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Conserved domains on  [gi|62420884|ref|NP_006173|]
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discoidin domain-containing receptor 2 precursor [Homo sapiens]

Protein Classification

discoidin domain-containing receptor 2( domain architecture ID 10044224)

discoidin domain-containing receptor 2 (DDR2) is a receptor tyrosine-protein kinase containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular kinase domain that catalyzes the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
557-851 0e+00

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


:

Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 661.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05095   1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMEKFMDKDFALEVSENQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNS--SSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05095  81 IIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQPEGQlaLPSNALTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSD 794
Cdd:cd05095 161 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCREQPYSQLSD 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 795 EQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQ 851
Cdd:cd05095 241 EQVIENTGEFFRDQGRQTYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
32-184 1.44e-52

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


:

Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 179.86  E-value: 1.44e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  32 YPLGMSGGqIPDEDITASSQWSESTAAKYGRLDSeegDGAWCPEIpvepDDLKEFLQIDLHTLHFITLVGTQGRHaGGHG 111
Cdd:cd00057   1 EPLGMESG-LADDQITASSSYSSGWEASRARLNS---DNAWTPAV----NDPPQWLQVDLGKTRRVTGIQTQGRK-GGGS 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 112 IEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSmNVCMRVELYG 184
Cdd:cd00057  72 SEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNG-NISLRLELYG 143
 
Name Accession Description Interval E-value
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
557-851 0e+00

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 661.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05095   1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMEKFMDKDFALEVSENQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNS--SSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05095  81 IIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQPEGQlaLPSNALTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSD 794
Cdd:cd05095 161 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCREQPYSQLSD 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 795 EQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQ 851
Cdd:cd05095 241 EQVIENTGEFFRDQGRQTYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
563-849 9.32e-129

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: 386.13  E-value: 9.32e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    563 LTFKEKLGEGQFGEVHLCEVEGmekfkdkdfaldVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKG------------KGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    643 VCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:smart00221  69 VCTEEEPLMIVMEYMPGGDLLDYLRKNRPKELSLSD--------LLSFALQIARGMEYLESKNFIHRDLAARNCLVGENL 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    723 TIKIADFGMSRNLYSGDYYRIQGRAvLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIENTG 802
Cdd:smart00221 141 VVKISDFGLSRDLYDDDYYKVKGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGE-EPYPGMSNAEVLEYLK 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 62420884    803 EFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:smart00221 219 KGYR-------LPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
563-849 4.03e-115

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: 350.64  E-value: 4.03e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   563 LTFKEKLGEGQFGEVHLCEvegmekfkdkdfALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGT------------LKGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   643 VCITDDPLCMITEYMENGDLNQFLSRHEPPnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:pfam07714  69 VCTQGEPLYIVTEYMPGGDLLDFLRKHKRK---------LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   723 TIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCqEQPYSQLSDEQVIentg 802
Cdd:pfam07714 140 VVKISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLG-EQPYPGMSNEEVL---- 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 62420884   803 EFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:pfam07714 215 EFLEDGYR---LPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
32-184 1.44e-52

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 179.86  E-value: 1.44e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  32 YPLGMSGGqIPDEDITASSQWSESTAAKYGRLDSeegDGAWCPEIpvepDDLKEFLQIDLHTLHFITLVGTQGRHaGGHG 111
Cdd:cd00057   1 EPLGMESG-LADDQITASSSYSSGWEASRARLNS---DNAWTPAV----NDPPQWLQVDLGKTRRVTGIQTQGRK-GGGS 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 112 IEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSmNVCMRVELYG 184
Cdd:cd00057  72 SEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNG-NISLRLELYG 143
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
30-185 2.95e-38

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 139.18  E-value: 2.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884     30 CRYPLGMSGgqipDEDITASSQwseSTAAKYGRLDsEEGDGAWCPEIPvepdDLKEFLQIDLHTLHFITLVGTQGRHAGG 109
Cdd:smart00231   2 CNEPLGLES----DSQITASSS---YWAAKIARLN-GGSDGGWCPAKN----DLPPWIQVDLGRLRTVTGVITGRRHGNG 69
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884    110 HGIEfapmYKINYSRDGTRWISWRNRHGKqVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHsMNVCMRVELYGC 185
Cdd:smart00231  70 DWVT----YKLEYSDDGVNWTTYKDGNSK-VFPGNSDAGTVVLNDFPPPIVARYVRILPTGWN-GNIILRVELLGC 139
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
567-841 1.11e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 123.97  E-value: 1.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVlvAVKMLRADANKN--ARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:COG0515  13 RLLGRGGMGVVYL--------------ARDLRLGRPV--ALKVLRPELAADpeARERFRREARALARLNHPNIVRVYDVG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPPnsSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:COG0515  77 EEDGRPYLVMEYVEGESLADLLRRRGPL--PPAEALRI--------LAQLAEALAAAHAAGIVHRDIKPANILLTPDGRV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGDYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIentgef 804
Cdd:COG0515 147 KLIDFGIARALGGATLTQ-TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT--GRPPFDGDSPAELL------ 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 62420884 805 fRDQGRQTYLPQPAICPD---SVYKLMLSCWRRDTKNRPS 841
Cdd:COG0515 218 -RAHLREPPPPPSELRPDlppALDAIVLRALAKDPEERYQ 256
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
46-182 3.06e-24

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 98.67  E-value: 3.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    46 ITASSQWSESTAAKYgRLDSEEgDGAWCPEipvePDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGieFAPMYKINYSRD 125
Cdd:pfam00754   2 ITASSSYSGEGPAAA-ALDGDP-NTAWSAW----SGDDPQWIQVDLGKPKKITGVVTQGRQDGSNG--YVTSYKIEYSLD 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884   126 GTRWISWRNRHGKqvldGNSNPYDIFLKDLEPPIVARFVRFIPVTDHS-MNVCMRVEL 182
Cdd:pfam00754  74 GENWTTVKDEKIP----GNNDNNTPVTNTFDPPIKARYVRIVPTSWNGgNGIALRAEL 127
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
569-774 1.58e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 84.81  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  569 LGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLRADANKNARNDF-------------LKEIKIMSRLKDP 635
Cdd:PTZ00024  17 LGEGTYGKVEK--------------AYDTLTGK--IVAIKKVKIIEISNDVTKDrqlvgmcgihfttLRELKIMNEIKHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  636 NIIHLLAVCITDDPLCMITEYMEnGDLNQFLSRHeppnssssdVRtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:PTZ00024  81 NIMGLVDVYVEGDFINLVMDIMA-SDLKKVVDRK---------IR-LTESQVKCILLQILNGLNVLHKWYFMHRDLSPAN 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884  716 CLVGKNYTIKIADFGMSR----NLYSGDYYRIQGRA--------VLPIrWMSWESILLG--KFTTASDVWAFG 774
Cdd:PTZ00024 150 IFINSKGICKIADFGLARrygyPPYSDTLSKDETMQrreemtskVVTL-WYRAPELLMGaeKYHFAVDMWSVG 221
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
567-733 2.77e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 63.66  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  567 EKLGEGqfgevhlceveGM-EKFKDKDFALDVsanqpvLVAVKMLRAD--ANKNARNDFLKEIKIMSRLKDPNIihllaV 643
Cdd:NF033483  13 ERIGRG-----------GMaEVYLAKDTRLDR------DVAVKVLRPDlaRDPEFVARFRREAQSAASLSHPNI-----V 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  644 CITD----DP---LCMitEYMENGDLNQFLSRHEP-PNSsssdvRTVSYTnlkfmaTQIASGMKYLSSLNFVHRDLATRN 715
Cdd:NF033483  71 SVYDvgedGGipyIVM--EYVDGRTLKDYIREHGPlSPE-----EAVEIM------IQILSALEHAHRNGIVHRDIKPQN 137
                        170
                 ....*....|....*...
gi 62420884  716 CLVGKNYTIKIADFGMSR 733
Cdd:NF033483 138 ILITKDGRVKVTDFGIAR 155
 
Name Accession Description Interval E-value
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
557-851 0e+00

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 661.30  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05095   1 EFPRKLLTFKEKLGEGQFGEVHLCEAEGMEKFMDKDFALEVSENQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNS--SSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05095  81 IIRLLAVCITDDPLCMITEYMENGDLNQFLSRQQPEGQlaLPSNALTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSD 794
Cdd:cd05095 161 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCREQPYSQLSD 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 795 EQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQ 851
Cdd:cd05095 241 EQVIENTGEFFRDQGRQTYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
557-851 0e+00

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: 575.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05051   1 EFPREKLEFVEKLGEGQFGEVHLCEANGLSDLTSDDFIGNDNKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEP--PNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05051  81 IVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAetQGASATNSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLSD 794
Cdd:cd05051 161 NCLVGPNYTIKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKEQPYEHLTD 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 795 EQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQ 851
Cdd:cd05051 241 EQVIENAGEFFRDDGMEVYLSRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFLQR 297
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
557-851 0e+00

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 527.24  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFkdkdfaLDVSAN----QPVLVAVKMLRADANKNARNDFLKEIKIMSRL 632
Cdd:cd05097   1 EFPRQQLRLKEKLGEGQFGEVHLCEAEGLAEF------LGEGAPefdgQPVLVAVKMLRADVTKTARNDFLKEIKIMSRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 633 KDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPN--SSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRD 710
Cdd:cd05097  75 KNPNIIRLLGVCVSDDPLCMITEYMENGDLNQFLSQREIEStfTHANNIPSVSIANLLYMAVQIASGMKYLASLNFVHRD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 711 LATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYS 790
Cdd:cd05097 155 LATRNCLVGNHYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLCKEQPYS 234
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 791 QLSDEQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQ 851
Cdd:cd05097 235 LLSDEQVIENTGEFFRNQGRQIYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFLRE 295
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
557-849 1.30e-176

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


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 511.02  E-value: 1.30e-176
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05096   1 KFPRGHLLFKEKLGEGQFGEVHLCEVVNPQDLPTLQFPFNVRKGRPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHE---------PPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFV 707
Cdd:cd05096  81 IIRLLGVCVDEDPLCMITEYMENGDLNQFLSSHHlddkeengnDAVPPAHCLPAISYSSLLHVALQIASGMKYLSSLNFV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 708 HRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQ 787
Cdd:cd05096 161 HRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLCKEQ 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 788 PYSQLSDEQVIENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05096 241 PYGELTDEQVIENAGEFFRDQGRQVYLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIHAFL 302
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
563-849 9.32e-129

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: 386.13  E-value: 9.32e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    563 LTFKEKLGEGQFGEVHLCEVEGmekfkdkdfaldVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKG------------KGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    643 VCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:smart00221  69 VCTEEEPLMIVMEYMPGGDLLDYLRKNRPKELSLSD--------LLSFALQIARGMEYLESKNFIHRDLAARNCLVGENL 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    723 TIKIADFGMSRNLYSGDYYRIQGRAvLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIENTG 802
Cdd:smart00221 141 VVKISDFGLSRDLYDDDYYKVKGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGE-EPYPGMSNAEVLEYLK 218
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 62420884    803 EFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:smart00221 219 KGYR-------LPKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
563-849 2.09e-127

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 382.65  E-value: 2.09e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    563 LTFKEKLGEGQFGEVHLCEVEGMEKFKDkdfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLKGKGGKKK------------VEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLG 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    643 VCITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:smart00219  69 VCTEEEPLYIVMEYMEGGDLLSYLRKNRP---------KLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENL 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    723 TIKIADFGMSRNLYSGDYYRIQGRAvLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCqEQPYSQLSDEQVIENTG 802
Cdd:smart00219 140 VVKISDFGLSRDLYDDDYYRKRGGK-LPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLG-EQPYPGMSNEEVLEYLK 217
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 62420884    803 EFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:smart00219 218 NGYR-------LPQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
567-849 1.92e-124

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: 374.95  E-value: 1.92e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEkfkdkdfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGD-------------GKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTE 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPPNSSSSDvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd00192  68 EEPLYLVMEYMEGGDLLDFLRKSRPVFPSPEP-STLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIENTGEFFR 806
Cdd:cd00192 147 SDFGLSRDIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGA-TPYPGLSNEEVLEYLRKGYR 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 807 dqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd00192 226 -------LPKPENCPDELYELMLSCWQLDPEDRPTFSELVERL 261
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
563-849 4.03e-115

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: 350.64  E-value: 4.03e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   563 LTFKEKLGEGQFGEVHLCEvegmekfkdkdfALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGT------------LKGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLG 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   643 VCITDDPLCMITEYMENGDLNQFLSRHEPPnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:pfam07714  69 VCTQGEPLYIVTEYMPGGDLLDFLRKHKRK---------LTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   723 TIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCqEQPYSQLSDEQVIentg 802
Cdd:pfam07714 140 VVKISDFGLSRDIYDDDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLG-EQPYPGMSNEEVL---- 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 62420884   803 EFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:pfam07714 215 EFLEDGYR---LPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
557-846 9.04e-103

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: 319.71  E-value: 9.04e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEkfkdkdfaldvSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05048   1 EIPLSAVRFLEELGEGAFGKVYKGELLGPS-----------SEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEP---PNSSSSDVRTVS---YTNLKFMATQIASGMKYLSSLNFVHRD 710
Cdd:cd05048  70 IVCLLGVCTKEQPQCMLFEYMAHGDLHEFLVRHSPhsdVGVSSDDDGTASsldQSDFLHIAIQIAAGMEYLSSHHYVHRD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 711 LATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYS 790
Cdd:cd05048 150 LAARNCLVGDGLTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSY-GLQPYY 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 791 QLSDEQVIEntgeffRDQGRQTyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd05048 229 GYSNQEVIE------MIRSRQL-LPCPEDCPARVYSLMVECWHEIPSRRPRFKEIH 277
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
557-849 2.04e-101

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: 315.94  E-value: 2.04e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKdfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDK-----------MLVAVKTLKDASSPDARKDFEREAELLTNLQHEN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPP----NSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLA 712
Cdd:cd05049  70 IVKFYGVCTEGDPLLMVFEYMEHGDLNKFLRSHGPDaaflASEDSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLA 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 713 TRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQL 792
Cdd:cd05049 150 TRNCLVGTNLVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTY-GKQPWFQL 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 793 SDEQVIEntgefFRDQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05049 229 SNTEVIE-----CITQGRL--LQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRL 278
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
560-850 3.52e-91

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: 289.17  E-value: 3.52e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKdfaldvsanqpVLVAVKMLRaDANKNARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd05092   4 RRDIVLKWELGEGAFGKVFLAECHNLLPEQDK-----------MLVAVKALK-EATESARQDFQREAELLTVLQHQHIVR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLSRHEP-----PNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05092  72 FYGVCTEGEPLIMVFEYMRHGDLNRFLRSHGPdakilDGGEGQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSD 794
Cdd:cd05092 152 NCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTY-GKQPWYQLSN 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 795 EQVIENTgeffrDQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLL 850
Cdd:cd05092 231 TEAIECI-----TQGRE--LERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
557-849 1.26e-85

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: 274.79  E-value: 1.26e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMekFKDKDFaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05050   1 EYPRNNIEYVRDIGQGAFGRVFQARAPGL--LPYEPF---------TMVAVKMLKEEASADMQADFQREAALMAEFDHPN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEP---PNSSSSDVRTVSYTNLKF---------MATQIASGMKYLSSL 704
Cdd:cd05050  70 IVKLLGVCAVGKPMCLLFEYMAYGDLNEFLRHRSPraqCSLSHSTSSARKCGLNPLplscteqlcIAKQVAAGMAYLSER 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 705 NFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFC 784
Cdd:cd05050 150 KFVHRDLATRNCLVGENMVVKIADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYG 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 785 QeQPYSQLSDEQVIentgEFFRDqgrQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05050 230 M-QPYYGMAHEEVI----YYVRD---GNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRIL 286
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
557-850 1.45e-85

