKLQqHSDKIIRLYDYEiTDQ 596
Cdd:cd05584   1 LKVLGKGGYGKVFQVRkttgSDKGKIFAMKV--LKKAsivrnqkDTAHTKAERN---ILEAVK-HPFIVDLHYAFQ-TGG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVME--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQP 673
Cdd:cd05584  74 KLYLILEylSGG-ELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLdAQGHVKLTDFGLCKESIH 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTsvVKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF-----QQIINQIskLHAii 748
Cdd:cd05584 153 DGT--VTHTFCGTIEYMAPEILTRSGHGK-----------AVDWWSLGALMYDMLTGAPPFtaenrKKTIDKI--LKG-- 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23308722 749 dpnhEIEFPDIPEKDLQDVLKCCLKRDPKQRI-SIPE----LLAHPY 790
Cdd:cd05584 216 ----KLNLPPYLTNEARDLLKKLLKRNVSSRLgSGPGdaeeIKAHPF 258
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
524-791 1.69e-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: 74.66  E-value: 1.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTLdsyRNEIAYLNKLQQHSDkIIRLYDYEIT------DQ 596
Cdd:cd06636  17 IFELVEVVGNGTYGQVYKGRHVKTgQLAAIKVMDVTEDEEEEI---KLEINMLKKYSHHRN-IATYYGAFIKksppghDD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVME-CGNIDLNSWLKKKKSIdpwERKSYW-----KNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIAN 669
Cdd:cd06636  93 QLWLVMEfCGAGSVTDLVKNTKGN---ALKEDWiayicREILRGLAHLHAHKVIHRDIKGQNVLLTENAeVKLVDFGVSA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMqpDTTSVVKDSQVGTVNYMPPEAIkdmsSSRENgkSKSKISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAII- 748
Cdd:cd06636 170 QL--DRTVGRRNTFIGTPYWMAPEVI----ACDEN--PDATYDYRSDIWSLGITAIEMAEGAPPLCD-MHPMRALFLIPr 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23308722 749 DPNHEIEFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06636 241 NPPPKLKSKKWSKKFI-DFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
523-792 2.11e-14

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: 75.09  E-value: 2.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVNLE-EADNQTLDSYRNEIAYLNKLQqHSDKIirlyDYE---ITDQY 597
Cdd:cd06635  25 KLFSDLREIGHGSFGAVYFARDVRtSEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQRIK-HPNSI----EYKgcyLREHT 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPdt 675
Cdd:cd06635 100 AWLVMEyCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEpGQVKLADFGSASIASP-- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 tsvvKDSQVGTVNYMPPEAIKDMSSSRENGkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIdpnhEIE 755
Cdd:cd06635 178 ----ANSFVGTPYWMAPEVILAMDEGQYDG--------KVDVWSLGITCIELAERKPPLFN-MNAMSALYHIA----QNE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23308722 756 FPDIPEKDLQDVLK----CCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06635 241 SPTLQSNEWSDYFRnfvdSCLQKIPQDRPTSEELLKHMFVL 281
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
525-790 2.16e-14

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: 74.04  E-value: 2.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSG--GSSKVFQVlNEKKQIYAIKYVnleEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVM 602
Cdd:cd14662   2 YELVKDIGSGnfGVARLMRN-KETKELVAVKYI---ERGLKIDENVQREIINHRSLRHPN--IIRFKEVVLTPTHLAIVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIvDG----MLKLIDFGIAN----QMQP 673
Cdd:cd14662  76 EyAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLL-DGspapRLKICDFGYSKssvlHSQP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTsvvkdsqVGTVNYMPPEAIkdmsSSRE-NGKSKskispksDVWSLGCILYYMTYGKTPFQ------QIINQISKLHA 746
Cdd:cd14662 155 KST-------VGTPAYIAPEVL----SRKEyDGKVA-------DVWSCGVTLYVMLVGAYPFEdpddpkNFRKTIQRIMS 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 747 IidpnhEIEFPDIPE--KDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14662 217 V-----QYKIPDYVRvsQDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
531-789 2.57e-14

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: 74.03  E-value: 2.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVME-CGNID 608
Cdd:cd13978   1 LGSGGFGTVSKARHvSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERAR--HSYVLPLLGVCVERRSLGLVMEyMENGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWLKKKKSIDPWERKsyWKNMLEA------VHTIHQhGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTT---SV 678
Cdd:cd13978  79 LKSLLEREIQDVPWSLR--FRIIHEIalgmnfLHNMDP-PLLHHDLKPENILLDNHFhVKISDFGLSKLGMKSISanrRR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIkDMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQIsKLHAIIDPNHEIEFPD 758
Cdd:cd13978 156 GTENLGGTPIYMAPEAF-DDFNKKPT--------SKSDVYSFAIVIWAVLTRKEPFENAINPL-LIMQIVSKGDRPSLDD 225
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 759 IPE-------KDLQDVLKCCLKRDPKQRISIPELLAHP 789
Cdd:cd13978 226 IGRlkqienvQELISLMIRCWDGNPDARPTFLECLDRL 263
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
585-812 2.63e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 76.21  E-value: 2.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  585 IIRLYDYEITDQYIYMVMECGNI-DLNSWLKKK-KSIDPWERKS---YWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDG 658
Cdd:PTZ00267 127 IVKHFDDFKSDDKLLLIMEYGSGgDLNKQIKQRlKEHLPFQEYEvglLFYQIVLALDEVHSRKMMHRDLKSANiFLMPTG 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  659 MLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQ--- 735
Cdd:PTZ00267 207 IIKLGDFGFSKQYSDSVSLDVASSFCGTPYYLAPELWERKRYSKK-----------ADMWSLGVILYELLTLHRPFKgps 275
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722  736 --QIINQIskLHAIIDPnheieFPDIPEKDLQDVLKCCLKRDPKQRISIPELLahpyvqiqthpvnqmakgTTEEMKYV 812
Cdd:PTZ00267 276 qrEIMQQV--LYGKYDP-----FPCPVSSGMKALLDPLLSKNPALRPTTQQLL------------------HTEFLKYV 329
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
525-797 2.78e-14

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: 75.45  E-value: 2.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEA-DNQTLDSYRNEIAYLNKLQQHSdKIIRLYDYEITDQYIYMVM 602
Cdd:cd05618  22 FDLLRVIGRGSYAKVLLVrLKKTERIYAMKVVKKELVnDDEDIDWVQTEKHVFEQASNHP-FLVGLHSCFQTESRLFFVI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQP-DTTSV 678
Cdd:cd05618 101 EYVNGgDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLdSEGHIKLTDYGMCKEgLRPgDTTST 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VkdsqVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQI-------INQISKLHAIIdPN 751
Cdd:cd05618 181 F----CGTPNYIAPEILRGEDYG-----------FSVDWWALGVLMFEMMAGRSPFDIVgssdnpdQNTEDYLFQVI-LE 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 23308722 752 HEIEFPDIPEKDLQDVLKCCLKRDPKQRISipellAHP---YVQIQTHP 797
Cdd:cd05618 245 KQIRIPRSLSVKAASVLKSFLNKDPKERLG-----CHPqtgFADIQGHP 288
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
525-792 3.27e-14

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: 74.26  E-value: 3.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVN-LEEADNQTLDSYRneiaYLNKLQQHSDkIIRLYD-YEITDQYI--- 598
Cdd:cd06639  24 WDIIETIGKGTYGKVYKVTNKKDgSLAAVKILDpISDVDEEIEAEYN----ILRSLPNHPN-VVKFYGmFYKADQYVggq 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 -YMVMECGN----IDL-NSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQM 671
Cdd:cd06639  99 lWLVLELCNggsvTELvKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTtEGGVKLVDFGVSAQL 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QpdTTSVVKDSQVGTVNYMPPEAI---KDMSSSREngkskskisPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAII 748
Cdd:cd06639 179 T--SARLRRNTSVGTPFWMAPEVIaceQQYDYSYD---------ARCDVWSLGITAIELADGDPPLFD-MHPVKALFKIP 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 749 -DPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06639 247 rNPPPTLLNPEKWCRGFSHFISQCLIKDFEKRPSVTHLLEHPFIK 291
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
566-791 3.32e-14

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: 73.41  E-value: 3.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 566 DSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVMECGN--------IDLNSWLKKKKSIdpwerkSYWKNMLEAVHT 637
Cdd:cd14193  46 EEVKNEIEVMNQLN-HAN-LIQLYDAFESRNDIVLVMEYVDggelfdriIDENYNLTELDTI------LFIKQICEGIQY 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 638 IHQHGIVHSDLKPANFLIVD---GMLKLIDFGIANQMQPDTTSVVkdsQVGTVNYMPPEAIK-DMSSsrengkskskisP 713
Cdd:cd14193 118 MHQMYILHLDLKPENILCVSreaNQVKIIDFGLARRYKPREKLRV---NFGTPEFLAPEVVNyEFVS------------F 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 714 KSDVWSLGCILYYMTYGKTPF-----QQIINQIskLHAIIDPNHEiEFPDIPEkDLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd14193 183 PTDMWSLGVIAYMLLSGLSPFlgeddNETLNNI--LACQWDFEDE-EFADISE-EAKDFISKLLIKEKSWRMSASEALKH 258

                ...
gi 23308722 789 PYV 791
Cdd:cd14193 259 PWL 261
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
566-791 3.53e-14

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: 73.46  E-value: 3.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 566 DSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVMEC--GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGI 643
Cdd:cd14192  46 EEVKNEINIMNQLNHVN--LIQLYDAFESKTNLTLIMEYvdGGELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYI 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVD---GMLKLIDFGIANQMQPDTTSVVkdsQVGTVNYMPPEAIK-DMSSsrengkskskisPKSDVWS 719
Cdd:cd14192 124 LHLDLKPENILCVNstgNQIKIIDFGLARRYKPREKLKV---NFGTPEFLAPEVVNyDFVS------------FPTDMWS 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 720 LGCILYYMTYGKTPF-----QQIINQIskLHAIIDPNHEiEFPDIPEkDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14192 189 VGVITYMLLSGLSPFlgetdAETMNNI--VNCKWDFDAE-AFENLSE-EAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
567-791 3.56e-14

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: 74.53  E-value: 3.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 567 SYRnEIAYLNKLQQhsDKIIRLYDYEITD-QYIYMVMECGNIDLNSWLKKKksidPWERK---SYWKNMLEAVHTIHQHG 642
Cdd:cd07856  56 TYR-ELKLLKHLRH--ENIISLSDIFISPlEDIYFVTELLGTDLHRLLTSR----PLEKQfiqYFLYQILRGLKYVHSAG 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 643 IVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSVVKdsqvgTVNYMPPEAIkdMSSSRENgkskskisPKSDVWSLG 721
Cdd:cd07856 129 VIHRDLKPSNILVNENCdLKICDFGLARIQDPQMTGYVS-----TRYYRAPEIM--LTWQKYD--------VEVDIWSAG 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 722 CILYYMTYGKT--PFQQIINQISKLHAIID--PNHEIE----------FPDIPEKDLQ--------------DVLKCCLK 773
Cdd:cd07856 194 CIFAEMLEGKPlfPGKDHVNQFSIITELLGtpPDDVINticsentlrfVQSLPKRERVpfsekfknadpdaiDLLEKMLV 273
                       250
                ....*....|....*...
gi 23308722 774 RDPKQRISIPELLAHPYV 791
Cdd:cd07856 274 FDPKKRISAAEALAHPYL 291
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
525-790 3.81e-14

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 74.00  E-value: 3.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVnLEEADNQTLD--SYRnEIAYLNKLqqHSDKIIRLYDYEITDQYIYMV 601
Cdd:cd07846   3 YENLGLVGEGSYGMVMKCRHkETGQIVAIKKF-LESEDDKMVKkiAMR-EIKMLKQL--RHENLVNLIEVFRRKKRWYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECgnID---LNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQpdTTS 677
Cdd:cd07846  79 FEF--VDhtvLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSqSGVVKLCDFGFARTLA--APG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPE-AIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKtPFQQIINQISKLHAIID------P 750
Cdd:cd07846 155 EVYTDYVATRWYRAPElLVGDTKYGK-----------AVDVWAVGCLVTEMLTGE-PLFPGDSDIDQLYHIIKclgnliP 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 751 NHEIEF-----------PDIPEKD------------LQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07846 223 RHQELFqknplfagvrlPEVKEVEplerrypklsgvVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
530-791 4.82e-14

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: 73.87  E-value: 4.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 530 QIGSGgSSKVFQVLNEK---KQIyAIKYVNLEEADNQTLdsYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVMECGN 606
Cdd:cd06659  28 KIGEG-STGVVCIAREKhsgRQV-AVKMMDLRKQQRREL--LFNEVVIMRDYQHPN--VVEMYKSYLVGEELWVLMEYLQ 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSvvKDSQVG 685
Cdd:cd06659 102 GGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLtLDGRVKLSDFGFCAQISKDVPK--RKSLVG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 686 TVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAIIDPNHEIEFPDIPEkd 763
Cdd:cd06659 180 TPYWMAPEVISRCPYGTE-----------VDIWSLGIMVIEMVDGEPPYfsDSPVQAMKRLRDSPPPKLKNSHKASPV-- 246
                       250       260
                ....*....|....*....|....*...
gi 23308722 764 LQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06659 247 LRDFLERMLVRDPQERATAQELLDHPFL 274
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
527-785 7.13e-14

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: 73.08  E-value: 7.13e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILK-QIGSGGSSKVF-----QVLNEK-KQIYAIKyvNLEEADNQTLDSYRNEIAYLNKLQ-QHsdkIIRLYDYEITDQYI 598
Cdd:cd05092   8 VLKwELGEGAFGKVFlaechNLLPEQdKMLVAVK--ALKEATESARQDFQREAELLTVLQhQH---IVRFYGVCTEGEPL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVME-CGNIDLNSWLKKK----KSIDPWERKSYWK----NMLEAVHTIHQHGI-------VHSDLKPANFLIVDGML-K 661
Cdd:cd05092  83 IMVFEyMRHGDLNRFLRSHgpdaKILDGGEGQAPGQltlgQMLQIASQIASGMVylaslhfVHRDLATRNCLVGQGLVvK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 662 LIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQIINQ 740
Cdd:cd05092 163 IGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTES-----------DIWSFGVVLWEIfTYGKQPWYQLSNT 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23308722 741 isklHAI--IDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05092 232 ----EAIecITQGRELERPRTCPPEVYAIMQGCWQREPQQRHSIKDI 274
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
638-792 7.36e-14

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 73.55  E-value: 7.36e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 638 IHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQM--QPDTTSVVKDSQVGTVNYMPPEAikdMSSSREngkskskISPK 714
Cdd:cd07855 125 IHSANVIHRDLKPSNLLVnENCELKIGDFGMARGLctSPEEHKYFMTEYVATRWYRAPEL---MLSLPE-------YTQA 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 715 SDVWSLGCILYYMTY------GK--------------TPFQQIINQI--SKLHAIID--PNHE-IEFPDI-PEKDLQ--D 766
Cdd:cd07855 195 IDMWSVGCIFAEMLGrrqlfpGKnyvhqlqliltvlgTPSQAVINAIgaDRVRRYIQnlPNKQpVPWETLyPKADQQalD 274
                       170       180
                ....*....|....*....|....*.
gi 23308722 767 VLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd07855 275 LLSQMLRFDPSERITVAEALQHPFLA 300
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
525-815 7.50e-14

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: 73.91  E-value: 7.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVNlEEADNQT--LDSYRNEIayLNKLQQHSDkIIRLYDYEITD------ 595
Cdd:cd07876  23 YQQLKPIGSGAQGIVCAAFDTVLGInVAVKKLS-RPFQNQThaKRAYRELV--LLKCVNHKN-IISLLNVFTPQksleef 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVMECgnIDLNSWLKKKKSIDPwERKSYW-KNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIAnqmQP 673
Cdd:cd07876  99 QDVYLVMEL--MDANLCQVIHMELDH-ERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIVVkSDCTLKILDFGLA---RT 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKDSQVGTVNYMPPEAIKDMsSSRENgkskskispkSDVWSLGCILYYMTYGKTPFQQI--INQISKLHAII-DP 750
Cdd:cd07876 173 ACTNFMMTPYVVTRYYRAPEVILGM-GYKEN----------VDIWSVGCIMGELVKGSVIFQGTdhIDQWNKVIEQLgTP 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 751 NHEIE-------------------------FPD--IPEKDLQDVLKCCLKR---------DPKQRISIPELLAHPYVQIQ 794
Cdd:cd07876 242 SAEFMnrlqptvrnyvenrpqypgisfeelFPDwiFPSESERDKLKTSQARdllskmlviDPDKRISVDEALRHPYITVW 321
                       330       340
                ....*....|....*....|....*..
gi 23308722 795 THPVN------QMAKGTTEEMKYVLGQ 815
Cdd:cd07876 322 YDPAEaeapppQIYDAQLEEREHAIEE 348
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
525-779 8.61e-14

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 72.82  E-value: 8.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEE-ADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd14209   3 FDRIKTLGTGSFGRVMLVRHkETGNYYAMKILDKQKvVKLKQVEHTLNEKRILQAI--NFPFLVKLEYSFKDNSNLYMVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E--CGNiDLNSWLKKKKSI-DPWERkSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSV 678
Cdd:cd14209  81 EyvPGG-EMFSHLRRIGRFsEPHAR-FYAAQIVLAFEYLHSLDLIYRDLKPENLLIdQQGYIKVTDFGFAKRVKGRTWTL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VkdsqvGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFqqIINQISKLHAIIdPNHEIEFPD 758
Cdd:cd14209 159 C-----GTPEYLAPEIILSKGYNK-----------AVDWWALGVLIYEMAAGYPPF--FADQPIQIYEKI-VSGKVRFPS 219
                       250       260
                ....*....|....*....|.
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd14209 220 HFSSDLKDLLRNLLQVDLTKR 240
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
524-790 9.52e-14

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: 73.09  E-value: 9.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 524 IYSILKQIGSGGSSKVFQVL---NEKKQIYAIKYVnleEADNQTLD-----SYRnEIAYLNKLqqHSDKIIRLYD--YEI 593
Cdd:cd07842   1 KYEIEGCIGRGTYGRVYKAKrknGKDGKEYAIKKF---KGDKEQYTgisqsACR-EIALLREL--KHENVVSLVEvfLEH 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQYIYMVMECGNIDLNSWLK-----KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-----DGMLKLI 663
Cdd:cd07842  75 ADKSVYLLFDYAEHDLWQIIKfhrqaKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVMgegpeRGVVKIG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 664 DFGIANQMQ-PDTTSVVKDSQVGTVNYMPPE----------AIkdmsssrengkskskispksDVWSLGCILYYMT---- 728
Cdd:cd07842 155 DLGLARLFNaPLKPLADLDPVVVTIWYRAPElllgarhytkAI--------------------DIWAIGCIFAELLtlep 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 729 --YGK-------TPFQQiiNQISKLHAIIDPNHEIEFPDI---PE-KDLQ----------------------------DV 767
Cdd:cd07842 215 ifKGReakikksNPFQR--DQLERIFEVLGTPTEKDWPDIkkmPEyDTLKsdtkastypnsllakwmhkhkkpdsqgfDL 292
                       330       340
                ....*....|....*....|...
gi 23308722 768 LKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07842 293 LRKLLEYDPTKRITAEEALEHPY 315
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
525-791 1.05e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 72.91  E-value: 1.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLE-EADNQTLDSYRnEIAYLNKLQQHSdkIIRLYDYEITDQ------ 596
Cdd:cd07864   9 FDIIGIIGEGTYGQVYKAKDKDTgELVALKKVRLDnEKEGFPITAIR-EIKILRQLNHRS--VVNLKEIVTDKQdaldfk 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 ----YIYMVMECGNIDLNSWLKKKK-SIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA-- 668
Cdd:cd07864  86 kdkgAFYLVFEYMDHDLMGLLESGLvHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNkGQIKLADFGLArl 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 ---NQMQPDTTSVVkdsqvgTVNYMPPEAIkdMSSSRengkskskISPKSDVWSLGCILYYMtYGKTPFQQIINQISKLH 745
Cdd:cd07864 166 ynsEESRPYTNKVI------TLWYRPPELL--LGEER--------YGPAIDVWSCGCILGEL-FTKKPIFQANQELAQLE 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 746 AII----DPNHEI-------------------------EFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd07864 229 LISrlcgSPCPAVwpdviklpyfntmkpkkqyrrrlreEFSFIPTPAL-DLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
525-788 1.13e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 72.14  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV---LNEKkqIYAIKYV--NLEEADNqtldsyrnEIAYLNKLQQhsDKIIRLY------DYEI 593
Cdd:cd14047   8 FKEIELIGSGGFGQVFKAkhrIDGK--TYAIKRVklNNEKAER--------EVKALAKLDH--PNIVRYNgcwdgfDYDP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQ----------YIYMVME-CGNIDLNSWLKK--KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGM 659
Cdd:cd14047  76 ETSssnssrsktkCLFIQMEfCEKGTLESWIEKrnGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNiFLVDTGK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 660 LKLIDFGIANQMqpdTTSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYG-------KT 732
Cdd:cd14047 156 VKIGDFGLVTSL---KNDGKRTKSKGTLSYMSPEQISSQDYGKE-----------VDIYALGLILFELLHVcdsafekSK 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 733 PFQQIINQisKLHAIIDPNHEIEFPdipekdlqdVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd14047 222 FWTDLRNG--ILPDIFDKRYKIEKT---------IIKKMLSKKPEDRPNASEILRT 266
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
535-797 1.23e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 72.38  E-value: 1.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 535 GSSKVFQVLNEK---KQIyAIKYVNLEEADNQTLdsYRNEIAYLNklQQHSDKIIRLYDYEITDQYIYMVMECGNIDLNS 611
Cdd:cd06658  33 GSTGIVCIATEKhtgKQV-AVKKMDLRKQQRREL--LFNEVVIMR--DYHHENVVDMYNSYLVGDELWVVMEFLEGGALT 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 612 WLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSvvKDSQVGTVNYM 690
Cdd:cd06658 108 DIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTsDGRIKLSDFGFCAQVSKEVPK--RKSLVGTPYWM 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 691 PPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQI-SKLHAIIDPNHEIEfpdipeKDL 764
Cdd:cd06658 186 APEVISRLPYGTE-----------VDIWSLGIMVIEMIDGEPPYfneppLQAMRRIrDNLPPRVKDSHKVS------SVL 248
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 765 QDVLKCCLKRDPKQRISIPELLAHPYVQIQTHP 797
Cdd:cd06658 249 RGFLDLMLVREPSQRATAQELLQHPFLKLAGPP 281
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
551-790 1.29e-13

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: 71.67  E-value: 1.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 551 AIKYVNLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVMECGNID-LNSWLKKKKSIDPwER--KSY 627
Cdd:cd14082  32 AIKVIDKLRFPTKQESQLRNEVAILQQL--SHPGVVNLECMFETPERVFVVMEKLHGDmLEMILSSEKGRLP-ERitKFL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 628 WKNMLEAVHTIHQHGIVHSDLKPANFLIVDG----MLKLIDFGIANQMQPDTtsvVKDSQVGTVNYMPPEAIKDMSSSRe 703
Cdd:cd14082 109 VTQILVALRYLHSKNIVHCDLKPENVLLASAepfpQVKLCDFGFARIIGEKS---FRRSVVGTPAYLAPEVLRNKGYNR- 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 704 ngkskskispKSDVWSLGCILYYMTYGKTPFQQ---IINQISklhaiidpNHEIEFPDIP----EKDLQDVLKCCLKRDP 776
Cdd:cd14082 185 ----------SLDMWSVGVIIYVSLSGTFPFNEdedINDQIQ--------NAAFMYPPNPwkeiSPDAIDLINNLLQVKM 246
                       250
                ....*....|....
gi 23308722 777 KQRISIPELLAHPY 790
Cdd:cd14082 247 RKRYSVDKSLSHPW 260
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
636-797 1.29e-13

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: 72.39  E-value: 1.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 636 HTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTsvVKdSQVGTVNYMPPEAIKDMSSSrengkskskisPK 714
Cdd:cd05605 116 EHLHSERIVYRDLKPENILLDDhGHVRISDLGLAVEIPEGET--IR-GRVGTVGYMAPEVVKNERYT-----------FS 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 715 SDVWSLGCILYYMTYGKTPFQQIINQISKLHaiIDPNHEIEFPDIPEKDLQDVLKCC---LKRDPKQRISIPELLAHpyv 791
Cdd:cd05605 182 PDWWGLGCLIYEMIEGQAPFRARKEKVKREE--VDRRVKEDQEEYSEKFSEEAKSICsqlLQKDPKTRLGCRGEGAE--- 256

                ....*.
gi 23308722 792 QIQTHP 797
Cdd:cd05605 257 DVKSHP 262
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
598-790 1.36e-13

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 73.15  E-value: 1.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKnMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTT 676
Cdd:cd07877  97 VYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQ-ILRGLKYIHSADIIHRDLKPSNLAVnEDCELKILDFGLARHTDDEMT 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVvkdsqVGTVNYMPPEAIKDMSSSRENgkskskispkSDVWSLGCILYYMTYGKT--PFQQIINQISKLHAIID----- 749
Cdd:cd07877 176 GY-----VATRWYRAPEIMLNWMHYNQT----------VDIWSVGCIMAELLTGRTlfPGTDHIDQLKLILRLVGtpgae 240
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23308722 750 -----PNHEIE-----FPDIPEKDLQDV-----------LKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd07877 241 llkkiSSESARnyiqsLTQMPKMNFANVfiganplavdlLEKMLVLDSDKRITAAQALAHAY 302
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
525-790 1.62e-13

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: 72.99  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYVNLEEADNQTLDSY----RNEIAyLNKlqqhSDKIIRLYDYEITDQYIY 599
Cdd:cd05610   6 FVIVKPISRGAFGKVYLGRkKNNSKLYAVKVVKKADMINKNMVHQvqaeRDALA-LSK----SPFIVHLYYSLQSANNVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA-------- 668
Cdd:cd05610  81 LVMEylIGG-DVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNeGHIKLTDFGLSkvtlnrel 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQMQPDTT-SVVKDSQ------------------------------------------VGTVNYMPPEAIkdmsSSRENG 705
Cdd:cd05610 160 NMMDILTTpSMAKPKNdysrtpgqvlslisslgfntptpyrtpksvrrgaarvegeriLGTPDYLAPELL----LGKPHG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 706 kskskisPKSDVWSLGCILYYMTYGKTPF-----QQIINQISklhaiidpNHEIEFPDIPEK---DLQDVLKCCLKRDPK 777
Cdd:cd05610 236 -------PAVDWWALGVCLFEFLTGIPPFndetpQQVFQNIL--------NRDIPWPEGEEElsvNAQNAIEILLTMDPT 300
                       330
                ....*....|...
gi 23308722 778 QRISIPELLAHPY 790
Cdd:cd05610 301 KRAGLKELKQHPL 313
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
527-787 1.86e-13

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


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 71.61  E-value: 1.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQ------VLNEKKQIYAIKYVNleeaDNqtlDSYRNEIAYLNKL----QQHSDKIIRLYDYEITDQ 596
Cdd:cd05032  10 LIRELGQGSFGMVYEglakgvVKGEPETRVAIKTVN----EN---ASMRERIEFLNEAsvmkEFNCHHVVRLLGVVSTGQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVME-CGNIDLNSWLKKKKS---------IDPWERKSYW-----KNM--LEAVHtihqhgIVHSDLKPANFLIV-DG 658
Cdd:cd05032  83 PTLVVMElMAKGDLKSYLRSRRPeaennpglgPPTLQKFIQMaaeiaDGMayLAAKK------FVHRDLAARNCMVAeDL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 659 MLKLIDFGIANQMQpDTTSVVKDSQ-VGTVNYMPPEAIKD---MSSSrengkskskispksDVWSLGCILYYM-TYGKTP 733
Cdd:cd05032 157 TVKIGDFGMTRDIY-ETDYYRKGGKgLLPVRWMAPESLKDgvfTTKS--------------DVWSFGVVLWEMaTLAEQP 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 23308722 734 FQQIINQiSKLHAIIDPNHeIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd05032 222 YQGLSNE-EVLKFVIDGGH-LDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVS 273
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
525-792 1.87e-13