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: 274.22  E-value: 1.45e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHlcevEGMekfkdkdfALDVSANQPVL-VAVKMLRADANKNARNDFLKEIKIMSRLKDP 635
Cdd:cd05032   2 ELPREKITLIRELGQGSFGMVY----EGL--------AKGVVKGEPETrVAIKTVNENASMRERIEFLNEASVMKEFNCH 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd05032  70 HVVRLLGVVSTGQPTLVVMELMAKGDLKSYLRSRRPEAENNPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCqEQPYSQLSDE 795
Cdd:cd05032 150 CMVAEDLTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLA-EQPYQGLSNE 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 796 QVIentgEFFRDQGrqtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLL 850
Cdd:cd05032 229 EVL----KFVIDGG---HLDLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
569-849 1.77e-83

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: 268.13  E-value: 1.77e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevEGMEKfkdkdfALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd05044   3 LGSGAFGEVF----EGTAK------DILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDND 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEPPNSSSSdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVG-KNY---TI 724
Cdd:cd05044  73 PQYIILELMEGGDLLSYLRAARPTAFTPP---LLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSsKDYrerVV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIentgEF 804
Cdd:cd05044 150 KIGDFGLARDIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQ-QPYPARNNLEVL----HF 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62420884 805 FRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05044 225 VRAGGR---LDQPDNCPDDLYELMLRCWSTDPEERPSFARILEQL 266
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
560-853 4.78e-79

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: 257.25  E-value: 4.78e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKdfaldvsanqpVLVAVKMLRaDANKNARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd05094   4 RRDIVLKRELGEGAFGKVFLAECYNLSPTKDK-----------MLVAVKTLK-DPTLAARKDFQREAELLTNLQHDHIVK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLSRHEP---------PNSSSSDVrtvSYTNLKFMATQIASGMKYLSSLNFVHRD 710
Cdd:cd05094  72 FYGVCGDGDPLIMVFEYMKHGDLNKFLRAHGPdamilvdgqPRQAKGEL---GLSQMLHIATQIASGMVYLASQHFVHRD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 711 LATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYS 790
Cdd:cd05094 149 LATRNCLVGANLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTY-GKQPWF 227
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 791 QLSDEQVIENTgeffrDQGRqtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQG 853
Cdd:cd05094 228 QLSNTEVIECI-----TQGR--VLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALG 283
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
560-849 6.88e-79

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: 256.89  E-value: 6.88e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKdfaldvsanqpVLVAVKMLRaDANKNARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd05093   4 RHNIVLKRELGEGAFGKVFLAECYNLCPEQDK-----------ILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSD---VRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05093  72 FYGVCVEGDPLIMVFEYMKHGDLNKFLRAHGPDAVLMAEgnrPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNC 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQ 796
Cdd:cd05093 152 LVGENLLVKIGDFGMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTY-GKQPWYQLSNNE 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 797 VIENTgeffrDQGRqtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05093 231 VIECI-----TQGR--VLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLL 276
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
557-845 6.72e-78

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: 254.26  E-value: 6.72e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 635
Cdd:cd05053   8 ELPRDRLTLGKPLGEGAFGQVVKAEAVGLDN----------KPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYT-NLKF-----MATQIASGMKYLSSLNFVHR 709
Cdd:cd05053  78 NIINLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRVPEeQLTQkdlvsFAYQVARGMEYLASKKCIHR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 710 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPY 789
Cdd:cd05053 158 DLAARNVLVTEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL-GGSPY 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 790 SQLSDEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05053 237 PGIPVEELFKLLKEGHR-------MEKPQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
561-849 8.46e-78

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: 253.06  E-value: 8.46e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 561 KLLTFKEKLGEGQFGEVHLceveGMEKFKDKdfaldvsanQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHL 640
Cdd:cd05033   4 SYVTIEKVIGGGEFGEVCS----GSLKLPGK---------KEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 LAVCITDDPLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd05033  71 EGVVTKSRPVMIVTEYMENGSLDKFLREND---------GKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNS 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 NYTIKIADFGMSRNLYSGD--YYRIQGRavLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVI 798
Cdd:cd05033 142 DLVCKVSDFGLSRRLEDSEatYTTKGGK--IPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSY-GERPYWDMSNQDVI 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 799 ENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05033 219 KAVEDGYR-------LPPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTL 262
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
567-849 1.81e-77

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: 251.89  E-value: 1.81e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDkdfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05060   1 KELGHGNFGSVR----KGVYLMKS---------GKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKG 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DdPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05060  68 E-PLMLVMELAPLGPLLKYLKKR----------REIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSG-DYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIEntgefF 805
Cdd:cd05060 137 SDFGMSRALGAGsDYYRATTAGRWPLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGA-KPYGEMKGPEVIA-----M 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 62420884 806 RDQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05060 211 LESGER--LPRPEECPQEIYSIMLSCWKYRPEDRPTFSELESTF 252
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
557-845 2.49e-77

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 252.31  E-value: 2.49e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHlcevEGMEKFKDKDfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05036   2 EVPRKNLTLIRALGQGAFGEVY----EGTVSGMPGD-------PSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPN 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVrtvSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05036  71 IVRCIGVCFQRLPRFILLELMAGGDLKSFLRENRPRPEQPSSL---TMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LV---GKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLS 793
Cdd:cd05036 148 LLtckGPGRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSL-GYMPYPGKS 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 62420884 794 DEQVIentgEFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05036 227 NQEVM----EFVTSGGR---MDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTI 271
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
567-849 1.86e-75

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: 246.04  E-value: 1.86e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevegMEKFkdkdfaldvsaNQPVLVAVKMLRADANKNArnDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05034   1 KKLGAGQFGEVW------MGVW-----------NGTTKVAVKTLKPGTMSPE--AFLQEAQIMKKLRHDKLVQLYAVCSD 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05034  62 EEPIYIVTELMSKGSLLDYLR--------TGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKV 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRnLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIENTGEFFR 806
Cdd:cd05034 134 ADFGLAR-LIEDDEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGR-VPYPGMTNREVLEQVERGYR 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 807 dqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05034 212 -------MPKPPGCPDELYDIMLQCWKKEPEERPTFEYLQSFL 247
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
557-843 1.85e-74

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: 244.24  E-value: 1.85e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHlcevEGMekfkdkdfaldvsANQPVLVAVKMLRADANKnaRNDFLKEIKIMSRLKDPN 636
Cdd:cd05068   4 EIDRKSLKLLRKLGSGQFGEVW----EGL-------------WNNTTPVAVKTLKPGTMD--PEDFLREAQIMKKLRHPK 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRheppnssssDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05068  65 LIQLYAVCTLEEPIYIITELMKHGSLLEYLQG---------KGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05068 136 LVGENNICKVADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGR-IPYPGMTNAE 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQ 843
Cdd:cd05068 215 VLQQVERGYR-------MPCPPNCPPQLYDIMLECWKADPMERPTFE 254
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
558-845 2.16e-74

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: 244.30  E-value: 2.16e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 558 FPRKLLTFKEKLGEGQFGEVHLCEVEGMEkfkdkdfaldvSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNI 637
Cdd:cd05046   2 FPRSNLQEITTLGRGEFGEVFLAKAKGIE-----------EEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNV 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMENGDLNQFL-------SRHEPPNSSSSDVrtVSytnlkfMATQIASGMKYLSSLNFVHRD 710
Cdd:cd05046  71 VRLLGLCREAEPHYMILEYTDLGDLKQFLratkskdEKLKPPPLSTKQK--VA------LCTQIALGMDHLSNARFVHRD 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 711 LATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQgRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYS 790
Cdd:cd05046 143 LAARNCLVSSQREVKVSLLSLSKDVYNSEYYKLR-NALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQ-GELPFY 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 791 QLSDEQVIEntgeffRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05046 221 GLSDEEVLN------RLQAGKLELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSEL 269
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
557-846 7.33e-73

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


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 239.63  E-value: 7.33e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHlcevEGMEKFKDKdfaldvsanqpvLVAVKMLRADANknARNDFLKEIKIMSRLKDPN 636
Cdd:cd05052   2 EIERTDITMKHKLGGGQYGEVY----EGVWKKYNL------------TVAVKTLKEDTM--EVEEFLKEAAVMKEIKHPN 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05052  64 LVQLLGVCTREPPFYIITEFMPYGNLLDYLRECNR--------EELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNC 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRnLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05052 136 LVGENHLVKVADFGLSR-LMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGM-SPYPGIDLSQ 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd05052 214 VYELLEKGYR-------MERPEGCPPKVYELMRACWQWNPSDRPSFAEIH 256
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
557-849 2.57e-71

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: 236.45  E-value: 2.57e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEV---HLcEVEGMEkfkdkdfaldvsanQPVLVAVKMLRADANKNARNDFLKEIKIMSRLK 633
Cdd:cd05090   1 ELPLSAVRFMEELGECAFGKIykgHL-YLPGMD--------------HAQLVAIKTLKDYNNPQQWNEFQQEASLMTELH 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 634 DPNIIHLLAVCITDDPLCMITEYMENGDLNQFL---SRHEPPNSSSSDVRTVSYT----NLKFMATQIASGMKYLSSLNF 706
Cdd:cd05090  66 HPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLimrSPHSDVGCSSDEDGTVKSSldhgDFLHIAIQIAAGMEYLSSHFF 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 707 VHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQE 786
Cdd:cd05090 146 VHKDLAARNILVGEQLHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSF-GL 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 787 QPYSQLSDEQVIENTgeffrdQGRQtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05090 225 QPYYGFSNQEVIEMV------RKRQ-LLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARL 280
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
558-845 7.33e-71

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: 234.97  E-value: 7.33e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 558 FPRKLLTFKEKLGEGQFGEVHLCEVegmekfkdkDFALDvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNI 637
Cdd:cd05038   1 FEERHLKFIKQLGEGHFGSVELCRY---------DPLGD---NTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYI 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCitDDP----LCMITEYMENGDLNQFLSRHEPPNSSSsdvRTVSYtnlkfmATQIASGMKYLSSLNFVHRDLAT 713
Cdd:cd05038  69 VKYKGVC--ESPgrrsLRLIMEYLPSGSLRDYLQRHRDQIDLK---RLLLF------ASQICKGMEYLGSQRYIHRDLAA 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMSRNL-YSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQ------E 786
Cdd:cd05038 138 RNILVESEDLVKISDFGLAKVLpEDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDpsqsppA 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 787 QPYSQLSDEQ---VIENTGEFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05038 218 LFLRMIGIAQgqmIVTRLLELLKSGER---LPRPPSCPDEVYDLMKECWEYEPQDRPSFSDL 276
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
563-845 9.88e-70

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: 231.18  E-value: 9.88e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLceveGMEKFKDKdfaldvsanqpvlVAVKMLRADANknARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd05059   6 LTFLKELGSGQFGVVHL----GKWRGKID-------------VAIKMIKEGSM--SEDDFIEEAKVMMKLSHPKLVQLYG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05059  67 VCTKQRPIFIVTEYMANGCLLNYLRERRGKFQTEQ---------LLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfCQEQPYSQLSDEQVIENTG 802
Cdd:cd05059 138 VVKVSDFGLARYVLDDEYTSSVG-TKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFS-EGKMPYERFSNSEVVEHIS 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 803 EFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05059 216 QGYR-------LYRPHLAPTEVYTIMYSCWHEKPEERPTFKIL 251
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
565-846 1.54e-69

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: 231.45  E-value: 1.54e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCEVEGMekfkdkdfaldVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd05091  10 FMEELGEDRFGKVYKGHLFGT-----------APGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPPNS--SSSDVRTVSYT----NLKFMATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd05091  79 TKEQPMSMIFSYCSHGDLHEFLVMRSPHSDvgSTDDDKTVKSTlepaDFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 GKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVI 798
Cdd:cd05091 159 FDKLNVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSY-GLQPYCGYSNQDVI 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 62420884 799 ENTgeffrdQGRQTyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd05091 238 EMI------RNRQV-LPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIH 278
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
557-845 2.45e-69

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: 231.01  E-value: 2.45e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHlcevEGMEKfkdkdfalDVSANQP-VLVAVKMLRADANKNARNDFLKEIKIMSRLKDP 635
Cdd:cd05061   2 EVSREKITLLRELGQGSFGMVY----EGNAR--------DIIKGEAeTRVAVKTVNESASLRERIEFLNEASVMKGFTCH 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd05061  70 HVVRLLGVVSKGQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCqEQPYSQLSDE 795
Cdd:cd05061 150 CMVAHDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLA-EQPYQGLSNE 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 796 QVIentgEFFRDQGrqtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05061 229 QVL----KFVMDGG---YLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEI 271
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
567-846 3.79e-67

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: 223.86  E-value: 3.79e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGmeKFKDKDfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05041   1 EKIGRGNFGDVY----RG--VLKPDN----------TEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQ 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPpnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05041  65 KQPIMIVMELVPGGSLLTFLRKKGA---------RLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVientgeffR 806
Cdd:cd05041 136 SDFGMSREEEDGEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSL-GATPYPGMSNQQT--------R 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 62420884 807 DQGRQTY-LPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd05041 207 EQIESGYrMPAPELCPEAVYRLMLQCWAYDPENRPSFSEIY 247
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
569-849 1.24e-66

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: 222.03  E-value: 1.24e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLceveGmeKFKDKDfaldvsanqpvlVAVKMLRADA-NKNARNDFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd13999   1 IGSGSFGEVYK----G--KWRGTD------------VAIKKLKVEDdNDELLKEFRREVSILSKLRHPNIVQFIGACLSP 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEPPnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd13999  63 PPLCIVTEYMPGGSLYDLLHKKKIP---------LSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMSRNLysGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIENTGEffrd 807
Cdd:cd13999 134 DFGLSRIK--NSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLT--GEVPFKELSPIQIAAAVVQ---- 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62420884 808 qgRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd13999 206 --KGLRPPIPPDCPPELSKLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
557-846 1.77e-66

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: 222.31  E-value: 1.77e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHlcevEGmeKFKDKdfaldvsanqpVLVAVKMLRADaNKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05148   2 ERPREEFTLERKLGSGYFGEVW----EG--LWKNR-----------VRVAIKILKSD-DLLKQQDFQKEVQALKRLRHKH 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05148  64 LISLFAVCSVGEPVYIITELMEKGSLLAFLR--------SPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSR----NLYSGDYYRIqgravlPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQL 792
Cdd:cd05148 136 LVGEDLVCKVADFGLARlikeDVYLSSDKKI------PYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQ-VPYPGM 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 62420884 793 SDEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd05148 209 NNHEVYDQITAGYR-------MPCPAKCPQEIYKIMLECWAAEPEDRPSFKALR 255
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
567-845 1.43e-65

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: 219.91  E-value: 1.43e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmekfkdkdfaLDVSANQPVLVAVKMLRAD--ANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd05040   1 EKLGDGSFGVVRRGE-------------WTTPSGKVIQVAVKCLKSDvlSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ItDDPLCMITEYMENGDLNQFLSRHEPPnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd05040  68 L-SSPLMMVTELAPLGSLLDRLRKDQGH---------FLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKV 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSG-DYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEqPYSQLSDEQVIENTge 803
Cdd:cd05040 138 KIGDFGLMRALPQNeDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEE-PWLGLNGSQILEKI-- 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62420884 804 ffrDQGRQTyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05040 215 ---DKEGER-LERPDDCPQDIYNVMLQCWAHKPADRPTFVAL 252
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
563-849 2.50e-65

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: 219.46  E-value: 2.50e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHlcevEGMekfkdkdfaLDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd05063   7 ITKQKVIGAGEFGEVF----RGI---------LKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRHEPPNSSssdvrtvsyTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05063  74 VVTKFKPAMIITEYMENGALDKYLRDHDGEFSS---------YQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLY---SGDYYRIQGRavLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIE 799
Cdd:cd05063 145 ECKVSDFGLSRVLEddpEGTYTTSGGK--IPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSF-GERPYWDMSNHEVMK 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 800 NTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05063 222 AINDGFR-------LPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLL 264
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
557-845 9.90e-64