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: 72.34  E-value: 1.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVnlEEADNQT--LDSYRnEIAYLNKLQQhsDKIIRLYDYEITDQY---- 597
Cdd:cd07849   7 YQNLSYIGEGAYGMVCSAVHKpTGQKVAIKKI--SPFEHQTycLRTLR-EIKILLRFKH--ENIIGILDIQRPPTFesfk 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 -IYMVMECGNIDLNSWLKKKK-SIDPWERKSYwkNMLEAVHTIHQHGIVHSDLKPANFLI---VDgmLKLIDFGIANQMQ 672
Cdd:cd07849  82 dVYIVQELMETDLYKLIKTQHlSNDHIQYFLY--QILRGLKYIHSANVLHRDLKPSNLLLntnCD--LKICDFGLARIAD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 P--DTTSVVKDsQVGTVNYMPPEAikdMSSSREngkskskISPKSDVWSLGCILYYMTYGK------------------- 731
Cdd:cd07849 158 PehDHTGFLTE-YVATRWYRAPEI---MLNSKG-------YTKAIDIWSVGCILAEMLSNRplfpgkdylhqlnlilgil 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 732 -TP----FQQIINQISKLHAIIDPNH-----EIEFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd07849 227 gTPsqedLNCIISLKARNYIKSLPFKpkvpwNKLFPNADPKAL-DLLDKMLTFNPHKRITVEEALAHPYLE 296
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
528-797 1.95e-13

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: 72.30  E-value: 1.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVfqVLNEKK---QIYAIKY----VNLEEADNQTLDSYRNeiaYLNKLQQHSDKIIRLYDYEITDQyIYM 600
Cdd:cd05604   1 LKVIGKGSFGKV--LLAKRKrdgKYYAVKVlqkkVILNRKEQKHIMAERN---VLLKNVKHPFLVGLHYSFQTTDK-LYF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ--MQPDTT 676
Cdd:cd05604  75 VLDFVNGgELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLdSQGHIVLTDFGLCKEgiSNSDTT 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVkdsqVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF-----QQIINQIskLHAIIDPN 751
Cdd:cd05604 155 TTF----CGTPEYLAPEVIRKQPYDN-----------TVDWWCLGSVLYEMLYGLPPFycrdtAEMYENI--LHKPLVLR 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 752 HEIEFPDIpekdlqDVLKCCLKRDPKQRISIPEllahPYVQIQTHP 797
Cdd:cd05604 218 PGISLTAW------SILEELLEKDRQLRLGAKE----DFLEIKNHP 253
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
521-792 2.01e-13

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: 71.95  E-value: 2.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 521 KGRIYSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRnEIAYLNKLQqHSDkIIRLYDYEITDQYIY 599
Cdd:cd07872   4 KMETYIKLEKLGEGTYATVFKGRSKlTENLVALKEIRLEHEEGAPCTAIR-EVSLLKDLK-HAN-IVTLHDIVHTDKSLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDLNSWLKKKKSIDPWER-KSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTS 677
Cdd:cd07872  81 LVFEYLDKDLKQYMDDCGNIMSMHNvKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINErGELKLADFGLARAKSVPTKT 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VvkDSQVGTVNYMPPEAIkdMSSSRENgkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQiSKLHAI---------- 747
Cdd:cd07872 161 Y--SNEVVTLWYRPPDVL--LGSSEYS--------TQIDMWGVGCIFFEMASGRPLFPGSTVE-DELHLIfrllgtptee 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 748 ----IDPNHEIEFPDIPEKDLQ--------------DVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd07872 228 twpgISSNDEFKNYNFPKYKPQplinhaprldtegiELLTKFLQYESKKRISAEEAMKHAYFR 290
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
520-785 2.24e-13

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: 71.58  E-value: 2.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 520 VKGRIYSILKQIGSGGSSKVFQV----LNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITD 595
Cdd:cd05094   2 IKRRDIVLKRELGEGAFGKVFLAecynLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQH--DHIVKFYGVCGDG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVME-CGNIDLNSWLKKKKS-----IDPWERKSYWK----NMLE--------AVHTIHQHgIVHSDLKPANFLIVD 657
Cdd:cd05094  80 DPLIMVFEyMKHGDLNKFLRAHGPdamilVDGQPRQAKGElglsQMLHiatqiasgMVYLASQH-FVHRDLATRNCLVGA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 658 GML-KLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQ 735
Cdd:cd05094 159 NLLvKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTES-----------DVWSFGVILWEIfTYGKQPWF 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 736 QIINqiSKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05094 228 QLSN--TEVIECITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEI 275
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
529-797 2.50e-13

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: 72.07  E-value: 2.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEA-DNQTLDSYRNEIAYLNKLQQHSdKIIRLYDYEITDQYIYMVMECGN 606
Cdd:cd05588   1 RVIGRGSYAKVLMVeLKKTKRIYAMKVIKKELVnDDEDIDWVQTEKHVFETASNHP-FLVGLHSCFQTESRLFFVIEFVN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 I-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQP-DTTSVVkds 682
Cdd:cd05588  80 GgDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLdSEGHIKLTDYGMCKEgLRPgDTTSTF--- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 qVGTVNYMPPEAIK--DMSSSrengkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKlhaiiDPNHE-IEFPDI 759
Cdd:cd05588 157 -CGTPNYIAPEILRgeDYGFS-------------VDWWALGVLMFEMLAGRSPFDIVGSSDNP-----DQNTEdYLFQVI 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 23308722 760 PEKDL----------QDVLKCCLKRDPKQRisipeLLAHP---YVQIQTHP 797
Cdd:cd05588 218 LEKPIriprslsvkaASVLKGFLNKNPAER-----LGCHPqtgFADIQSHP 263
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
520-785 2.50e-13

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: 71.34  E-value: 2.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 520 VKGRIYSILKQIGSGGSSKVFQ------VLNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEI 593
Cdd:cd05049   2 IKRDTIVLKRELGEGAFGKVFLgecynlEPEQDKMLVAVKTLK-DASSPDARKDFEREAELLTNLQH--ENIVKFYGVCT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQYIYMV---MECGniDLNSWLKKK-------KSIDPWERKSYWKNMLEAVHTI--------HQHgIVHSDLKPANFLI 655
Cdd:cd05049  79 EGDPLLMVfeyMEHG--DLNKFLRSHgpdaaflASEDSAPGELTLSQLLHIAVQIasgmvylaSQH-FVHRDLATRNCLV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 656 VDGML-KLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTP 733
Cdd:cd05049 156 GTNLVvKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTES-----------DVWSFGVVLWEIfTYGKQP 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 23308722 734 FQQIINqiSKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05049 225 WFQLSN--TEVIECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDI 274
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
531-788 2.98e-13

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: 70.82  E-value: 2.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQI-YAIKYVNleeADNQTLDSYRNEIAYLNKLQQHSDkIIRLYD--YEITDQYIyMVME-CGN 606
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGTkMALKFVP---KPSTKLKDFLREYNISLELSVHPH-IIKTYDvaFETEDYYV-FAQEyAPY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG---MLKLIDFGianqMQPDTTSVVKdSQ 683
Cdd:cd13987  76 GDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKdcrRVKLCDFG----LTRRVGSTVK-RV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 684 VGTVNYMPPEaikdMSSSRENGksKSKISPKSDVWSLGCILYYMTYGKTPFQQIinqisklhAIIDPNHEiEF------- 756
Cdd:cd13987 151 SGTIPYTAPE----VCEAKKNE--GFVVDPSIDVWAFGVLLFCCLTGNFPWEKA--------DSDDQFYE-EFvrwqkrk 215
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 757 ----PDIPEKDLQDVLKCC---LKRDPKQRISIPELLAH 788
Cdd:cd13987 216 ntavPSQWRRFTPKALRMFkklLAPEPERRCSIKEVFKY 254
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
531-780 3.48e-13

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 71.09  E-value: 3.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKV--FQVLNeKKQIYAIKYVN---LEEADNQTLDSYRNEIayLNKLqqHSDKIIRL-YDYEiTDQYIYMVMEC 604
Cdd:cd05607  10 LGKGGFGEVcaVQVKN-TGQMYACKKLDkkrLKKKSGEKMALLEKEI--LEKV--NSPFIVSLaYAFE-TKTHLCLVMSL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 ---GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMqPDTTSVVK 680
Cdd:cd05607  84 mngGDLKYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDnGNCRLSDLGLAVEV-KEGKPITQ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 dsQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQQIINQISK---LHAIIDPNHEIEFP 757
Cdd:cd05607 163 --RAGTNGYMAPEILKEESYS-----------YPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKeelKRRTLEDEVKFEHQ 229
                       250       260
                ....*....|....*....|...
gi 23308722 758 DIPEkDLQDVLKCCLKRDPKQRI 780
Cdd:cd05607 230 NFTE-EAKDICRLFLAKKPENRL 251
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
523-803 3.49e-13

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 72.76  E-value: 3.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  523 RIYSILKQIGSGGSSKVFQV--LNEKKQIyAIKYVnLEEAdnqtldSYRNEIAYLNKLQQHSDkIIRLYDYEITDQ---- 596
Cdd:PTZ00036  66 KSYKLGNIIGNGSFGVVYEAicIDTSEKV-AIKKV-LQDP------QYKNRELLIMKNLNHIN-IIFLKDYYYTECfkkn 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  597 ----YIYMVMECGNIDLNSWLK----KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG--MLKLIDFG 666
Cdd:PTZ00036 137 ekniFLNVVMEFIPQTVHKYMKhyarNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNthTLKLCDFG 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  667 IANQMQPDTTSVvkdSQVGTVNYMPPEAIKDMSSsrengkskskISPKSDVWSLGCILYYMTYGKTPF--QQIINQISKL 744
Cdd:PTZ00036 217 SAKNLLAGQRSV---SYICSRFYRAPELMLGATN----------YTTHIDLWSLGCIIAEMILGYPIFsgQSSVDQLVRI 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  745 -----------HAIIDPNH-EIEFPDIPEKDLQDV------------LKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQ 800
Cdd:PTZ00036 284 iqvlgtptedqLKEMNPNYaDIKFPDVKPKDLKKVfpkgtpddainfISQFLKYEPLKRLNPIEALADPFFDDLRDPCIK 363

                 ...
gi 23308722  801 MAK 803
Cdd:PTZ00036 364 LPK 366
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
529-791 4.03e-13

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: 70.34  E-value: 4.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTLDSYRNEIAYLnKLQQHSDKIIRLYDYEITDQYIYMVMEC--- 604
Cdd:cd14198  14 KELGRGKFAVVRQCISKSTgQEYAAKFLKKRRRGQDCRAEILHEIAVL-ELAKSNPRVVNLHEVYETTSEIILILEYaag 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 GNI------DLNSWLKKKKSIdpwerkSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD----GMLKLIDFGIANQMQpd 674
Cdd:cd14198  93 GEIfnlcvpDLAEMVSENDII------RLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiyplGDIKIVDFGMSRKIG-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 tTSVVKDSQVGTVNYMPPEAIKdmsssrengksKSKISPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHaiID 749
Cdd:cd14198 165 -HACELREIMGTPEYLAPEILN-----------YDPITTATDMWNIGVIAYMLLTHESPFvgednQETFLNISQVN--VD 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 750 PNHEIeFPDIPEKdLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14198 231 YSEET-FSSVSQL-ATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
525-810 4.24e-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: 70.83  E-value: 4.24e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQI-GSGGSSKVFQVLNEKK-QIYAIKYVnleeadnQTLDSYRNEIAYLNKLQQ--HSDKIIRLYD--YEiTDQYI 598
Cdd:cd14170   3 YKVTSQVlGLGINGKVLQIFNKRTqEKFALKML-------QDCPKARREVELHWRASQcpHIVRIVDVYEnlYA-GRKCL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMEC-GNIDLNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIANQM 671
Cdd:cd14170  75 LIVMEClDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTskrpNAILKLTDFGFAKET 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 qpdTTSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFqqiinqISKLHAIIDPN 751
Cdd:cd14170 155 ---TSHNSLTTPCYTPYYVAPEVLGPEKYDKS-----------CDMWSLGVIMYILLCGYPPF------YSNHGLAISPG 214
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 752 H-------EIEFPDiPE-----KDLQDVLKCCLKRDPKQRISIPELLAHPYVQiQTHPVNQMAKGTTEEMK 810
Cdd:cd14170 215 MktrirmgQYEFPN-PEwsevsEEVKMLIRNLLKTEPTQRMTITEFMNHPWIM-QSTKVPQTPLHTSRVLK 283
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
589-780 4.62e-13

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: 71.19  E-value: 4.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 589 YDYEITDQYIYmVMECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFG 666
Cdd:cd05595  62 YAFQTHDRLCF-VMEYANGgELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLdKDGHIKITDFG 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 667 IANQMQPDTTSVvkDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFqqiINQI-SKLH 745
Cdd:cd05595 141 LCKEGITDGATM--KTFCGTPEYLAPEVLEDNDYGR-----------AVDWWGLGVVMYEMMCGRLPF---YNQDhERLF 204
                       170       180       190
                ....*....|....*....|....*....|....*
gi 23308722 746 AIIdPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05595 205 ELI-LMEEIRFPRTLSPEAKSLLAGLLKKDPKQRL 238
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
523-792 5.38e-13

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: 70.82  E-value: 5.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 523 RIYSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLE-EADNQTLDSYRNEIAYLNKLQqHSDKIIRLYDYeITDQYIYM 600
Cdd:cd06634  15 KLFSDLREIGHGSFGAVYFARDvRNNEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQKLR-HPNTIEYRGCY-LREHTAWL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPdttsv 678
Cdd:cd06634  93 VMEyCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEpGLVKLGDFGSASIMAP----- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vKDSQVGTVNYMPPEAIKDMSSSRENGkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFPD 758
Cdd:cd06634 168 -ANSFVGTPYWMAPEVILAMDEGQYDG--------KVDVWSLGITCIELAERKPPLFN-MNAMSALYHIAQNESPALQSG 237
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd06634 238 HWSEYFRNFVDSCLQKIPQDRPTSDVLLKHRFLL 271
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
525-789 5.87e-13

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 72.21  E-value: 5.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  525 YSILKQIGSGGSSKVfqvLNEKK----QIYAIKYVNLEEADNQTLDSYRNEIA------YLNKLQQHSDKIIRLYDYEIT 594
Cdd:PTZ00283  34 YWISRVLGSGATGTV---LCAKRvsdgEPFAVKVVDMEGMSEADKNRAQAEVCcllncdFFSIVKCHEDFAKKDPRNPEN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  595 DQYIYMVMECGNI-DLNSWLKKK-KSIDPW---ERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIA 668
Cdd:PTZ00283 111 VLMIALVLDYANAgDLRQEIKSRaKTNRTFrehEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCsNGLVKLGDFGFS 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  669 NQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPF-----QQIINQisK 743
Cdd:PTZ00283 191 KMYAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKK-----------ADMFSLGVLLYELLTLKRPFdgenmEEVMHK--T 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 23308722  744 LHAIIDPnheieFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHP 789
Cdd:PTZ00283 258 LAGRYDP-----LPPSISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
525-801 6.69e-13

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: 70.97  E-value: 6.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVL-NEKKQIYAIKYVNleEADNQTLDSYR--NEIAYLnKLQQHSD----KIIRLYDYEITDQY 597
Cdd:cd07859   2 YKIQEVIGKGSYGVVCSAIdTHTGEKVAIKKIN--DVFEHVSDATRilREIKLL-RLLRHPDiveiKHIMLPPSRREFKD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDT- 675
Cdd:cd07859  79 IYVVFELMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILAnADCKLKICDFGLARVAFNDTp 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVVKDSQVGTVNYMPPEAIkdmsssrenGKSKSKISPKSDVWSLGCILYYMTYGK--------------------TPFQ 735
Cdd:cd07859 159 TAIFWTDYVATRWYRAPELC---------GSFFSKYTPAIDIWSIGCIFAEVLTGKplfpgknvvhqldlitdllgTPSP 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 736 QIINQISKLHA-----IIDPNHEI----EFPDIPEKDLqDVLKCCLKRDPKQRISIPELLAHPYV--------QIQTHPV 798
Cdd:cd07859 230 ETISRVRNEKArrylsSMRKKQPVpfsqKFPNADPLAL-RLLERLLAFDPKDRPTAEEALADPYFkglakverEPSAQPI 308

                ...
gi 23308722 799 NQM 801
Cdd:cd07859 309 TKL 311
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
638-790 6.79e-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: 69.77  E-value: 6.79e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 638 IHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANqmqpDTTSVVKDSQVGTVNYMPPEAIK-----DMSSsrengkskski 711
Cdd:cd05606 114 MHNRFIVYRDLKPANILLDEhGHVRISDLGLAC----DFSKKKPHASVGTHGYMAPEVLQkgvayDSSA----------- 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 712 spksDVWSLGCILYYMTYGKTPFQQiiNQISKLHAI--IDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRI-----SIPE 784
Cdd:cd05606 179 ----DWFSLGCMLYKLLKGHSPFRQ--HKTKDKHEIdrMTLTMNVELPDSFSPELKSLLEGLLQRDVSKRLgclgrGATE 252

                ....*.
gi 23308722 785 LLAHPY 790
Cdd:cd05606 253 VKEHPF 258
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
525-804 6.97e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 72.85  E-value: 6.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   525 YSILKQIGSGGSSKVFQVLNEKKQIY----AIKYVNLEEADNQTLDSyrnEIAYLNKLQQHSdkIIRLYDYEIT--DQYI 598
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFfcwkAISYRGLKEREKSQLVI---EVNVMRELKHKN--IVRYIDRFLNkaNQKL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   599 YMVME-CGNIDLNSWLKK-KKSIDPWERKSY---WKNMLEAVHTIHQ-------HGIVHSDLKPANFLIVDGM------- 659
Cdd:PTZ00266   90 YILMEfCDAGDLSRNIQKcYKMFGKIEEHAIvdiTRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIrhigkit 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   660 -----------LKLIDFGIANQMQPDTTSvvkDSQVGTVNYMPPEAIKDMSSSRENgkskskispKSDVWSLGCILYYMT 728
Cdd:PTZ00266  170 aqannlngrpiAKIGDFGLSKNIGIESMA---HSCVGTPYYWSPELLLHETKSYDD---------KSDMWALGCIIYELC 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   729 YGKTPFQQiINQISKLHAIIDPNheiefPDIP----EKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQTHPVNQMAKG 804
Cdd:PTZ00266  238 SGKTPFHK-ANNFSQLISELKRG-----PDLPikgkSKELNILIKNLLNLSAKERPSALQCLGYQIIKNVGPPVGAAGGG 311
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
643-791 7.18e-13

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: 69.91  E-value: 7.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 643 IVHSDLKPANFLI-VDGMLKLIDFGIANQMqpdTTSVVKdSQVGTVNYMPPEAIkdmsSSRENGKSKskispksDVWSLG 721
Cdd:cd06619 116 ILHRDVKPSNMLVnTRGQVKLCDFGVSTQL---VNSIAK-TYVGTNAYMAPERI----SGEQYGIHS-------DVWSLG 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 722 CILYYMTYGKTPFQQII-NQ-----ISKLHAIIDPnheiEFPDIPEKDLQDV----LKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06619 181 ISFMELALGRFPYPQIQkNQgslmpLQLLQCIVDE----DPPVLPVGQFSEKfvhfITQCMRKQPKERPAPENLMDHPFI 256
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
531-790 7.71e-13

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: 70.68  E-value: 7.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVL-NEKKQIYAIKYVNleeadnQTLDSYRNEIAYL----NKLQQHSDK----IIRLYDYEITDQYIYMV 601
Cdd:cd05586   1 IGKGTFGQVYQVRkKDTRRIYAMKVLS------KKVIVAKKEVAHTigerNILVRTALDespfIVGLKFSFQTPTDLYLV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ME--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGI--ANQMQPDTT 676
Cdd:cd05586  75 TDymSGG-ELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLdANGHIALCDFGLskADLTDNKTT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVkdsqVGTVNYMPPEAIKDmsssrENGkskskISPKSDVWSLGCILYYMTYGKTPFQQIINQisKLHAIIDPNhEIEF 756
Cdd:cd05586 154 NTF----CGTTEYLAPEVLLD-----EKG-----YTKMVDFWSLGVLVFEMCCGWSPFYAEDTQ--QMYRNIAFG-KVRF 216
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 757 P-DIPEKDLQDVLKCCLKRDPKQRI----SIPELLAHPY 790
Cdd:cd05586 217 PkDVLSDEGRSFVKGLLNRNPKHRLgahdDAVELKEHPF 255
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
596-792 7.73e-13

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: 70.93  E-value: 7.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPD 674
Cdd:cd07853  77 EEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVnSNCVLKICDFGLARVEEPD 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 tTSVVKDSQVGTVNYMPPEAIkdMSSSRENGkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIID----P 750
Cdd:cd07853 157 -ESKHMTQEVVTQYYRAPEIL--MGSRHYTS--------AVDIWSVGCIFAELLGRRILFQA-QSPIQQLDLITDllgtP 224
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 751 N-------------HEIEFPDIPeKDLQ--------------DVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd07853 225 SleamrsacegaraHILRGPHKP-PSLPvlytlssqatheavHLLCRMLVFDPDKRISAADALAHPYLD 292
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
531-786 9.21e-13

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 69.30  E-value: 9.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIyAIKYV--NLEEADNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQYIYMVMECGNI- 607
Cdd:cd14145  14 IGIGGFGKVYRAIWIGDEV-AVKAArhDPDEDISQTIENVRQE-AKLFAMLKHPN-IIALRGVCLKEPNLCLVMEFARGg 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 DLNSWLKKKKsIDPWERKSYWKNMLEAVHTIHQHGIV---HSDLKPANFLIV---------DGMLKLIDFGIANQMQPDT 675
Cdd:cd14145  91 PLNRVLSGKR-IPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILekvengdlsNKILKITDFGLAREWHRTT 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 tsvvKDSQVGTVNYMPPEAIKdmSSSRENGKskskispksDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIE 755
Cdd:cd14145 170 ----KMSAAGTYAWMAPEVIR--SSMFSKGS---------DVWSYGVLLWELLTGEVPFRG-IDGLAVAYGVAMNKLSLP 233
                       250       260       270
                ....*....|....*....|....*....|.
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14145 234 IPSTCPEPFARLMEDCWNPDPHSRPPFTNIL 264
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
531-790 1.05e-12

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: 69.91  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQ-IYAIKyvNLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEI-TDQYIYMVMECGNI- 607
Cdd:cd05585   2 IGKGSFGKVMQVRKKDTSrIYALK--TIRKAHIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFqSPEKLYLVLAFINGg 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIA--NQMQPDTTsvvkDSQV 684
Cdd:cd05585  80 ELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLdYTGHIALCDFGLCklNMKDDDKT----NTFC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 685 GTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF-QQIINQISKlHAIIDPnheIEFPDIPEKD 763
Cdd:cd05585 156 GTPEYLAPELLLGHGYTK-----------AVDWWTLGVLLYEMLTGLPPFyDENTNEMYR-KILQEP---LRFPDGFDRD 220
                       250       260       270
                ....*....|....*....|....*....|
gi 23308722 764 LQDVLKCCLKRDPKQRISI---PELLAHPY 790
Cdd:cd05585 221 AKDLLIGLLNRDPTKRLGYngaQEIKNHPF 250
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
525-792 1.07e-12

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 70.09  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNlEEADNQTlDSYRN--EIAYLNKLQQhsDKIIRLYDY---EITDQY- 597
Cdd:cd07858   7 YVPIKPIGRGAYGIVCSAKNsETNEKVAIKKIA-NAFDNRI-DAKRTlrEIKLLRHLDH--ENVIAIKDImppPHREAFn 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 -IYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANqmqpdT 675
Cdd:cd07858  83 dVYIVYELMDTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLnANCDLKICDFGLAR-----T 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVVKD---SQVGTVNYMPPEAIkdMSSSRENGKSkskispksDVWSLGCILYYMTYGKTPFQ--QIINQISKLHAIIDP 750
Cdd:cd07858 158 TSEKGDfmtEYVVTRWYRAPELL--LNCSEYTTAI--------DVWSVGCIFAELLGRKPLFPgkDYVHQLKLITELLGS 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 751 --NHEIEF-------------PDIPEKDLQ-----------DVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd07858 228 psEEDLGFirnekarryirslPYTPRQSFArlfphanplaiDLLEKMLVFDPSKRITVEEALAHPYLA 295
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
598-791 1.08e-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: 69.25  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMEC--GNiDLNSWLKKKKSIDPWERKS--YWKNMLEAVHTIHQHGIVHSDLKPANFLIV----DGMLKLIDFGIAN 669
Cdd:cd14172  76 LLIIMECmeGG-ELFSRIQERGDQAFTEREAseIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskekDAVLKLTDFGFAK 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QmqpdtTSVVKDSQVG--TVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQIsklhai 747
Cdd:cd14172 155 E-----TTVQNALQTPcyTPYYVAPEVLGPEKYDKS-----------CDMWSLGVIMYILLCGFPPFYSNTGQA------ 212
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 748 IDPNH-------EIEFPDiPE-----KDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14172 213 ISPGMkrrirmgQYGFPN-PEwaevsEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
569-666 1.34e-12

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: 66.52  E-value: 1.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 569 RNEIAYLNKLQQHSDKIIRLYDYEITDQYIymVME-CGNIDLNSWLKKKKsidpwERKSYWKNMLEAVHTIHQHGIVHSD 647
Cdd:COG3642   4 RREARLLRELREAGVPVPKVLDVDPDDADL--VMEyIEGETLADLLEEGE-----LPPELLRELGRLLARLHRAGIVHGD 76
                        90
                ....*....|....*....
gi 23308722 648 LKPANFLIVDGMLKLIDFG 666
Cdd:COG3642  77 LTTSNILVDDGGVYLIDFG 95
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
531-786 1.54e-12

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: 68.91  E-value: 1.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIyAIKYV--NLEEADNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQYIYMVMECG-NI 607
Cdd:cd14146   2 IGVGGFGKVYRATWKGQEV-AVKAArqDPDEDIKATAESVRQE-AKLFSMLRHPN-IIKLEGVCLEEPNLCLVMEFArGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 DLNSWL---------KKKKSIDPWERKSYWKNMLEAVHTIHQHGIV---HSDLKPANFLIVDGM---------LKLIDFG 666
Cdd:cd14146  79 TLNRALaaanaapgpRRARRIPPHILVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIehddicnktLKITDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 667 IANQMQPDTtsvvKDSQVGTVNYMPPEAIKdmSSSRENGKskskispksDVWSLGCILYYMTYGKTPFQQiINQISKLHA 746
Cdd:cd14146 159 LAREWHRTT----KMSAAGTYAWMAPEVIK--SSLFSKGS---------DIWSYGVLLWELLTGEVPYRG-IDGLAVAYG 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 747 IIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14146 223 VAVNKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALIL 262
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
522-791 1.67e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 68.53  E-value: 1.67e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 522 GRIYsILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNE--IAYLNKLQQHSDKIIRlydyeitdqyIY 599
Cdd:cd06652  16 GRVY-LCYDADTGRELAVKQVQFDPESPETSKEVNALECEIQLLKNLLHEriVQYYGCLRDPQERTLS----------IF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 M-VMECGNIdlNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTS 677
Cdd:cd06652  85 MeYMPGGSI--KDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRdSVGNVKLGDFGASKRLQTICLS 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVK-DSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQqiinQISKLHAIIDPNHEIEF 756
Cdd:cd06652 163 GTGmKSVTGTPYWMSPEVISGEGYGRK-----------ADIWSVGCTVVEMLTEKPPWA----EFEAMAAIFKIATQPTN 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 757 PDIPEKdLQDVLKCCLKR---DPKQRISIPELLAHPYV 791
Cdd:cd06652 228 PQLPAH-VSDHCRDFLKRifvEAKLRPSADELLRHTFV 264
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
564-791 1.70e-12

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 67.98  E-value: 1.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 564 TLDSYRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGI 643
Cdd:cd14024  27 SLRSYQECLAPYDRLGPHEG-VCSVLEVVIGQDRAYAFFSRHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGV 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDGM-LKLIDFGIANQM---QPDTTSVVKDsqvGTVNYMPPEAIKDMSSSrengkskskISPKSDVWS 719
Cdd:cd14024 106 ILRDLKLRRFVFTDELrTKLVLVNLEDSCplnGDDDSLTDKH---GCPAYVGPEILSSRRSY---------SGKAADVWS 173
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23308722 720 LGCILYYMTYGKTPFQQIinQISKLHAIIDPNhEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14024 174 LGVCLYTMLLGRYPFQDT--EPAALFAKIRRG-AFSLPAWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
525-791 1.80e-12

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: 68.52  E-value: 1.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLdsYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVME 603
Cdd:cd06646  11 YELIQRVGSGTYGDVYKARNlHTGELAAVKIIKLEPGDDFSL--IQQEIFMVKECKHCN--IVAYFGSYLSREKLWICME 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQpdTTSVVKD 681
Cdd:cd06646  87 yCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDnGDVKLADFGVAAKIT--ATIAKRK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEaikdMSSSRENGKSKSKIspksDVWSLGCILYYMTYGKTPFQQIiNQISKLHAIIDPNheIEFPDIPE 761
Cdd:cd06646 165 SFIGTPYWMAPE----VAAVEKNGGYNQLC----DIWAVGITAIELAELQPPMFDL-HPMRALFLMSKSN--FQPPKLKD 233
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 762 K-----DLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06646 234 KtkwssTFHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
531-779 2.41e-12

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: 68.09  E-value: 2.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIyAIKYVNL--EEADNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQYIYMVMECGNID 608
Cdd:cd14148   2 IGVGGFGKVYKGLWRGEEV-AVKAARQdpDEDIAVTAENVRQE-ARLFWMLQHPN-IIALRGVCLNPPHLCLVMEYARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 -LNSWLKKKKsIDPWERKSYWKNMLEAVHTIHQHGIV---HSDLKPANFLIV---------DGMLKLIDFGIANQMQPDT 675
Cdd:cd14148  79 aLNRALAGKK-VPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILepienddlsGKTLKITDFGLAREWHKTT 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 tsvvKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIE 755
Cdd:cd14148 158 ----KMSAAGTYAWMAPEVIRLSLFSKSS-----------DVWSFGVLLWELLTGEVPYRE-IDALAVAYGVAMNKLTLP 221
                       250       260
                ....*....|....*....|....
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd14148 222 IPSTCPEPFARLLEECWDPDPHGR 245
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
522-793 2.57e-12

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: 68.19  E-value: 2.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 522 GRIYsILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLDSYRNE--IAYLNKLQQHSDKIIRLY-DYeitdqyi 598
Cdd:cd06651  21 GRVY-LCYDVDTGRELAAKQVQFDPESPETSKEVSALECEIQLLKNLQHEriVQYYGCLRDRAEKTLTIFmEY------- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 ymvMECGNIdlNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTS 677
Cdd:cd06651  93 ---MPGGSV--KDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRdSAGNVKLGDFGASKRLQTICMS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVK-DSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEiEF 756
Cdd:cd06651 168 GTGiRSVTGTPYWMSPEVISGEGYGRK-----------ADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIATQPTNP-QL 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 757 PDIPEKDLQDVLKCCLKrDPKQRISIPELLAHPYVQI 793
Cdd:cd06651 236 PSHISEHARDFLGCIFV-EARHRPSAEELLRHPFAQL 271
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
568-790 2.80e-12

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 67.37  E-value: 2.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 568 YRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSD 647
Cdd:cd14022  31 YQESLAPCFCLPAHSN-INQITEIILGETKAYVFFERSYGDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRD 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 648 LKPANFLIVDG---MLKLIDFGIANQMQPDTTSVvkDSQVGTVNYMPPEAIKdmSSSRENGKSKskispksDVWSLGCIL 724
Cdd:cd14022 110 LKLRKFVFKDEertRVKLESLEDAYILRGHDDSL--SDKHGCPAYVSPEILN--TSGSYSGKAA-------DVWSLGVML 178
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 725 YYMTYGKTPFQQIinQISKLHAIIDPNHeIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14022 179 YTMLVGRYPFHDI--EPSSLFSKIRRGQ-FNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 241
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
525-791 3.47e-12

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: 67.69  E-value: 3.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSkVFQVLNEK--KQIYAIKYVN--LEEADNQTldsyrNEIAYLNKLQQhsDKIIRLYD-YEITDQYIy 599
Cdd:cd14113   9 YSEVAELGRGRFS-VVKKCDQRgtKRAVATKFVNkkLMKRDQVT-----HELGVLQSLQH--PQLVGLLDtFETPTSYI- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNID-LNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM----LKLIDFGIANQMqpD 674
Cdd:cd14113  80 LVLEMADQGrLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLskptIKLADFGDAVQL--N 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKdSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLhaiid 749
Cdd:cd14113 158 TTYYIH-QLLGSPEFAAPEIILGNPVS-----------LTSDLWSIGVLTYVLLSGVSPFldesvEETCLNICRL----- 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 23308722 750 pnhEIEFPD-----IPEKdLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14113 221 ---DFSFPDdyfkgVSQK-AKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
596-802 3.80e-12

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: 68.92  E-value: 3.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVMECGNIDLNSWLKKKKSidpWERKSYW-KNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIAnqmQP 673
Cdd:cd07875 102 QDVYIVMELMDANLCQVIQMELD---HERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIVVkSDCTLKILDFGLA---RT 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKDSQVGTVNYMPPEAIKDMsSSRENgkskskispkSDVWSLGCILYYMTYGKTPF---------QQIINQI--- 741
Cdd:cd07875 176 AGTSFMMTPYVVTRYYRAPEVILGM-GYKEN----------VDIWSVGCIMGEMIKGGVLFpgtdhidqwNKVIEQLgtp 244
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 742 -----SKLHAII------DPNH-----EIEFPDI-----------PEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQ 794
Cdd:cd07875 245 cpefmKKLQPTVrtyvenRPKYagysfEKLFPDVlfpadsehnklKASQARDLLSKMLVIDASKRISVDEALQHPYINVW 324

                ....*...
gi 23308722 795 THPVNQMA 802
Cdd:cd07875 325 YDPSEAEA 332
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
525-791 3.93e-12

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: 67.76  E-value: 3.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNqtLDSYRNEIAYLnKLQQHSDKIIRLYDYEITDQyIYMVME 603
Cdd:cd06645  13 FELIQRIGSGTYGDVYKARNvNTGELAAIKVIKLEPGED--FAVVQQEIIMM-KDCKHSNIVAYFGSYLRRDK-LWICME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQpdTTSVVKD 681
Cdd:cd06645  89 fCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDnGHVKLADFGVSAQIT--ATIAKRK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAikdMSSSRENGKSKSKispksDVWSLGCILYYMTYGKTPFQQIiNQISKLHAIIDPNheIEFPDIPE 761
Cdd:cd06645 167 SFIGTPYWMAPEV---AAVERKGGYNQLC-----DIWAVGITAIELAELQPPMFDL-HPMRALFLMTKSN--FQPPKLKD 235
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 762 K-----DLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06645 236 KmkwsnSFHHFVKMALTKNPKKRPTAEKLLQHPFV 270
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
525-791 5.36e-12

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: 67.63  E-value: 5.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQV--LNEKKQIYAIKYVNleeaDNQTL-DSYRNEIAYLNKLQQH--SDK--IIRLYDYEITDQY 597
Cdd:cd14135   2 YRVYGYLGKGVFSNVVRArdLARGNQEVAIKIIR----NNELMhKAGLKELEILKKLNDAdpDDKkhCIRLLRHFEHKNH 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKK---KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG--MLKLIDFGIA---- 668
Cdd:cd14135  78 LCLVFESLSMNLREVLKKygkNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKknTLKLCDFGSAsdig 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 -NQMQPDTTSVVkdsqvgtvnYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILY--------------------YM 727
Cdd:cd14135 158 eNEITPYLVSRF---------YRAPEIILGLPYD-----------YPIDMWSVGCTLYelytgkilfpgktnnhmlklMM 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 728 TY-GKTPFQQI-----------------------INQISKLHAI--IDPNHEI-----EFPDIPEKD------LQDVLKC 770
Cdd:cd14135 218 DLkGKFPKKMLrkgqfkdqhfdenlnfiyrevdkVTKKEVRRVMsdIKPTKDLktlliGKQRLPDEDrkkllqLKDLLDK 297
                       330       340
                ....*....|....*....|.
gi 23308722 771 CLKRDPKQRISIPELLAHPYV 791
Cdd:cd14135 298 CLMLDPEKRITPNEALQHPFI 318
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
525-790 6.23e-12

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: 66.59  E-value: 6.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTlDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVME 603
Cdd:cd14184   3 YKIGKVIGDGNFAVVKECVERSTgKEFALKIIDKAKCCGKE-HLIENEVSILRRVKHPN--IIMLIEEMDTPAELYLVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV---DGM--LKLIDFGIANQMQPDTTS 677
Cdd:cd14184  80 lVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCeypDGTksLKLGDFGLATVVEGPLYT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VvkdsqVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHeIEFP 757
Cdd:cd14184 160 V-----CGTPTYVAPEIIAETGYGLK-----------VDIWAAGVITYILLCGFPPFRSENNLQEDLFDQILLGK-LEFP 222
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 23308722 758 ----DIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14184 223 spywDNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
519-790 6.34e-12

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: 67.05  E-value: 6.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 519 SVKGRIYSILKQIGSGGSSKVFQVLNEKKQIyAIKYVNLEEADNQTLDSYR-NEIAYLNKLQQHSDkIIRLYD-YEIT-- 594
Cdd:cd14031   6 SPGGRFLKFDIELGRGAFKTVYKGLDTETWV-EVAWCELQDRKLTKAEQQRfKEEAEMLKGLQHPN-IVRFYDsWESVlk 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 595 -DQYIYMVMEC-GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHG--IVHSDLKPANFLIV--DGMLKLIDFGIA 668
Cdd:cd14031  84 gKKCIVLVTELmTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgpTGSVKIGDLGLA 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQMQpdtTSVVKdSQVGTVNYMPPEAIKDMSSSrengkskskispKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAII 748
Cdd:cd14031 164 TLMR---TSFAK-SVIGTPEFMAPEMYEEHYDE------------SVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVT 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 749 DPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14031 228 SGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAF 269
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
570-791 7.04e-12

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: 66.48  E-value: 7.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 570 NEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVMEC--GNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSD 647
Cdd:cd14190  50 LEIQVMNQLNHRN--LIQLYEAIETPNEIVLFMEYveGGELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLD 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 648 LKPANFLIVDG---MLKLIDFGIANQMQPDTTSVVkdsQVGTVNYMPPEAIK-DMSSsrengkskskisPKSDVWSLGCI 723
Cdd:cd14190 128 LKPENILCVNRtghQVKIIDFGLARRYNPREKLKV---NFGTPEFLSPEVVNyDQVS------------FPTDMWSMGVI 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 724 LYYMTYGKTPF-----QQIINQISKLHAIIDpnhEIEFPDIPEkDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14190 193 TYMLLSGLSPFlgdddTETLNNVLMGNWYFD---EETFEHVSD-EAKDFVSNLIIKERSARMSATQCLKHPWL 261
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
528-792 7.43e-12

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: 67.39  E-value: 7.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVLNEKKQ-IYAIKYVNLEeadnqTLDSYRNEIayLNKLQQ----HSDKIIRLYDYEITDQYIYMVM 602
Cdd:cd06650  10 ISELGAGNGGVVFKVSHKPSGlVMARKLIHLE-----IKPAIRNQI--IRELQVlhecNSPYIVGFYGAFYSDGEISICM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 EcgNID---LNSWLKK----------KKSIDPWERKSYWKnmleavhtiHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA 668
Cdd:cd06650  83 E--HMDggsLDQVLKKagripeqilgKVSIAVIKGLTYLR---------EKHKIMHRDVKPSNILVNSrGEIKLCDFGVS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 NQMqpdtTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPF----QQIINQISKL 744
Cdd:cd06650 152 GQL----IDSMANSFVGTRSYMSPERLQGTHYSVQS-----------DIWSMGLSLVEMAVGRYPIpppdAKELELMFGC 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 745 HAIIDPNHEIEFPDIPEK-------------------------------------DLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd06650 217 QVEGDAAETPPRPRTPGRplssygmdsrppmaifelldyivnepppklpsgvfslEFQDFVNKCLIKNPAERADLKQLMV 296

                ....*
gi 23308722 788 HPYVQ 792
Cdd:cd06650 297 HAFIK 301
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
563-791 7.64e-12

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 67.10  E-value: 7.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 563 QTLDSYRNEIAYLNKLQQHSdkiiRLYdyeitdqyiyMVMECGN-IDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQH 641
Cdd:cd14171  63 QIYDVYANSVQFPGESSPRA----RLL----------IVMELMEgGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 642 GIVHSDLKPANFLIV----DGMLKLIDFGIA-----NQMQPDTTSVVKDSQVgtvnympPEAIKDMSSSRENGKSKSKI- 711
Cdd:cd14171 129 NIAHRDLKPENLLLKdnseDAPIKLCDFGFAkvdqgDLMTPQFTPYYVAPQV-------LEAQRRHRKERSGIPTSPTPy 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 712 --SPKSDVWSLGCILYYMT------YGKTPFQQIINQISKlhAIIdpNHEIEFPD----IPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd14171 202 tyDKSCDMWSLGVIIYIMLcgyppfYSEHPSRTITKDMKR--KIM--TGSYEFPEeewsQISEMAKDIVRKLLCVDPEER 277
                       250
                ....*....|..
gi 23308722 780 ISIPELLAHPYV 791
Cdd:cd14171 278 MTIEEVLHHPWL 289
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
594-792 9.54e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 66.89  E-value: 9.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQYIYMVMECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQm 671
Cdd:cd05620  67 TKEHLFFVMEFLNGgDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLdRDGHIKIADFGMCKE- 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 qpdttSVVKDSQV----GTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPFQ-----QIINQIS 742
Cdd:cd05620 146 -----NVFGDNRAstfcGTPDYIAPEILQGLKYT-----------FSVDWWSFGVLLYEMLIGQSPFHgddedELFESIR 209
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 23308722 743 klhaiIDPNHeieFPDIPEKDLQDVLKCCLKRDPKQRISIP-ELLAHPYVQ 792
Cdd:cd05620 210 -----VDTPH---YPRWITKESKDILEKLFERDPTRRLGVVgNIRGHPFFK 252
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
596-797 1.06e-11

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: 67.42  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVMECGNIDLNSWLKKKKSidpWERKSYW-KNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIAnqmQP 673
Cdd:cd07874  95 QDVYLVMELMDANLCQVIQMELD---HERMSYLlYQMLCGIKHLHSAGIIHRDLKPSNIVVkSDCTLKILDFGLA---RT 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKDSQVGTVNYMPPEAIKDMsSSRENgkskskispkSDVWSLGCILYYMTYGKTPF---------QQIINQI--- 741
Cdd:cd07874 169 AGTSFMMTPYVVTRYYRAPEVILGM-GYKEN----------VDIWSVGCIMGEMVRHKILFpgrdyidqwNKVIEQLgtp 237
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 742 -----SKLHAIIDPNHEIE-----------FPD-----------IPEKDLQDVLKCCLKRDPKQRISIPELLAHPYVQIQ 794
Cdd:cd07874 238 cpefmKKLQPTVRNYVENRpkyagltfpklFPDslfpadsehnkLKASQARDLLSKMLVIDPAKRISVDEALQHPYINVW 317

                ...
gi 23308722 795 THP 797
Cdd:cd07874 318 YDP 320
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
631-784 1.10e-11

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: 65.98  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 631 MLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIA------------NQMQPDTTSVVKdSQVGTVNYMPPEAIKD 697
Cdd:cd14027  99 IIEGMAYLHGKGVIHKDLKPENILVdNDFHIKIADLGLAsfkmwskltkeeHNEQREVDGTAK-KNAGTLYYMAPEHLND 177
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 698 MSSsrengksksKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEiEFPDIPE---KDLQDVLKCCLKR 774
Cdd:cd14027 178 VNA---------KPTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRP-DVDDITEycpREIIDLMKLCWEA 247
                       170
                ....*....|
gi 23308722 775 DPKQRISIPE 784
Cdd:cd14027 248 NPEARPTFPG 257
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
530-791 1.16e-11

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: 66.58  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 530 QIGSGGSSKV-FQVLNEKKQIYAIKYVNLEEADNQTLdsYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVMECGNID 608
Cdd:cd06657  27 KIGEGSTGIVcIATVKSSGKLVAVKKMDLRKQQRREL--LFNEVVIMRDYQH--ENVVEMYNSYLVGDELWVVMEFLEGG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSvvKDSQVGTV 687
Cdd:cd06657 103 ALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLThDGRVKLSDFGFCAQVSKEVPR--RKSLVGTP 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 688 NYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFqqiINQIS-KLHAIIDPNHEIEFPDIPEKD--L 764
Cdd:cd06657 181 YWMAPELISRLPYGPE-----------VDIWSLGIMVIEMVDGEPPY---FNEPPlKAMKMIRDNLPPKLKNLHKVSpsL 246
                       250       260
                ....*....|....*....|....*..
gi 23308722 765 QDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd06657 247 KGFLDRLLVRDPAQRATAAELLKHPFL 273
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
565-790 1.45e-11

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 65.45  E-value: 1.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 565 LDSYRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIV 644
Cdd:cd14023  28 LKHYQDKIRPYIQLPSHRN-ITGIVEVILGDTKAYVFFEKDFGDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIV 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 645 HSDLKPANFLIVD---GMLKLIDFGIANQMQPDTTSVvkDSQVGTVNYMPPEAIKDMSSsrengksksKISPKSDVWSLG 721
Cdd:cd14023 107 LGDLKLRKFVFSDeerTQLRLESLEDTHIMKGEDDAL--SDKHGCPAYVSPEILNTTGT---------YSGKSADVWSLG 175
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 722 CILYYMTYGKTPFQQiiNQISKLHAIIDpNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14023 176 VMLYTLLVGRYPFHD--SDPSALFSKIR-RGQFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
529-734 1.84e-11

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: 66.19  E-value: 1.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLN-EKKQIYAIKYVN----LEEADNQTLDSYRNeiaYLNKLQQHSDKIIRLYDYEITDQyIYMVME 603
Cdd:cd05575   1 KVIGKGSFGKVLLARHkAEGKLYAVKVLQkkaiLKRNEVKHIMAERN---VLLKNVKHPFLVGLHYSFQTKDK-LYFVLD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQP-DTTSVV 679
Cdd:cd05575  77 YVNGgELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLdSQGHVVLTDFGLCKEgIEPsDTTSTF 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 680 kdsqVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF 734
Cdd:cd05575 157 ----CGTPEYLAPEVLRKQPYDR-----------TVDWWCLGAVLYEMLYGLPPF 196
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
525-780 1.94e-11

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 66.62  E-value: 1.94e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVnleeaDNQTLDSYRNEIAYLNK-----LQQHSD---KIIRLYDYEITD 595
Cdd:cd05633   7 FSVHRIIGRGGFGEVYGCRKaDTGKMYAMKCL-----DKKRIKMKQGETLALNErimlsLVSTGDcpfIVCMTYAFHTPD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANqmqpD 674
Cdd:cd05633  82 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEhGHVRISDLGLAC----D 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKDSQVGTVNYMPPEAIKDMSSSRENGkskskispksDVWSLGCILYYMTYGKTPFQQiiNQISKLHAI--IDPNH 752
Cdd:cd05633 158 FSKKKPHASVGTHGYMAPEVLQKGTAYDSSA----------DWFSLGCMLFKLLRGHSPFRQ--HKTKDKHEIdrMTLTV 225
                       250       260
                ....*....|....*....|....*...
gi 23308722 753 EIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05633 226 NVELPDSFSPELKSLLEGLLQRDVSKRL 253
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
525-723 1.99e-11

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: 66.12  E-value: 1.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVNleeadNQTldSYRN----EIAYLNKLQQHSDK-----IIRLYDYEIT 594
Cdd:cd14212   1 YLVLDLLGQGTFGQVVKCQDlKTNKLVAVKVLK-----NKP--AYFRqamlEIAILTLLNTKYDPedkhhIVRLLDHFMH 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 595 DQYIYMVMECGNIDLNSWLKKKK----SIDpwERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD---GMLKLIDFGI 667
Cdd:cd14212  74 HGHLCIVFELLGVNLYELLKQNQfrglSLQ--LIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNldsPEIKLIDFGS 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 668 ANqMQPDTTSvvkdSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCI 723
Cdd:cd14212 152 AC-FENYTLY----TYIQSRFYRSPEVLLGLPYS-----------TAIDMWSLGCI 191
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
525-780 2.16e-11

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: 66.26  E-value: 2.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd05593  17 FDYLKLLGKGTFGKVILVREKASgKYYAMKILKKEVIIAKDEVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVvkDS 682
Cdd:cd05593  97 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLdKDGHIKITDFGLCKEGITDAATM--KT 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 QVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQIINQisKLHAIIdPNHEIEFPDIPEK 762
Cdd:cd05593 175 FCGTPEYLAPEVLEDNDYGR-----------AVDWWGLGVVMYEMMCGRLPFYNQDHE--KLFELI-LMEDIKFPRTLSA 240
                       250
                ....*....|....*...
gi 23308722 763 DLQDVLKCCLKRDPKQRI 780
Cdd:cd05593 241 DAKSLLSGLLIKDPNKRL 258
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
490-780 2.28e-11

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: 66.21  E-value: 2.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 490 CFQQQQHQILATPLQNLQVLASSSANECISVKGRiysilkqigSGGSSKVFQVLnEKKQIYAIKYVNLEEADNQTLDSYR 569
Cdd:cd05594  14 SLTKPKHKVTMNDFEYLKLLGKGTFGKVILVKEK---------ATGRYYAMKIL-KKEVIVAKDEVAHTLTENRVLQNSR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 570 NeiAYLNKLQqhsdkiirlYDYEITDQYIYmVMECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIH-QHGIVHSD 647
Cdd:cd05594  84 H--PFLTALK---------YSFQTHDRLCF-VMEYANGgELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 648 LKPANFLI-VDGMLKLIDFGIANQMQPDTTSVvkDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYY 726
Cdd:cd05594 152 LKLENLMLdKDGHIKITDFGLCKEGIKDGATM--KTFCGTPEYLAPEVLEDNDYGR-----------AVDWWGLGVVMYE 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 23308722 727 MTYGKTPFQQIINQisKLHAIIdPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05594 219 MMCGRLPFYNQDHE--KLFELI-LMEEIRFPRTLSPEAKSLLSGLLKKDPKQRL 269
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
525-791 3.60e-11

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: 64.63  E-value: 3.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEEADNQTlDSYRNEIAYLNKLQqHSDKIIRLYDYEITDQyIYMVME 603
Cdd:cd14183   8 YKVGRTIGDGNFAVVKEcVERSTGREYALKIINKSKCRGKE-HMIQNEVSILRRVK-HPNIVLLIEEMDMPTE-LYLVME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV---DG--MLKLIDFGIANQMQPDTTS 677
Cdd:cd14183  85 lVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYehqDGskSLKLGDFGLATVVDGPLYT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VvkdsqVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNhEIEFP 757
Cdd:cd14183 165 V-----CGTPTYVAPEIIAETGYGLK-----------VDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMG-QVDFP 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 758 ----DIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14183 228 spywDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
553-791 5.68e-11

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: 63.89  E-value: 5.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 553 KYVNLEEADNQTLDSYRNE--IAYLNKLQQHSDKIIRLY-DYeitdqyiymvMECGNIdlNSWLKKKKSIDPWERKSYWK 629
Cdd:cd06653  46 KEVNALECEIQLLKNLRHDriVQYYGCLRDPEEKKLSIFvEY----------MPGGSV--KDQLKAYGALTENVTRRYTR 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 630 NMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTS-VVKDSQVGTVNYMPPEAIKDMSSSREngks 707
Cdd:cd06653 114 QILQGVSYLHSNMIVHRDIKGANILRdSAGNVKLGDFGASKRIQTICMSgTGIKSVTGTPYWMSPEVISGEGYGRK---- 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 708 kskispkSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDpKQRISIPELLA 787
Cdd:cd06653 190 -------ADVWSVACTVVEMLTEKPPWAE-YEAMAAIFKIATQPTKPQLPDGVSDACRDFLRQIFVEE-KRRPTAEFLLR 260

                ....
gi 23308722 788 HPYV 791
Cdd:cd06653 261 HPFV 264
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
529-799 5.70e-11

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: 64.61  E-value: 5.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVfqVLNEKK---QIYAIKYVN----LEEADNQTLDSYRNeiaYLNKLQQHSDKIIRLYDYEiTDQYIYMV 601
Cdd:cd05603   1 KVIGKGSFGKV--LLAKRKcdgKFYAVKVLQkktiLKKKEQNHIMAERN---VLLKNLKHPFLVGLHYSFQ-TSEKLYFV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQP-DTTS 677
Cdd:cd05603  75 LDYVNGgELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLdCQGHVVLTDFGLCKEgMEPeETTS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVkdsqVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQiiNQISKLHAIIdPNHEIEFP 757
Cdd:cd05603 155 TF----CGTPEYLAPEVLRKEPYDR-----------TVDWWCLGAVLYEMLYGLPPFYS--RDVSQMYDNI-LHKPLHLP 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 758 DIPEKDLQDVLKCCLKRDPKQRISIPEllahPYVQIQTH----PVN 799
Cdd:cd05603 217 GGKTVAACDLLQGLLHKDQRRRLGAKA----DFLEIKNHvffsPIN 258
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
627-790 7.63e-11

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: 64.30  E-value: 7.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 627 YWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ--MQPDTTSVVkdsqVGTVNYMPPEAIKDMSSSRe 703
Cdd:cd05571 100 YGAEIVLALGYLHSQGIVYRDLKLENLLLdKDGHIKITDFGLCKEeiSYGATTKTF----CGTPEYLAPEVLEDNDYGR- 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 704 ngkskskispKSDVWSLGCILYYMTYGKTPFQqiinqiSKLHAIIDP---NHEIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05571 175 ----------AVDWWGLGVVMYEMMCGRLPFY------NRDHEVLFElilMEEVRFPSTLSPEAKSLLAGLLKKDPKKRL 238
                       170
                ....*....|....*
gi 23308722 781 -----SIPELLAHPY 790
Cdd:cd05571 239 gggprDAKEIMEHPF 253
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
531-735 9.24e-11