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: 215.36  E-value: 9.90e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHlcevEGMekFKDKDfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05056   2 EIQREDITLGRCIGEGQFGDVY----QGV--YMSPE-------NEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPH 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCiTDDPLCMITEYMENGDLNQFLSRheppNSSSSDVRTvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05056  69 IVKLIGVI-TENPVWIVMELAPLGELRSYLQV----NKYSLDLAS-----LILYAYQLSTALAYLESKRFVHRDIAARNV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQ 796
Cdd:cd05056 139 LVSSPDCVKLGDFGLSRYMEDESYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILML-GVKPFQGVKNND 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 62420884 797 VI---ENtGEffrdqgrqtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05056 217 VIgriEN-GE---------RLPMPPNCPPTLYSLMTKCWAYDPSKRPRFTEL 258
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
569-845 2.67e-63

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: 213.96  E-value: 2.67e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVhlCEVEgmekfkdkdfaLDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd05066  12 IGAGEFGEV--CSGR-----------LKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEPpnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd05066  79 PVMIVTEYMENGSLDAFLRKHDG---------QFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 729 FGMSRNLY---SGDYYRIQGRavLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIENTGEFF 805
Cdd:cd05066 150 FGLSRVLEddpEAAYTTRGGK--IPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSY-GERPYWEMSNQDVIKAIEEGY 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 62420884 806 RdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05066 227 R-------LPAPMDCPAALHQLMLDCWQKDRNERPKFEQI 259
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
551-845 2.13e-62

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 212.09  E-value: 2.13e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 551 KDVAVEEfprKLLTFKEKLGEGQFGEVHlcevEGMEKFKDKDFaldvsanqpVLVAVKMLRADANKNAR-NDFLKEIKIM 629
Cdd:cd05074   2 KDVLIQE---QQFTLGRMLGKGEFGSVR----EAQLKSEDGSF---------QKVAVKMLKADIFSSSDiEEFLREAACM 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 630 SRLKDPNIIHLLAVCITDD-----PLCM-ITEYMENGDLNQFL--SR--HEPPNSSSSdvrtvsyTNLKFMaTQIASGMK 699
Cdd:cd05074  66 KEFDHPNVIKLIGVSLRSRakgrlPIPMvILPFMKHGDLHTFLlmSRigEEPFTLPLQ-------TLVRFM-IDIASGME 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 700 YLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRiQGRAV-LPIRWMSWESILLGKFTTASDVWAFGVTLW 778
Cdd:cd05074 138 YLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIYSGDYYR-QGCASkLPVKWLALESLADNVYTTHSDVWAFGVTMW 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 779 ETFTFCQeQPYSQlsdeqvIENTgEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05074 217 EIMTRGQ-TPYAG------VENS-EIYNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHL 275
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
557-845 4.28e-62

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: 211.05  E-value: 4.28e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHlcevEGMEKFKDKDfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05062   2 EVAREKITMSRELGQGSFGMVY----EGIAKGVVKD-------EPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05062  71 VVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNC 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCqEQPYSQLSDEQ 796
Cdd:cd05062 151 MVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLA-EQPYQGMSNEQ 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 62420884 797 VIentgEFFRDQGrqtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05062 230 VL----RFVMEGG---LLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 271
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
563-849 1.18e-61

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 209.70  E-value: 1.18e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHlcevEGMEKFKDKDFaldvsanqpVLVAVKMLRADANKNAR-NDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd05035   1 LKLGKILGEGEFGSVM----EAQLKQDDGSQ---------LKVAVKTMKVDIHTYSEiEEFLSEAACMKDFDHPNVMRLI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPL------CMITEYMENGDLNQFL--SRHEPpNSSSSDVRTVsytnLKFMAtQIASGMKYLSSLNFVHRDLAT 713
Cdd:cd05035  68 GVCFTASDLnkppspMVILPFMKHGDLHSYLlySRLGG-LPEKLPLQTL----LKFMV-DIAKGMEYLSNRNFIHRDLAA 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMSRNLYSGDYYRiQGR-AVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQL 792
Cdd:cd05035 142 RNCMLDENMTVCVADFGLSRKIYSGDYYR-QGRiSKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQ-TPYPGV 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 793 SDEQVIentgEFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05035 220 ENHEIY----DYLRNGNR---LKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVL 269
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
557-845 5.56e-61

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: 209.44  E-value: 5.56e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKdkdfaldvsANQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 635
Cdd:cd05099   8 EFPRDRLVLGKPLGEGCFGQVVRAEAYGIDKSR---------PDQTVTVAVKMLKDNATDKDLADLISEMELMKLIgKHK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSS-DVRTVSYTNLKF-----MATQIASGMKYLSSLNFVHR 709
Cdd:cd05099  79 NIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTfDITKVPEEQLSFkdlvsCAYQVARGMEYLESRRCIHR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 710 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPY 789
Cdd:cd05099 159 DLAARNVLVTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTL-GGSPY 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 790 SQLSDEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05099 238 PGIPVEELFKLLREGHR-------MDKPSNCTHELYMLMRECWHAVPTQRPTFKQL 286
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
563-846 1.43e-60

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 206.78  E-value: 1.43e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVhlcevegMEKFKDKDFALdvsanqpVLVAVKMLR-ADANKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd05075   2 LALGKTLGEGEFGSV-------MEGQLNQDDSV-------LKVAVKTMKiAICTRSEMEDFLSEAVCMKEFDHPNVMRLI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITD-------DPLcMITEYMENGDLNQFL--SRheppnSSSSDVRTVSYTNLKFMaTQIASGMKYLSSLNFVHRDLA 712
Cdd:cd05075  68 GVCLQNtesegypSPV-VILPFMKHGDLHSFLlySR-----LGDCPVYLPTQMLVKFM-TDIASGMEYLSSKNFIHRDLA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 713 TRNCLVGKNYTIKIADFGMSRNLYSGDYYRiQGR-AVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQ 791
Cdd:cd05075 141 ARNCMLNENMNVCVADFGLSKKIYNGDYYR-QGRiSKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQ-TPYPG 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 792 LSDEQVIentgEFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd05075 219 VENSEIY----DYLRQGNR---LKQPPDCLDGLYELMSSCWLLNPKDRPSFETLR 266
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
559-846 2.26e-60

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: 205.66  E-value: 2.26e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLCEVEGmEKfkdkdfaldvsanqpvlVAVKMLRADANknARNDFLKEIKIMSRLKDPNII 638
Cdd:cd05039   4 NKKDLKLGELIGKGEFGDVMLGDYRG-QK-----------------VAVKCLKDDST--AAQAFLAEASVMTTLRHPNLV 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENGDLNQFL-SRHeppnssssdvRTV-SYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05039  64 QLLGVVLEGNGLYIVTEYMAKGSLVDYLrSRG----------RAViTRKDQLGFALDVCEGMEYLESKKFVHRDLAARNV 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRnlySGDYYRIQGRavLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05039 134 LVSEDNVAKVSDFGLAK---EASSNQDGGK--LPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGR-VPYPRIPLKD 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd05039 208 VVPHVEKGYR-------MEAPEGCPPEVYKVMKNCWELDPAKRPTFKQLR 250
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
567-849 2.63e-60

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: 205.16  E-value: 2.63e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekfkdkdFALDVSANQpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05084   2 ERIGRGNFGEV---------------FSGRLRADN-TPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLsRHEPPNSSSSDvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05084  66 KQPIYIVMELVQGGDFLTFL-RTEGPRLKVKE--------LIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQvienTGEFFR 806
Cdd:cd05084 137 SDFGMSREEEDGVYAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSL-GAVPYANLSNQQ----TREAVE 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 807 DQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05084 212 QGVR---LPCPENCPDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
566-845 3.28e-60

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: 205.49  E-value: 3.28e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVhlCEVEgmekfkdkdfaLDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05065   9 EEVIGAGEFGEV--CRGR-----------LKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05065  76 KSRPVMIITEFMENGALDSFLRQNDG---------QFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNL---YSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIENTG 802
Cdd:cd05065 147 VSDFGLSRFLeddTSDPTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSY-GERPYWDMSNQDVINAIE 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 803 EFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05065 226 QDYR-------LPPPMDCPTALHQLMLDCWQKDRNLRPKFGQI 261
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
557-845 5.69e-60

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: 206.40  E-value: 5.69e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKDKdfaldvsanQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 635
Cdd:cd05101  20 EFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPK---------EAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHK 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSS-DVRTVSYTNLKFM-----ATQIASGMKYLSSLNFVHR 709
Cdd:cd05101  91 NIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSyDINRVPEEQMTFKdlvscTYQLARGMEYLASQKCIHR 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 710 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPY 789
Cdd:cd05101 171 DLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTL-GGSPY 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 790 SQLSDEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05101 250 PGIPVEELFKLLKEGHR-------MDKPANCTNELYMMMRDCWHAVPSQRPTFKQL 298
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
557-845 1.93e-59

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: 204.48  E-value: 1.93e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKdkdfaldvsANQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 635
Cdd:cd05098   9 ELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDK---------PNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPP------NSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHR 709
Cdd:cd05098  80 NIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPgmeycyNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 710 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPY 789
Cdd:cd05098 160 DLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTL-GGSPY 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 790 SQLSDEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05098 239 PGVPVEELFKLLKEGHR-------MDKPSNCTNELYMMMRDCWHAVPSQRPTFKQL 287
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
567-845 7.54e-59

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 201.55  E-value: 7.54e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVegmekfkdkdfaLDvSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05058   1 EVIGKGHFGCVYHGTL------------ID-SDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLP 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMIT-EYMENGDLNQFLsRHEPPNSSSSDvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05058  68 SEGSPLVVlPYMKHGDLRNFI-RSETHNPTVKD--------LIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVK 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNLYSGDYYRIQGR--AVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIEntge 803
Cdd:cd05058 139 VADFGLARDIYDKEYYSVHNHtgAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTR-GAPPYPDVDSFDITV---- 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62420884 804 fFRDQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05058 214 -YLLQGRR--LLQPEYCPDPLYEVMLSCWHPKPEMRPTFSEL 252
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
557-852 1.39e-58

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: 202.33  E-value: 1.39e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVhlceVEGMekfkdkdfALDVSANQPVL-VAVKMLRADANKNARNDFLKEIKIMSRL-KD 634
Cdd:cd05055  31 EFPRNNLSFGKTLGAGAFGKV----VEAT--------AYGLSKSDAVMkVAVKMLKPTAHSSEREALMSELKIMSHLgNH 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 635 PNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05055  99 ENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSY--------QVAKGMAFLASKNCIHRDLAAR 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLS- 793
Cdd:cd05055 171 NVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSL-GSNPYPGMPv 249
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 794 DEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQ 852
Cdd:cd05055 250 DSKFYKLIKEGYR-------MAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGKQ 301
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
552-849 5.15e-58

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


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 200.16  E-value: 5.15e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 552 DVAVEefpRKLLTFKEKLGEGQFGEVhlceVEGMEKFKDkdfaldvsaNQPVLVAVKMLRADaNKNARN--DFLKEIKIM 629
Cdd:cd14204   1 DVMID---RNLLSLGKVLGEGEFGSV----MEGELQQPD---------GTNHKVAVKTMKLD-NFSQREieEFLSEAACM 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 630 SRLKDPNIIHLLAVCITDDPL-----CMITEYMENGDLNQFL--SRHEppnssSSDVRTVSYTNLKFMaTQIASGMKYLS 702
Cdd:cd14204  64 KDFNHPNVIRLLGVCLEVGSQripkpMVILPFMKYGDLHSFLlrSRLG-----SGPQHVPLQTLLKFM-IDIALGMEYLS 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 703 SLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRiQGR-AVLPIRWMSWESILLGKFTTASDVWAFGVTLWETF 781
Cdd:cd14204 138 SRNFLHRDLAARNCMLRDDMTVCVADFGLSKKIYSGDYYR-QGRiAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIA 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 782 TFCQeQPYSQLSDEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14204 217 TRGM-TPYPGVQNHEIYDYLLHGHR-------LKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENL 276
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
563-852 7.49e-58

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: 198.64  E-value: 7.49e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLceveGMEKFKDKdfaldvsanqpvlVAVKMLRADANknARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd05112   6 LTFVQEIGSGQFGLVHL----GYWLNKDK-------------VAIKTIREGAM--SEEDFIEEAEVMMKLSHPKLVQLYG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSrheppnsssSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05112  67 VCLEQAPICLVFEFMEHGCLSDYLR---------TQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQ 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGDYYRIQGRAvLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIENTG 802
Cdd:cd05112 138 VVKVSDFGMTRFVLDDQYTSSTGTK-FPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSE-GKIPYENRSNSEVVEDIN 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 803 EFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQeihlLLLQQ 852
Cdd:cd05112 216 AGFR-------LYKPRLASTHVYEIMNHCWKERPEDRPSFS----LLLRQ 254
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
569-845 3.79e-57

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: 197.64  E-value: 3.79e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVH--LCEVEGmEKFKdkdfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05057  15 LGSGAFGTVYkgVWIPEG-EKVK-------------IPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDpLCMITEYMENGDLNQFLSRHEPpnssssdvRTVSYTNLKFmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05057  81 SQ-VQLITQLMPLGCLLDYVRNHRD--------NIGSQLLLNW-CVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSG-DYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEqPYSQLSDEQV---IENTG 802
Cdd:cd05057 151 TDFGLAKLLDVDeKEYHAEG-GKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAK-PYEGIPAVEIpdlLEKGE 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 803 EffrdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05057 229 R----------LPQPPICTIDVYMVLVKCWMIDAESRPTFKEL 261
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
557-845 4.46e-57

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: 199.09  E-value: 4.46e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKFKdkdfaldvsANQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 635
Cdd:cd05100   8 ELSRTRLTLGKPLGEGCFGQVVMAEAIGIDKDK---------PNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSS------DVRTVSYTNLKFMATQIASGMKYLSSLNFVHR 709
Cdd:cd05100  79 NIINLLGACTQDGPLYVLVEYASKGNLREYLRARRPPGMDYSfdtcklPEEQLTFKDLVSCAYQVARGMEYLASQKCIHR 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 710 DLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPY 789
Cdd:cd05100 159 DLAARNVLVTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTL-GGSPY 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 790 SQLSDEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05100 238 PGIPVEELFKLLKEGHR-------MDKPANCTHELYMIMRECWHAVPSQRPTFKQL 286
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
557-849 9.40e-55

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: 190.48  E-value: 9.40e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvlVAVKMLRADANKNARndFLKEIKIMSRLKDPN 636
Cdd:cd05067   3 EVPRETLKLVERLGAGQFGEVWMGYYNGHTK-----------------VAIKSLKQGSMSPDA--FLAEANLMKQLQHQR 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVcITDDPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05067  64 LVRLYAV-VTQEPIYIITEYMENGSLVDFLK--------TPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANI 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05067 135 LVSDTLSCKIADFGLARLIEDNEYTAREG-AKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGR-IPYPGMTNPE 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05067 213 VIQNLERGYR-------MPRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVL 258
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
563-845 1.13e-54

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: 190.94  E-value: 1.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHlcevegmekfkdKDFALDVSANQPVL-VAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd05045   2 LVLGKTLGEGEFGKVV------------KATAFRLKGRAGYTtVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFL--SRHEPP---------NSSS---SDVRTVSYTNLKFMATQIASGMKYLSSLNFV 707
Cdd:cd05045  70 GACSQDGPLLLIVEYAKYGSLRSFLreSRKVGPsylgsdgnrNSSYldnPDERALTMGDLISFAWQISRGMQYLAEMKLV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 708 HRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQ 787
Cdd:cd05045 150 HRDLAARNVLVAEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTL-GGN 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 788 PYSQLSDEQVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05045 229 PYPGIAPERLFNLLKTGYR-------MERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
567-846 1.47e-54

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: 189.45  E-value: 1.47e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMekFKDKdfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05085   2 ELLGKGNFGEVY----KGT--LKDK-----------TPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQ 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEppnsssSDVRTVSYtnLKFmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05085  65 RQPIYIVMELVPGGDFLSFLRKKK------DELKTKQL--VKF-SLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKI 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGdYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTF--CqeqPYSQLSDEQVIENTGEF 804
Cdd:cd05085 136 SDFGMSRQEDDG-VYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLgvC---PYPGMTNQQAREQVEKG 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62420884 805 FRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd05085 212 YR-------MSAPQRCPEDIYKIMQRCWDYNPENRPKFSELQ 246
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
557-845 1.50e-54