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: 64.05  E-value: 9.24e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKK-QIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLY--DYEITDQYIYMVME-CGN 606
Cdd:cd13988   1 LGQGATANVFRGRHKKTgDLYAVKVFN-NLSFMRPLDVQMREFEVLKKLNH--KNIVKLFaiEEELTTRHKVLVMElCPC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLKkkksiDPweRKSY----------WKNMLEAVHTIHQHGIVHSDLKPANFLIV---DG--MLKLIDFGIANQM 671
Cdd:cd13988  78 GSLYTVLE-----EP--SNAYglpeseflivLRDVVAGMNHLRENGIVHRDIKPGNIMRVigeDGqsVYKLTDFGAAREL 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 672 QPDTTSVvkdSQVGTVNYMPPEAIKDMSSSRENGkskSKISPKSDVWSLGCILYYMTYGKTPFQ 735
Cdd:cd13988 151 EDDEQFV---SLYGTEEYLHPDMYERAVLRKDHQ---KKYGATVDLWSIGVTFYHAATGSLPFR 208
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
525-780 1.12e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 63.91  E-value: 1.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLN-EKKQIYAIKYVnleeaDNQTLDSYRNEIAYLNK-----LQQHSD---KIIRLYDYEITD 595
Cdd:cd14223   2 FSVHRIIGRGGFGEVYGCRKaDTGKMYAMKCL-----DKKRIKMKQGETLALNErimlsLVSTGDcpfIVCMSYAFHTPD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANqmqpD 674
Cdd:cd14223  77 KLSFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEfGHVRISDLGLAC----D 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKDSQVGTVNYMPPEAIKDMSSSRENGkskskispksDVWSLGCILYYMTYGKTPFQQiiNQISKLHAI--IDPNH 752
Cdd:cd14223 153 FSKKKPHASVGTHGYMAPEVLQKGVAYDSSA----------DWFSLGCMLFKLLRGHSPFRQ--HKTKDKHEIdrMTLTM 220
                       250       260
                ....*....|....*....|....*...
gi 23308722 753 EIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd14223 221 AVELPDSFSPELRSLLEGLLQRDVNRRL 248
STKc_TTBK2 cd14129
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 2; STKs catalyze ...
525-737 1.30e-10

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: 62.76  E-value: 1.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYvnleEADNQTLDSYRNEIAYLNKLQQhSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd14129   2 WKVLRKIGGGGFGEIYDALDLlTRENVALKV----ESAQQPKQVLKMEVAVLKKLQG-KDHVCRFIGCGRNDRFNYVVMQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSwLKKKKSIDPWERKSYWK---NMLEAVHTIHQHGIVHSDLKPANFLIvdGMLK-------LIDFGIANQMQP 673
Cdd:cd14129  77 LQGRNLAD-LRRSQSRGTFTISTTLRlgrQILESIESIHSVGFLHRDIKPSNFAM--GRFPstcrkcyMLDFGLARQFTN 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 674 DTTSVVKDSQV----GTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQI 737
Cdd:cd14129 154 SCGDVRPPRAVagfrGTVRYASINAHRNREMGRHD-----------DLWSLFYMLVEFVVGQLPWRKI 210
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
529-779 1.63e-10

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


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 62.74  E-value: 1.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLNEKKQIYAIKYVnleEADNQTLDSYRNEiAYLNKLQQHsDKIIRLYDYeITDQYIYMV---MECG 605
Cdd:cd05073  17 KKLGAGQFGEVWMATYNKHTKVAVKTM---KPGSMSVEAFLAE-ANVMKTLQH-DKLVKLHAV-VTKEPIYIItefMAKG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NI------DLNSWLKKKKSIDpwerksYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGML-KLIDFGIANQMQpDTTSV 678
Cdd:cd05073  91 SLldflksDEGSKQPLPKLID------FSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVcKIADFGLARVIE-DNEYT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIINqiSKLHAIIDPNHEIEFP 757
Cdd:cd05073 164 AREGAKFPIKWTAPEAINFGSFTIKS-----------DVWSFGILLMeIVTYGRIPYPGMSN--PEVIRALERGYRMPRP 230
                       250       260
                ....*....|....*....|..
gi 23308722 758 DIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05073 231 ENCPEELYNIMMRCWKNRPEER 252
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
525-734 2.09e-10

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: 63.11  E-value: 2.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQI-YAIKYVN----LEEADNQTLDSYRNeiaYLNKLQQHSDKIIRLYDYEITDQYIY 599
Cdd:cd05602   9 FHFLKVIGKGSFGKVLLARHKSDEKfYAVKVLQkkaiLKKKEEKHIMSERN---VLLKNVKHPFLVGLHFSFQTTDKLYF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQPDTTS 677
Cdd:cd05602  86 VLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLdSQGHIVLTDFGLCKEnIEPNGTT 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 678 vvkDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF 734
Cdd:cd05602 166 ---STFCGTPEYLAPEVLHKQPYDR-----------TVDWWCLGAVLYEMLYGLPPF 208
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
525-790 2.12e-10

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: 63.33  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSG--GSSKVFQVLNEKKqIYAIK-YVNLEEADNQTLDSYRNEIAYLnkLQQHSDKIIRLYdYEITD-QYIYM 600
Cdd:cd05629   3 FHTVKVIGKGafGEVRLVQKKDTGK-IYAMKtLLKSEMFKKDQLAHVKAERDVL--AESDSPWVVSLY-YSFQDaQYLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMEC--GNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIA--------- 668
Cdd:cd05629  79 IMEFlpGG-DLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIdRGGHIKLSDFGLStgfhkqhds 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 669 -------------------NQMQPDTTSVV---KD--------------SQVGTVNYMPPEAIKDMSSSREngkskskis 712
Cdd:cd05629 158 ayyqkllqgksnknridnrNSVAVDSINLTmssKDqiatwkknrrlmaySTVGTPDYIAPEIFLQQGYGQE--------- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 713 pkSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEFPD-----IPEKDLQDVLKCclkrDPKQRI---SIPE 784
Cdd:cd05629 229 --CDWWSLGAIMFECLIGWPPFCS-ENSHETYRKIINWRETLYFPDdihlsVEAEDLIRRLIT----NAENRLgrgGAHE 301

                ....*.
gi 23308722 785 LLAHPY 790
Cdd:cd05629 302 IKSHPF 307
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
526-787 2.66e-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: 61.96  E-value: 2.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGGSSKVFQvlNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKlQQHSDkIIRLYDYEITDQYIYMVMECG 605
Cdd:cd14150   3 SMLKRIGTGSFGTVFR--GKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRK-TRHVN-ILLFMGFMTRPNFAIITQWCE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKKKS-IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSVVKDSQ 683
Cdd:cd14150  79 GSSLYRHLHVTETrFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLtVKIGDFGLATVKTRWSGSQQVEQP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 684 VGTVNYMPPEAIKDMSSSrengksksKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAI----IDPNHEIEFPDI 759
Cdd:cd14150 159 SGSILWMAPEVIRMQDTN--------PYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVgrgyLSPDLSKLSSNC 230
                       250       260
                ....*....|....*....|....*...
gi 23308722 760 PeKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd14150 231 P-KAMKRLLIDCLKFKREERPLFPQILV 257
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
525-734 2.86e-10

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 61.86  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK-QIYAIKYVNLEEADNQtldSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd14110   5 YAFQTEINRGRFSVVRQCEEKRSgQMLAAKIIPYKPEDKQ---LVLREYQVLRRL--SHPRIAQLHSAYLSPRHLVLIEE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTsVVKD 681
Cdd:cd14110  80 lCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEkNLLKIVDLGNAQPFNQGKV-LMTD 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 23308722 682 SQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPF 734
Cdd:cd14110 159 KKGDYVETMAPELLEGQGAGPQT-----------DIWAIGVTAFIMLSADYPV 200
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
598-785 2.98e-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: 62.50  E-value: 2.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNIDLNSWLKKKKS--IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG-MLKLIDFGIANQMQP 673
Cdd:cd05055 114 ILVITEyCCYGDLLNFLRRKREsfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGkIVKICDFGLARDIMN 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQIINQiSKLHAIIDPNH 752
Cdd:cd05055 194 DSNYVVKGNARLPVKWMAPESIFNCVYTFES-----------DVWSYGILLWEIfSLGSNPYPGMPVD-SKFYKLIKEGY 261
                       170       180       190
                ....*....|....*....|....*....|...
gi 23308722 753 EIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05055 262 RMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQI 294
pknD PRK13184
serine/threonine-protein kinase PknD;
635-792 3.44e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 64.02  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  635 VHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFG--IANQMQPDTTSVVKDSQ--------------VGTVNYMPPEAIKD 697
Cdd:PRK13184 126 IEYVHSKGVLHRDLKPDNILLgLFGEVVILDWGaaIFKKLEEEDLLDIDVDErnicyssmtipgkiVGTPDYMAPERLLG 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  698 MSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQIINQ-ISKLHAIIDPNHEIEFPDIPEKDLQDVLKcCLKRDP 776
Cdd:PRK13184 206 VPASEST-----------DIYALGVILYQMLTLSFPYRRKKGRkISYRDVILSPIEVAPYREIPPFLSQIAMK-ALAVDP 273
                        170
                 ....*....|....*....
gi 23308722  777 KQRI-SIPELLA--HPYVQ 792
Cdd:PRK13184 274 AERYsSVQELKQdlEPHLQ 292
STKc_TTBK1 cd14130
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase 1; STKs catalyze ...
525-737 3.58e-10

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: 61.58  E-value: 3.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYvnleEADNQTLDSYRNEIAYLNKLQQhSDKIIRLYDYEITDQYIYMVME 603
Cdd:cd14130   2 WKVLKKIGGGGFGEIYEAMDLlTRENVALKV----ESAQQPKQVLKMEVAVLKKLQG-KDHVCRFIGCGRNEKFNYVVMQ 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSwLKKKKSIDPWERKSYW---KNMLEAVHTIHQHGIVHSDLKPANFLIvdGMLK-------LIDFGIANQMQP 673
Cdd:cd14130  77 LQGRNLAD-LRRSQPRGTFTLSTTLrlgKQILESIEAIHSVGFLHRDIKPSNFAM--GRLPstyrkcyMLDFGLARQYTN 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 674 DTTSVVKDSQV----GTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQQI 737
Cdd:cd14130 154 TTGEVRPPRNVagfrGTVRYASVNAHKNREMGRHD-----------DLWSLFYMLVEFAVGQLPWRKI 210
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
529-780 5.26e-10

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 61.74  E-value: 5.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVfqVLNEKK---QIYAIKY----VNLEEADnqtLDSYRNEIAYLNKLQQHSdKIIRLYDYEITDQYIYMV 601
Cdd:cd05591   1 KVLGKGSFGKV--MLAERKgtdEVYAIKVlkkdVILQDDD---VDCTMTEKRILALAAKHP-FLTALHSCFQTKDRLFFV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQPDTTSv 678
Cdd:cd05591  75 MEYVNGgDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLdAEGHCKLADFGMCKEgILNGKTT- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vkDSQVGTVNYMPPEAIKDMsssrENGKSKskispksDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIdpNHEIEFPD 758
Cdd:cd05591 154 --TTFCGTPDYIAPEILQEL----EYGPSV-------DWWALGVLMYEMMAGQPPFEA-DNEDDLFESIL--HDDVLYPV 217
                       250       260
                ....*....|....*....|..
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05591 218 WLSKEAVSILKAFMTKNPAKRL 239
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
634-787 5.50e-10

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, 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. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk 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: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 61.31  E-value: 5.50e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 634 AVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAI--KDMSSSrengksksk 710
Cdd:cd05043 128 GMSYLHRRGVIHKDIAARNCVIDDELqVKITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLvnKEYSSA--------- 198
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 711 ispkSDVWSLGCILY-YMTYGKTPFQQIinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd05043 199 ----SDVWSFGVLLWeLMTLGQTPYVEI--DPFEMAAYLKDGYRLAQPINCPDELFAVMACCWALDPEERPSFQQLVQ 270
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
529-787 6.57e-10

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: 60.85  E-value: 6.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQvlNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVMECGNID 608
Cdd:cd14151  14 QRIGSGSFGTVYK--GKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVN--ILLFMGYSTKPQLAIVTQWCEGSS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWL-------KKKKSIDpwerksYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQPDTTSVVK 680
Cdd:cd14151  90 LYHHLhiietkfEMIKLID------IARQTAQGMDYLHAKSIIHRDLKSNNiFLHEDLTVKIGDFGLATVKSRWSGSHQF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 681 DSQVGTVNYMPPEAIKDMSSSrengksksKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAI----IDPNHEIEF 756
Cdd:cd14151 164 EQLSGSILWMAPEVIRMQDKN--------PYSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVgrgyLSPDLSKVR 235
                       250       260       270
                ....*....|....*....|....*....|.
gi 23308722 757 PDIPeKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd14151 236 SNCP-KAMKRLMAECLKKKRDERPLFPQILA 265
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
532-787 7.97e-10

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 60.36  E-value: 7.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 532 GSGGSSKVFQVLNEKKQIyAIKYVNLEEADNQTLD--SYRNEIAYLNK-LQQHSDKII-------RLYDYeitdqyiymv 601
Cdd:cd14060   4 GSFGSVYRAIWVSQDKEV-AVKKLLKIEKEAEILSvlSHRNIIQFYGAiLEAPNYGIVteyasygSLFDY---------- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 mecgnidLNSwlKKKKSIDPWERKSYWKNMLEAVHTIHQHG---IVHSDLKPANFLIV-DGMLKLIDFGiANQMQPDTTS 677
Cdd:cd14060  73 -------LNS--NESEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAaDGVLKICDFG-ASRFHSHTTH 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VvkdSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQIinQISKLHAIIDPNHeiEFP 757
Cdd:cd14060 143 M---SLVGTFPWMAPEVIQSLPVSE-----------TCDTYSYGVVLWEMLTREVPFKGL--EGLQVAWLVVEKN--ERP 204
                       250       260       270
                ....*....|....*....|....*....|...
gi 23308722 758 DIPE---KDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd14060 205 TIPSscpRSFAELMRRCWEADVKERPSFKQIIG 237
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
530-786 7.99e-10

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 60.44  E-value: 7.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 530 QIGSGGSSKVFQVLNEKKQIyAIKyvNLEEaDNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVME-CGNID 608
Cdd:cd05039  13 LIGKGEFGDVMLGDYRGQKV-AVK--CLKD-DSTAAQAFLAEASVMTTLRH--PNLVQLLGVVLEGNGLYIVTEyMAKGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIAnqmqpdttsvvKDSQVG 685
Cdd:cd05039  87 LVDYLRSRgrAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSeDNVAKVSDFGLA-----------KEASSN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 686 T------VNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQIinQISKLHAIIDPNHEIEFPD 758
Cdd:cd05039 156 QdggklpIKWTAPEALREKKFSTKS-----------DVWSFGILLWEIySFGRVPYPRI--PLKDVVPHVEKGYRMEAPE 222
                       250       260
                ....*....|....*....|....*...
gi 23308722 759 IPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05039 223 GCPPEVYKVMKNCWELDPAKRPTFKQLR 250
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
529-785 8.64e-10

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 60.82  E-value: 8.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVL------NEKKQIYAIKyvNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMVM 602
Cdd:cd05093  11 RELGEGAFGKVFLAEcynlcpEQDKILVAVK--TLKDASDNARKDFHREAELLTNLQH--EHIVKFYGVCVEGDPLIMVF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKK--------KSIDPWERKSywKNMLEAVHTI--------HQHgIVHSDLKPANFLIVDGML-KLID 664
Cdd:cd05093  87 EyMKHGDLNKFLRAHgpdavlmaEGNRPAELTQ--SQMLHIAQQIaagmvylaSQH-FVHRDLATRNCLVGENLLvKIGD 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 665 FGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQIINqiSK 743
Cdd:cd05093 164 FGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTES-----------DVWSLGVVLWEIfTYGKQPWYQLSN--NE 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 744 LHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05093 231 VIECITQGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEI 272
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
529-779 9.70e-10

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: 60.20  E-value: 9.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQV-LNEKKQIYAIKYVNLEEADnqtlDSYRNE-IAYLNKLQQHSDKIIrLYDYEITDQYIYMVME-CG 605
Cdd:cd14025   2 EKVGSGGFGQVYKVrHKHWKTWLAIKCPPSLHVD----DSERMElLEEAKKMEMAKFRHI-LPVYGICSEPVGLVMEyME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKKKSidPWERK-------SYWKNMLeavHTIhQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQM-QPDTT 676
Cdd:cd14025  77 TGSLEKLLASEPL--PWELRfriihetAVGMNFL---HCM-KPPLLHLDLKPANILLDAHYhVKISDFGLAKWNgLSHSH 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSQVGTVNYMPPEAIkdMSSSRENGkskskisPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEF 756
Cdd:cd14025 151 DLSRDGLRGTIAYLPPERF--KEKNRCPD-------TKHDVYSFAIVIWGILTQKKPFAG-ENNILHIMVKVVKGHRPSL 220
                       250       260
                ....*....|....*....|....*....
gi 23308722 757 PDIPEK------DLQDVLKCCLKRDPKQR 779
Cdd:cd14025 221 SPIPRQrpsecqQMICLMKRCWDQDPRKR 249
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
644-779 1.18e-09

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: 61.01  E-value: 1.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDG-MLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGC 722
Cdd:cd05106 234 IHRDVAARNVLLTDGrVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQS-----------DVWSYGI 302
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 723 ILYYM-TYGKTPFQQIINQiSKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05106 303 LLWEIfSLGKSPYPGILVN-SKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTER 359
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
531-666 1.23e-09

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: 57.07  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQI-YAIKYVNLEEadNQTLDSYRNEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVME-CGNID 608
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIgVAVKIGDDVN--NEEGEDLESEMDILRRLKGLELNIPKVLVTEDVDGPNILLMElVKGGT 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 609 LNSWLKK--KKSIDPwerKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFG 666
Cdd:cd13968  79 LIAYTQEeeLDEKDV---ESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGnVKLIDFG 136
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
620-781 1.27e-09

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 60.59  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 620 DPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI---VDGMLKLI--DFGIA------NQMQPDTTSVVkdSQVGTVN 688
Cdd:cd14018 136 SYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLeldFDGCPWLViaDFGCCladdsiGLQLPFSSWYV--DRGGNAC 213
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 689 YMPPEAIKDMSssrenGKSKSKISPKSDVWSLGCILYYMTYGKTPFQqiinQISKLHAIIDPNHEIEFPDIPEK---DLQ 765
Cdd:cd14018 214 LMAPEVSTAVP-----GPGVVINYSKADAWAVGAIAYEIFGLSNPFY----GLGDTMLESRSYQESQLPALPSAvppDVR 284
                       170
                ....*....|....*.
gi 23308722 766 DVLKCCLKRDPKQRIS 781
Cdd:cd14018 285 QVVKDLLQRDPNKRVS 300
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
625-790 1.28e-09

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 60.60  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  625 KSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqPDTTSVVkdsqVGTVNYMPPEAIKdmssSRE 703
Cdd:PTZ00263 121 KFYHAELVLAFEYLHSKDIIYRDLKPENLLLdNKGHVKVTDFGFAKKV-PDRTFTL----CGTPEYLAPEVIQ----SKG 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  704 NGkskskisPKSDVWSLGCILYYMTYGKTPF--QQIINQISKLHAiidpnHEIEFPDIPEKDLQDVLKCCLKRDPKQRI- 780
Cdd:PTZ00263 192 HG-------KAVDWWTMGVLLYEFIAGYPPFfdDTPFRIYEKILA-----GRLKFPNWFDGRARDLVKGLLQTDHTKRLg 259
                        170
                 ....*....|....
gi 23308722  781 SIPELLA----HPY 790
Cdd:PTZ00263 260 TLKGGVAdvknHPY 273
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
525-792 1.31e-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: 60.84  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVlnEKK---QIYAIKYVNLEEA-DNQTLDSYRNEIAYLnkLQQHSDKIIRLYdYEITDQY-IY 599
Cdd:cd05627   4 FESLKVIGRGAFGEVRLV--QKKdtgHIYAMKILRKADMlEKEQVAHIRAERDIL--VEADGAWVVKMF-YSFQDKRnLY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQ----- 672
Cdd:cd05627  79 LIMEfLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLdAKGHVKLSDFGLCTGLKkahrt 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 ----------PDTTSV------------------VKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCIL 724
Cdd:cd05627 159 efyrnlthnpPSDFSFqnmnskrkaetwkknrrqLAYSTVGTPDYIAPEVFMQTGYNK-----------LCDWWSLGVIM 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 725 YYMTYGKTPFQQIINQiSKLHAIIDPNHEIEFP---DIPEKDLQDVLKCCLkrDPKQRI---SIPELLAHPYVQ 792
Cdd:cd05627 228 YEMLIGYPPFCSETPQ-ETYRKVMNWKETLVFPpevPISEKAKDLILRFCT--DAENRIgsnGVEEIKSHPFFE 298
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
530-790 1.42e-09

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: 59.63  E-value: 1.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 530 QIGSGGSSKVFQVLNEKKQIYA----IKYVNLEEADNQtldSYRNEIAYLNKLQQHSdkIIRLYDY-------EITDQYI 598
Cdd:cd14033   8 EIGRGSFKTVYRGLDTETTVEVawceLQTRKLSKGERQ---RFSEEVEMLKGLQHPN--IVRFYDSwkstvrgHKCIILV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNidLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHG--IVHSDLKPANFLIV--DGMLKLIDFGIANQMQpd 674
Cdd:cd14033  83 TELMTSGT--LKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITgpTGSVKIGDLGLATLKR-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 tTSVVKdSQVGTVNYMPPEAIKDmsssrengksksKISPKSDVWSLGCILYYMTYGKTPFQQIIN--QI-SKLHAIIDPN 751
Cdd:cd14033 159 -ASFAK-SVIGTPEFMAPEMYEE------------KYDEAVDVYAFGMCILEMATSEYPYSECQNaaQIyRKVTSGIKPD 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23308722 752 --HEIEFPDipekdLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14033 225 sfYKVKVPE-----LKEIIEGCIRTDKDERFTIQDLLEHRF 260
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
518-734 1.52e-09

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: 59.82  E-value: 1.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 518 ISVKGRiysilkQIGSGGSSKVFQ-VLNEK----KQIYAIKYVNLEEADNQtldsYRNEIAYLNKLQQhsDKIIRLYDYE 592
Cdd:cd14158  16 ISVGGN------KLGEGGFGVVFKgYINDKnvavKKLAAMVDISTEDLTKQ----FEQEIQVMAKCQH--ENLVELLGYS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 593 IT-DQY--IYMVMECGNI-DLNSWLKKKKSIdPWE-RKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGML-KLIDFG 666
Cdd:cd14158  84 CDgPQLclVYTYMPNGSLlDRLACLNDTPPL-SWHmRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVpKISDFG 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 667 IANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRengkskskispkSDVWSLGCILYYMTYGKTPF 734
Cdd:cd14158 163 LARASEKFSQTIMTERIVGTTAYMAPEALRGEITPK------------SDIFSFGVVLLEIITGLPPV 218
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
644-785 1.53e-09

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: 60.81  E-value: 1.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDG-MLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDmsssrengkskSKISPKSDVWSLGC 722
Cdd:cd05105 259 VHRDLAARNVLLAQGkIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFD-----------NLYTTLSDVWSYGI 327
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 723 ILYYM-TYGKTPFQQIINQiSKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05105 328 LLWEIfSLGGTPYPGMIVD-STFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHL 390
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
531-790 1.63e-09

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: 59.20  E-value: 1.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNE--KKQIyAIKYVNleeADNQTLDSYRNEIAYLNKLQQHsdKIIRLYD-YEITDQYIYMV--MECG 605
Cdd:cd14115   1 IGRGRFSIVKKCLHKatRKDV-AVKFVS---KKMKKKEQAAHEAALLQHLQHP--QYITLHDtYESPTSYILVLelMDDG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NidLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM----LKLIDFGIANQMqpdTTSVVKD 681
Cdd:cd14115  75 R--LLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvprVKLIDLEDAVQI---SGHRHVH 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 SQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF------QQIINqISKLHAIIDPNHeie 755
Cdd:cd14115 150 HLLGNPEFAAPEVIQGTPVS-----------LATDIWSIGVLTYVMLSGVSPFldeskeETCIN-VCRVDFSFPDEY--- 214
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 756 FPDIPEKdLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14115 215 FGDVSQA-ARDFINVILQEDPRRRPTAATCLQHPW 248
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
527-779 2.22e-09

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 59.13  E-value: 2.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKKQIYAIKyvNLEEAdNQTLDSYRNEiAYLNKLQQHsDKIIRLYDYeITDQYIYMVME-CG 605
Cdd:cd05067  11 LVERLGAGQFGEVWMGYYNGHTKVAIK--SLKQG-SMSPDAFLAE-ANLMKQLQH-QRLVRLYAV-VTQEPIYIITEyME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKKKSIDPWERK--SYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQpDTTSVVKDS 682
Cdd:cd05067  85 NGSLVDFLKTPSGIKLTINKllDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLsCKIADFGLARLIE-DNEYTAREG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 QVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIINqiSKLHAIIDPNHEIEFPDIPE 761
Cdd:cd05067 164 AKFPIKWTAPEAINYGTFTIKS-----------DVWSFGILLTeIVTHGRIPYPGMTN--PEVIQNLERGYRMPRPDNCP 230
                       250
                ....*....|....*...
gi 23308722 762 KDLQDVLKCCLKRDPKQR 779
Cdd:cd05067 231 EELYQLMRLCWKERPEDR 248
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
531-734 2.46e-09

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


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 59.05  E-value: 2.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNQTLdSYRNEIAYLNKLQQHSdkIIRLYDY---EITDQYIYMVMECGNI 607
Cdd:cd14664   1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEGTQGGDH-GFQAEIQTLGMIRHRN--IVRLRGYcsnPTTNLLVYEYMPNGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 608 D--LNSWLKKKKSIDpWERKSywKNMLEAVHTI---HQHG---IVHSDLKPANFLIVDGMLKLI-DFGIANQMQPDTTSV 678
Cdd:cd14664  78 GelLHSRPESQPPLD-WETRQ--RIALGSARGLaylHHDCsplIIHRDVKSNNILLDEEFEAHVaDFGLAKLMDDKDSHV 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 679 VKdSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPF 734
Cdd:cd14664 155 MS-SVAGSYGYIAPEYAYTGKVSEKS-----------DVYSYGVVLLELITGKRPF 198
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
528-724 2.70e-09

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: 59.06  E-value: 2.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQVLNE-KKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQhsdkiIRLYDY-----EITDQYIYMV 601
Cdd:cd14049  11 IARLGKGGYGKVYKVRNKlDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQH-----PNIVGYhtawmEHVQLMLYIQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNIDLNSWLKKKKSiDPWERK---------------SYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIV-DGMLKLID 664
Cdd:cd14049  86 MQLCELSLWDWIVERNK-RPCEEEfksapytpvdvdvttKILQQLLEGVTYIHSMGIVHRDLKPRNiFLHGsDIHVRIGD 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 665 FGIA--NQMQPDTTSVVKD--------SQVGTVNYMPPEAIK----DMSSsrengkskskispksDVWSLGCIL 724
Cdd:cd14049 165 FGLAcpDILQDGNDSTTMSrlnglthtSGVGTCLYAAPEQLEgshyDFKS---------------DMYSIGVIL 223
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
638-787 3.25e-09

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: 58.56  E-value: 3.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 638 IHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKdMsssrengKSKSKISPKSD 716
Cdd:cd14062 105 LHAKNIIHRDLKSNNiFLHEDLTVKIGDFGLATVKTRWSGSQQFEQPTGSILWMAPEVIR-M-------QDENPYSFQSD 176
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 717 VWSLGCILYYMTYGKTPFQQIIN--QISKL--HAIIDPNHEIEFPDIPeKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd14062 177 VYAFGIVLYELLTGQLPYSHINNrdQILFMvgRGYLRPDLSKVRSDTP-KALRRLMEDCIKFQRDERPLFPQILA 250
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
627-790 3.48e-09