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 190.78  E-value: 1.50e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDP- 635
Cdd:cd05054   3 EFPRDRLKLGKPLGRGAFGKVIQASAFGIDK-----------SATCRTVAVKMLKEGATASEHKALMTELKILIHIGHHl 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDD-PLCMITEYMENGDLNQFLS--RHE---PPNSSSSDVRTVSY-----------TNLKFMATQIASGM 698
Cdd:cd05054  72 NVVNLLGACTKPGgPLMVIVEFCKFGNLSNYLRskREEfvpYRDKGARDVEEEEDddelykepltlEDLICYSFQVARGM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 699 KYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSG-DYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTL 777
Cdd:cd05054 152 EFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDpDYVR-KGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLL 230
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 778 WETFTFcQEQPYSQLS-DEqvientgEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05054 231 WEIFSL-GASPYPGVQmDE-------EFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSEL 291
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
567-849 1.84e-54

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 189.72  E-value: 1.84e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVegmekfkdkdfaldVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05042   1 QEIGNGWFGKVLLGEI--------------YSGTSVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05042  67 AIPYLLVMEFCDLGDLKAYLRSEREHERGDSDTRT-----LQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYYRIQGRAVLPIRWMSWEsiLLGKF---------TTASDVWAFGVTLWETFTFcQEQPYSQLSDEQV 797
Cdd:cd05042 142 GDYGLAHSRYKEDYIETDDKLWFPLRWTAPE--LVTEFhdrllvvdqTKYSNIWSLGVTLWELFEN-GAQPYSNLSDLDV 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 798 IENTgefFRDQgrQTYLPQPAI---CPDSVYKLMLSCWRRDTKnRPSFQEIHLLL 849
Cdd:cd05042 219 LAQV---VREQ--DTKLPKPQLelpYSDRWYEVLQFCWLSPEQ-RPAAEDVHLLL 267
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
564-845 2.85e-54

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 188.51  E-value: 2.85e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    564 TFKEKLGEGQFGEVHLCEvegmekfkdkdfalDVSANQpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAV 643
Cdd:smart00220   2 EILEKLGEGSFGKVYLAR--------------DKKTGK--LVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDV 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    644 CITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:smart00220  66 FEDEDKLYLVMEYCEGGDLFDLLKKR----------GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    724 IKIADFGMSRNLYSGDYYRiqgRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWEtfTFCQEQPYSQLSDEQVIentge 803
Cdd:smart00220 136 VKLADFGLARQLDPGEKLT---TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYE--LLTGKPPFPGDDQLLEL----- 205
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 62420884    804 fFRDQGRQTYLPQP--AICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:smart00220 206 -FKKIGKPKPPFPPpeWDISPEAKDLIRKLLVKDPEKRLTAEEA 248
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
560-845 6.17e-54

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: 187.78  E-value: 6.17e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvlVAVKMLRADANknARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd05113   3 PKDLTFLKELGTGQFGVVKYGKWRGQYD-----------------VAIKMIKEGSM--SEDEFIEEAKVMMNLSHEKLVQ 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVG 719
Cdd:cd05113  64 LYGVCTKQRPIFIITEYMANGCLLNYLREMR---------KRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVN 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 720 KNYTIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIE 799
Cdd:cd05113 135 DQGVVKVSDFGLSRYVLDDEYTSSVG-SKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSL-GKMPYERFTNSETVE 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 62420884 800 NTGeffrdQGRQTYLPQPAicPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05113 213 HVS-----QGLRLYRPHLA--SEKVYTIMYSCWHEKADERPTFKIL 251
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
557-849 1.01e-53

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction 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. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, 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). The EphA10 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: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 187.44  E-value: 1.01e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVhlCEvegmekfkdkdFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05064   1 ELDNKSIKIERILGTGRFGEL--CR-----------GCLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05064  68 IVRLEGVITRGNTMMIVTEYMSNGALDSFLRKHEG---------QLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFG-MSRNLYSGDYYRIQGRAvlPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDE 795
Cdd:cd05064 139 LVNSDLVCKISGFRrLQEDKSEAIYTTMSGKS--PVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSY-GERPYWDMSGQ 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 62420884 796 QVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05064 216 DVIKAVEDGFR-------LPAPRNCPNLLHQLMLDCWQKERGERPRFSQIHSIL 262
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
569-845 1.48e-53

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: 185.17  E-value: 1.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdfaldvsanqpvlVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd00180   1 LGKGSFGKVYKARDKETGKK----------------VAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETEN 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEPPNSSSsdvrtvsytNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd00180  65 FLYLVMEYCEGGSLKDLLKENKGPLSEE---------EALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLAD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 729 FGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETftfcqeqpysqlsdeqvientgeffrdq 808
Cdd:cd00180 136 FGLAKDLDSDDSLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------- 187
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 62420884 809 grqtylpqpaicpDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd00180 188 -------------EELKDLIRRMLQYDPKKRPSAKEL 211
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
561-845 1.98e-53

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 186.69  E-value: 1.98e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 561 KLLTFKEKLGEGQFGevhlCEVEGMEKFKDKDfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHL 640
Cdd:cd05115   4 NLLIDEVELGSGNFG----CVKKGVYKMRKKQ----------IDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRM 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 LAVCITDDpLCMITEYMENGDLNQFLSrheppnsSSSDVRTVSytNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd05115  70 IGVCEAEA-LMLVMEMASGGPLNKFLS-------GKKDEITVS--NVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 NYTIKIADFGMSRNLYSGD-YYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIE 799
Cdd:cd05115 140 QHYAKISDFGLSKALGADDsYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQ-KPYKKMKGPEVMS 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 62420884 800 ntgefFRDQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05115 219 -----FIEQGKR--MDCPAECPPEMYALMSDCWIYKWEDRPNFLTV 257
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
568-849 2.96e-53

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: 185.51  E-value: 2.96e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvlVAVKMLRAdaNKNARNDFLKEIKIMSRLKDPNIIHLLAVcITD 647
Cdd:cd14203   2 KLGQGCFGEVWMGTWNGTTK-----------------VAIKTLKP--GTMSPEAFLEEAQIMKKLRHDKLVQLYAV-VSE 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd14203  62 EPIYIVTEFMSKGSLLDFLK--------DGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIENTGEFFRd 807
Cdd:cd14203 134 DFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR-VPYPGMNNREVLEQVERGYR- 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62420884 808 qgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14203 211 ------MPCPPGCPESLHELMCQCWRKDPEERPTFEYLQSFL 246
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
567-849 1.16e-52

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 184.77  E-value: 1.16e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVegmekfkdkdfaldVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd14206   3 QEIGNGWFGKVILGEI--------------FSDYTPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd14206  69 TIPFLLIMEFCQLGDLKRYLRAQRKADGMTPDLPTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYYRIQGRAVLPIRWMSWEsiLLGKF---------TTASDVWAFGVTLWETFTFcQEQPYSQLSDEQV 797
Cdd:cd14206 149 GDYGLSHNNYKEDYYLTPDRLWIPLRWVAPE--LLDELhgnlivvdqSKESNVWSLGVTIWELFEF-GAQPYRHLSDEEV 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 798 IEntgefFRDQGRQTYLPQPAI---CPDSVYKLMLSCWrRDTKNRPSFQEIHLLL 849
Cdd:cd14206 226 LT-----FVVREQQMKLAKPRLklpYADYWYEIMQSCW-LPPSQRPSVEELHLQL 274
FA58C cd00057
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
32-184 1.44e-52

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 238014 [Multi-domain]  Cd Length: 143  Bit Score: 179.86  E-value: 1.44e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  32 YPLGMSGGqIPDEDITASSQWSESTAAKYGRLDSeegDGAWCPEIpvepDDLKEFLQIDLHTLHFITLVGTQGRHaGGHG 111
Cdd:cd00057   1 EPLGMESG-LADDQITASSSYSSGWEASRARLNS---DNAWTPAV----NDPPQWLQVDLGKTRRVTGIQTQGRK-GGGS 71
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 112 IEFAPMYKINYSRDGTRWISWRNRHGKQVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHSmNVCMRVELYG 184
Cdd:cd00057  72 SEWVTSYKVQYSLDGETWTTYKDKGEEKVFTGNSDGSTPVTNDFPPPIVARYIRILPTTWNG-NISLRLELYG 143
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
560-849 1.53e-51

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: 181.88  E-value: 1.53e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLcEVEGMEKFKDKDFALDVSANQPVLVAVKMLRADANKnarndflkeikiMSRLKDPNIIH 639
Cdd:cd05043   5 RERVTLSDLLQEGTFGRIFH-GILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSL------------LYGLSHQNLLP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITD-DPLCMITEYMENGDLNQFL--SRHEPPNSSssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05043  72 ILHVCIEDgEKPMVLYPYMNWGNLKLFLqqCRLSEANNP----QALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05043 148 VIDDELQVKITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQ-TPYVEIDPFE 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 797 VIentgEFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05043 227 MA----AYLKDGYR---LAQPINCPDELFAVMACCWALDPEERPSFQQLVQCL 272
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
558-847 1.92e-51

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: 181.75  E-value: 1.92e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 558 FPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsaNQPVLVAVKMLRADANKNARnDFLKEIKIMSRLKDPNI 637
Cdd:cd14205   1 FEERHLKFLQQLGKGNFGSVEMCRYDPLQD------------NTGEVVAVKKLQHSTEEHLR-DFEREIEILKSLQHDNI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCIT--DDPLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd14205  68 VKYKGVCYSagRRNLRLIMEYLPYGSLRDYLQKHK---------ERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRN 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMSRNL-YSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQE--QPYSQL 792
Cdd:cd14205 139 ILVENENRVKIGDFGLTKVLpQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKskSPPAEF 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 793 -----SDEQ---VIENTGEFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHL 847
Cdd:cd14205 219 mrmigNDKQgqmIVFHLIELLKNNGR---LPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLAL 278
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
563-845 7.95e-51

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: 179.29  E-value: 7.95e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvlVAVKMLRADANknARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd05114   6 LTFMKELGSGLFGVVRLGKWRAQYK-----------------VAIKAIREGAM--SEEDFIEEAKVMMKLTHPKLVQLYG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRHEppNSSSSDVrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05114  67 VCTQQKPIYIVTEFMENGCLLNYLRQRR--GKLSRDM-------LLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIENTG 802
Cdd:cd05114 138 VVKVSDFGMTRYVLDDQYTSSSG-AKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTE-GKMPFESKSNYEVVEMVS 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 803 EFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05114 216 RGHR-------LYRPKLASKSVYEVMYSCWHEKPEGRPTFADL 251
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
568-849 2.82e-50

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: 177.46  E-value: 2.82e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHlcevEGMEKFKDKDfaldvsanqpVLVAVKMLRADANKNA-RNDFLKEIKIMSRLKDPNIIHLLAVCiT 646
Cdd:cd05116   2 ELGSGNFGTVK----KGYYQMKKVV----------KTVAVKILKNEANDPAlKDELLREANVMQQLDNPYIVRMIGIC-E 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05116  67 AESWMLVMEMAELGPLNKFLQKN----------RHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGD-YYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIEntgefF 805
Cdd:cd05116 137 SDFGLSKALRADEnYYKAQTHGKWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQ-KPYKGMKGNEVTQ-----M 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 62420884 806 RDQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05116 211 IEKGER--MECPAGCPPEMYDLMKLCWTYDVDERPGFAAVELRL 252
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
557-849 7.89e-50

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: 176.80  E-value: 7.89e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvlVAVKMLRAdaNKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05070   5 EIPRESLQLIKRLGNGQFGEVWMGTWNGNTK-----------------VAIKTLKP--GTMSPESFLEEAQIMKKLKHDK 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVcITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05070  66 LVQLYAV-VSEEPIYIVTEYMSKGSLLDFLKDGEG--------RALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05070 137 LVGNGLICKIADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR-VPYPGMNNRE 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05070 215 VLEQVERGYR-------MPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFL 260
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
558-847 7.99e-50

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 177.39  E-value: 7.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 558 FPRKLLTFKEKLGEGQFGEVHLCEVEGMekfkdkdfaldvSANQPVLVAVKMLRADANKNARnDFLKEIKIMSRLKDPNI 637
Cdd:cd05081   1 FEERHLKYISQLGKGNFGSVELCRYDPL------------GDNTGALVAVKQLQHSGPDQQR-DFQREIQILKALHSDFI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDD--PLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd05081  68 VKYRGVSYGPGrrSLRLVMEYLPSGCLRDFLQRHR---------ARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARN 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMSRNL-YSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQE--QPYSQL 792
Cdd:cd05081 139 ILVESEAHVKIADFGLAKLLpLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKscSPSAEF 218
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 793 -------SDEQVIENTGEFFRDQGRqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHL 847
Cdd:cd05081 219 lrmmgceRDVPALCRLLELLEEGQR---LPAPPACPAEVHELMKLCWAPSPQDRPSFSALGP 277
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
569-849 3.34e-49

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: 175.23  E-value: 3.34e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVhlceVEGMEKfkdKDfALDVSAnqpvlvAVKMLRADANKNARNDFLKEIKIMSRL-KDPNIIHLLAVCITD 647
Cdd:cd05047   3 IGEGNFGQV----LKARIK---KD-GLRMDA------AIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHR 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRH-----EPPNS-SSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd05047  69 GYLYLAIEYAPHGNLLDFLRKSrvletDPAFAiANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGEN 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFGMSRnlySGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIENT 801
Cdd:cd05047 149 YVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSL-GGTPYCGMTCAELYEKL 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 62420884 802 GEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05047 225 PQGYR-------LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 265
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
557-849 4.02e-48

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: 172.15  E-value: 4.02e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVegmekfkdkdfaldvsaNQPVLVAVKMLRAdaNKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05072   3 EIPRESIKLVKKLGAGQFGEVWMGYY-----------------NNSTKVAVKTLKP--GTMSVQAFLEEANLMKTLQHDK 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05072  64 LVRLYAVVTKEEPIYIITEYMAKGSLLDFLK--------SDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANV 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQ 796
Cdd:cd05072 136 LVSESLMCKIADFGLARVIEDNEYTAREG-AKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTY-GKIPYPGMSNSD 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05072 214 VMSALQRGYR-------MPRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVL 259
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
563-849 6.54e-48

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 172.49  E-value: 6.54e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVhlceVEGMEKfkdKDfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRL-KDPNIIHLL 641
Cdd:cd05089   4 IKFEDVIGEGNFGQV----IKAMIK---KD-------GLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVR------TVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd05089  70 GACENRGYLYIAIEYAPYGNLLDFLRKSRVLETDPAFAKehgtasTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARN 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMSRnlySGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDE 795
Cdd:cd05089 150 VLVGENLVSKIADFGLSR---GEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSL-GGTPYCGMTCA 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 62420884 796 QVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05089 226 ELYEKLPQGYR-------MEKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQL 272
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
557-849 1.55e-47

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: 170.64  E-value: 1.55e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvlVAVKMLRAdaNKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05069   8 EIPRESLRLDVKLGQGCFGEVWMGTWNGTTK-----------------VAIKTLKP--GTMMPEAFLQEAQIMKKLRHDK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVcITDDPLCMITEYMENGDLNQFLSRheppnsssSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05069  69 LVPLYAV-VSEEPIYIVTEFMGKGSLLDFLKE--------GDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05069 140 LVGDNLVCKIADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGR-VPYPGMVNRE 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05069 218 VLEQVERGYR-------MPCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFL 263
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
558-845 2.54e-47

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 170.11  E-value: 2.54e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 558 FPRKLLTFKEKLGEGQFGEVHLC--EVEGmekfkdkdfaldvsANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDP 635
Cdd:cd05079   1 FEKRFLKRIRDLGEGHFGKVELCryDPEG--------------DNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITD--DPLCMITEYMENGDLNQFLsrhePPNSSSSDVRTVsytnLKFmATQIASGMKYLSSLNFVHRDLAT 713
Cdd:cd05079  67 NIVKYKGICTEDggNGIKLIMEFLPSGSLKEYL----PRNKNKINLKQQ----LKY-AVQICKGMDYLGSRQYVHRDLAA 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMSRNLYSG-DYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQpYSQL 792
Cdd:cd05079 138 RNVLVESEHQVKIGDFGLTKAIETDkEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSE-SSPM 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 793 SdeqvientgEFFR----DQGRQTY------------LPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05079 217 T---------LFLKmigpTHGQMTVtrlvrvleegkrLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNL 276
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
557-849 2.70e-47

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: 169.87  E-value: 2.70e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvlVAVKMLRAdaNKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05071   5 EIPRESLRLEVKLGQGCFGEVWMGTWNGTTR-----------------VAIKTLKP--GTMSPEAFLQEAQVMKKLRHEK 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVcITDDPLCMITEYMENGDLNQFLSrheppNSSSSDVRTVSYTNlkfMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05071  66 LVQLYAV-VSEEPIYIVTEYMSKGSLLDFLK-----GEMGKYLRLPQLVD---MAAQIASGMAYVERMNYVHRDLRAANI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05071 137 LVGENLVCKVADFGLARLIEDNEYTARQG-AKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGR-VPYPGMVNRE 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05071 215 VLDQVERGYR-------MPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFL 260
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
563-845 1.75e-46

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: 166.97  E-value: 1.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGmekfkdkdfaldvsanQPVlvAVKMLRADANKNArndFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd05083   8 LTLGEIIGEGEFGAVLQGEYMG----------------QKV--AVKNIKCDVTAQA---FLEETAVMTKLQHKNLVRLLG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VcITDDPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05083  67 V-ILHNGLYIVMELMSKGNLVNFLR--------SRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSR-NLYSGDYYRiqgravLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIENT 801
Cdd:cd05083 138 VAKISDFGLAKvGSMGVDNSR------LPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGR-APYPKMSVKEVKEAV 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 62420884 802 GEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05083 211 EKGYR-------MEPPEGCPPDVYSIMTSCWEAEPGKRPSFKKL 247
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
557-845 1.90e-46

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: 169.39  E-value: 1.90e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDP- 635
Cdd:cd05102   3 EFPRDRLRLGKVLGHGAFGKVVEASAFGIDK-----------SSSCETVAVKMLKEGATASEHKALMSELKILIHIGNHl 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCI-TDDPLCMITEYMENGDLNQFL--------------------------------SRHEPPNSSSSDVRTV 682
Cdd:cd05102  72 NVVNLLGACTkPNGPLMVIVEFCKYGNLSNFLrakregfspyrersprtrsqvrsmveavradrRSRQGSDRVASFTEST 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 SYTN------------------LKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSG-DYYRi 743
Cdd:cd05102 152 SSTNqprqevddlwqspltmedLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDpDYVR- 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 744 QGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLsdeQVIENTGEFFRDQGRqtyLPQPAICPDS 823
Cdd:cd05102 231 KGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSL-GASPYPGV---QINEEFCQRLKDGTR---MRAPEYATPE 303
                       330       340
                ....*....|....*....|..
gi 62420884 824 VYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05102 304 IYRIMLSCWHGDPKERPTFSDL 325
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
557-849 5.57e-46

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: 170.19  E-value: 5.57e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVhlceVEGMekfkdkdfALDVSANQPVL-VAVKMLRADANKNARNDFLKEIKIMSRLkDP 635
Cdd:cd05107  33 EMPRDNLVLGRTLGSGAFGRV----VEAT--------AHGLSHSQSTMkVAVKMLKSTARSSEKQALMSELKIMSHL-GP 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 --NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRH-------------------------------------------- 669
Cdd:cd05107 100 hlNIVNLLGACTKGGPIYIITEYCRYGDLVDYLHRNkhtflqyyldknrddgslisggstplsqrkshvslgsesdggym 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 670 -------------------------EPPNSSS-------------------SDVRTVSYTNLKFMATQIASGMKYLSSLN 705
Cdd:cd05107 180 dmskdesadyvpmqdmkgtvkyadiESSNYESpydqylpsapertrrdtliNESPALSYMDLVGFSYQVANGMEFLASKN 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 706 FVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQ 785
Cdd:cd05107 260 CVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTL-G 338
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 786 EQPYSQLS-DEQvientgeFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05107 339 GTPYPELPmNEQ-------FYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLV 396
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
560-845 7.25e-46

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: 165.15  E-value: 7.25e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLRADANKNArndFLKEIKIMSRLKDPNIIH 639
Cdd:cd05082   5 MKELKLLQTIGKGEFGDVMLGDYRGNK------------------VAVKCIKNDATAQA---FLAEASVMTQLRHSNLVQ 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDD-PLCMITEYMENGDLNQFLSrheppnsssSDVRTVSYTN--LKFmATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05082  64 LLGVIVEEKgGLYIVTEYMAKGSLVDYLR---------SRGRSVLGGDclLKF-SLDVCEAMEYLEGNNFVHRDLAARNV 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSgdyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05082 134 LVSEDNVAKVSDFGLTKEASS-----TQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGR-VPYPRIPLKD 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05082 208 VVPRVEKGYK-------MDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQL 249
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
557-849 8.98e-46

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: 165.20  E-value: 8.98e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLcevegmekfkdkdfaldVSANQPVLVAVKMLRADANknARNDFLKEIKIMSRLKDPN 636
Cdd:cd05073   7 EIPRESLKLEKKLGAGQFGEVWM-----------------ATYNKHTKVAVKTMKPGSM--SVEAFLAEANVMKTLQHDK 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVcITDDPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd05073  68 LVKLHAV-VTKEPIYIITEFMAKGSLLDFLK--------SDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANI 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQ 796
Cdd:cd05073 139 LVSASLVCKIADFGLARVIEDNEYTAREG-AKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGR-IPYPGMSNPE 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 797 VIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05073 217 VIRALERGYR-------MPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVL 262
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
557-852 1.30e-45

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: 168.10  E-value: 1.30e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdKDFALDVsanqpvlvAVKMLRADANKNARNDFLKEIKIMSRL-KDP 635
Cdd:cd05106  34 EFPRDNLQFGKTLGAGAFGKVVEATAFGLGK---EDNVLRV--------AVKMLKASAHTDEREALMSELKILSHLgQHK 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDL------------NQFLSRHEPPNSSSS-------------------------- 677
Cdd:cd05106 103 NIVNLLGACTHGGPVLVITEYCCYGDLlnflrkkaetflNFVMALPEISETSSDyknitlekkyirsdsgfssqgsdtyv 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 678 ----------------------DVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNL 735
Cdd:cd05106 183 emrpvsssssqssdskdeedteDSWPLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDI 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 736 YSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQlsdeqvIENTGEFFRDQGRQTYLP 815
Cdd:cd05106 263 MNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSL-GKSPYPG------ILVNSKFYKMVKRGYQMS 335
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 62420884 816 QPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQ 852
Cdd:cd05106 336 RPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQRQ 372
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
557-842 1.62e-45

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: 168.66  E-value: 1.62e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVhlceVEGMekfkdkdfALDVSANQPVL-VAVKMLRADANKNARNDFLKEIKIMSRL-KD 634
Cdd:cd05105  33 EFPRDGLVLGRILGSGAFGKV----VEGT--------AYGLSRSQPVMkVAVKMLKPTARSSEKQALMSELKIMTHLgPH 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 635 PNIIHLLAVCITDDPLCMITEYMENGDL--------NQFLSRH-EPPNS-------SSSDVRTVSYTNLKFMAT------ 692
Cdd:cd05105 101 LNIVNLLGACTKSGPIYIITEYCFYGDLvnylhknrDNFLSRHpEKPKKdldifgiNPADESTRSYVILSFENKgdymdm 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 693 ----------------------------------------------------------------QIASGMKYLSSLNFVH 708
Cdd:cd05105 181 kqadttqyvpmleikeaskysdiqrsnydrpasykgsndsevknllsddgseglttldllsftyQVARGMEFLASKNCVH 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 709 RDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQP 788
Cdd:cd05105 261 RDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSL-GGTP 339
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 789 YSQLsdeqVIENTgefFRDQGRQTY-LPQPAICPDSVYKLMLSCWRRDTKNRPSF 842
Cdd:cd05105 340 YPGM----IVDST---FYNKIKSGYrMAKPDHATQEVYDIMVKCWNSEPEKRPSF 387
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
565-849 2.60e-45

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: 164.01  E-value: 2.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCEVEGmekfkdkdfalDVSANQpvlVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd05087   1 YLKEIGHGWFGKVFLGEVNS-----------GLSSTQ---VVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQC 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd05087  67 AEVTPYLLVMEFCPLGDLKGYLRSCRAAESMAPDPLT-----LQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWE-------SILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQV 797
Cdd:cd05087 142 KIGDYGLSHCKYKEDYFVTADQLWVPLRWIAPElvdevhgNLLVVDQTKQSNVWSLGVTIWELFEL-GNQPYRHYSDRQV 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 798 IENTgefFRDQgrQTYLPQPAI---CPDSVYKLMLSCWRRdTKNRPSFQEIHLLL 849
Cdd:cd05087 221 LTYT---VREQ--QLKLPKPQLklsLAERWYEVMQFCWLQ-PEQRPTAEEVHLLL 269
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
557-845 4.63e-45

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: 165.56  E-value: 4.63e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanQPV--LVAVKMLRADANKNARNDFLKEIKIMSRL-K 633
Cdd:cd14207   3 EFARERLKLGKSLGRGAFGKVVQASAFGIKK-------------SPTcrVVAVKMLKEGATASEYKALMTELKILIHIgH 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 634 DPNIIHLLAVCITDD-PLCMITEYMENGDLNQFL-------------SRHEPP--------------------------- 672
Cdd:cd14207  70 HLNVVNLLGACTKSGgPLMVIVEYCKYGNLSNYLkskrdffvtnkdtSLQEELikekkeaeptggkkkrlesvtssesfa 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 673 ------NSSSSDV------------RTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRN 734
Cdd:cd14207 150 ssgfqeDKSLSDVeeeeedsgdfykRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARD 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 735 LYSG-DYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLsdeQVIEntgEFFRDQGRQTY 813
Cdd:cd14207 230 IYKNpDYVR-KGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSL-GASPYPGV---QIDE---DFCSKLKEGIR 301
                       330       340       350
                ....*....|....*....|....*....|..
gi 62420884 814 LPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14207 302 MRAPEFATSEIYQIMLDCWQGDPNERPRFSEL 333
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
557-852 5.96e-45

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: 166.23  E-value: 5.96e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDP- 635
Cdd:cd05104  31 EFPRDRLRFGKTLGAGAFGKVVEATAYGLAK-----------ADSAMTVAVKMLKPSAHSTEREALMSELKVLSYLGNHi 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRH---------------------------------------------- 669
Cdd:cd05104 100 NIVNLLGACTVGGPTLVITEYCCYGDLLNFLRRKrdsficpkfedlaeaalyrnllhqremacdslneymdmkpsvsyvv 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 670 EPPNSSSSDVRTVSYT-------------------NLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFG 730
Cdd:cd05104 180 PTKADKRRGVRSGSYVdqdvtseileedelaldteDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFG 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 731 MSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLS-DEQVIENTGEFFRdqg 809
Cdd:cd05104 260 LARDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSL-GSSPYPGMPvDSKFYKMIKEGYR--- 335
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 62420884 810 rqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQQ 852
Cdd:cd05104 336 ----MDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIEQQ 374
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
558-845 1.04e-44

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 162.76  E-value: 1.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 558 FPRKLLTFKEKLGEGQFGEVHL-CevegmekfkdKDFALDVSANqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd05080   1 FHKRYLKKIRDLGEGHFGKVSLyC----------YDPTNDGTGE---MVAVKALKADCGPQHRSGWKQEIDILKTLYHEN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCIT--DDPLCMITEYMENGDLNQFLSRHeppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05080  68 IVKYKGCCSEqgGKSLQLIMEYVPLGSLRDYLPKH-----------SIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAAR 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSG-DYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPYSQLS 793
Cdd:cd05080 137 NVLLDNDRLVKIGDFGLAKAVPEGhEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTK 216
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 794 DEQVIENTgeffrdQG------------RQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05080 217 FLEMIGIA------QGqmtvvrlielleRGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENL 274
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
563-849 7.54e-44

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


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 160.93  E-value: 7.54e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHlcevegmeKFKDKDFALDVSAnqpvlvAVKMLRADANKNARNDFLKEIKIMSRL-KDPNIIHLL 641
Cdd:cd05088   9 IKFQDVIGEGNFGQVL--------KARIKKDGLRMDA------AIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHEPPNS------SSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd05088  75 GACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETdpafaiANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMSRnlySGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDE 795
Cdd:cd05088 155 ILVGENYVAKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSL-GGTPYCGMTCA 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 62420884 796 QVIENTGEFFRdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd05088 231 ELYEKLPQGYR-------LEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSL 277
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
569-845 7.57e-44

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: 160.19  E-value: 7.57e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevegmekfkdKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd05109  15 LGSGAFGTVY------------KGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTST 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 pLCMITEYMENGDLNQFLsRHEPPNSSSSDVRTvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd05109  83 -VQLVTQLMPYGCLLDYV-RENKDRIGSQDLLN--------WCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 729 FGMSR--NLYSGDYYRIQGRavLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIEntgefFR 806
Cdd:cd05109 153 FGLARllDIDETEYHADGGK--VPIKWMALESILHRRFTHQSDVWSYGVTVWELMTF-GAKPYDGIPAREIPD-----LL 224
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 62420884 807 DQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05109 225 EKGER--LPQPPICTIDVYMIMVKCWMIDSECRPRFREL 261
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
557-854 3.59e-43

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: 160.15  E-value: 3.59e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVhlceVEGmekfkdKDFALDVSANQPVlVAVKMLRADANKNARNDFLKEIKIMSRL-KDP 635
Cdd:cd05103   3 EFPRDRLKLGKPLGRGAFGQV----IEA------DAFGIDKTATCRT-VAVKMLKEGATHSEHRALMSELKILIHIgHHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCIT-DDPLCMITEYMENGDLNQFL--------------------------------SRHEPPNSSSS----- 677
Cdd:cd05103  72 NVVNLLGACTKpGGPLMVIVEFCKFGNLSAYLrskrsefvpyktkgarfrqgkdyvgdisvdlkRRLDSITSSQSsassg 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 678 --------DV------------RTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYS 737
Cdd:cd05103 152 fveekslsDVeeeeagqedlykDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYK 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 738 G-DYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLS-DEqvientgEFFRDQGRQTYLP 815
Cdd:cd05103 232 DpDYVR-KGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSL-GASPYPGVKiDE-------EFCRRLKEGTRMR 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 62420884 816 QPAICPDSVYKLMLSCWRRDTKNRPSFQEI--HLLLLQQGD 854
Cdd:cd05103 303 APDYTTPEMYQTMLDCWHGEPSQRPTFSELveHLGNLLQAN 343
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
569-845 3.66e-43

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 159.42  E-value: 3.66e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVH--LCEVEGmEKFKdkdfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05108  15 LGSGAFGTVYkgLWIPEG-EKVK-------------IPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DdPLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05108  81 S-TVQLITQLMPFGCLLDYVREHK---------DNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDY-YRIQGRAVlPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQV--IENTGE 803
Cdd:cd05108 151 TDFGLAKLLGAEEKeYHAEGGKV-PIKWMALESILHRIYTHQSDVWSYGVTVWELMTF-GSKPYDGIPASEIssILEKGE 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62420884 804 ffrdqgrqtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05108 229 ---------RLPQPPICTIDVYMIMVKCWMIDADSRPKFREL 261
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
569-845 2.50e-41

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: 152.80  E-value: 2.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevegmekfkdKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCiTDD 648
Cdd:cd05111  15 LGSGVFGTVH------------KGIWIPEGDSIKIPVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGIC-PGA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEppnSSSSDVRTVSYtnlkfmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd05111  82 SLQLVTQLLPLGSLLDHVRQHR---GSLGPQLLLNW------CVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVAD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 729 FGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFCQEqPYSQLSDEQVIEntgefFRDQ 808
Cdd:cd05111 153 FGVADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAE-PYAGMRLAEVPD-----LLEK 226
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 62420884 809 GRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05111 227 GER--LAQPQICTIDVYMVMVKCWMIDENIRPTFKEL 261
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
567-849 3.02e-40