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: 58.74  E-value: 3.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 627 YWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSVvkDSQVGTVNYMPPEAIKDmsssreng 705
Cdd:cd05608 110 YTAQIISGLEHLHQRRIIYRDLKPENVLLDDdGNVRISDLGLAVELKDGQTKT--KGYAGTPGFMAPELLLG-------- 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 706 kskSKISPKSDVWSLGCILYYMTYGKTPF----QQIINQISKLHAIIDPnheIEFPDIPEKDLQDVLKCCLKRDPKQRI- 780
Cdd:cd05608 180 ---EEYDYSVDYFTLGVTLYEMIAARGPFrargEKVENKELKQRILNDS---VTYSEKFSPASKSICEALLAKDPEKRLg 253
                       170
                ....*....|....
gi 23308722 781 ----SIPELLAHPY 790
Cdd:cd05608 254 frdgNCDGLRTHPF 267
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
569-791 3.60e-09

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 58.50  E-value: 3.60e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 569 RNEIAYLNKLQQHSdkIIRLYDYEIT--DQYIYMVMECGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHS 646
Cdd:cd14088  47 KNEINILKMVKHPN--ILQLVDVFETrkEYFIFLELATGR-EVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHR 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 647 DLKPANFLIVDGM----LKLIDFGIANQmqpdTTSVVKDSqVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGC 722
Cdd:cd14088 124 NLKLENLVYYNRLknskIVISDFHLAKL----ENGLIKEP-CGTPEYLAPEVVGRQRYGRP-----------VDCWAIGV 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 723 ILYYMTYGKTPFQQIINQ-------ISKLHAIIDPNHEIEFP--DIPEKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14088 188 IMYILLSGNPPFYDEAEEddyenhdKNLFRKILAGDYEFDSPywDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
644-779 3.62e-09

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: 59.53  E-value: 3.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDGML-KLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGC 722
Cdd:cd05104 236 IHRDLAARNILLTHGRItKICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFES-----------DVWSYGI 304
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 723 ILYYM-TYGKTPFQQIINQiSKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05104 305 LLWEIfSLGSSPYPGMPVD-SKFYKMIKEGYRMDSPEFAPSEMYDIMRSCWDADPLKR 361
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
557-785 5.83e-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: 58.44  E-value: 5.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 557 LEEADNQTldSYRNEIAYLNKLQQHSD-KIIRLYDYEITDQYIYMVMECGNI-DLNSWLKKKKSIDPW------------ 622
Cdd:cd05045  38 LKENASSS--ELRDLLSEFNLLKQVNHpHVIKLYGACSQDGPLLLIVEYAKYgSLRSFLRESRKVGPSylgsdgnrnssy 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 623 -----ERKSYWKNML-------EAVHTIHQHGIVHSDLKPANFLIVDG-MLKLIDFGIANQMQPDTTSVVKDSQVGTVNY 689
Cdd:cd05045 116 ldnpdERALTMGDLIsfawqisRGMQYLAEMKLVHRDLAARNVLVAEGrKMKISDFGLSRDVYEEDSYVKRSKGRIPVKW 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 690 MPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIINQisKLHAIIDPNHEIEFPDIPEKDLQDVL 768
Cdd:cd05045 196 MAIESLFDHIYTTQS-----------DVWSFGVLLWeIVTLGGNPYPGIAPE--RLFNLLKTGYRMERPENCSEEMYNLM 262
                       250
                ....*....|....*..
gi 23308722 769 KCCLKRDPKQRISIPEL 785
Cdd:cd05045 263 LTCWKQEPDKRPTFADI 279
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
529-792 7.97e-09

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: 58.40  E-value: 7.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQV-LNEKKQIYAIKY----VNLEEADNQ-TLDSYRN-EIAYLNKLQQHsdkiirLYDYEITDQYIYMV 601
Cdd:cd05619  11 KMLGKGSFGKVFLAeLKGTNQFFAIKAlkkdVVLMDDDVEcTMVEKRVlSLAWEHPFLTH------LFCTFQTKENLFFV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQmqpdttSVV 679
Cdd:cd05619  85 MEYLNGgDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLdKDGHIKIADFGMCKE------NML 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQV----GTVNYMPPEAIkdmsssrengkSKSKISPKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHeiE 755
Cdd:cd05619 159 GDAKTstfcGTPDYIAPEIL-----------LGQKYNTSVDWWSFGVLLYEMLIGQSPFHG-QDEEELFQSIRMDNP--F 224
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 756 FPDIPEKDLQDVLKCCLKRDPKQRISIP-ELLAHPYVQ 792
Cdd:cd05619 225 YPRWLEKEAKDILVKLFVREPERRLGVRgDIRQHPFFR 262
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
521-788 9.45e-09

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 57.16  E-value: 9.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 521 KGRIYSILKQIGSGGSS------KVFQVLNEKKQIYAiKYVNLEEADNQT----LDSYRNE-IAYLNKLQQHSDKIIRL- 588
Cdd:cd14112  13 RGRFSVIVKAVDSTTETdahcavKIFEVSDEASEAVR-EFESLRTLQHENvqrlIAAFKPSnFAYLVMEKLQEDVFTRFs 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 589 YDYEITDQYIYMVMecgnidlnswlkkkksidpwerksywKNMLEAVHTIHQHGIVHSDLKPANFLIVDG---MLKLIDF 665
Cdd:cd14112  92 SNDYYSEEQVATTV--------------------------RQILDALHYLHFKGIAHLDVQPDNIMFQSVrswQVKLVDF 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 666 GIAnqmQPDTTSVVKDSQvGTVNYMPPEAIKDmsssrengksKSKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLH 745
Cdd:cd14112 146 GRA---QKVSKLGKVPVD-GDTDWASPEFHNP----------ETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETK 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 746 AIIDpNHEIEFPDIPEKDLQDVLK---CCLKRDPKQRISIPELLAH 788
Cdd:cd14112 212 ENVI-FVKCRPNLIFVEATQEALRfatWALKKSPTRRMRTDEALEH 256
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
566-791 1.04e-08

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: 57.14  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 566 DSYRNEIAYLNKLQQHsdKIIRLYDYEITDQ---YIYMVMECGNIDLNSWLKKKKSIDPwER--KSYWKNMLEAVHTIHQ 640
Cdd:cd14109  41 PFLMREVDIHNSLDHP--NIVQMHDAYDDEKlavTVIDNLASTIELVRDNLLPGKDYYT-ERqvAVFVRQLLLALKHMHD 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 641 HGIVHSDLKPANFLIVDGMLKLIDFGIANQMQpdttsvvkDSQVGTVNYMPPEAIKDMSSSRENgkskskISPKSDVWSL 720
Cdd:cd14109 118 LGIAHLDLRPEDILLQDDKLKLADFGQSRRLL--------RGKLTTLIYGSPEFVSPEIVNSYP------VTLATDMWSV 183
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 721 GCILYYMTYGKTPFQQiINQISKLHAIIDPNHeiEFPDIP----EKDLQDVLKCCLKRDPKQRISIPELLAHPYV 791
Cdd:cd14109 184 GVLTYVLLGGISPFLG-DNDRETLTNVRSGKW--SFDSSPlgniSDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
529-785 1.11e-08

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


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 56.81  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQ--VLNEKKQIYAIKYvnleeadNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYeITDQYIYMVMEC-- 604
Cdd:cd05083  12 EIIGEGEFGAVLQgeYMGQKVAVKNIKC-------DVTAQAFLEETAVMTKLQHKN--LVRLLGV-ILHNGLYIVMELms 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 -GNidLNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIA--NQMQPDTTSV 678
Cdd:cd05083  82 kGN--LVNFLRSRgrALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSeDGVAKISDFGLAkvGSMGVDNSRL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vkdsqvgTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQI-INQISKLhaiIDPNHEIEF 756
Cdd:cd05083 160 -------PVKWTAPEALKNKKFSSKS-----------DVWSYGVLLWEVfSYGRAPYPKMsVKEVKEA---VEKGYRMEP 218
                       250       260
                ....*....|....*....|....*....
gi 23308722 757 PDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05083 219 PEGCPPDVYSIMTSCWEAEPGKRPSFKKL 247
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
631-790 1.16e-08

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: 57.71  E-value: 1.16e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 631 MLEAVHTIHQHGIVHSDLKPANFLIVDG--------------------MLKLIDFGIANQMQPDTTSVVkdsqvGTVNYM 690
Cdd:cd14214 126 LCHALKFLHENQLTHTDLKPENILFVNSefdtlynesksceeksvkntSIRVADFGSATFDHEHHTTIV-----ATRHYR 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 691 PPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQ-----ISKLHAIIdPNHEI----------- 754
Cdd:cd14214 201 PPEVILELGWAQP-----------CDVWSLGCILFEYYRGFTLFQTHENRehlvmMEKILGPI-PSHMIhrtrkqkyfyk 268
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23308722 755 -------------------------EFPDIPEK-DLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14214 269 gslvwdenssdgryvsenckplmsyMLGDSLEHtQLFDLLRRMLEFDPALRITLKEALLHPF 330
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
531-783 1.24e-08

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: 57.01  E-value: 1.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIY------AIKYVNLEEADNQTldsyrnEIAYLNKLQQHS-DKIIRLYDYEITDQYIYMVME 603
Cdd:cd13992   3 CGSGASSHTGEPKYVKKVGVyggrtvAIKHITFSRTEKRT------ILQELNQLKELVhDNLNKFIGICINPPNIAVVTE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKK-SIDpWE-RKSYWKNMLEAVHTIH-QHGIVHSDLKPANFLiVDG--MLKLIDFGIANQMQPDTTS 677
Cdd:cd13992  77 yCTRGSLQDVLLNREiKMD-WMfKSSFIKDIVKGMNYLHsSSIGYHGRLKSSNCL-VDSrwVVKLTDFGLRNLLEEQTNH 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVN-YMPPEAIKDMSSSREngkskskISPKSDVWSLGCILY---------YMTYGKTPFQQIINQISKLHA- 746
Cdd:cd13992 155 QLDEDAQHKKLlWTAPELLRGSLLEVR-------GTQKGDVYSFAIILYeilfrsdpfALEREVAIVEKVISGGNKPFRp 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 747 -IIDPNHEIefpdipEKDLQDVLKCCLKRDPKQRISIP 783
Cdd:cd13992 228 eLAVLLDEF------PPRLVLLVKQCWAENPEKRPSFK 259
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
525-791 1.44e-08

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: 57.40  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYV-NLEEADNQTLdsyrNEIAYLNKLQQhSDK-----IIRLYDYEITDQY 597
Cdd:cd14225  45 YEILEVIGKGSFGQVVKALDHKtNEHVAIKIIrNKKRFHHQAL----VEVKILDALRR-KDRdnshnVIHMKEYFYFRNH 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKKKK----SIDPWERKSYwkNMLEAVHTIHQHGIVHSDLKPANFLIV---DGMLKLIDFGianq 670
Cdd:cd14225 120 LCITFELLGMNLYELIKKNNfqgfSLSLIRRFAI--SLLQCLRLLYRERIIHCDLKPENILLRqrgQSSIKVIDFG---- 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 671 mqpdtTSVVKDSQVGTV----NYMPPEAIKDMSSSrengkskskisPKSDVWSLGCIL--YYMTYGKTPFQQIINQISKL 744
Cdd:cd14225 194 -----SSCYEHQRVYTYiqsrFYRSPEVILGLPYS-----------MAIDMWSLGCILaeLYTGYPLFPGENEVEQLACI 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 745 HAIID--PNHEIE-------FPD---IPE--------------KDLQDVLKC-----------CLKRDPKQRISIPELLA 787
Cdd:cd14225 258 MEVLGlpPPELIEnaqrrrlFFDskgNPRcitnskgkkrrpnsKDLASALKTsdplfldfirrCLEWDPSKRMTPDEALQ 337

                ....
gi 23308722 788 HPYV 791
Cdd:cd14225 338 HEWI 341
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
525-779 1.87e-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: 56.29  E-value: 1.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIYAIKYvnLEEADNQTLDSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMV--- 601
Cdd:cd05148   8 FTLERKLGSGYFGEVWEGLWKNRVRVAIKI--LKSDDLLKQQDFQKEVQALKRL--RHKHLISLFAVCSVGEPVYIItel 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNidLNSWLK--KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGML-KLIDFGIANQMQPDTTSV 678
Cdd:cd05148  84 MEKGS--LLAFLRspEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVcKVADFGLARLIKEDVYLS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vKDSQVgTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQIINQisKLHAIIDPNHEIEFP 757
Cdd:cd05148 162 -SDKKI-PYKWTAPEAASHGTFSTKS-----------DVWSFGILLYEMfTYGQVPYPGMNNH--EVYDQITAGYRMPCP 226
                       250       260
                ....*....|....*....|..
gi 23308722 758 DIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05148 227 AKCPQEIYKIMLECWAAEPEDR 248
STKc_CK1_fungal cd14127
Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; ...
525-735 2.73e-08

Catalytic domain of the Serine/Threonine protein kinase, Fungal Casein Kinase 1 homolog 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. This subfamily is composed of fungal CK1 homolog 1 proteins, also called Yck1 in Saccharomyces cerevisiae and Cki1 in Schizosaccharomyces pombe. Yck1 (or Yck1p) and Cki1 are plasma membrane-anchored proteins. Yck1 phosphorylates and regulates Khd1p, a RNA-binding protein that represses translation of bud-localized mRNA. Cki1 phosphorylates and regulates phosphatidylinositol (PI)-(4)P-5-kinase, which catalyzes the last step in the sythesis of PI(4,5)P2, which is involved in actin cytoskeleton remodeling and membrane traffic. The fungal CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271029 [Multi-domain]  Cd Length: 277  Bit Score: 55.96  E-value: 2.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQ---VLNekKQIYAIKYVNLEEADNQTLDSYRneiAYlnKLQQHSDKIIRLYDYEITDQYIYMV 601
Cdd:cd14127   2 YKVGKKIGEGSFGVIFEgtnLLN--GQQVAIKFEPRKSDAPQLRDEYR---TY--KLLAGCPGIPNVYYFGQEGLHNILV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNI---DLNSWLKKKKSIDPWERKSywKNMLEAVHTIHQHGIVHSDLKPANFLI------VDGMLKLIDFGIANQMQ 672
Cdd:cd14127  75 IDLLGPsleDLFDLCGRKFSVKTVVMVA--KQMLTRVQTIHEKNLIYRDIKPDNFLIgrpgtkNANVIHVVDFGMAKQYR 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23308722 673 PDTTSV-----VKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYMTYGKTPFQ 735
Cdd:cd14127 153 DPKTKQhipyrEKKSLSGTARYMSINTHLGREQSRRD-----------DLEALGHVFMYFLRGSLPWQ 209
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
626-785 2.82e-08

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 55.98  E-value: 2.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 626 SYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGM-LKLIDFGIANQMQPDTTS---VVKDSQVGTVNYMPPEAIKDMSS 700
Cdd:cd13991 102 HYLGQALEGLEYLHSRKILHGDVKADNVLLsSDGSdAFLCDFGHAECLDPDGLGkslFTGDYIPGTETHMAPEVVLGKPC 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 701 SREngkskskispkSDVWSLGCILYYMTYGKTPFQQIINQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd13991 182 DAK-----------VDVWSSCCMMLHMLNGCHPWTQYYSGPLCLKIANEPPPLREIPPSCAPLTAQAIQAGLRKEPVHRA 250

                ....*
gi 23308722 781 SIPEL 785
Cdd:cd13991 251 SAAEL 255
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
633-785 3.57e-08

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 55.37  E-value: 3.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 633 EAVHTIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQmqpdtTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskski 711
Cdd:cd05082 113 EAMEYLEGNNFVHRDLAARNVLVSeDNVAKVSDFGLTKE-----ASSTQDTGKLPVKWTAPEALREKKFSTKS------- 180
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 712 spksDVWSLGCILYYM-TYGKTPFQQIinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05082 181 ----DVWSFGILLWEIySFGRVPYPRI--PLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQL 249
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
527-787 3.96e-08

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: 55.81  E-value: 3.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQvlNEKKQIYAIKYVNLEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMVMECGN 606
Cdd:cd14149  16 LSTRIGSGSFGTVYK--GKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVN--ILLFMGYMTKDNLAIVTQWCEG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLK-KKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSVVKDSQV 684
Cdd:cd14149  92 SSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLtVKIGDFGLATVKSRWSGSQQVEQPT 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 685 GTVNYMPPEAIKDMSSSrengksksKISPKSDVWSLGCILYYMTYGKTPFQQIINQISKLHAI----IDPNHEIEFPDIP 760
Cdd:cd14149 172 GSILWMAPEVIRMQDNN--------PFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVgrgyASPDLSKLYKNCP 243
                       250       260
                ....*....|....*....|....*..
gi 23308722 761 eKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd14149 244 -KAMKRLVADCIKKVKEERPLFPQILS 269
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
527-786 4.94e-08

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


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 55.05  E-value: 4.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVF------QVlnekkqiyAIKYVNLEEADNQTLDSYRNEIAylNKLQQHSDKIIRLYDYEITDQYIYM 600
Cdd:cd14063   4 IKEVIGKGRFGRVHrgrwhgDV--------AIKLLNIDYLNEEQLEAFKEEVA--AYKNTRHDNLVLFMGACMDPPHLAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VME-CGNIDLNSWLKKKKSIDPWER-KSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFG------IANQMQ 672
Cdd:cd14063  74 VTSlCKGRTLYSLIHERKEKFDFNKtVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVVITDFGlfslsgLLQPGR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 673 PDTTSVVKDsqvGTVNYMPPEAIKDMSSSRENGkSKSKISPKSDVWSLGCILYYMTYGKTPFQ-----QIINQISKLHAI 747
Cdd:cd14063 154 REDTLVIPN---GWLCYLAPEIIRALSPDLDFE-ESLPFTKASDVYAFGTVWYELLAGRWPFKeqpaeSIIWQVGCGKKQ 229
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 748 IDPNHeiefpDIPeKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14063 230 SLSQL-----DIG-REVKDILMQCWAYDPEKRPTFSDLL 262
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
525-724 5.21e-08

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: 55.91  E-value: 5.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKKQIY-AIKYVNLEEADNQTLDSyrnEIAYLNKLQQHsDK-----IIRLYDYEITDQYI 598
Cdd:cd14224  67 YEVLKVIGKGSFGQVVKAYDHKTHQHvALKMVRNEKRFHRQAAE---EIRILEHLKKQ-DKdntmnVIHMLESFTFRNHI 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNIDLNSWLKKKK----SIdPWERKsYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD---GMLKLIDFGianqm 671
Cdd:cd14224 143 CMTFELLSMNLYELIKKNKfqgfSL-QLVRK-FAHSILQCLDALHRNKIIHCDLKPENILLKQqgrSGIKVIDFG----- 215
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 672 qpdtTSVVKDSQVGTV----NYMPPEAIKDMSSSRengkskskispKSDVWSLGCIL 724
Cdd:cd14224 216 ----SSCYEHQRIYTYiqsrFYRAPEVILGARYGM-----------PIDMWSFGCIL 257
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
638-780 5.30e-08

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: 55.77  E-value: 5.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 638 IHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQ-MQP-DTTSVVkdsqVGTVNYMPPEAIKDMSSSRengkskskispK 714
Cdd:cd05589 117 LHEHKIVYRDLKLDNLLLdTEGYVKIADFGLCKEgMGFgDRTSTF----CGTPEFLAPEVLTDTSYTR-----------A 181
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 715 SDVWSLGCILYYMTYGKTPF-----QQIINQISklhaiidpNHEIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05589 182 VDWWGLGVLIYEMLVGESPFpgddeEEVFDSIV--------NDEVRYPRFLSTEAISIMRRLLRKNPERRL 244
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
531-786 5.85e-08

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: 55.04  E-value: 5.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVlNEKKQIYAIKYV--NLEEADNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQYIYMVMECGNID 608
Cdd:cd14147  11 IGIGGFGKVYRG-SWRGELVAVKAArqDPDEDISVTAESVRQE-ARLFAMLAHPN-IIALKAVCLEEPNLCLVMEYAAGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIV---HSDLKPANFLIV---------DGMLKLIDFGIANQMQPDTt 676
Cdd:cd14147  88 PLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLqpienddmeHKTLKITDFGLAREWHKTT- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 svvKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDPNHEIEF 756
Cdd:cd14147 167 ---QMSAAGTYAWMAPEVIKASTFSK-----------GSDVWSFGVLLWELLTGEVPYRG-IDCLAVAYGVAVNKLTLPI 231
                       250       260       270
                ....*....|....*....|....*....|
gi 23308722 757 PDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14147 232 PSTCPEPFAQLMADCWAQDPHRRPDFASIL 261
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
527-779 8.82e-08

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 54.33  E-value: 8.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKKQIYAIKYVNLEEADNqtlDSYRNEIAYLNKLQqHSdKIIRLYDYEITDQYIYMVMEC-G 605
Cdd:cd05068  12 LLRKLGSGQFGEVWEGLWNNTTPVAVKTLKPGTMDP---EDFLREAQIMKKLR-HP-KLIQLYAVCTLEEPIYIITELmK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKKKS-------IDPWERKSYWKNMLEAVHTIHQhgivhsDLKPANFLIVD-GMLKLIDFGIANQMQPDTts 677
Cdd:cd05068  87 HGSLLEYLQGKGRslqlpqlIDMAAQVASGMAYLESQNYIHR------DLAARNVLVGEnNICKVADFGLARVIKVED-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 vVKDSQVGT---VNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILY-YMTYGKTPF-----QQIINQisklhaiI 748
Cdd:cd05068 159 -EYEAREGAkfpIKWTAPEAANYNRFS-----------IKSDVWSFGILLTeIVTYGRIPYpgmtnAEVLQQ-------V 219
                       250       260       270
                ....*....|....*....|....*....|.
gi 23308722 749 DPNHEIEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05068 220 ERGYRMPCPPNCPPQLYDIMLECWKADPMER 250
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
571-757 1.18e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 54.85  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  571 EIAYLNKLQQHSdkIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKP 650
Cdd:PHA03207 136 EIDILKTISHRA--IINLIHAYRWKSTVCMVMPKYKCDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKT 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  651 AN-FLIVDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIK-DMSSSRengkskskispkSDVWSLGCILYYMT 728
Cdd:PHA03207 214 ENiFLDEPENAVLGDFGAACKLDAHPDTPQCYGWSGTLETNSPELLAlDPYCAK------------TDIWSAGLVLFEMS 281
                        170       180       190
                 ....*....|....*....|....*....|...
gi 23308722  729 YGKTPF--QQIINQISKLHAIID--PNHEIEFP 757
Cdd:PHA03207 282 VKNVTLfgKQVKSSSSQLRSIIRcmQVHPLEFP 314
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
638-780 1.30e-07

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 54.32  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 638 IHQHGIVHSDLKPANFLI-VDGMLKLIDFGIA--NQMQPDTTSVVkdsqVGTVNYMPPEAIKDMSSSRengkskskispK 714
Cdd:cd05587 113 LHSKGIIYRDLKLDNVMLdAEGHIKIADFGMCkeGIFGGKTTRTF----CGTPDYIAPEIIAYQPYGK-----------S 177
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 715 SDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDpnHEIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05587 178 VDWWAYGVLLYEMLAGQPPFDG-EDEDELFQSIME--HNVSYPKSLSKEAVSICKGLLTKHPAKRL 240
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
526-792 1.39e-07

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: 53.82  E-value: 1.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGGSSKVFQ------VLNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQQHsdKIIRLYDYEITDQYIY 599
Cdd:cd05061   9 TLLRELGQGSFGMVYEgnardiIKGEAETRVAVKTVN-ESASLRERIEFLNEASVMKGFTCH--HVVRLLGVVSKGQPTL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMEC-GNIDLNSWLKKKKSI---DPWERKSYWKNMLEAVHTI-------HQHGIVHSDLKPANFLIV-DGMLKLIDFGI 667
Cdd:cd05061  86 VVMELmAHGDLKSYLRSLRPEaenNPGRPPPTLQEMIQMAAEIadgmaylNAKKFVHRDLAARNCMVAhDFTVKIGDFGM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 668 ANQMQpdTTSVVKDSQVG--TVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYM-TYGKTPFQQIINQiSKL 744
Cdd:cd05061 166 TRDIY--ETDYYRKGGKGllPVRWMAPESLKDGVFT-----------TSSDMWSFGVVLWEItSLAEQPYQGLSNE-QVL 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 23308722 745 HAIIDPNHeIEFPDIPEKDLQDVLKCCLKRDPKQR---ISIPELLA---HPYVQ 792
Cdd:cd05061 232 KFVMDGGY-LDQPDNCPERVTDLMRMCWQFNPKMRptfLEIVNLLKddlHPSFP 284
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
585-785 1.45e-07

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: 53.47  E-value: 1.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 585 IIRLYDYEITDQYIYMVME-CGNIDLNSWLKKKKsiDPWERKSYWKNMLEA---VHTIHQHGIVHSDLKPANFLIVDG-M 659
Cdd:cd05085  55 IVKLIGVCTQRQPIYIVMElVPGGDFLSFLRKKK--DELKTKQLVKFSLDAaagMAYLESKNCIHRDLAARNCLVGENnA 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 660 LKLIDFGIANQMQPDTTSVVKDSQVgTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQII 738
Cdd:cd05085 133 LKISDFGMSRQEDDGVYSSSGLKQI-PIKWTAPEALNYGRYSSES-----------DVWSFGILLWeTFSLGVCPYPGMT 200
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 23308722 739 NQISKLHaiIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05085 201 NQQAREQ--VEKGYRMSAPQRCPEDIYKIMQRCWDYNPENRPKFSEL 245
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
525-734 1.70e-07

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: 54.27  E-value: 1.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVlnEKK---QIYAIKYvnLEEAD---NQTLDSYRNEIAYLnkLQQHSDKIIRLYdYEITDQY- 597
Cdd:cd05628   3 FESLKVIGRGAFGEVRLV--QKKdtgHVYAMKI--LRKADmleKEQVGHIRAERDIL--VEADSLWVVKMF-YSFQDKLn 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPD- 674
Cdd:cd05628  76 LYLIMEfLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLdSKGHVKLSDFGLCTGLKKAh 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 --------TTSVVKD------------------------SQVGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGC 722
Cdd:cd05628 156 rtefyrnlNHSLPSDftfqnmnskrkaetwkrnrrqlafSTVGTPDYIAPEVFMQTGYNK-----------LCDWWSLGV 224
                       250
                ....*....|..
gi 23308722 723 ILYYMTYGKTPF 734
Cdd:cd05628 225 IMYEMLIGYPPF 236
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
568-727 1.78e-07

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 54.10  E-value: 1.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 568 YRNEIAYLnKLQQHSDKIIRLYDYEITdQYIYMVME-CGNIDLNSWLKKKKSiDPWERKSYWKNMLEAVHTIHQHGIVHS 646
Cdd:cd13977  82 SSKSDLYL-LLVETSLKGERCFDPRSA-CYLWFVMEfCDGGDMNEYLLSRRP-DRQTNTSFMLQLSSALAFLHRNQIVHR 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 647 DLKPANFLIVDG----MLKLIDFGIAN-----QMQPDTTSVVK----DSQVGTVNYMPPEAIKDMSSSRengkskskisp 713
Cdd:cd13977 159 DLKPDNILISHKrgepILKVADFGLSKvcsgsGLNPEEPANVNkhflSSACGSDFYMAPEVWEGHYTAK----------- 227
                       170
                ....*....|....
gi 23308722 714 kSDVWSLGCILYYM 727
Cdd:cd13977 228 -ADIFALGIIIWAM 240
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
644-786 1.82e-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: 54.25  E-value: 1.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDGML-KLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIkdmsssrengkSKSKISPKSDVWSLGC 722
Cdd:cd05107 261 VHRDLAARNVLICEGKLvKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESI-----------FNNLYTTLSDVWSFGI 329
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 723 ILYYM-TYGKTPF------QQIINQISKLHAIIDPNHeiefpdiPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05107 330 LLWEIfTLGGTPYpelpmnEQFYNAIKRGYRMAKPAH-------ASDEIYEIMQKCWEEKFEIRPDFSQLV 393
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
566-779 1.87e-07