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 149.63  E-value: 3.02e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVegmekfkdkdfaldVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05086   3 QEIGNGWFGKVLLGEI--------------YTGTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVrtvsyTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05086  69 AIPYLLVFEFCDLGDLKTYLANQQEKLRGDSQI-----MLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKV 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYYRIQGRAVLPIRWMSWE-------SILLGKFTTASDVWAFGVTLWETFTFCQeQPYSQLSDEQVIE 799
Cdd:cd05086 144 GDYGIGFSRYKEDYIETDDKKYAPLRWTAPElvtsfqdGLLAAEQTKYSNIWSLGVTLWELFENAA-QPYSDLSDREVLN 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 800 NTgefFRDqgRQTYLPQPAI---CPDSVYKLMLSCWRRDTKnRPSFQEIHLLL 849
Cdd:cd05086 223 HV---IKE--RQVKLFKPHLeqpYSDRWYEVLQFCWLSPEK-RPTAEEVHRLL 269
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
567-851 4.63e-40

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: 148.44  E-value: 4.63e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLRADANKNARNDFLK-EIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd06606   6 ELLGKGSFGSVYL--------------ALNLDTGE--LMAVKEVELSGDSEEELEALErEIRILSSLKHPNIVRYLGTER 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSR----HEPpnssssDVRtvSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd06606  70 TENTLNIFLEYVPGGSLASLLKKfgklPEP------VVR--KYTR------QILEGLEYLHSNGIVHRDIKGANILVDSD 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDE-QVIen 800
Cdd:cd06606 136 GVVKLADFGCAKRLAEIATGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMAT--GKPPWSELGNPvAAL-- 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 62420884 801 tgefFRDqGRQTYLPQ-PAICPDSVYKLMLSCWRRDTKNRPSFQEihllLLQ 851
Cdd:cd06606 212 ----FKI-GSSGEPPPiPEHLSEEAKDFLRKCLQRDPKKRPTADE----LLQ 254
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
569-845 1.02e-39

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: 147.54  E-value: 1.02e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLRADANKNA---RNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14061   2 IGVGGFGKVYRGIWRGEE------------------VAVKAARQDPDEDIsvtLENVRQEARLFWMLRHPNIIALRGVCL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLS-RHEPPNssssdvRTVSYtnlkfmATQIASGMKYLSS---LNFVHRDLATRNCLVGK- 720
Cdd:cd14061  64 QPPNLCLVMEYARGGALNRVLAgRKIPPH------VLVDW------AIQIARGMNYLHNeapVPIIHRDLKSSNILILEa 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 -------NYTIKIADFGMSRNLY-------SGDYyriqgravlpiRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQE 786
Cdd:cd14061 132 ienedleNKTLKITDFGLAREWHkttrmsaAGTY-----------AWMAPEVIKSSTFSKASDVWSYGVLLWELLT--GE 198
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 787 QPYSQLSDEQVIENTGEffrdqgRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14061 199 VPYKGIDGLAVAYGVAV------NKLTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADI 251
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
569-845 6.40e-39

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


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 146.75  E-value: 6.40e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevegmekfkdKDFALDVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd05110  15 LGSGAFGTVY------------KGIWVPEGETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSPT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 pLCMITEYMENGDLNQFLsrHEPPNSSSSDVrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd05110  83 -IQLVTQLMPHGCLLDYV--HEHKDNIGSQL-------LLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 729 FGMSRnLYSGDY--YRIQGrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcQEQPYSQLSDEQVIEntgefFR 806
Cdd:cd05110 153 FGLAR-LLEGDEkeYNADG-GKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTF-GGKPYDGIPTREIPD-----LL 224
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 62420884 807 DQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05110 225 EKGER--LPQPPICTIDVYMVMVKCWMIDADSRPKFKEL 261
FA58C smart00231
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ...
30-185 2.95e-38

Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.


Pssm-ID: 214572  Cd Length: 139  Bit Score: 139.18  E-value: 2.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884     30 CRYPLGMSGgqipDEDITASSQwseSTAAKYGRLDsEEGDGAWCPEIPvepdDLKEFLQIDLHTLHFITLVGTQGRHAGG 109
Cdd:smart00231   2 CNEPLGLES----DSQITASSS---YWAAKIARLN-GGSDGGWCPAKN----DLPPWIQVDLGRLRTVTGVITGRRHGNG 69
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884    110 HGIEfapmYKINYSRDGTRWISWRNRHGKqVLDGNSNPYDIFLKDLEPPIVARFVRFIPVTDHsMNVCMRVELYGC 185
Cdd:smart00231  70 DWVT----YKLEYSDDGVNWTTYKDGNSK-VFPGNSDAGTVVLNDFPPPIVARYVRILPTGWN-GNIILRVELLGC 139
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
604-847 2.17e-36

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: 137.24  E-value: 2.17e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRADANKnarndflkEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSssdvRTVS 683
Cdd:cd14059  18 EVAVKKVRDEKET--------DIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPS----LLVD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 684 YtnlkfmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNL--------YSGDyyriqgravlpIRWMS 755
Cdd:cd14059  86 W------SKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELsekstkmsFAGT-----------VAWMA 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 756 WESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIENTGEffrdqgRQTYLPQPAICPDSVYKLMLSCWRRD 835
Cdd:cd14059 149 PEVIRNEPCSEKVDIWSFGVVLWELLT--GEIPYKDVDSSAIIWGVGS------NSLQLPVPSTCPDGFKLLMKQCWNSK 220
                       250
                ....*....|....
gi 62420884 836 TKNRPSFQEI--HL 847
Cdd:cd14059 221 PRNRPSFRQIlmHL 234
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
569-852 2.53e-36

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: 138.25  E-value: 2.53e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLRADANKNAR---NDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14146   2 IGVGGFGKVYRATWKGQE------------------VAVKAARQDPDEDIKataESVRQEAKLFSMLRHPNIIKLEGVCL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRhEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFV---HRDLATRNCLVGK-- 720
Cdd:cd14146  64 EEPNLCLVMEFARGGTLNRALAA-ANAAPGPRRARRIPPHILVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEki 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 ------NYTIKIADFGMSRNLYSGDYYRIQGRAVlpirWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSD 794
Cdd:cd14146 143 ehddicNKTLKITDFGLAREWHRTTKMSAAGTYA----WMAPEVIKSSLFSKGSDIWSYGVLLWELLT--GEVPYRGIDG 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 795 EQVIENTGEffrdqgRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQeihlLLLQQ 852
Cdd:cd14146 217 LAVAYGVAV------NKLTLPIPSTCPEPFAKLMKECWEQDPHIRPSFA----LILEQ 264
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
569-845 7.26e-36

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: 136.41  E-value: 7.26e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmeKFKDKDfaldvsanqpvlVAVKMLRADANKNArndFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd14058   1 VGRGSFGVVCKA------RWRNQI------------VAVKIIESESEKKA---FEVEVRQLSRVDHPNIIKLYGACSNQK 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEP-PNSSSSDVrtVSYtnlkfmATQIASGMKYLSSLN---FVHRDLATRNCLVGKNYT- 723
Cdd:cd14058  60 PVCLVMEYAEGGSLYNVLHGKEPkPIYTAAHA--MSW------ALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTv 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 IKIADFG--------MSRNlysgdyyriQGRAvlpiRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSde 795
Cdd:cd14058 132 LKICDFGtacdisthMTNN---------KGSA----AWMAPEVFEGSKYSEKCDVFSWGIILWEVIT--RRKPFDHIG-- 194
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 796 qvientGEFFR-----DQGRQtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14058 195 ------GPAFRimwavHNGER--PPLIKNCPKPIESLMTRCWSKDPEKRPSMKEI 241
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
567-841 7.92e-36

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: 136.56  E-value: 7.92e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVlvAVKMLRAD--ANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14014   6 RLLGRGGMGEVYR--------------ARDTLLGRPV--AIKVLRPElaEDEEFRERFLREARALARLSHPNIVRVYDVG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPPnsssSDVRTVSytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd14014  70 EDDGRPYIVMEYVEGGSLADLLRERGPL----PPREALR------ILAQIADALAAAHRAGIVHRDIKPANILLTEDGRV 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGDYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcqEQPYSQLSDEQVIENTGEF 804
Cdd:cd14014 140 KLTDFGIARALGDSGLTQ-TGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTG--RPPFDGDSPAAVLAKHLQE 216
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 62420884 805 FRDQGRQtylPQPAIcPDSVYKLMLSCWRRDTKNRPS 841
Cdd:cd14014 217 APPPPSP---LNPDV-PPALDAIILRALAKDPEERPQ 249
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
569-844 8.06e-36

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: 136.43  E-value: 8.06e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegmekfkdkdfALDVSANqpVLVAVKMLRADAN-KNARNDFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd13978   1 LGSGGFGTVSK--------------ARHVSWF--GMVAIKCLHSSPNcIEERKALLKEAEKMERARHSYVLPLLGVCVER 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEPPNSSSsdvrtvsytnLKF-MATQIASGMKYLSSLN--FVHRDLATRNCLVGKNYTI 724
Cdd:cd13978  65 RSLGLVMEYMENGSLKSLLEREIQDVPWS----------LRFrIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHV 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSR-NLYSGDYYRIQGRAVL--PIRWMSWESI--LLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIe 799
Cdd:cd13978 135 KISDFGLSKlGMKSISANRRRGTENLggTPIYMAPEAFddFNKKPTSKSDVYSFAIVIWAVLT--RKEPFENAINPLLI- 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 800 ntgEFFRDQGRQTYL-----PQPAICPDSVYKLMLSCWRRDTKNRPSFQE 844
Cdd:cd13978 212 ---MQIVSKGDRPSLddigrLKQIENVQELISLMIRCWDGNPDARPTFLE 258
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
607-845 1.87e-35

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: 135.31  E-value: 1.87e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 607 VKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVrtvsytn 686
Cdd:cd14065  20 VMVMKELKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELLKSMDEQLPWSQRV------- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 687 lkFMATQIASGMKYLSSLNFVHRDLATRNCLV---GKNYTIKIADFGMSRNLysGDYYRIQGRAVLPIR------WMSWE 757
Cdd:cd14065  93 --SLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREM--PDEKTKKPDRKKRLTvvgspyWMAPE 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 758 SILLGKFTTASDVWAFGVTLWETFTfcqeqpySQLSDEQVIENTGEFFRD-QGRQTYLPQPaiCPDSVYKLMLSCWRRDT 836
Cdd:cd14065 169 MLRGESYDEKVDVFSFGIVLCEIIG-------RVPADPDYLPRTMDFGLDvRAFRTLYVPD--CPPSFLPLAIRCCQLDP 239

                ....*....
gi 62420884 837 KNRPSFQEI 845
Cdd:cd14065 240 EKRPSFVEL 248
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
563-845 4.05e-34

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: 132.09  E-value: 4.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLRADANKNARN---DFLKEIKIMSRLKDPNIIH 639
Cdd:cd14145   8 LVLEEIIGIGGFGKVYRAIWIGDE------------------VAVKAARHDPDEDISQtieNVRQEAKLFAMLKHPNIIA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLS-RHEPPNSsssdvrtvsytnLKFMATQIASGMKYLSS---LNFVHRDLATRN 715
Cdd:cd14145  70 LRGVCLKEPNLCLVMEFARGGPLNRVLSgKRIPPDI------------LVNWAVQIARGMNYLHCeaiVPVIHRDLKSSN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGK--------NYTIKIADFGMSRnlysgDYYR-IQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQE 786
Cdd:cd14145 138 ILILEkvengdlsNKILKITDFGLAR-----EWHRtTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT--GE 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 787 QPYSQLSDEQVIENTGEffrdqgRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14145 211 VPFRGIDGLAVAYGVAM------NKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNI 263
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
605-845 5.13e-34

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: 131.26  E-value: 5.13e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADANKN---ARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLS-RHEPPNSsssdvr 680
Cdd:cd14148  20 VAVKAARQDPDEDiavTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNRALAgKKVPPHV------ 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 681 tvsytnLKFMATQIASGMKYLSSLNFV---HRDLATRNCLVGK--------NYTIKIADFGMSRNLYSGDYYRIQGRAVl 749
Cdd:cd14148  94 ------LVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEpienddlsGKTLKITDFGLAREWHKTTKMSAAGTYA- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 750 pirWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIENTGEffrdqgRQTYLPQPAICPDSVYKLML 829
Cdd:cd14148 167 ---WMAPEVIRLSLFSKSSDVWSFGVLLWELLT--GEVPYREIDALAVAYGVAM------NKLTLPIPSTCPEPFARLLE 235
                       250
                ....*....|....*.
gi 62420884 830 SCWRRDTKNRPSFQEI 845
Cdd:cd14148 236 ECWDPDPHGRPDFGSI 251
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
563-852 3.68e-33

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: 128.99  E-value: 3.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGMekfkdkdfaldvsanqpvLVAVKMLRADANKN---ARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd14147   5 LRLEEVIGIGGFGKVYRGSWRGE------------------LVAVKAARQDPDEDisvTAESVRQEARLFAMLAHPNIIA 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLS-RHEPPNSsssdvrtvsytnLKFMATQIASGMKYLSS---LNFVHRDLATRN 715
Cdd:cd14147  67 LKAVCLEEPNLCLVMEYAAGGPLSRALAgRRVPPHV------------LVNWAVQIARGMHYLHCealVPVIHRDLKSNN 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKN--------YTIKIADFGMSRNLYSGDYYRIQGRAVlpirWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQ 787
Cdd:cd14147 135 ILLLQPienddmehKTLKITDFGLAREWHKTTQMSAAGTYA----WMAPEVIKASTFSKGSDVWSFGVLLWELLT--GEV 208
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 788 PYSQLSDEQVIENTGEffrdqgRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIhlllLQQ 852
Cdd:cd14147 209 PYRGIDCLAVAYGVAV------NKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASI----LQQ 263
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
567-774 1.35e-31

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: 124.90  E-value: 1.35e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekFKdkdfALDVSANQPVlvAVKMLRADANK-----NArndfLKEIKIMSRLKDPNIIHLL 641
Cdd:cd07829   5 EKLGEGTYGVV----------YK----AKDKKTGEIV--ALKKIRLDNEEegipsTA----LREISLLKELKHPNIVKLL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENgDLNQFLSRHEPPnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd07829  65 DVIHTENKLYLVFEYCDQ-DLKKYLDKRPGP---------LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRD 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 722 YTIKIADFGMSRnlysgdYYRIqgravlPIRWMSWES---------ILLG--KFTTASDVWAFG 774
Cdd:cd07829 135 GVLKLADFGLAR------AFGI------PLRTYTHEVvtlwyrapeILLGskHYSTAVDIWSVG 186
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
569-783 2.19e-31

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: 123.82  E-value: 2.19e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfkdkdfaLDVSANQpvLVAVKML-------------RADANKNARNDFLKEIKIMSRLKDP 635
Cdd:cd14008   1 LGRGSFGKVKLA--------------LDTETGQ--LYAIKIFnksrlrkrregknDRGKIKNALDDVRREIAIMKKLDHP 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVcItDDP----LCMITEYMENGDLNQFLSRHEPPNSSSSDVRtvsytnlkFMATQIASGMKYLSSLNFVHRDL 711
Cdd:cd14008  65 NIVRLYEV-I-DDPesdkLYLVLEYCEGGPVMELDSGDRVPPLPEETAR--------KYFRDLVLGLEYLHENGIVHRDI 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 712 ATRNCLVGKNYTIKIADFGMSRNLYSGDYYrIQGRAVLPIrWMSWE------SILLGKfttASDVWAFGVTLWeTFTF 783
Cdd:cd14008 135 KPENLLLTADGTVKISDFGVSEMFEDGNDT-LQKTAGTPA-FLAPElcdgdsKTYSGK---AADIWALGVTLY-CLVF 206
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
569-845 3.47e-31