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 53.54  E-value: 1.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 566 DSYRNEIAYLNKLQQhsDKIIRLYDYeITDQYIYMVME-CGNIDLNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHG 642
Cdd:cd05069  52 EAFLQEAQIMKKLRH--DKLVPLYAV-VSEEPIYIVTEfMGKGSLLDFLKEGdgKYLKLPQLVDMAAQIADGMAYIERMN 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 643 IVHSDLKPANFLIVDGML-KLIDFGIANQMQpDTTSVVKDSQVGTVNYMPPEAikdmsssrengKSKSKISPKSDVWSLG 721
Cdd:cd05069 129 YIHRDLRAANILVGDNLVcKIADFGLARLIE-DNEYTARQGAKFPIKWTAPEA-----------ALYGRFTIKSDVWSFG 196
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 722 CILYYM-TYGKTPFQQIINQisKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05069 197 ILLTELvTKGRVPYPGMVNR--EVLEQVERGYRMPCPQGCPESLHELMKLCWKKDPDER 253
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
529-779 2.07e-07

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: 53.06  E-value: 2.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQVLNEKKQIYAIKYVnleEADNQTLDSYRNEIAYLNKLQqHsDKIIRLYDYEITDQYIYMV---MECG 605
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGTTKVAVKTL---KPGTMSPEAFLQEAQIMKKLR-H-DKLVQLYAVCSDEEPIYIVtelMSKG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NidLNSWLKkkksiDPWERKSYWKNMLEAVHTI-------HQHGIVHSDLKPANFLIVDG-MLKLIDFGIANQMQPDTTS 677
Cdd:cd05034  76 S--LLDYLR-----TGEGRALRLPQLIDMAAQIasgmaylESRNYIHRDLAARNILVGENnVCKVADFGLARLIEDDEYT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 vvkdSQVGT---VNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILY-YMTYGKTPF-----QQIINQISKLHAII 748
Cdd:cd05034 149 ----AREGAkfpIKWTAPEAALYGRFT-----------IKSDVWSFGILLYeIVTYGRVPYpgmtnREVLEQVERGYRMP 213
                       250       260       270
                ....*....|....*....|....*....|.
gi 23308722 749 DPnheiefPDIPEkDLQDVLKCCLKRDPKQR 779
Cdd:cd05034 214 KP------PGCPD-ELYDIMLQCWKKEPEER 237
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
529-779 2.30e-07

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 53.04  E-value: 2.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSG--GSSK--VFQVLNEKKQIyAIKYVNLEEADNQTLDSYRNEIaylNKLQQHSDK-IIRLYDyeITDQYIYM-VM 602
Cdd:cd05116   1 GELGSGnfGTVKkgYYQMKKVVKTV-AVKILKNEANDPALKDELLREA---NVMQQLDNPyIVRMIG--ICEAESWMlVM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECGNID-LNSWLKKKKSIDPwerksywKNMLEAVHTI-------HQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQP 673
Cdd:cd05116  75 EMAELGpLNKFLQKNRHVTE-------KNITELVHQVsmgmkylEESNFVHRDLAARNVLLVtQHYAKISDFGLSKALRA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 674 DTTSV-VKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIinQISKLHAIIDPN 751
Cdd:cd05116 148 DENYYkAQTHGKWPVKWYAPECMNYYKFSSKS-----------DVWSFGVLMWeAFSYGQKPYKGM--KGNEVTQMIEKG 214
                       250       260
                ....*....|....*....|....*...
gi 23308722 752 HEIEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05116 215 ERMECPAGCPPEMYDLMKLCWTYDVDER 242
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
569-792 2.34e-07

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: 53.90  E-value: 2.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 569 RNEIAYLNK-----LQQHSDKIIRLYdYEITDQ-YIYMVME-CGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQH 641
Cdd:cd05625  42 RNQVAHVKAerdilAEADNEWVVRLY-YSFQDKdNLYFVMDyIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKM 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 642 GIVHSDLKPANFLI-VDGMLKLIDFGI--------------------------------------ANQMQPDTTSVVKDS 682
Cdd:cd05625 121 GFIHRDIKPDNILIdRDGHIKLTDFGLctgfrwthdskyyqsgdhlrqdsmdfsnewgdpencrcGDRLKPLERRAARQH 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 Q-------VGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF---------QQIINQISKLHa 746
Cdd:cd05625 201 QrclahslVGTPNYIAPEVLLRTGYTQ-----------LCDWWSVGVILFEMLVGQPPFlaqtpletqMKVINWQTSLH- 268
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 23308722 747 iIDPNHEIEfpdiPE-KDLqdVLKCClkRDPKQRI---SIPELLAHPYVQ 792
Cdd:cd05625 269 -IPPQAKLS----PEaSDL--IIKLC--RGPEDRLgknGADEIKAHPFFK 309
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
525-784 2.39e-07

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: 53.46  E-value: 2.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVfqVLNEKK---QIYAIKY----VNLEEADNQTLDSYRNEIAYLNK----LQQHSDkiirlydYEI 593
Cdd:cd05616   2 FNFLMVLGKGSFGKV--MLAERKgtdELYAVKIlkkdVVIQDDDVECTMVEKRVLALSGKppflTQLHSC-------FQT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 594 TDQyIYMVMECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQM 671
Cdd:cd05616  73 MDR-LYFVMEYVNGgDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLdSEGHIKIADFGMCKEN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 672 QPDttSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQiINQISKLHAIIDpn 751
Cdd:cd05616 152 IWD--GVTTKTFCGTPDYIAPEIIAYQPYGKS-----------VDWWAFGVLLYEMLAGQAPFEG-EDEDELFQSIME-- 215
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 752 HEIEFPDIPEKDLQDVLKCCLKRDPKQRISI-PE 784
Cdd:cd05616 216 HNVAYPKSMSKEAVAICKGLMTKHPGKRLGCgPE 249
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
531-788 2.39e-07

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


Pssm-ID: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 52.88  E-value: 2.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVNLEEADNQTLdsyrNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVMECGNI-D 608
Cdd:cd14065   1 LGKGFFGEVYKVTHrETGKVMVMKELKRFDEQRSFL----KEVKLMRRLS-HPN-ILRFIGVCVKDNKLNFITEYVNGgT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 609 LNSWLKKKKSIDPW-ERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLI--DFGIANQMqPDTTSVVKD-- 681
Cdd:cd14065  75 LEELLKSMDEQLPWsQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreANRGRNAVvaDFGLAREM-PDEKTKKPDrk 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 682 ---SQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYymtygktpfqQIINQISKlhaiiDPNH------ 752
Cdd:cd14065 154 krlTVVGSPYWMAPEMLRGESYDEK-----------VDVFSFGIVLC----------EIIGRVPA-----DPDYlprtmd 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 753 ---------EIEFPDIPEKDLQDVLKCClKRDPKQRISIPELLAH 788
Cdd:cd14065 208 fgldvrafrTLYVPDCPPSFLPLAIRCC-QLDPEKRPSFVELEHH 251
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
633-789 2.48e-07

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: 53.00  E-value: 2.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 633 EAVHTIHQHGIVHSDLKPANFLIVD------GMLKLIDFGIANQMQPDTTSVVKdsqvGTVNYMPPEAIKdmsssrengk 706
Cdd:cd14000 123 DGLRYLHSAMIIYRDLKSHNVLVWTlypnsaIIIKIADYGISRQCCRMGAKGSE----GTPGFRAPEIAR---------- 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 707 SKSKISPKSDVWSLGCILYYMTYGKTPF---QQIINQISKLHAIIDPNHEIEfpDIPEKDLQDVLKCCLKRDPKQR---I 780
Cdd:cd14000 189 GNVIYNEKVDVFSFGMLLYEILSGGAPMvghLKFPNEFDIHGGLRPPLKQYE--CAPWPEVEVLMKKCWKENPQQRptaV 266

                ....*....
gi 23308722 781 SIPELLAHP 789
Cdd:cd14000 267 TVVSILNSP 275
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
531-735 2.51e-07

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: 53.29  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLnEKKQIYAIKYVNlEEAD---NQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQY---IYMVMEC 604
Cdd:cd14159   1 IGEGGFGCVYQAV-MRNTEYAVKRLK-EDSEldwSVVKNSFLTEVEKLSRFR-HPN-IVDLAGYSAQQGNyclIYVYLPN 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 GNIDLNSWLKKKKSIDPWE-RKSYWKNMLEAVHTIHQH--GIVHSDLKPANFLIVDG-MLKLIDFGIAN----QMQPDTT 676
Cdd:cd14159  77 GSLEDRLHCQVSCPCLSWSqRLHVLLGTARAIQYLHSDspSLIHGDVKSSNILLDAAlNPKLGDFGLARfsrrPKQPGMS 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 677 SVVKDSQV--GTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQ 735
Cdd:cd14159 157 STLARTQTvrGTLAYLPEEYVKTGTLSVE-----------IDVYSFGVVLLELLTGRRAME 206
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
640-733 2.51e-07

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: 53.51  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 640 QHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMqpdtTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVW 718
Cdd:cd06649 122 KHQIMHRDVKPSNILVNSrGEIKLCDFGVSGQL----IDSMANSFVGTRSYMSPERLQGTHYSVQS-----------DIW 186
                        90
                ....*....|....*
gi 23308722 719 SLGCILYYMTYGKTP 733
Cdd:cd06649 187 SMGLSLVELAIGRYP 201
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
578-781 2.92e-07

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 52.63  E-value: 2.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 578 LQQHSD-KIIRLYDYEITDQYIYMVME-CGNIDLNSWL-------KKKKSIDPWERKSYWKNMLEAVHTIHQhgivhsDL 648
Cdd:cd05084  48 LKQYSHpNIVRLIGVCTQKQPIYIVMElVQGGDFLTFLrtegprlKVKELIRMVENAAAGMEYLESKHCIHR------DL 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 649 KPANFLIVD-GMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-Y 726
Cdd:cd05084 122 AARNCLVTEkNVLKISDFGMSREEEDGVYAATGGMKQIPVKWTAPEALNYGRYSSES-----------DVWSFGILLWeT 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 727 MTYGKTPFQQIINQISKlhAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRIS 781
Cdd:cd05084 191 FSLGAVPYANLSNQQTR--EAVEQGVRLPCPENCPDEVYRLMEQCWEYDPRKRPS 243
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
531-779 3.32e-07

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: 52.84  E-value: 3.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEKKQIY-AIKYVNLE-EADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDY------EITDQYIYMVM 602
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYvAIKKCRQElSPSDKNRERWCLEVQIMKKLNH--PNVVSARDVppelekLSPNDLPLLAM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKS---IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDG----MLKLIDFGIANQMqpD 674
Cdd:cd13989  79 EyCSGGDLRKVLNQPENccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGggrvIYKLIDLGYAKEL--D 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTSVVKdSQVGTVNYMPPEAIKdmsSSRENgkskskisPKSDVWSLGCILYYMTYGKTPF---------QQIINQISKLH 745
Cdd:cd13989 157 QGSLCT-SFVGTLQYLAPELFE---SKKYT--------CTVDYWSFGTLAFECITGYRPFlpnwqpvqwHGKVKQKKPEH 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 23308722 746 AII--DPNHEIEF-PDIPEKD---------LQDVLKCCLKRDPKQR 779
Cdd:cd13989 225 ICAyeDLTGEVKFsSELPSPNhlssilkeyLESWLQLMLRWDPRQR 270
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
566-787 3.71e-07

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 52.19  E-value: 3.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 566 DSYRNEIAYLNKLqqHSDKIIRLYDYEITDQYIYMVME-CGNIDLNSWLKK-KKSIDPWERKSYWKNMLEAVHTIHQHGI 643
Cdd:cd05113  44 DEFIEEAKVMMNL--SHEKLVQLYGVCTKQRPIFIITEyMANGCLLNYLREmRKRFQTQQLLEMCKDVCEAMEYLESKQF 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSvvkdSQVGT---VNYMPPEAIKDMSSSREngkskskispkSDVWS 719
Cdd:cd05113 122 LHRDLAARNCLVNDqGVVKVSDFGLSRYVLDDEYT----SSVGSkfpVRWSPPEVLMYSKFSSK-----------SDVWA 186
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 720 LGCILYYM-TYGKTPFQQIINQISKLHaiIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd05113 187 FGVLMWEVySLGKMPYERFTNSETVEH--VSQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLS 253
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
531-779 5.23e-07

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: 52.23  E-value: 5.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLN-EKKQIYAIKYVNLEeADNQTLDSYRNEIAYLNKLQQ----HSDKIIRLYDYEITDQYIYMVMECG 605
Cdd:cd14039   1 LGTGGFGNVCLYQNqETGEKIAIKSCRLE-LSVKNKDRWCHEIQIMKKLNHpnvvKACDVPEEMNFLVNDVPLLAMEYCS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 606 NIDLNSWLKKKKS---IDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGML--KLIDFGIANQMqpDTTSV 678
Cdd:cd14039  80 GGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqeINGKIvhKIIDLGYAKDL--DQGSL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 VKdSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYMTYGKTPF----------QQIINQISK-LHAI 747
Cdd:cd14039 158 CT-SFVGTLQYLAPELFENKSYT-----------VTVDYWSFGTMVFECIAGFRPFlhnlqpftwhEKIKKKDPKhIFAV 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 23308722 748 IDPNHEIEFPD-IPEKD---------LQDVLKCCLKRDPKQR 779
Cdd:cd14039 226 EEMNGEVRFSThLPQPNnlcslivepMEGWLQLMLNWDPVQR 267
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
625-697 5.86e-07

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: 52.44  E-value: 5.86e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 625 KSYWKNMLEAVHTIHQHGIVHSDLKPANFLI--VDGMLKLIDFGIAnqmqpdttsvvKDSQVGtVNYMPPEAIKD 697
Cdd:cd14013 123 KSIMRQILVALRKLHSTGIVHRDVKPQNIIVseGDGQFKIIDLGAA-----------ADLRIG-INYIPKEFLLD 185
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
514-780 6.66e-07

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: 52.31  E-value: 6.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 514 ANECISVKGRIYSILKQIGSGGSSKVfqVLNEKK---QIYAIKY----VNLEEADNQTLDSYRNEIAYLNK----LQQHS 582
Cdd:cd05615   1 SNNLDRVRLTDFNFLMVLGKGSFGKV--MLAERKgsdELYAIKIlkkdVVIQDDDVECTMVEKRVLALQDKppflTQLHS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 583 DkiirlydYEITDQyIYMVMECGNI-DLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGML 660
Cdd:cd05615  79 C-------FQTVDR-LYFVMEYVNGgDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLdSEGHI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 661 KLIDFGIANQMQPDttSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTPFQQiINQ 740
Cdd:cd05615 151 KIADFGMCKEHMVE--GVTTRTFCGTPDYIAPEIIAYQPYGRS-----------VDWWAYGVLLYEMLAGQPPFDG-EDE 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 741 ISKLHAIIDpnHEIEFPDIPEKDLQDVLKCCLKRDPKQRI 780
Cdd:cd05615 217 DELFQSIME--HNVSYPKSLSKEAVSICKGLMTKHPAKRL 254
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
586-797 8.45e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 51.40  E-value: 8.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  586 IRLYDYEITDQYIYMVM---ECGniDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM--L 660
Cdd:PHA03390  72 IKLYYSVTTLKGHVLIMdyiKDG--DLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKdrI 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  661 KLIDFGIANQMqpDTTSVvkdsQVGTVNYMPPEAIKdmsssRENgkskskISPKSDVWSLGCILYYMTYGKTPFQ----Q 736
Cdd:PHA03390 150 YLCDYGLCKII--GTPSC----YDGTLDYFSPEKIK-----GHN------YDVSFDWWAVGVLTYELLTGKHPFKededE 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722  737 IINqISKLHAIIdpNHEIEFPDIPEKDLQDVLKCCLKRDPKQRIsipellaHPYVQIQTHP 797
Cdd:PHA03390 213 ELD-LESLLKRQ--QKKLPFIKNVSKNANDFVQSMLKYNINYRL-------TNYNEIIKHP 263
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
631-790 8.91e-07

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: 51.78  E-value: 8.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 631 MLEAVHTIHQHGIVHSDLKPANFLIVDGM--------------------LKLIDFGIANQMQPDTTSVVKdsqvgTVNYM 690
Cdd:cd14213 125 ICKSVNFLHHNKLTHTDLKPENILFVQSDyvvkynpkmkrdertlknpdIKVVDFGSATYDDEHHSTLVS-----TRHYR 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 691 PPEAIKDMSSSRengkskskispKSDVWSLGCIL--YYMtyGKTPFQqiiNQISKLH-AIID------PNHEI------- 754
Cdd:cd14213 200 APEVILALGWSQ-----------PCDVWSIGCILieYYL--GFTVFQ---THDSKEHlAMMErilgplPKHMIqktrkrk 263
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 755 ---------------------------EF---PDIPEKDLQDVLKCCLKRDPKQRISIPELLAHPY 790
Cdd:cd14213 264 yfhhdqldwdehssagryvrrrckplkEFmlsQDVDHEQLFDLIQKMLEYDPAKRITLDEALKHPF 329
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
521-730 1.16e-06

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 51.42  E-value: 1.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 521 KGRiYSILKQIGSGGSSKVFQVLNEKKQIY-AIKYVnlEEADNQTlDSYRNEIAYLNKLQQHS------DKIIRLYDY-E 592
Cdd:cd14136   9 NGR-YHVVRKLGWGHFSTVWLCWDLQNKRFvALKVV--KSAQHYT-EAALDEIKLLKCVREADpkdpgrEHVVQLLDDfK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 593 ITD---QYIYMVMECGNIDLNSWLKK-----------KKSIdpwerksywKNMLEAVHTIH-QHGIVHSDLKPANFLIVD 657
Cdd:cd14136  85 HTGpngTHVCMVFEVLGPNLLKLIKRynyrgiplplvKKIA---------RQVLQGLDYLHtKCGIIHTDIKPENVLLCI 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 658 GML--KLIDFGIANQMQPDTTSVVKDSQvgtvnYMPPEAI--KDMSSSrengkskskispkSDVWSLGCILYYMTYG 730
Cdd:cd14136 156 SKIevKIADLGNACWTDKHFTEDIQTRQ-----YRSPEVIlgAGYGTP-------------ADIWSTACMAFELATG 214
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
634-779 1.41e-06

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: 51.12  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 634 AVHTIHQHGIVHSDLKPANFLIVDG----MLKLIDFGIANQMqpDTTSVVKdSQVGTVNYMPPEAIKDMSSSrengksks 709
Cdd:cd14038 113 ALRYLHENRIIHRDLKPENIVLQQGeqrlIHKIIDLGYAKEL--DQGSLCT-SFVGTLQYLAPELLEQQKYT-------- 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 710 kisPKSDVWSLGCILYYMTYGKTPF----QQI-----INQISKLHAII--DPNHEIEFPD----------IPEKDLQDVL 768
Cdd:cd14038 182 ---VTVDYWSFGTLAFECITGFRPFlpnwQPVqwhgkVRQKSNEDIVVyeDLTGAVKFSSvlptpnnlngILAGKLERWL 258
                       170
                ....*....|.
gi 23308722 769 KCCLKRDPKQR 779
Cdd:cd14038 259 QCMLMWHPRQR 269
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
518-746 1.53e-06

putative serine/threonine kinase; Provisional


Pssm-ID: 165211 [Multi-domain]  Cd Length: 294  Bit Score: 50.72  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  518 ISVKGRIYSILKQIGSGGSSKVFQVLNEKKQIYAIKYV-NLEEADNQTLDSyrnEIAYLNKLQQhSDKIIRLYDYEITDQ 596
Cdd:PHA02882   7 IDITGKEWKIDKLIGCGGFGCVYETQCASDHCINNQAVaKIENLENETIVM---ETLVYNNIYD-IDKIALWKNIHNIDH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  597 ------------------YIYMVMECGNIDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANfLIVDG 658
Cdd:PHA02882  83 lgipkyygcgsfkrcrmyYRFILLEKLVENTKEIFKRIKCKNKKLIKNIMKDMLTTLEYIHEHGISHGDIKPEN-IMVDG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  659 MLK--LIDFGIANQMQPDTTSV-----VKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLG-CILYYMTYg 730
Cdd:PHA02882 162 NNRgyIIDYGIASHFIIHGKHIeyskeQKDLHRGTLYYAGLDAHNGACVTRRG-----------DLESLGyCMLKWAGI- 229
                        250
                 ....*....|....*.
gi 23308722  731 KTPFQQIINQISKLHA 746
Cdd:PHA02882 230 KLPWKGFGHNGNLIHA 245
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
638-781 1.55e-06

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: 50.84  E-value: 1.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 638 IHQHGIVHSDLKPANFLI-VDGMLKLIDFGIAnqMQPDTTSVVKD----SQVGTVNYMPPEAIK------DMSSSREngk 706
Cdd:cd14055 123 RPKIPIAHRDLKSSNILVkNDGTCVLADFGLA--LRLDPSLSVDElansGQVGTARYMAPEALEsrvnleDLESFKQ--- 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 707 skskispkSDVWSLGCILYYMT-----------YgKTPFQQIINQisklHAIIDPN-----HEIEFPDIPEK-------- 762
Cdd:cd14055 198 --------IDVYSMALVLWEMAsrceasgevkpY-ELPFGSKVRE----RPCVESMkdlvlRDRGRPEIPDSwlthqgmc 264
                       170
                ....*....|....*....
gi 23308722 763 DLQDVLKCCLKRDPKQRIS 781
Cdd:cd14055 265 VLCDTITECWDHDPEARLT 283
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
526-786 1.60e-06

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 50.52  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGGSSKVfqVLNEKKQIY--AIKYVNlEEADNQtlDSYRNEIAYLNKLQqHSdKIIRLYDYEITDQYIYMVME 603
Cdd:cd05059   7 TFLKELGSGQFGVV--HLGKWRGKIdvAIKMIK-EGSMSE--DDFIEEAKVMMKLS-HP-KLVQLYGVCTKQRPIFIVTE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 -CGNIDLNSWLKKKKSIDpwerKSYW-----KNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTT 676
Cdd:cd05059  80 yMANGCLLNYLRERRGKF----QTEQllemcKDVCEAMEYLESNGFIHRDLAARNCLVgEQNVVKVSDFGLARYVLDDEY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SvvkdSQVGT---VNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYM-TYGKTPFQQIINqiSKLHAIIDPNH 752
Cdd:cd05059 156 T----SSVGTkfpVKWSPPEVFMYSKFSSK-----------SDVWSFGVLMWEVfSEGKMPYERFSN--SEVVEHISQGY 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 753 EIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05059 219 RLYRPHLAPTEVYTIMYSCWHEKPEERPTFKILL 252
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
614-785 1.60e-06

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: 50.72  E-value: 1.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 614 KKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPP 692
Cdd:cd05111 101 QHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLkSPSQVQVADFGVADLLYPDDKKYFYSEAKTPIKWMAL 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 693 EAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCC 771
Cdd:cd05111 181 ESIHFGKYTHQS-----------DVWSYGVTVWeMMTFGAEPYAGM--RLAEVPDLLEKGERLAQPQICTIDVYMVMVKC 247
                       170
                ....*....|....
gi 23308722 772 LKRDPKQRISIPEL 785
Cdd:cd05111 248 WMIDENIRPTFKEL 261
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
620-792 1.80e-06

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: 50.40  E-value: 1.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 620 DPWERKSYWKNMLEAVHTIHQ--------H---GIVHSDLKPAN-FLIVDGMLKL--IDFGIANQMQPDTTSVVKDSQVG 685
Cdd:cd14011 102 PPPELQDYKLYDVEIKYGLLQisealsflHndvKLVHGNICPESvVINSNGEWKLagFDFCISSEQATDQFPYFREYDPN 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 686 TV-------NYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQIINQIS--KLHAIIDPNHEIE 755
Cdd:cd14011 182 LPplaqpnlNYLAPEYILSKTCDPAS-----------DMFSLGVLIYAIyNKGKPLFDCVNNLLSykKNSNQLRQLSLSL 250
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 23308722 756 FPDIPEKdLQDVLKCCLKRDPKQRISIPELLAHPYVQ 792
Cdd:cd14011 251 LEKVPEE-LRDHVKTLLNVTPEVRPDAEQLSKIPFFD 286
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
644-794 1.84e-06

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 48.94  E-value: 1.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    644 VHSDLKPAN-FLIVDGMLKLidFGIANQMQPDTtsvvkdSQVGTVnYMPPEAIKDMSSSREngkskskispkSDVWSLGC 722
Cdd:smart00750  33 LHRQAKSGNiLLTWDGLLKL--DGSVAFKTPEQ------SRPDPY-FMAPEVIQGQSYTEK-----------ADIYSLGI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722    723 ILYYMTYGKTPFQQiINQISK-LHAIID--PNHEIEFPDIPEKDLQ-----DVLKCCLKRDPKQRISIPELLAHPYVQIQ 794
Cdd:smart00750  93 TLYEALDYELPYNE-ERELSAiLEILLNgmPADDPRDRSNLEGVSAarsfeDFMRLCASRLPQRREAANHYLAHCRALFA 171
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
571-779 1.96e-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: 49.91  E-value: 1.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 571 EIAYLNKLQQHsDKIIRLYDYeITDQYIYMVME-CGNIDLNSWLKKK--KSIDPWERKSYWKNMLEAVHTIHQHGIVHSD 647
Cdd:cd14203  39 EEAQIMKKLRH-DKLVQLYAV-VSEEPIYIVTEfMSKGSLLDFLKDGegKYLKLPQLVDMAAQIASGMAYIERMNYIHRD 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 648 LKPANFLIVDGML-KLIDFGIANQMQPDTTSVVKDSQVgTVNYMPPEAikdmsssrengKSKSKISPKSDVWSLGCILYY 726
Cdd:cd14203 117 LRAANILVGDNLVcKIADFGLARLIEDNEYTARQGAKF-PIKWTAPEA-----------ALYGRFTIKSDVWSFGILLTE 184
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 727 M-TYGKTPF-----QQIINQISKLHAIIDPnheiefPDIPEKdLQDVLKCCLKRDPKQR 779
Cdd:cd14203 185 LvTKGRVPYpgmnnREVLEQVERGYRMPCP------PGCPES-LHELMCQCWRKDPEER 236
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
637-792 2.00e-06

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


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 50.51  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 637 TIHQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMQPDTTSVVKD--SQVGTVNYMPPEAIKD-MSSSRENgkskskIS 712
Cdd:cd13998 116 TQGKPAIAHRDLKSKNILVKnDGTCCIADFGLAVRLSPSTGEEDNAnnGQVGTKRYMAPEVLEGaINLRDFE------SF 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 713 PKSDVWSLGCILYYMT------------YgKTPFQQIInqisklhaiidPNHeiefPDIpeKDLQDVLkcCLKrdpKQRI 780
Cdd:cd13998 190 KRVDIYAMGLVLWEMAsrctdlfgiveeY-KPPFYSEV-----------PNH----PSF--EDMQEVV--VRD---KQRP 246
                       170
                ....*....|...
gi 23308722 781 SIPE-LLAHPYVQ 792
Cdd:cd13998 247 NIPNrWLSHPGLQ 259
PRK14879 PRK14879
Kae1-associated kinase Bud32;
621-668 2.17e-06

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 49.52  E-value: 2.17e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 23308722  621 PWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIA 668
Cdd:PRK14879  94 GMEELELSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDFGLA 141
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
644-786 2.21e-06

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 50.75  E-value: 2.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDG-MLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGC 722
Cdd:cd05102 194 IHRDLAARNILLSENnVVKICDFGLARDIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQS-----------DVWSFGV 262
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 723 ILYYM-TYGKTPFQQI-INQisKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05102 263 LLWEIfSLGASPYPGVqINE--EFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPTFSDLV 326
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
526-786 2.53e-06