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: 123.54  E-value: 3.47e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGmekfkdkdfaldvsanqPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd14066   1 IGSGGFGTVYKGVLEN-----------------GTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESD 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEppnssSSDVrtVSYTNLKFMATQIASGMKYL---SSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd14066  64 EKLLVYEYMPNGSLEDRLHCHK-----GSPP--LPWPQRLKIAKGIARGLEYLheeCPPPIIHGDIKSSNILLDEDFEPK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIENTGEFF 805
Cdd:cd14066 137 LTDFGLARLIPPSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT--GKPAVDENRENASRKDLVEWV 214
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 806 RDQGRQTYL--------PQPAICPDSV---YKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14066 215 ESKGKEELEdildkrlvDDDGVEEEEVealLRLALLCTRSDPSLRPSMKEV 265
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
567-779 1.22e-30

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: 121.42  E-value: 1.22e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmeKFKDKDfaldvsanqpvLVAVKMLR-ADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd08215   6 RVIGKGSFGSAYLVR-----RKSDGK-----------LYVLKEIDlSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNS--SSSDVrtvsytnLKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd08215  70 ENGKLCIVMEYADGGDLAQKIKKQKKKGQpfPEEQI-------LDWF-VQICLALKYLHSRKILHRDLKTQNIFLTKDGV 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 724 IKIADFGMSRNLYSGD----------YYriqgravlpirwMSWEsILLGK-FTTASDVWAFGVTLWE 779
Cdd:cd08215 142 VKLGDFGISKVLESTTdlaktvvgtpYY------------LSPE-LCENKpYNYKSDIWALGCVLYE 195
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
569-846 1.27e-30

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


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 121.85  E-value: 1.27e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVhlcevegmekfkdkdFALDVSANQPVLVAVKMLRADanKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd14154   1 LGKGFFGQA---------------IKVTHRETGEVMVMKELIRFD--EEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDK 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEPPNSSSSDVRtvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd14154  64 KLNLITEYIPGGTLKDVLKDMARPLPWAQRVR---------FAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVAD 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 729 FGMSR-----NLYSGDYYRIQGRAVL--PIR-----------WMSWESILLGKFTTASDVWAFGVTLWETFTFCQeqpys 790
Cdd:cd14154 135 FGLARliveeRLPSGNMSPSETLRHLksPDRkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVE----- 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 791 qlSDEQVIENTGEFFRDQG--RQTYLPQpaiCPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd14154 210 --ADPDYLPRTKDFGLNVDsfREKFCAG---CPPPFFKLAFLCCDLDPEKRPPFETLE 262
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
564-844 1.50e-30

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: 121.18  E-value: 1.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVK-MLRADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd06627   3 QLGDLIGRGAFGSVYK--------------GLNLNTGE--FVAIKqISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVrtvsYTnlkfmaTQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd06627  67 SVKTKDSLYIILEYVENGSLASIIKKFGKFPESLVAV----YI------YQVLEGLAYLHEQGVIHRDIKGANILTTKDG 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSgdyyrIQGRAVLPI---RWMSWESILLGKFTTASDVWAFGVTLWETFT----FCQEQPYSQLsde 795
Cdd:cd06627 137 LVKLADFGVATKLNE-----VEKDENSVVgtpYWMAPEVIEMSGVTTASDIWSVGCTVIELLTgnppYYDLQPMAAL--- 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 62420884 796 qvientgefFRdQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQE 844
Cdd:cd06627 209 ---------FR-IVQDDHPPLPENISPELRDFLLQCFQKDPTLRPSAKE 247
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
570-845 1.08e-29

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: 118.14  E-value: 1.08e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 570 GEGQFGEVHLcevegmekfkdkdfALDVSANQPVlvAVKMLradanknarNDFLKEIKIMSRLKDPNIIHLLAVCITDDP 649
Cdd:cd14060   2 GGGSFGSVYR--------------AIWVSQDKEV--AVKKL---------LKIEKEAEILSVLSHRNIIQFYGAILEAPN 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 650 LCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYL---SSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd14060  57 YGIVTEYASYGSLFDYLN--------SNESEEMDMDQIMTWATDIAKGMHYLhmeAPVKVIHRDLKSRNVVIAADGVLKI 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYYRIQGraVLPirWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQV----IENtG 802
Cdd:cd14060 129 CDFGASRFHSHTTHMSLVG--TFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLT--REVPFKGLEGLQVawlvVEK-N 201
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 803 EffrdqgRQTYlpqPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14060 202 E------RPTI---PSSCPRSFAELMRRCWEADVKERPSFKQI 235
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
567-841 1.11e-29

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 123.97  E-value: 1.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVlvAVKMLRADANKN--ARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:COG0515  13 RLLGRGGMGVVYL--------------ARDLRLGRPV--ALKVLRPELAADpeARERFRREARALARLNHPNIVRVYDVG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPPnsSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:COG0515  77 EEDGRPYLVMEYVEGESLADLLRRRGPL--PPAEALRI--------LAQLAEALAAAHAAGIVHRDIKPANILLTPDGRV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGDYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIentgef 804
Cdd:COG0515 147 KLIDFGIARALGGATLTQ-TGTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLT--GRPPFDGDSPAELL------ 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 62420884 805 fRDQGRQTYLPQPAICPD---SVYKLMLSCWRRDTKNRPS 841
Cdd:COG0515 218 -RAHLREPPPPPSELRPDlppALDAIVLRALAKDPEERYQ 256
Pkinase pfam00069
Protein kinase domain;
563-845 5.73e-29

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 115.42  E-value: 5.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   563 LTFKEKLGEGQFGEVHLCevegmekfKDKDfaldvsANQpvLVAVKMLRAD-ANKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKA--------KHRD------TGK--IVAIKKIKKEkIKKKKDKNILREIKILKKLNHPNIVRLY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   642 AVCITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLN-FVhrdlATRNclvgk 720
Cdd:pfam00069  65 DAFEDKDNLYLVLEYVEGGSLFDLLSEK----------GAFSEREAKFIMKQILEGLESGSSLTtFV----GTPW----- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884   721 nytikiadfgmsrnlysgdyyriqgravlpirWMSWESILLGKFTTASDVWAFGVTLWEtfTFCQEQPYSQLSDEQvien 800
Cdd:pfam00069 126 --------------------------------YMAPEVLGGNPYGPKVDVWSLGCILYE--LLTGKPPFPGINGNE---- 167
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 62420884   801 TGEFFRDQGRQTYLPqPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:pfam00069 168 IYELIIDQPYAFPEL-PSNLSEEAKDLLKKLLKKDPSKRLTATQA 211
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
567-845 9.59e-29

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: 115.69  E-value: 9.59e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14003   6 KTLGEGSFGKVKL--------------ARHKLTGE--KVAIKIIdKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPpnSSSSDVRtvsytnlKFMAtQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd14003  70 TENKIYLVMEYASGGELFDYIVNNGR--LSEDEAR-------RFFQ-QLISAVDYCHSNGIVHRDLKLENILLDKNGNLK 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNLYSGDY---------YriqgravlpirwMSWEsILLGK--FTTASDVWAFGVTLWetFTFCQEQPYSQlSD 794
Cdd:cd14003 140 IIDFGLSNEFRGGSLlktfcgtpaY------------AAPE-VLLGRkyDGPKADVWSLGVILY--AMLTGYLPFDD-DN 203
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 795 EQVIentgefFRDQGRQTYLPQPAICPDSVyKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14003 204 DSKL------FRKILKGKYPIPSHLSPDAR-DLIRRMLVVDPSKRITIEEI 247
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
604-854 4.25e-28

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 114.11  E-value: 4.25e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRADANknaRNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrtVS 683
Cdd:cd14155  20 VMALKMNTLSSN---RANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQLLDSNEP----------LS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 684 YTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN---YTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESIL 760
Cdd:cd14155  87 WTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDengYTAVVGDFGLAEKIPDYSDGKEKLAVVGSPYWMAPEVLR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 761 LGKFTTASDVWAFGVTLWETFTFCQeqpysqlSDEQVIENTGEFFRD-QGRQTYLPQpaiCPDSVYKLMLSCWRRDTKNR 839
Cdd:cd14155 167 GEPYNEKADVFSYGIILCEIIARIQ-------ADPDYLPRTEDFGLDyDAFQHMVGD---CPPDFLQLAFNCCNMDPKSR 236
                       250
                ....*....|....*..
gi 62420884 840 PSFQEI--HLLLLQQGD 854
Cdd:cd14155 237 PSFHDIvkTLEEILEKL 253
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
563-845 6.01e-28

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 113.73  E-value: 6.01e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHlcevEGMEKFKDKDFALDVSanqpvlVAVKMLRADaNKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd05037   1 ITFHEHLGQGTFTNIY----DGILREVGDGRVQEVE------VLLKVLDSD-HRDISESFFETASLMSQISHKHLVKLYG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLcMITEYMENGDLNQFLSR--HEPPNSSSSDVrtvsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLV-- 718
Cdd:cd05037  70 VCVADENI-MVQEYVRYGPLDKYLRRmgNNVPLSWKLQV-----------AKQLASALHYLEDKKLIHGNVRGRNILLar 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 -GKNYT---IKIADFGMSRNLYSGDYyriqgrAVLPIRWMSWE--SILLGKFTTASDVWAFGVTLWETFTFCQEqPYSQL 792
Cdd:cd05037 138 eGLDGYppfIKLSDPGVPITVLSREE------RVDRIPWIAPEclRNLQANLTIAADKWSFGTTLWEICSGGEE-PLSAL 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 793 SDEQVIentgEFFRDQGRqtyLPQPAICPdsVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05037 211 SSQEKL----QFYEDQHQ---LPAPDCAE--LAELIMQCWTYEPTKRPSFRAI 254
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
564-777 1.55e-27

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: 112.57  E-value: 1.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLCevegMEKfkdkdfaldvSANQpvLVAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd05117   3 ELGKVLGRGSFGVVRLA----VHK----------KTGE--EYAVKIIdKKKLKSEDEEMLRREIEILKRLDHPNIVKLYE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRHEppNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLV---G 719
Cdd:cd05117  67 VFEDDKNLYLVMELCTGGELFDRIVKKG--SFSEREAAKI--------MKQILSAVAYLHSQGIVHRDLKPENILLaskD 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 720 KNYTIKIADFGMSRNLYSGD---------YYriqgravlpirwMSWESILLGKFTTASDVWAFGVTL 777
Cdd:cd05117 137 PDSPIKIIDFGLAKIFEEGEklktvcgtpYY------------VAPEVLKGKGYGKKCDIWSLGVIL 191
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
569-845 4.65e-27

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: 110.77  E-value: 4.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevegmeKFKDKDfaldvsanQPVLVAVK-MLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd14009   1 IGRGSFATVW--------KGRHKQ--------TGEVVAIKeISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTE 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEPPNSSSsdVRtvsytnlKFMaTQIASGMKYLSSLNFVHRDLATRNCLV---GKNYTI 724
Cdd:cd14009  65 DFIYLVLEYCAGGDLSQYIRKRGRLPEAV--AR-------HFM-QQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGDYyriqgRAVL---PIrWMSWESILLGKFTTASDVWAFGVTLWETFT----FcQEQPYSQLsdEQV 797
Cdd:cd14009 135 KIADFGFARSLQPASM-----AETLcgsPL-YMAPEILQFQKYDAKADLWSVGAILFEMLVgkppF-RGSNHVQL--LRN 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 62420884 798 IENTGEFFRDQGRQTYLPQpaiCPDSVYKLMlscwRRDTKNRPSFQEI 845
Cdd:cd14009 206 IERSDAVIPFPIAAQLSPD---CKDLLRRLL----RRDPAERISFEEF 246
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
568-792 9.18e-27

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 110.02  E-value: 9.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEvegmekfkdkdfalDVSANQpvLVAVKMLRADANKNARNdfLKEIKIMSRLKD----PNIIHLLAV 643
Cdd:cd05118   6 KIGEGAFGTVWLAR--------------DKVTGE--KVAIKKIKNDFRHPKAA--LREIKLLKHLNDveghPNIVKLLDV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 cITDDP---LCMITEYMENgDLNQFLsRHEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLV-G 719
Cdd:cd05118  68 -FEHRGgnhLCLVFELMGM-NLYELI-KDYPRGLPLDLIKSYLY--------QLLQALDFLHSNGIIHRDLKPENILInL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 720 KNYTIKIADFGMSRNLYSGDYY-RIQGRAvlpirWMSWEsILLGK--FTTASDVWAFGVTLWETFT----FCQEQPYSQL 792
Cdd:cd05118 137 ELGQLKLADFGLARSFTSPPYTpYVATRW-----YRAPE-VLLGAkpYGSSIDIWSLGCILAELLTgrplFPGDSEVDQL 210
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
564-777 1.15e-26

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 109.97  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLCEvegmekfkdkdfalDVSANQPVLVAVKML-RADANKNARNDFL-KEIKIMSRLKDPNIIHLL 641
Cdd:cd14080   3 RLGKTIGEGSYSKVKLAE--------------YTKSGLKEKVACKIIdKKKAPKDFLEKFLpRELEILRKLRHPNIIQVY 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHeppnSSSSDVRTvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14080  69 SIFERGSKVFIFMEYAEHGDLLEYIQKR----GALSESQA------RIWFRQLALAVQYLHSLDIAHRDLKCENILLDSN 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 722 YTIKIADFGMSRnlYSGDYYR------------------IQGRAVLPirwmswesillgkftTASDVWAFGVTL 777
Cdd:cd14080 139 NNVKLSDFGFAR--LCPDDDGdvlsktfcgsaayaapeiLQGIPYDP---------------KKYDIWSLGVIL 195
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
562-792 3.22e-26

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: 108.44  E-value: 3.22e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 562 LLTFKEKLGEGQFGEVhlcevegmekFKdkdfALDVSANQpvLVAVKMLrADANKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd05122   1 LFEILEKIGKGGFGVV----------YK----ARHKKTGQ--IVAIKKI-NLESKEKKESILNEIAILKKCKHPNIVKYY 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHeppnssssdVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd05122  64 GSYLKKDELWIVMEFCSGGSLKDLLKNT---------NKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 722 YTIKIADFG--------MSRNLYSGDYYriqgravlpirWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQL 792
Cdd:cd05122 135 GEVKLIDFGlsaqlsdgKTRNTFVGTPY-----------WMAPEVIQGKPYGFKADIWSLGITAIEMAE--GKPPYSEL 200
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
599-846 9.16e-26

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 107.72  E-value: 9.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 599 ANQPVLVAVKMLRADanKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLsRHEPPNSSSSD 678
Cdd:cd14222  16 ATGKVMVMKELIRCD--EETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFL-RADDPFPWQQK 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 679 VRtvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIR------ 752
Cdd:cd14222  93 VS---------FAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPPPDKPTTKKRtlrknd 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 753 ------------WMSWESILLGKFTTASDVWAFGVTLWETFTfcqeQPYsqlSDEQVIENTGEF------FRDQgrqtYL 814
Cdd:cd14222 164 rkkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEIIG----QVY---ADPDCLPRTLDFglnvrlFWEK----FV 232
                       250       260       270
                ....*....|....*....|....*....|..
gi 62420884 815 PQPaiCPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd14222 233 PKD--CPPAFFPLAAICCRLEPDSRPAFSKLE 262
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
562-779 9.87e-25

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 104.21  E-value: 9.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 562 LLTFKEKLGEGQFGEVhlcevegmekFKdkdfALDVSANQpvLVAVKMLRAdaNKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd06614   1 LYKNLEKIGEGASGEV----------YK----ATDRATGK--EVAIKKMRL--RKQNKELIINEILIMKECKHPNIVDYY 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLnqflsrheppnsssSDVrtVSYTNLKFMATQIA-------SGMKYLSSLNFVHRDLATR 714
Cdd:cd06614  63 DSYLVGDELWVVMEYMDGGSL--------------TDI--ITQNPVRMNESQIAyvcrevlQGLEYLHSQNVIHRDIKSD 126
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSGDYYR--IQGRAVlpirWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd06614 127 NILLSKDGSVKLADFGFAAQLTKEKSKRnsVVGTPY----WMAPEVIKRKDYGPKVDIWSLGIMCIE 189
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
568-845 1.01e-24