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 49.86  E-value: 2.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGgsskVFQV--LNEKKQIY--AIKYVNlEEADNQtlDSYRNEIAYLNKLQqHSdKIIRLYDYEITDQYIYMV 601
Cdd:cd05114   7 TFMKELGSG----LFGVvrLGKWRAQYkvAIKAIR-EGAMSE--EDFIEEAKVMMKLT-HP-KLVQLYGVCTQQKPIYIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ---MECGNIdLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTS 677
Cdd:cd05114  78 tefMENGCL-LNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDtGVVKVSDFGMTRYVLDDQYT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 vvkdSQVGT---VNYMPPEAI--KDMSSSrengkskskispkSDVWSLGCILY-YMTYGKTPFQQIINQisKLHAIIDPN 751
Cdd:cd05114 157 ----SSSGAkfpVKWSPPEVFnySKFSSK-------------SDVWSFGVLMWeVFTEGKMPFESKSNY--EVVEMVSRG 217
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 752 HEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05114 218 HRLYRPKLASKSVYEVMYSCWHEKPEGRPTFADLL 252
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
644-786 2.55e-06

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 50.40  E-value: 2.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIV-DGMLKLIDFGIANQMQpdTTSVVKDSQVG--TVNYMPPEAIKDMSSSRENgkskskispksDVWSL 720
Cdd:cd05100 156 IHRDLAARNVLVTeDNVMKIADFGLARDVH--NIDYYKKTTNGrlPVKWMAPEALFDRVYTHQS-----------DVWSF 222
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 721 GCILYYM-TYGKTPFQQIinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05100 223 GVLLWEIfTLGGSPYPGI--PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLV 287
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
528-741 2.75e-06

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: 50.07  E-value: 2.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQ----VLNEKKQIYAIKYVNL-EEADNQTLDSYRNEIAYLNKLQqHSDkIIRLYDYEITDQYIYMVM 602
Cdd:cd05048  10 LEELGEGAFGKVYKgellGPSSEESAISVAIKTLkENASPKTQQDFRREAELMSDLQ-HPN-IVCLLGVCTKEQPQCMLF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKK--------KSIDPWERKSYWKnmLEAVHTIHQ----------HGIVHSDLKPANFLIVDGM-LKL 662
Cdd:cd05048  88 EyMAHGDLHEFLVRHsphsdvgvSSDDDGTASSLDQ--SDFLHIAIQiaagmeylssHHYVHRDLAARNCLVGDGLtVKI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 663 IDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPF-----QQ 736
Cdd:cd05048 166 SDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTES-----------DVWSFGVVLWEIfSYGLQPYygysnQE 234

                ....*
gi 23308722 737 IINQI 741
Cdd:cd05048 235 VIEMI 239
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
644-786 4.53e-06

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 49.63  E-value: 4.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIV-DGMLKLIDFGIANQMQpdTTSVVKDSQVG--TVNYMPPEAIKDMSSSRENgkskskispksDVWSL 720
Cdd:cd05098 157 IHRDLAARNVLVTeDNVMKIADFGLARDIH--HIDYYKKTTNGrlPVKWMAPEALFDRIYTHQS-----------DVWSF 223
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 721 GCILYYM-TYGKTPFQQIinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05098 224 GVLLWEIfTLGGSPYPGV--PVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLV 288
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
644-786 5.30e-06

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 49.62  E-value: 5.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDG-MLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGC 722
Cdd:cd14207 202 IHRDLAARNILLSENnVVKICDFGLARDIYKNPDYVRKGDARLPLKWMAPESIFDKIYSTKS-----------DVWSYGV 270
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 723 ILYYM-TYGKTPFQQIinQI-----SKLHAIIdpnhEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14207 271 LLWEIfSLGASPYPGV--QIdedfcSKLKEGI----RMRAPEFATSEIYQIMLDCWQGDPNERPRFSELV 334
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
625-695 5.30e-06

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 50.07  E-value: 5.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722  625 KSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMqpdTTSVVKDSQVGTVN--YMPPEAI 695
Cdd:PLN03224 312 KGVMRQVLTGLRKLHRIGIVHRDIKPENLLVtVDGQVKIIDFGAAVDM---CTGINFNPLYGMLDprYSPPEEL 382
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
644-788 5.34e-06

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 49.59  E-value: 5.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGC 722
Cdd:cd05103 201 IHRDLAARNILLSEnNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQS-----------DVWSFGV 269
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 723 ILYYM-TYGKTPFQ--QIINQISKLhaiIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLAH 788
Cdd:cd05103 270 LLWEIfSLGASPYPgvKIDEEFCRR---LKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEH 335
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
594-764 5.37e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 49.49  E-value: 5.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  594 TDQYIYMVMECGNIDLNSWLKKKKSIdpwerksywknmLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA--NQ 670
Cdd:PHA03209 141 SDLYTYLTKRSRPLPIDQALIIEKQI------------LEGLRYLHAQRIIHRDVKTENIFINDvDQVCIGDLGAAqfPV 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  671 MQPDTTSVvkdsqVGTVNYMPPEAI-KDMSSSRengkskskispkSDVWSLGCILYYM-TYGKTPFQ------------- 735
Cdd:PHA03209 209 VAPAFLGL-----AGTVETNAPEVLaRDKYNSK------------ADIWSAGIVLFEMlAYPSTIFEdppstpeeyvksc 271
                        170       180       190
                 ....*....|....*....|....*....|.
gi 23308722  736 --QIINQISKLHAiidpnHEIEFPDIPEKDL 764
Cdd:PHA03209 272 hsHLLKIISTLKV-----HPEEFPRDPGSRL 297
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
585-668 5.71e-06

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


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 47.98  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   585 IIRLYDYE---ITDQYIymvmecGNIDLNSWLKKKksidpweRKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLK 661
Cdd:TIGR03724  63 VIYDVDPDnktIVMEYI------EGKPLKDVIEEN-------GDELAREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKVY 129

                  ....*..
gi 23308722   662 LIDFGIA 668
Cdd:TIGR03724 130 LIDFGLG 136
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
644-787 6.03e-06

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: 48.71  E-value: 6.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDGML-KLIDFGIANQMQPDTTSVVKDSQVG---TVNYMPPEAI---KDMSSSrengkskskispksD 716
Cdd:cd05065 128 VHRDLAARNILVNSNLVcKVSDFGLSRFLEDDTSDPTYTSSLGgkiPIRWTAPEAIayrKFTSAS--------------D 193
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 717 VWSLGCILY-YMTYGKTPF-----QQIINQISKLHAIIDPnheiefPDIPEKdLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd05065 194 VWSYGIVMWeVMSYGERPYwdmsnQDVINAIEQDYRLPPP------MDCPTA-LHQLMLDCWQKDRNLRPKFGQIVN 263
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
527-779 7.05e-06

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 48.53  E-value: 7.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQVLNEKKQIYAIKYVnleEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYDYeITDQYIYMVMECGN 606
Cdd:cd05070  13 LIKRLGNGQFGEVWMGTWNGNTKVAIKTL---KPGTMSPESFLEEAQIMKKLKH--DKLVQLYAV-VSEEPIYIVTEYMS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 I-DLNSWLKkkksiDPWERKSYWKNMLE-------AVHTIHQHGIVHSDLKPANFLIVDGML-KLIDFGIANQMQpDTTS 677
Cdd:cd05070  87 KgSLLDFLK-----DGEGRALKLPNLVDmaaqvaaGMAYIERMNYIHRDLRSANILVGNGLIcKIADFGLARLIE-DNEY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPEAikdmsssrengKSKSKISPKSDVWSLGCILYYM-TYGKTPF-----QQIINQISKLHAIIDPN 751
Cdd:cd05070 161 TARQGAKFPIKWTAPEA-----------ALYGRFTIKSDVWSFGILLTELvTKGRVPYpgmnnREVLEQVERGYRMPCPQ 229
                       250       260
                ....*....|....*....|....*...
gi 23308722 752 heiefpDIPeKDLQDVLKCCLKRDPKQR 779
Cdd:cd05070 230 ------DCP-ISLHELMIHCWKKDPEER 250
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
526-786 7.78e-06

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 48.41  E-value: 7.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGGSSKVFQVLNEKKQIYAIKYVNlEEADNQtlDSYRNEIAYLNKLQQhsDKIIRLYDYEITDQYIYMV---M 602
Cdd:cd05112   7 TFVQEIGSGQFGLVHLGYWLNKDKVAIKTIR-EGAMSE--EDFIEEAEVMMKLSH--PKLVQLYGVCLEQAPICLVfefM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 ECGNidLNSWLKKKKSIdpWERKSYWKNML---EAVHTIHQHGIVHSDLKPANFLIVDG-MLKLIDFGIANQMQPDTTSv 678
Cdd:cd05112  82 EHGC--LSDYLRTQRGL--FSAETLLGMCLdvcEGMAYLEEASVIHRDLAARNCLVGENqVVKVSDFGMTRFVLDDQYT- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 679 vkdSQVGT---VNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYM-TYGKTPFQQIINqiSKLHAIIDPNHEI 754
Cdd:cd05112 157 ---SSTGTkfpVKWSSPEVFSFSRYSSK-----------SDVWSFGVLMWEVfSEGKIPYENRSN--SEVVEDINAGFRL 220
                       250       260       270
                ....*....|....*....|....*....|..
gi 23308722 755 EFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05112 221 YKPRLASTHVYEIMNHCWKERPEDRPSFSLLL 252
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
526-785 7.85e-06

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 48.57  E-value: 7.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGGSSKVFQV-------LNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQQHSDkIIRLYDYEITDQYI 598
Cdd:cd05053  15 TLGKPLGEGAFGQVVKAeavgldnKPNEVVTVAVKMLK-DDATEKDLSDLVSEMEMMKMIGKHKN-IINLLGACTQDGPL 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMEC---GNidLNSWLKKKKSIDPWERKSYWKNMLEAVHTIH----------------QHGIVHSDLKPANFLIVDG- 658
Cdd:cd05053  93 YVVVEYaskGN--LREFLRARRPPGEEASPDDPRVPEEQLTQKDlvsfayqvargmeylaSKKCIHRDLAARNVLVTEDn 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 659 MLKLIDFGIANQMQP-DTTSVVKDSQVgTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQ 736
Cdd:cd05053 171 VMKIADFGLARDIHHiDYYRKTTNGRL-PVKWMAPEALFDRVYTHQS-----------DVWSFGVLLWeIFTLGGSPYPG 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 23308722 737 IinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05053 239 I--PVEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ...
526-668 7.97e-06

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: 46.91  E-value: 7.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGGSSKVFQVLNEKKqiYAIKYvnleeADNQTLDSYRNEIAYLNKLQQHSD-KIIRLYDYEITDQYIYMVMEC 604
Cdd:cd05120   1 ISVKLIKEGGDNKVYLLGDPRE--YVLKI-----GPPRLKKDLEKEAAMLQLLAGKLSlPVPKVYGFGESDGWEYLLMER 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722 605 --GNIDLNSWLKKkkSIDPWER--KSYwKNMLEAVHTIHQHGIVHSDLKPANfLIVDGMLKL---IDFGIA 668
Cdd:cd05120  74 ieGETLSEVWPRL--SEEEKEKiaDQL-AEILAALHRIDSSVLTHGDLHPGN-ILVKPDGKLsgiIDWEFA 140
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
526-787 9.47e-06

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 48.11  E-value: 9.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGGSSKVFQ------VLNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQQHsdKIIRLYDYEITDQYIY 599
Cdd:cd05062   9 TMSRELGQGSFGMVYEgiakgvVKDEPETRVAIKTVN-EAASMRERIEFLNEASVMKEFNCH--HVVRLLGVVSQGQPTL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNI-DLNSWLKK---KKSIDPWERKSYWKNMLEAVHTI-------HQHGIVHSDLKPANFLIV-DGMLKLIDFGI 667
Cdd:cd05062  86 VIMELMTRgDLKSYLRSlrpEMENNPVQAPPSLKKMIQMAGEIadgmaylNANKFVHRDLAARNCMVAeDFTVKIGDFGM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 668 ANQMQPDTTSVVKDSQVGTVNYMPPEAIKDmsssrengkskSKISPKSDVWSLGCILYYM-TYGKTPFQQIINQisKLHA 746
Cdd:cd05062 166 TRDIYETDYYRKGGKGLLPVRWMSPESLKD-----------GVFTTYSDVWSFGVVLWEIaTLAEQPYQGMSNE--QVLR 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 23308722 747 IIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd05062 233 FVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIS 273
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
629-693 1.03e-05

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


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 48.93  E-value: 1.03e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 629 KNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIdfgianqmqpDTTS-VVKDSQ------VGTVNYMPPE 693
Cdd:COG4248 128 RNLAAAVAALHAAGYVHGDVNPSNILVsDTALVTLI----------DTDSfQVRDPGkvyrcvVGTPEFTPPE 190
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
527-785 1.12e-05

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: 48.18  E-value: 1.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 527 ILKQIGSGGSSKVFQ----VLNEKKQI-YAIKyVNLEEADNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQY--IY 599
Cdd:cd05057  11 KGKVLGSGAFGTVYKgvwiPEGEKVKIpVAIK-VLREETGPKANEEILDE-AYVMASVDHPH-LVRLLGICLSSQVqlIT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVMECGNIDlnSWLKKKK-SIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTS 677
Cdd:cd05057  88 QLMPLGCLL--DYVRNHRdNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVkTPNHVKITDFGLAKLLDVDEKE 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 678 VVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIinQISKLHAIIDPNHEIEF 756
Cdd:cd05057 166 YHAEGGKVPIKWMALESIQYRIYTHKS-----------DVWSYGVTVWeLMTFGAKPYEGI--PAVEIPDLLEKGERLPQ 232
                       250       260
                ....*....|....*....|....*....
gi 23308722 757 PDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05057 233 PPICTIDVYMVLVKCWMIDAESRPTFKEL 261
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
573-787 1.15e-05

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: 47.80  E-value: 1.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 573 AYLNKLQQHSDkIIRLYDYeITDQYIYMVME-CGNIDLNSWLKKKK-SIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKP 650
Cdd:cd05056  58 AYIMRQFDHPH-IVKLIGV-ITENPVWIVMElAPLGELRSYLQVNKySLDLASLILYAYQLSTALAYLESKRFVHRDIAA 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 651 ANFLIVD-GMLKLIDFGIANQMqpDTTSVVKDSQVG-TVNYMPPEAI--KDMSSSrengkskskispkSDVWSLG-CILY 725
Cdd:cd05056 136 RNVLVSSpDCVKLGDFGLSRYM--EDESYYKASKGKlPIKWMAPESInfRRFTSA-------------SDVWMFGvCMWE 200
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23308722 726 YMTYGKTPFQQIINqiSKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd05056 201 ILMLGVKPFQGVKN--NDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKA 260
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
595-780 1.18e-05

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


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 48.05  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 595 DQYIYMVMECGNIDLNSWLKKKKSIDPweRKSYWK---NMLEAVHTIHQHGIVHSDLKPANFLI----VDGMLKLIDFGI 667
Cdd:cd14015  99 EKYRFLVMPRFGRDLQKIFEKNGKRFP--EKTVLQlalRILDVLEYIHENGYVHADIKASNLLLgfgkNKDQVYLVDYGL 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 668 ANQMQPDTTSV--VKDSQV---GTVNYMPPEAIKDMSSSRENgkskskispksDVWSLG-CILYYMtYGKTPFQQIINQI 741
Cdd:cd14015 177 ASRYCPNGKHKeyKEDPRKahnGTIEFTSRDAHKGVAPSRRG-----------DLEILGyNMLQWL-CGKLPWEDNLKNP 244
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 23308722 742 SKLHAiidpNHEIEFPDIPEKdlqdVLKCCLKRDPKQRI 780
Cdd:cd14015 245 EYVQK----QKEKYMDDIPLL----LKKCFPGKDVPEEL 275
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
644-785 1.32e-05

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 48.04  E-value: 1.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIV-DGMLKLIDFGIANQMQpdTTSVVKDSQVG--TVNYMPPEAIKDMSSSRENgkskskispksDVWSL 720
Cdd:cd05099 156 IHRDLAARNVLVTeDNVMKIADFGLARGVH--DIDYYKKTSNGrlPVKWMAPEALFDRVYTHQS-----------DVWSF 222
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 721 GCILYYM-TYGKTPFQQIinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05099 223 GILMWEIfTLGGSPYPGI--PVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQL 286
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
630-693 1.34e-05

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 48.12  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 630 NMLEAVHTIHQHGIVHSDLKPANFLIVDGM----------------LKLIDFGIANQM--QPDTTSVVKDSQvgTVNYMP 691
Cdd:cd13981 114 ELLKVVEALHEVGIIHGDIKPDNFLLRLEIcadwpgegengwlskgLKLIDFGRSIDMslFPKNQSFKADWH--TDSFDC 191

                ..
gi 23308722 692 PE 693
Cdd:cd13981 192 IE 193
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
551-786 1.36e-05

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 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: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 47.70  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 551 AIKYVNLEEADNQTLDSYRNEI-AYLNKlqQHSDKIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKSI-DPWERKSYW 628
Cdd:cd14153  26 AIRLIDIERDNEEQLKAFKREVmAYRQT--RHENVVLFMGACMSPPHLAIITSLCKGRTLYSVVRDAKVVlDVNKTRQIA 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 629 KNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFG---IANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSsrENG 705
Cdd:cd14153 104 QEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGlftISGVLQAGRREDKLRIQSGWLCHLAPEIIRQLSP--ETE 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 706 KSKSKISPKSDVWSLGCILYYMTYGKTPFQqiiNQISKlhAIIDPNHEIEFPDIPE----KDLQDVLKCCLKRDPKQRIS 781
Cdd:cd14153 182 EDKLPFSKHSDVFAFGTIWYELHAREWPFK---TQPAE--AIIWQVGSGMKPNLSQigmgKEISDILLFCWAYEQEERPT 256

                ....*
gi 23308722 782 IPELL 786
Cdd:cd14153 257 FSKLM 261
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
529-785 1.75e-05

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: 47.34  E-value: 1.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSG--GSSK--VFQVLNEKKQIYAIKYVNLEEADNQTLDSYRnEIAYLNKLQQHSdkIIRLYDYEITDQYIyMVMEC 604
Cdd:cd05060   1 KELGHGnfGSVRkgVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLR-EASVMAQLDHPC--IVRLIGVCKGEPLM-LVMEL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 GNID-LNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTsVVKDS 682
Cdd:cd05060  77 APLGpLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNrHQAKISDFGMSRALGAGSD-YYRAT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 683 QVGT--VNYMPPEAI---KDMSSSrengkskskispksDVWSLGCILYYM-TYGKTPFQQIINQisKLHAIIDPNHEIEF 756
Cdd:cd05060 156 TAGRwpLKWYAPECInygKFSSKS--------------DVWSYGVTLWEAfSYGAKPYGEMKGP--EVIAMLESGERLPR 219
                       250       260
                ....*....|....*....|....*....
gi 23308722 757 PDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05060 220 PEECPQEIYSIMLSCWKYRPEDRPTFSEL 248
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
631-790 1.81e-05

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: 47.16  E-value: 1.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 631 MLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSvvkdsqvgtvnymppEAIKDMSSSRENGkSKS 709
Cdd:cd05576 122 MVVALDALHREGIVCRDLNPNNILLNDrGHIQLTYFSRWSEVEDSCDS---------------DAIENMYCAPEVG-GIS 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 710 KISPKSDVWSLGCILYYMTYGKTpfqqiinqISKLH-AIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRI-----SIP 783
Cdd:cd05576 186 EETEACDWWSLGALLFELLTGKA--------LVECHpAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTERLgagvaGVE 257

                ....*..
gi 23308722 784 ELLAHPY 790
Cdd:cd05576 258 DIKSHPF 264
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
525-750 1.81e-05

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: 47.70  E-value: 1.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEKK--QIYAIKYV-NLEEADnqtlDSYRNEIAYLNKLQQ----HSDKIIRLYDYEITDQY 597
Cdd:cd14215  14 YEIVSTLGEGTFGRVVQCIDHRRggARVALKIIkNVEKYK----EAARLEINVLEKINEkdpeNKNLCVQMFDWFDYHGH 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 598 IYMVMECGNIDLNSWLKKKK----SIDPWERKSYwkNMLEAVHTIHQHGIVHSDLKPANFLIVDG--------------- 658
Cdd:cd14215  90 MCISFELLGLSTFDFLKENNylpyPIHQVRHMAF--QVCQAVKFLHDNKLTHTDLKPENILFVNSdyeltynlekkrder 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 659 -----MLKLIDFGIANQMQPDTTSVVKdsqvgTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILYYMTYGKTP 733
Cdd:cd14215 168 svkstAIRVVDFGSATFDHEHHSTIVS-----TRHYRAPEVILELGWSQP-----------CDVWSIGCIIFEYYVGFTL 231
                       250
                ....*....|....*....
gi 23308722 734 FQQIINQ--ISKLHAIIDP 750
Cdd:cd14215 232 FQTHDNRehLAMMERILGP 250
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
525-730 1.88e-05

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: 47.72  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNE-KKQIYAIKYVnleeadnQTLDSYRN----EIAYLNKLQ-QHSDK--IIRLYDYEITDQ 596
Cdd:cd14229   2 YEVLDFLGRGTFGQVVKCWKRgTNEIVAVKIL-------KNHPSYARqgqiEVGILARLSnENADEfnFVRAYECFQHRN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVMECGNIDLNSWLKKKKsIDPWERK---SYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGM-----LKLIDFGIA 668
Cdd:cd14229  75 HTCLVFEMLEQNLYDFLKQNK-FSPLPLKvirPILQQVATALKKLKSLGLIHADLKPENIMLVDPVrqpyrVKVIDFGSA 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23308722 669 NQMQPDTTSVVKDSQVgtvnYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYG 730
Cdd:cd14229 154 SHVSKTVCSTYLQSRY----YRAPEIILGLPFCE-----------AIDMWSLGCVIAELFLG 200
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
566-745 1.91e-05

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 47.10  E-value: 1.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 566 DSYRNEIA----YLNKLQQHsDKIIRLYDYEITDQY-------IYMVMECGNIDLNSWLKKKKSIDpwERKSYWKNMLEA 634
Cdd:cd13975  38 DKHWNDLAlefhYTRSLPKH-ERIVSLHGSVIDYSYgggssiaVLLIMERLHRDLYTGIKAGLSLE--ERLQIALDVVEG 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 635 VHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANqmqpdTTSVVKDSQVGTVNYMPPEAikdMSSSRENgkskskisp 713
Cdd:cd13975 115 IRFLHSQGLVHRDIKLKNVLLdKKNRAKITDLGFCK-----PEAMMSGSIVGTPIHMAPEL---FSGKYDN--------- 177
                       170       180       190
                ....*....|....*....|....*....|...
gi 23308722 714 KSDVWSLGCILYYMTYGKTPFQQIINQI-SKLH 745
Cdd:cd13975 178 SVDVYAFGILFWYLCAGHVKLPEAFEQCaSKDH 210
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
54-188 2.00e-05

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 47.42  E-value: 2.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  54 QIMMMANNP---EDWLSLLLKLEKNSVPLSDALLN--KLIGRYSQAIEALppDKYGQ-NESFARIQVRFAELKAIQ-EPD 126
Cdd:COG2956  84 QDYLKAGLLdraEELLEKLLELDPDDAEALRLLAEiyEQEGDWEKAIEVL--ERLLKlGPENAHAYCELAELYLEQgDYD 161
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 127 DARDYFQMARANCKKFAFVHISFAQFELSQGNVKKSKQLLQKAVERG---AVPLEMLEIALRNLN 188
Cdd:COG2956 162 EAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDpdyLPALPRLAELYEKLG 226
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
529-777 2.17e-05

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: 46.89  E-value: 2.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVF----QVLNEKKQIYAIKYVNLEEADNQTLDsYRNEIAYLNKLQQHSdkIIRLYDyeITDQYIYMV--- 601
Cdd:cd05063  11 KVIGAGEFGEVFrgilKMPGRKEVAVAIKTLKPGYTEKQRQD-FLSEASIMGQFSHHN--IIRLEG--VVTKFKPAMiit 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 --MECGNIDlnSWLKKKK-SIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGML-KLIDFGIANQMQ--PDT 675
Cdd:cd05063  86 eyMENGALD--KYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLEcKVSDFGLSRVLEddPEG 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVVKDSQVgTVNYMPPEAI---KDMSSSrengkskskispksDVWSLGCILY-YMTYGKTPFQQIINQisKLHAIIDPN 751
Cdd:cd05063 164 TYTTSGGKI-PIRWTAPEAIayrKFTSAS--------------DVWSFGIVMWeVMSFGERPYWDMSNH--EVMKAINDG 226
                       250       260       270
                ....*....|....*....|....*....|
gi 23308722 752 HEIEFP-DIPEKDLQDVLKCCLK---RDPK 777
Cdd:cd05063 227 FRLPAPmDCPSAVYQLMLQCWQQdraRRPR 256
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
545-740 2.97e-05

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 46.94  E-value: 2.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 545 EKKQIYAIKYVNlEEADNQTLDSYRNEiAYLNKLQQHSDkIIRLYDYEITDQYIYMVME-CGNIDLNSWLKKKK---SID 620
Cdd:cd05091  34 EQTQAVAIKTLK-DKAEGPLREEFRHE-AMLRSRLQHPN-IVCLLGVVTKEQPMSMIFSyCSHGDLHEFLVMRSphsDVG 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 621 PWERKSYWKNMLEA---VHTIHQ----------HGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSVVKDSQVGT 686
Cdd:cd05091 111 STDDDKTVKSTLEPadfLHIVTQiaagmeylssHHVVHKDLATRNVLVFDKLnVKISDLGLFREVYAADYYKLMGNSLLP 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23308722 687 VNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQIINQ 740
Cdd:cd05091 191 IRWMSPEAIMYGKFSIDS-----------DIWSYGVVLWEVfSYGLQPYCGYSNQ 234
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
528-785 3.37e-05

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: 46.55  E-value: 3.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKV----FQVLNEKK-QIYAIKyvNLEEADNQTLDSYRNEIAYLNKLQQhsDKIIRLYD--YEITDQYIYM 600
Cdd:cd14205   9 LQQLGKGNFGSVemcrYDPLQDNTgEVVAVK--KLQHSTEEHLRDFEREIEILKSLQH--DNIVKYKGvcYSAGRRNLRL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 601 VMEC---GNidLNSWLKK-KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDT 675
Cdd:cd14205  85 IMEYlpyGS--LRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVeNENRVKIGDFGLTKVLPQDK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSV-VKDSQVGTVNYMPPEAIKDMSSSrengkskskisPKSDVWSLGCILY----YMTYGKTPFQQIINQISK------- 743
Cdd:cd14205 163 EYYkVKEPGESPIFWYAPESLTESKFS-----------VASDVWSFGVVLYelftYIEKSKSPPAEFMRMIGNdkqgqmi 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 744 -LHAI--IDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd14205 232 vFHLIelLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDL 276
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
528-785 3.64e-05

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: 46.61  E-value: 3.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKV------FQVLNEKKQIyAIKYVNLEEADNQTLDsYRNEIAYLNKLqqHSDKIIRL--YDYEITDQYIY 599
Cdd:cd05038   9 IKQLGEGHFGSVelcrydPLGDNTGEQV-AVKSLQPSGEEQHMSD-FKREIEILRTL--DHEYIVKYkgVCESPGRRSLR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 600 MVME---CGNidLNSWLKK-KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPD 674
Cdd:cd05038  85 LIMEylpSGS--LRDYLQRhRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVeSEDLVKISDFGLAKVLPED 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 675 TTS-VVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYG---KTPFQQIINQISKLHA--- 746
Cdd:cd05038 163 KEYyYVKEPGESPIFWYAPECLRESRFSSAS-----------DVWSFGVTLYELfTYGdpsQSPPALFLRMIGIAQGqmi 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 23308722 747 ------IIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05038 232 vtrlleLLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDL 276
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
525-730 4.08e-05

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: 46.62  E-value: 4.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 525 YSILKQIGSGGSSKVFQVLNEK-KQIYAIKYVnleeadnQTLDSYRN----EIAYLNKLQ-QHSDK--IIRLYDYEITDQ 596
Cdd:cd14228  17 YEVLEFLGRGTFGQVAKCWKRStKEIVAIKIL-------KNHPSYARqgqiEVSILSRLSsENADEynFVRSYECFQHKN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 597 YIYMVMECGNIDLNSWLKKKKsIDPWERKsYWKNMLEAVHT----IHQHGIVHSDLKPANFLIVDGM-----LKLIDFGI 667
Cdd:cd14228  90 HTCLVFEMLEQNLYDFLKQNK-FSPLPLK-YIRPILQQVATalmkLKSLGLIHADLKPENIMLVDPVrqpyrVKVIDFGS 167
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23308722 668 ANQMQPDTTSVVKDSQVgtvnYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYG 730
Cdd:cd14228 168 ASHVSKAVCSTYLQSRY----YRAPEIILGLPFCE-----------AIDMWSLGCVIAELFLG 215
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
641-740 4.21e-05

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


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 46.16  E-value: 4.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 641 HGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWS 719
Cdd:cd05090 143 HFFVHKDLAARNILVGEQLhVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDS-----------DIWS 211
                        90       100
                ....*....|....*....|..
gi 23308722 720 LGCILYYM-TYGKTPFQQIINQ 740
Cdd:cd05090 212 FGVVLWEIfSFGLQPYYGFSNQ 233
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
586-779 4.56e-05

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 46.51  E-value: 4.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  586 IRLYDYEITDQYIYMVME--CGNiDLNSWLKKKKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLI-VDGMLKL 662
Cdd:PTZ00426  94 VNLYGSFKDESYLYLVLEfvIGG-EFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLdKDGFIKM 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  663 IDFGIANQMQPDTTSVVkdsqvGTVNYMPPEAIKDMSSSRengkskskispKSDVWSLGCILYYMTYGKTPF-------- 734
Cdd:PTZ00426 173 TDFGFAKVVDTRTYTLC-----GTPEYIAPEILLNVGHGK-----------AADWWTLGIFIYEILVGCPPFyaneplli 236
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 23308722  735 -QQIINQIsklhaiidpnheIEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:PTZ00426 237 yQKILEGI------------IYFPKFLDNNCKHLMKKLLSHDLTKR 270
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
559-792 4.58e-05

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They 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 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: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 46.18  E-value: 4.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 559 EADNQTLDSYRNEIAYLNKLQqhSDKIIRLYDYEITDQYIYMVME-CGNIDLNSWLKKKKSIDPWERKSYwKNMLEAVHT 637
Cdd:cd05051  57 DASKNAREDFLKEVKIMSQLK--DPNIVRLLGVCTRDEPLCMIVEyMENGDLNQFLQKHEAETQGASATN-SKTLSYGTL 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 638 IH-------------QHGIVHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAI---KDMSS 700
Cdd:cd05051 134 LYmatqiasgmkyleSLNFVHRDLATRNCLVGPNYtIKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESIllgKFTTK 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 701 SrengkskskispksDVWSLGCILY-YMTYGK-TPF-----QQIINQISKLHAiiDPNHEIEFPDIP--EKDLQDVLKCC 771
Cdd:cd05051 214 S--------------DVWAFGVTLWeILTLCKeQPYehltdEQVIENAGEFFR--DDGMEVYLSRPPncPKEIYELMLEC 277
                       250       260
                ....*....|....*....|.
gi 23308722 772 LKRDPKQRISIPELlaHPYVQ 792
Cdd:cd05051 278 WRRDEEDRPTFREI--HLFLQ 296
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
644-786 4.61e-05

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: 46.55  E-value: 4.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDG-MLKLIDFGIANQMqpDTTSVVKDSQVG--TVNYMPPEAIKDMSSSRENgkskskispksDVWSL 720
Cdd:cd05101 168 IHRDLAARNVLVTENnVMKIADFGLARDI--NNIDYYKKTTNGrlPVKWMAPEALFDRVYTHQS-----------DVWSF 234
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23308722 721 GCILYYM-TYGKTPFQQIinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05101 235 GVLMWEIfTLGGSPYPGI--PVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLV 299
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
623-786 5.40e-05

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: 46.09  E-value: 5.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 623 ERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-GMLKLIDFGIA--------NqmqPDTTSVVKDSQVGTVNYMPPE 693
Cdd:cd13980  98 EKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSwNWVYLTDFASFkptylpedN---PADFSYFFDTSRRRTCYIAPE 174
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 694 A-IKDMSSSRENGKSKSKISPKSDVWSLGCILYYM-TYGKTPFqqiinQISKLHAI----IDPNHEIEfpDIPEKDLQDV 767
Cdd:cd13980 175 RfVDALTLDAESERRDGELTPAMDIFSLGCVIAELfTEGRPLF-----DLSQLLAYrkgeFSPEQVLE--KIEDPNIREL 247
                       170
                ....*....|....*....
gi 23308722 768 LKCCLKRDPKQRISIPELL 786
Cdd:cd13980 248 ILHMIQRDPSKRLSAEDYL 266
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
633-668 6.89e-05

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 46.42  E-value: 6.89e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 23308722  633 EAVHTIHQHGIVHSDLKPANFLIVDGMLKLIDFGIA 668
Cdd:PRK09605 439 EIVAKLHKAGIVHGDLTTSNFIVRDDRLYLIDFGLG 474
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
529-786 7.15e-05

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: 45.13  E-value: 7.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 529 KQIGSGGSSKVFQ-VLNEKKQIYAIKYVNLEEADNQtldsyrnEIAYLNK---LQQHSD-KIIRLYDYEITDQYIYMVME 603
Cdd:cd05041   1 EKIGRGNFGDVYRgVLKPDNTEVAVKTCRETLPPDL-------KRKFLQEariLKQYDHpNIVKLIGVCVQKQPIMIVME 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 C--GNiDLNSWLKKKK-----------SIDPWERKSYwknmLEAVHTIHQhgivhsDLKPANFLIVD-GMLKLIDFGIAN 669
Cdd:cd05041  74 LvpGG-SLLTFLRKKGarltvkqllqmCLDAAAGMEY----LESKNCIHR------DLAARNCLVGEnNVLKISDFGMSR 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSREngkskskispkSDVWSLGCILY-YMTYGKTPFQQIINQISKlhAII 748
Cdd:cd05041 143 EEEDGEYTVSDGLKQIPIKWTAPEALNYGRYTSE-----------SDVWSFGILLWeIFSLGATPYPGMSNQQTR--EQI 209
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23308722 749 DPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05041 210 ESGYRMPAPELCPEAVYRLMLQCWAYDPENRPSFSEIY 247
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
569-724 7.63e-05

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 45.90  E-value: 7.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 569 RNEIAYLNKL-QQHSDK--IIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKsIDPWERKsYWKNMLEAVHT----IHQH 641
Cdd:cd14211  43 QIEVSILSRLsQENADEfnFVRAYECFQHKNHTCLVFEMLEQNLYDFLKQNK-FSPLPLK-YIRPILQQVLTallkLKSL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 642 GIVHSDLKPANFLIVDGM-----LKLIDFGIANQMqpdtTSVVKDSQVGTVNYMPPEAIKDMSSSRengkskskispKSD 716
Cdd:cd14211 121 GLIHADLKPENIMLVDPVrqpyrVKVIDFGSASHV----SKAVCSTYLQSRYYRAPEIILGLPFCE-----------AID 185

                ....*...
gi 23308722 717 VWSLGCIL 724
Cdd:cd14211 186 MWSLGCVI 193
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
642-697 8.28e-05

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: 45.34  E-value: 8.28e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 642 GIVHSDLKPANFLIV-DGMLKLIDFGIA--NQMQPDTTSVVKDSQVGTVNYMPPEAIKD 697
Cdd:cd14056 120 AIAHRDLKSKNILVKrDGTCCIADLGLAvrYDSDTNTIDIPPNPRVGTKRYMAPEVLDD 178
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
528-727 9.03e-05

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: 45.47  E-value: 9.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQV-----LNEKKQIYAIKYVNLEEADNQTL---DSYRNEIAYLNKLQqHSDKI-IRLYDyEITDQYI 598
Cdd:cd14001   4 MKKLGYGTGVNVYLMkrsprGGSSRSPWAVKKINSKCDKGQRSlyqERLKEEAKILKSLN-HPNIVgFRAFT-KSEDGSL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 599 YMVMECGNIDLNSWLKKKKSI--DPWERKSYWK---NMLEAVHTIHQHG-IVHSDLKPANFLIVDG--MLKLIDFGIANQ 670
Cdd:cd14001  82 CLAMEYGGKSLNDLIEERYEAglGPFPAATILKvalSIARALEYLHNEKkILHGDIKSGNVLIKGDfeSVKLCDFGVSLP 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23308722 671 MQPDTT--SVVKDSQVGTVNYMPPEAIKdmsssrENGksksKISPKSDVWSLGCILYYM 727
Cdd:cd14001 162 LTENLEvdSDPKAQYVGTEPWKAKEALE------EGG----VITDKADIFAYGLVLWEM 210
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
644-785 9.62e-05

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: 45.21  E-value: 9.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDGM-LKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGC 722
Cdd:cd05050 152 VHRDLATRNCLVGENMvVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTES-----------DVWAYGV 220
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23308722 723 ILYYM-TYGKTPFQQIINQiSKLHAIIDPNhEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPEL 785
Cdd:cd05050 221 VLWEIfSYGMQPYYGMAHE-EVIYYVRDGN-VLSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
629-697 1.03e-04

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 45.94  E-value: 1.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722  629 KNMLEAVHTIHQHGIVHSDLKPANFLIVD--GMLKLIDFGIAnqmqpdttsvvKDSQVGtVNYMPPEAIKD 697
Cdd:PLN03225 262 RQILFALDGLHSTGIVHRDVKPQNIIFSEgsGSFKIIDLGAA-----------ADLRVG-INYIPKEFLLD 320
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
643-786 1.11e-04

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: 45.02  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 643 IVHSDLKPANFLIVD-GMLKLIDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLG 721
Cdd:cd05109 130 LVHRDLAARNVLVKSpNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILHRRFTHQS-----------DVWSYG 198
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23308722 722 CILY-YMTYGKTPFQQIinQISKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05109 199 VTVWeLMTFGAKPYDGI--PAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELV 262
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
635-788 1.11e-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: 45.09  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 635 VHTIHQHGIVHSDLKPANFLIVDGMLK--LIDFGIANQMQPDTtSVVKDsQVGTVNYMPPeaikDMSSSREngksksKIS 712
Cdd:cd13974 145 VEALHKKNIVHRDLKLGNMVLNKRTRKitITNFCLGKHLVSED-DLLKD-QRGSPAYISP----DVLSGKP------YLG 212
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 713 PKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIIDPNHEIefpdipEKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd13974 213 KPSDMWALGVVLFTMLYGQFPFydsipQELFRKIKAAEYTIPEDGRV------SENTVCLIRKLLVLNPQKRLTASEVLD 286

                .
gi 23308722 788 H 788
Cdd:cd13974 287 S 287
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
643-764 1.13e-04

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: 44.91  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 643 IVHSDLKPANFLIVDGM-LKLIDFGIAN--QMQPDTTSVVKDSQVG-TVNYMPPEAIKDMSSSRENgkskskisPKSDVW 718
Cdd:cd14026 123 LLHHDLKTQNILLDGEFhVKIADFGLSKwrQLSISQSRSSKSAPEGgTIIYMPPEEYEPSQKRRAS--------VKHDIY 194
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 23308722 719 SLGCILYYMTYGKTPFQQIINQISKLHAII-----DPNHEIEFPDIPEKDL 764
Cdd:cd14026 195 SYAIIMWEVLSRKIPFEEVTNPLQIMYSVSqghrpDTGEDSLPVDIPHRAT 245
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
566-779 1.14e-04

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 45.06  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 566 DSYRNEIAYLNKLQQhsDKIIRLYDYeITDQYIYMV---MECGNI------DLNSWLKKKKSIDpwerksYWKNMLEAVH 636
Cdd:cd05071  49 EAFLQEAQVMKKLRH--EKLVQLYAV-VSEEPIYIVteyMSKGSLldflkgEMGKYLRLPQLVD------MAAQIASGMA 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 637 TIHQHGIVHSDLKPANFLIVDGML-KLIDFGIANQMQpDTTSVVKDSQVGTVNYMPPEAikdmsssrengKSKSKISPKS 715
Cdd:cd05071 120 YVERMNYVHRDLRAANILVGENLVcKVADFGLARLIE-DNEYTARQGAKFPIKWTAPEA-----------ALYGRFTIKS 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 716 DVWSLGCILYYM-TYGKTPF-----QQIINQISKLHAIIDPnheiefPDIPEKdLQDVLKCCLKRDPKQR 779
Cdd:cd05071 188 DVWSFGILLTELtTKGRVPYpgmvnREVLDQVERGYRMPCP------PECPES-LHDLMCQCWRKEPEER 250
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
571-730 1.16e-04

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: 45.47  E-value: 1.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 571 EIAYLNKLQQHSD---KIIRLYDYEITDQYIYMVMECGNIDLNSWLKKKKsIDPWERKsYWKNMLEAVHT----IHQHGI 643
Cdd:cd14227  61 EVSILARLSTESAddyNFVRAYECFQHKNHTCLVFEMLEQNLYDFLKQNK-FSPLPLK-YIRPILQQVATalmkLKSLGL 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 644 VHSDLKPANFLIVDG-----MLKLIDFGIANQMQPDTTSVVKDSQVgtvnYMPPEAIKDMSSSRengkskskispKSDVW 718
Cdd:cd14227 139 IHADLKPENIMLVDPsrqpyRVKVIDFGSASHVSKAVCSTYLQSRY----YRAPEIILGLPFCE-----------AIDMW 203
                       170
                ....*....|..
gi 23308722 719 SLGCILYYMTYG 730
Cdd:cd14227 204 SLGCVIAELFLG 215
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
643-728 1.32e-04

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 44.77  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 643 IVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDTTSV--VKDSQVGTVNYMPPEaIKDMSSSRENgkskSKISPKSDVWS 719
Cdd:cd14144 121 IAHRDIKSKNILVkKNGTCCIADLGLAVKFISETNEVdlPPNTRVGTKRYMAPE-VLDESLNRNH----FDAYKMADMYS 195

                ....*....
gi 23308722 720 LGCILYYMT 728
Cdd:cd14144 196 FGLVLWEIA 204
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
531-786 1.43e-04

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: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 531 IGSGGSSKVFQVLNEK---KQIYAIKYVNLEEADNQTLDsYRNEIAYLNKLQQHSDkIIRLYDYEITDQYIYMVMEC--- 604
Cdd:cd05047   3 IGEGNFGQVLKARIKKdglRMDAAIKRMKEYASKDDHRD-FAGELEVLCKLGHHPN-IINLLGACEHRGYLYLAIEYaph 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 605 GNidLNSWLKKKKSI--DPWERKS--------------YWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGML-KLIDFGI 667
Cdd:cd05047  81 GN--LLDFLRKSRVLetDPAFAIAnstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVaKIADFGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 668 AnqmQPDTTSVVKDSQVGTVNYMppeAIKDMSSSrengksksKISPKSDVWSLGCILY-YMTYGKTPFQQIinQISKLHA 746
Cdd:cd05047 159 S---RGQEVYVKKTMGRLPVRWM---AIESLNYS--------VYTTNSDVWSYGVLLWeIVSLGGTPYCGM--TCAELYE 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 23308722 747 IIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd05047 223 KLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQIL 262
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
536-779 1.79e-04

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: 44.26  E-value: 1.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 536 SSKVFQVlnekkqiyAIKYVNLEE-ADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQyIYMVME---CGNidLNS 611
Cdd:cd05040  20 SGKVIQV--------AVKCLKSDVlSQPNAMDDFLKEVNAMHSLDHPN--LIRLYGVVLSSP-LMMVTElapLGS--LLD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 612 WLKKKKSIDPwerksywknmleaVHTIHQHGI--------------VHSDLKPANFLIV-DGMLKLIDFGIANQMqpdtt 676
Cdd:cd05040  87 RLRKDQGHFL-------------ISTLCDYAVqiangmayleskrfIHRDLAARNILLAsKDKVKIGDFGLMRAL----- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 677 SVVKDSQVGTVN------YMPPEAIKDMSSSrengkskskisPKSDVWSLGCILYYM-TYGKTPF-----QQIinqiskL 744
Cdd:cd05040 149 PQNEDHYVMQEHrkvpfaWCAPESLKTRKFS-----------HASDVWMFGVTLWEMfTYGEEPWlglngSQI------L 211
                       250       260       270
                ....*....|....*....|....*....|....*
gi 23308722 745 HAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQR 779
Cdd:cd05040 212 EKIDKEGERLERPDDCPQDIYNVMLQCWAHKPADR 246
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
528-785 2.11e-04

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 44.21  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFqvLNEKKQIYAIKYVNLEEAdnQTLDSYRNEIAYLNKLQ-----QHSDKIIRLYDYEITDQYIyMVM 602
Cdd:cd05087   2 LKEIGHGWFGKVF--LGEVNSGLSSTQVVVKEL--KASASVQDQMQFLEEAQpyralQHTNLLQCLAQCAEVTPYL-LVM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 603 E-CGNIDLNSWLKKKKSI-----DPWERKSYWKNMLEAVHTIHQHGIVHSDLKPAN-FLIVDGMLKLIDFGIANQMQPDT 675
Cdd:cd05087  77 EfCPLGDLKGYLRSCRAAesmapDPLTLQRMACEVACGLLHLHRNNFVHSDLALRNcLLTADLTVKIGDYGLSHCKYKED 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 676 TSVVKDSQVGTVNYMPPEAIKDMSSSrengKSKSKISPKSDVWSLGCILYYM-TYGKTPFQQIINQISKLHAIIDPNHEI 754
Cdd:cd05087 157 YFVTADQLWVPLRWIAPELVDEVHGN----LLVVDQTKQSNVWSLGVTIWELfELGNQPYRHYSDRQVLTYTVREQQLKL 232
                       250       260       270
                ....*....|....*....|....*....|....
gi 23308722 755 EFPDIP---EKDLQDVLKCCLKRdPKQRISIPEL 785
Cdd:cd05087 233 PKPQLKlslAERWYEVMQFCWLQ-PEQRPTAEEV 265
PHA02988 PHA02988
hypothetical protein; Provisional
565-786 2.39e-04

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 43.96  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  565 LDSYRNEIAYLNKLQqhSDKIIRLYDY--EITDQYIYMVME---CGNIDLNSWLKKKKSIDPWERKSYW---KNMLEAVH 636
Cdd:PHA02988  62 IDITENEIKNLRRID--SNNILKIYGFiiDIVDDLPRLSLIleyCTRGYLREVLDKEKDLSFKTKLDMAidcCKGLYNLY 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722  637 TihQHGIVHSDLKPANFLIV-DGMLKLIDFGIANQMqpdttSVVKDSQVGTVNYMPPEAIKDMSSSRengkskskiSPKS 715
Cdd:PHA02988 140 K--YTNKPYKNLTSVSFLVTeNYKLKIICHGLEKIL-----SSPPFKNVNFMVYFSYKMLNDIFSEY---------TIKD 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23308722  716 DVWSLGCILYYMTYGKTPFQQIINQiSKLHAIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:PHA02988 204 DIYSLGVVLWEIFTGKIPFENLTTK-EIYDLIINKNNSLKLPLDCPLEIKCIVEACTSHDSIKRPNIKEIL 273
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
526-787 2.89e-04

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: 43.51  E-value: 2.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 526 SILKQIGSGGSSKVFQ---VLNEKKQI-YAIKYVNLEEADNQTLDsYRNEIAYLNKLQQHSdkIIRLYDYeITDQYIYMV 601
Cdd:cd05033   7 TIEKVIGGGEFGEVCSgslKLPGKKEIdVAIKTLKSGYSDKQRLD-FLTEASIMGQFDHPN--VIRLEGV-VTKSRPVMI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 ----MECGNIDlnSWLKKKksidpwERKSYWKNMLEAVHTI-------HQHGIVHSDLKPANFLI-VDGMLKLIDFGIAN 669
Cdd:cd05033  83 vteyMENGSLD--KFLREN------DGKFTVTQLVGMLRGIasgmkylSEMNYVHRDLAARNILVnSDLVCKVSDFGLSR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMQ-PDTTSVVKDSQVgTVNYMPPEAI---KDMSSSrengkskskispksDVWSLGCILY-YMTYGKTPFQQIINQiSKL 744
Cdd:cd05033 155 RLEdSEATYTTKGGKI-PIRWTAPEAIayrKFTSAS--------------DVWSFGIVMWeVMSYGERPYWDMSNQ-DVI 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 23308722 745 HAIIDpNHEIEFP-DIPEKdLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd05033 219 KAVED-GYRLPPPmDCPSA-LYQLMLDCWQKDRNERPTFSQIVS 260
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
528-787 3.02e-04

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: 43.61  E-value: 3.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 528 LKQIGSGGSSKVFQV------LNEKKQIYAIKYVNlEEADNQTLDSYRNEIAYLNKLQQHSdkIIRLYDYEITDQYIYMV 601
Cdd:cd05046  10 ITTLGRGEFGEVFLAkakgieEEGGETLVLVKALQ-KTKDENLQSEFRRELDMFRKLSHKN--VVRLLGLCREAEPHYMI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 602 MECGNI-DLNSWLKKKKSIDPwERKSYWKNMLEAVHTIHQ----------HGIVHSDLKPANFLI-VDGMLKLIDFGIAN 669
Cdd:cd05046  87 LEYTDLgDLKQFLRATKSKDE-KLKPPPLSTKQKVALCTQialgmdhlsnARFVHRDLAARNCLVsSQREVKVSLLSLSK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 670 QMQPDTTSVVKDSQVgTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILYYM-TYGKTPFQQIINQiSKLHAII 748
Cdd:cd05046 166 DVYNSEYYKLRNALI-PLRWLAPEAVQEDDFSTKS-----------DVWSFGVLMWEVfTQGELPFYGLSDE-EVLNRLQ 232
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 23308722 749 DPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRISIPELLA 787
Cdd:cd05046 233 AGKLELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELVS 271
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
530-724 5.24e-04

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: 43.13  E-value: 5.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 530 QIGSGGSSKVFQVL---NEKKQIYAIKYVnleEADNQTLDSYRnEIAYLNKLQQHSDKIIRLYDYEITDQYIYMVMECGN 606
Cdd:cd07867   9 KVGRGTYGHVYKAKrkdGKDEKEYALKQI---EGTGISMSACR-EIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 607 IDLNSWLK----KKKSIDPWER-----KSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVD-----GMLKLIDFGIANQMQ 672
Cdd:cd07867  85 HDLWHIIKfhraSKANKKPMQLprsmvKSLLYQILDGIHYLHANWVLHRDLKPANILVMGegperGRVKIADMGFARLFN 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 23308722 673 PDTTSVVK-DSQVGTVNYMPPEAIkdmsssrengKSKSKISPKSDVWSLGCIL 724
Cdd:cd07867 165 SPLKPLADlDPVVVTFWYRAPELL----------LGARHYTKAIDIWAIGCIF 207
ABC1 pfam03109
ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. ...
565-675 5.44e-04

ABC1 atypical kinase-like domain; This family includes ABC1 from yeast and AarF from E. coli. These proteins have a nuclear or mitochondrial subcellular location in eukaryotes. The exact molecular functions of these proteins is not clear, however yeast ABC1 suppresses a cytochrome b mRNA translation defect and is essential for the electron transfer in the bc 1 complex and E. coli AarF is required for ubiquinone production. It has been suggested that members of the ABC1 family are novel chaperonins. These proteins are unrelated to the ABC transporter proteins.


Pssm-ID: 427143 [Multi-domain]  Cd Length: 245  Bit Score: 42.61  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722   565 LDsYRNEIAYLNKLQQHSDKIIRLYDYEITDQYI---YMVME-CGNIDLNSWLK-KKKSIDpweRKSYWKNMLEAVHT-I 638
Cdd:pfam03109 109 LD-FLREAANAEKFRENFADDPDVYVPKVYWELTterVLTMEyVDGIKIDDLDAlSEAGID---RKEIARRLVELFLEqI 184
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 23308722   639 HQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQMQPDT 675
Cdd:pfam03109 185 FRDGFFHADPHPGNILVrKDGRIVLLDFGLMGRLDEKF 222
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
636-725 6.39e-04

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: 42.73  E-value: 6.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 636 HTIHQHGIVHSDLKPANFLI-VDGMLKLIDFGIANQM--------QPDTTSVVKDSQVGTVNYMPPEA------IKDMSS 700
Cdd:cd14054 116 GDQYKPAIAHRDLNSRNVLVkADGSCVICDFGLAMVLrgsslvrgRPGAAENASISEVGTLRYMAPEVlegavnLRDCES 195
                        90       100
                ....*....|....*....|....*
gi 23308722 701 SrengkskskiSPKSDVWSLGCILY 725
Cdd:cd14054 196 A----------LKQVDVYALGLVLW 210
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
642-740 7.25e-04

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: 42.16  E-value: 7.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 642 GIVHSDLKPANFLIVDGML-KLIDFGIANQMQ--PDTTSVVKDSQVgTVNYMPPEAI--KDMSSSrengkskskispkSD 716
Cdd:cd05066 126 GYVHRDLAARNILVNSNLVcKVSDFGLSRVLEddPEAAYTTRGGKI-PIRWTAPEAIayRKFTSA-------------SD 191
                        90       100
                ....*....|....*....|....*
gi 23308722 717 VWSLGCILY-YMTYGKTPFQQIINQ 740
Cdd:cd05066 192 VWSYGIVMWeVMSYGERPYWEMSNQ 216
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
604-786 8.47e-04

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 42.26  E-value: 8.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 604 CGNIDLNSWLKK-KKSIDPWERKSYWKNMLEAVHTIHQHGIVHSDLKPANFLIVDGMLKLID---FGIANQMQPDTTSVV 679
Cdd:cd14152  78 CKGRTLYSFVRDpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVITDfglFGISGVVQEGRRENE 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 680 KDSQVGTVNYMPPEAIKDMSSSreNGKSKSKISPKSDVWSLGCILYYMTYGKTPF-----QQIINQISKLHAIIDPNHEI 754
Cdd:cd14152 158 LKLPHDWLCYLAPEIVREMTPG--KDEDCLPFSKAADVYAFGTIWYELQARDWPLknqpaEALIWQIGSGEGMKQVLTTI 235
                       170       180       190
                ....*....|....*....|....*....|..
gi 23308722 755 EFpdipEKDLQDVLKCCLKRDPKQRISIPELL 786
Cdd:cd14152 236 SL----GKEVTEILSACWAFDLEERPSFTLLM 263
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
596-781 8.72e-04

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 42.02  E-value: 8.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 596 QYIYM-VMECGniDLNSWLKKKKSIDPWERKSYWKNMLE-AVHT------IHQHGIVHSDLKPANFLIV-----DGMLKL 662
Cdd:cd05044  74 QYIILeLMEGG--DLLSYLRAARPTAFTPPLLTLKDLLSiCVDVakgcvyLEDMHFVHRDLAARNCLVSskdyrERVVKI 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23308722 663 IDFGIANQMQPDTTSVVKDSQVGTVNYMPPEAIKDMSSSRENgkskskispksDVWSLGCILY-YMTYGKTPFQQIINqI 741
Cdd:cd05044 152 GDFGLARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQS-----------DVWAFGVLMWeILTLGQQPYPARNN-L 219
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 23308722 742 SKLHaIIDPNHEIEFPDIPEKDLQDVLKCCLKRDPKQRIS 781
Cdd:cd05044 220 EVLH-FVRAGGRLDQPDNCPDDLYELMLRCWSTDPEERPS 258
 
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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