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: 104.09  E-value: 1.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLRAD---ANKNARNdFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14007   7 PLGKGKFGNVYL--------------AREKKSGF--IVALKVISKSqlqKSGLEHQ-LRREIEIQSHLRHPNILRLYGYF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPpnssSSDVRTVSYTnlkfmaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd14007  70 EDKKRIYLILEYAPNGELYKELKKQKR----FDEKEAAKYI------YQLALALDYLHSKNIIHRDIKPENILLGSNGEL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMS-------RNLYSG--DYyriqgravlpirwMSWEsILLGKFTTAS-DVWAFGVTLWEtftFCQ-EQPYSQLS 793
Cdd:cd14007 140 KLADFGWSvhapsnrRKTFCGtlDY-------------LPPE-MVEGKEYDYKvDIWSLGVLCYE---LLVgKPPFESKS 202
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 794 DEQVIENTgeffrDQGRQTYlpqpaicPDSVYK----LMLSCWRRDTKNRPSFQEI 845
Cdd:cd14007 203 HQETYKRI-----QNVDIKF-------PSSVSPeakdLISKLLQKDPSKRLSLEQV 246
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
603-849 1.66e-24

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 103.88  E-value: 1.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 603 VLVAVKMLRADanKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQF---LSRHEPPNSSSSdv 679
Cdd:cd14221  20 VMVMKELIRFD--EETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIiksMDSHYPWSQRVS-- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 680 rtvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVL-PIR------ 752
Cdd:cd14221  96 ----------FAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSLKkPDRkkrytv 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 753 -----WMSWESILLGKFTTASDVWAFGVTLWETFTFCQEQPysqlsdeQVIENTGEFFRDQgrQTYLPQ--PAICPDSVY 825
Cdd:cd14221 166 vgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEIIGRVNADP-------DYLPRTMDFGLNV--RGFLDRycPPNCPPSFF 236
                       250       260
                ....*....|....*....|....
gi 62420884 826 KLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14221 237 PIAVLCCDLDPEKRPSFSKLEHWL 260
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
603-842 2.19e-24

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: 103.84  E-value: 2.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 603 VLVAVKMLRADA--NKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRheppnsssSDVR 680
Cdd:cd14026  23 VTVAIKCLKLDSpvGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSLNELLHE--------KDIY 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 681 TVSYTNLKF-MATQIASGMKYLSSLN--FVHRDLATRNCLVGKNYTIKIADFGMSRnlysgdyYRI----QGRAVLP--- 750
Cdd:cd14026  95 PDVAWPLRLrILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSK-------WRQlsisQSRSSKSape 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 751 ---IRWMSWESILLGKFTTAS---DVWAFGVTLWETFTfcQEQPYSQLSDE-QVIENTGEFFRDQGRQTYLPQPAICPDS 823
Cdd:cd14026 168 ggtIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLS--RKIPFEEVTNPlQIMYSVSQGHRPDTGEDSLPVDIPHRAT 245
                       250
                ....*....|....*....
gi 62420884 824 VYKLMLSCWRRDTKNRPSF 842
Cdd:cd14026 246 LINLIESGWAQNPDERPSF 264
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
564-779 2.30e-24

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: 104.19  E-value: 2.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLRADANKNARN--DF--LKEIKIMSRLKDPNIIH 639
Cdd:cd07841   3 EKGKKLGEGTYAVVYK--------------ARDKETGR--IVAIKKIKLGERKEAKDgiNFtaLREIKLLQELKHPNIIG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMEnGDLNQFLSRheppnssssdvRTVSYT--NLKFMATQIASGMKYLSSLNFVHRDLATRNCL 717
Cdd:cd07841  67 LLDVFGHKSNINLVFEFME-TDLEKVIKD-----------KSIVLTpaDIKSYMLMTLRGLEYLHSNWILHRDLKPNNLL 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 718 VGKNYTIKIADFGMSRnlYSGDYYRIQGRAVLpIRWMSWESILLG--KFTTASDVWAFGVTLWE 779
Cdd:cd07841 135 IASDGVLKLADFGLAR--SFGSPNRKMTHQVV-TRWYRAPELLFGarHYGVGVDMWSVGCIFAE 195
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
564-783 2.87e-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: 103.77  E-value: 2.87e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLRA------DANKnarndfLKEIKIMSRLKD-PN 636
Cdd:cd07830   2 KVIKQLGDGTFGSVYL--------------ARNKETGE--LVAIKKMKKkfysweECMN------LREVKSLRKLNEhPN 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMEnGDLNQFLSRHEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd07830  60 IVKLKEVFRENDELYFVFEYME-GNLYQLMKDRKGKPFSESVIRSIIY--------QILQGLAHIHKHGFFHRDLKPENL 130
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSG----DYyriqgravLPIRWMSWESILL--GKFTTASDVWAFGVTLWETFTF 783
Cdd:cd07830 131 LVSGPEVVKIADFGLAREIRSRppytDY--------VSTRWYRAPEILLrsTSYSSPVDIWALGCIMAELYTL 195
F5_F8_type_C pfam00754
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
46-182 3.06e-24

F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.


Pssm-ID: 459925 [Multi-domain]  Cd Length: 127  Bit Score: 98.67  E-value: 3.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884    46 ITASSQWSESTAAKYgRLDSEEgDGAWCPEipvePDDLKEFLQIDLHTLHFITLVGTQGRHAGGHGieFAPMYKINYSRD 125
Cdd:pfam00754   2 ITASSSYSGEGPAAA-ALDGDP-NTAWSAW----SGDDPQWIQVDLGKPKKITGVVTQGRQDGSNG--YVTSYKIEYSLD 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884   126 GTRWISWRNRHGKqvldGNSNPYDIFLKDLEPPIVARFVRFIPVTDHS-MNVCMRVEL 182
Cdd:pfam00754  74 GENWTTVKDEKIP----GNNDNNTPVTNTFDPPIKARYVRIVPTSWNGgNGIALRAEL 127
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
569-845 3.22e-24

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: 102.87  E-value: 3.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevEGMEKFKDKDFALD----VSANQPVLVAVKMLRadanknarndflKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd06632   8 LGSGSFGSVY----EGFNGDTGDFFAVKevslVDDDKKSRESVKQLE------------QEIALLSKLRHPNIVQYYGTE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPpnssSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd06632  72 REEDNLYIFLEYVPGGSIHKLLQRYGA----FEEPVIRLYTR------QILSGLAYLHSRNTVHRDIKGANILVDTNGVV 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGDYYR-IQGRAVlpirWMSWESIL--LGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQV---I 798
Cdd:cd06632 142 KLADFGMAKHVEAFSFAKsFKGSPY----WMAPEVIMqkNSGYGLAVDIWSLGCTVLEMAT--GKPPWSQYEGVAAifkI 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 799 ENTGEFfrdqgrqtylpqPAIcPDSV----YKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06632 216 GNSGEL------------PPI-PDHLspdaKDFIRLCLQRDPEDRPTASQL 253
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
569-845 6.15e-24

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: 102.19  E-value: 6.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegMEKFKDkdfaldvsanqpvLVAVKMLRADANKNARND-FLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd14027   1 LDSGGFGKVSLC----FHRTQG-------------LVVLKTVYTGPNCIEHNEaLLEEGKMMNRLRHSRVVKLLGVILEE 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnlKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd14027  64 GKYSLVMEYMEKGNLMHVLKKVSVPLSVKG----------RII-LEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIA 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGM-SRNLYS---GDYYRIQGR-------AVLPIRWMSWESI--LLGKFTTASDVWAFGVTLWETFTfcQEQPYSQ-LS 793
Cdd:cd14027 133 DLGLaSFKMWSkltKEEHNEQREvdgtakkNAGTLYYMAPEHLndVNAKPTEKSDVYSFAIVLWAIFA--NKEPYENaIN 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 794 DEQVIentgeFFRDQGRQTYLPQ-PAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14027 211 EDQII-----MCIKSGNRPDVDDiTEYCPREIIDLMKLCWEANPEARPTFPGI 258
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
567-782 7.90e-24

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: 103.16  E-value: 7.90e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKfKDKDfaldvsanqpvLVAVKMLradANKNARNDF----LKEIKIMSRLKDPNIIHLLA 642
Cdd:cd07866  14 GKLGEGTFGEVY----KARQI-KTGR-----------VVALKKI---LMHNEKDGFpitaLREIKILKKLKHPNVVPLID 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCI------TDDPLC--MITEYMENgDLNQFLsrHEPpnssssDVRtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd07866  75 MAVerpdksKRKRGSvyMVTPYMDH-DLSGLL--ENP------SVK-LTESQIKCYMLQLLEGINYLHENHILHRDIKAA 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 715 NCLVGKNYTIKIADFGMSRNlYSGDYYRIQGR---------AVLPIRWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07866 145 NILIDNQGILKIADFGLARP-YDGPPPNPKGGggggtrkytNLVVTRWYRPPELLLGerRYTTAVDIWGIGCVFAEMFT 222
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
567-844 1.81e-23

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 100.44  E-value: 1.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekFKdkdfALDVSANQPVlVAVK-MLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14121   1 EKLGSGTYATV----------YK----AYRKSGAREV-VAVKcVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQW 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFL-SRHEPPNSsssdvrtvsyTNLKFMaTQIASGMKYLSSLNFVHRDLATRNCLV--GKNY 722
Cdd:cd14121  66 DEEHIYLIMEYCSGGDLSRFIrSRRTLPES----------TVRRFL-QQLASALQFLREHNISHMDLKPQNLLLssRYNP 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGDY-YRIQGRavlPIrWMSWESILLGKFTTASDVWAFGVTLWETFtFcQEQPYSQLSDEQVIENt 801
Cdd:cd14121 135 VLKLADFGFAQHLKPNDEaHSLRGS---PL-YMAPEMILKKKYDARVDLWSVGVILYECL-F-GRAPFASRSFEELEEK- 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 62420884 802 gefFRDQGRQTYLPQPAI---CPDsvykLMLSCWRRDTKNRPSFQE 844
Cdd:cd14121 208 ---IRSSKPIEIPTRPELsadCRD----LLLRLLQRDPDRRISFEE 246
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
604-849 3.15e-23

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


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 99.91  E-value: 3.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRADA--NKNARNDFLKEIKIMSRLKDPNIIHLLAVCItDDP--LCMITEYMENGDLnqFLSRHEppnssssDV 679
Cdd:cd14064  18 IVAIKRYRANTycSKSDVDMFCREVSILCRLNHPCVIQFVGACL-DDPsqFAIVTQYVSGGSL--FSLLHE-------QK 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 680 RTVSYTNLKFMATQIASGMKYLSSLN--FVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRavlP--IRWMS 755
Cdd:cd14064  88 RVIDLQSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTKQ---PgnLRWMA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 756 WESIL-LGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVienTGEFFRDQGRQtylPQPAICPDSVYKLMLSCWRR 834
Cdd:cd14064 165 PEVFTqCTRYSIKADVFSYALCLWELLT--GEIPFAHLKPAAA---AADMAYHHIRP---PIGYSIPKPISSLLMRGWNA 236
                       250
                ....*....|....*
gi 62420884 835 DTKNRPSFQEIHLLL 849
Cdd:cd14064 237 EPESRPSFVEIVALL 251
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
567-782 3.96e-23

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: 100.33  E-value: 3.96e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekFKdkdfALDVSANQpvLVAVKMLRADankNARNDF----LKEIKIMSRLKDPNIIHLLA 642
Cdd:cd07840   5 AQIGEGTYGQV----------YK----ARNKKTGE--LVALKKIRME---NEKEGFpitaIREIKLLQKLDHPNVVRLKE 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLC------MITEYMENgDLNQFLSRHEPPNSSSsdvrtvsytNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd07840  66 IVTSKGSAKykgsiyMVFEYMDH-DLTGLLDNPEVKFTES---------QIKCYMKQLLEGLQYLHSNGILHRDIKGSNI 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVlpIRWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07840 136 LINNDGVLKLADFGLARPYTKENNADYTNRVI--TLWYRPPELLLGatRYGPEVDMWSVGCILAELFT 201
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
567-847 4.41e-23

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: 99.88  E-value: 4.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKDFALDVSANQPVlvavkmlradaNKNARNDFLKEIKIMSRLKDPNIIHLLAVCit 646
Cdd:cd14025   2 EKVGSGGFGQVY----KVRHKHWKTWLAIKCPPSLHV-----------DDSERMELLEEAKKMEMAKFRHILPVYGIC-- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPPnssssdvrtvsyTNLKF-MATQIASGMKYLSSLN--FVHRDLATRNCLVGKNYT 723
Cdd:cd14025  65 SEPVGLVMEYMETGSLEKLLASEPLP------------WELRFrIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYH 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 IKIADFG-------MSRNLYSGDYYRIQGRAVLPIRWMSWESIllgkFTTASDVWAFGVTLWETFTfcQEQPYSQLSD-E 795
Cdd:cd14025 133 VKISDFGlakwnglSHSHDLSRDGLRGTIAYLPPERFKEKNRC----PDTKHDVYSFAIVIWGILT--QKKPFAGENNiL 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 796 QVIENTGeffrdQGRQTYLPQ-----PAICpDSVYKLMLSCWRRDTKNRPSFQEIHL 847
Cdd:cd14025 207 HIMVKVV-----KGHRPSLSPiprqrPSEC-QQMICLMKRCWDQDPRKRPTFQDITS 257
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
615-845 6.32e-23

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 99.13  E-value: 6.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 615 NKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRtvsytnlkfMATQI 694
Cdd:cd14156  28 NDVDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELLAREELPLSWREKVE---------LACDI 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 695 ASGMKYLSSLNFVHRDLATRNCLVGKNYTIK---IADFGMSRNLysGDYYRIQGRAVLPIR----WMSWESILLGKFTTA 767
Cdd:cd14156  99 SRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREV--GEMPANDPERKLSLVgsafWMAPEMLRGEPYDRK 176
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 768 SDVWAFGVTLWETFTFCQEQPysqlsdeQVIENTGEFFRD-QGRQTYLPQpaiCPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14156 177 VDVFSFGIVLCEILARIPADP-------EVLPRTGDFGLDvQAFKEMVPG---CPEPFLDLAASCCRMDAFKRPSFAEL 245
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
563-848 6.73e-23

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: 99.35  E-value: 6.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLcevegmekfkdkdfALDVsaNQPVLVAVKML------RADANKNARNDFLKEIKIMSRL-KDP 635
Cdd:cd13993   2 YQLISPIGEGAYGVVYL--------------AVDL--RTGRKYAIKCLyksgpnSKDGNDFQKLPQLREIDLHRRVsRHP 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd13993  66 NIITLHDVFETEVAIYIVLEYCPNGDLFEAITENRIYVGKTELIKNV--------FLQLIDAVKHCHSLGIYHRDIKPEN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNY-TIKIADFGMS-RNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWEtfTFCQEQPYSQLS 793
Cdd:cd13993 138 ILLSQDEgTVKLCDFGLAtTEKISMDFGVGSEFYMAPECFDEVGRSLKGYPCAAGDIWSLGIILLN--LTFGRNPWKIAS 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 794 DEQviENTGEFFRDqgRQTYLPQpaICPDS--VYKLMLSCWRRDTKNRPSFQEIHLL 848
Cdd:cd13993 216 ESD--PIFYDYYLN--SPNLFDV--ILPMSddFYNLLRQIFTVNPNNRILLPELQLL 266
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
569-849 1.09e-22

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: 98.23  E-value: 1.09e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMekfkdkdfaldvsanqpvlVAVKMLR-ADANKNARNDFLKEIKIMSRLKDPNIIhLLAVCITD 647
Cdd:cd14062   1 IGSGSFGTVYKGRWHGD-------------------VAVKKLNvTDPTPSQLQAFKNEVAVLRKTRHVNIL-LFMGYMTK 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd14062  61 PQLAIVTQWCEGSSLYKHLHVLE---------TKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIG 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMS--RNLYSGDYYRIQGRAvlPIRWMSWESILL---GKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDeqvientg 802
Cdd:cd14062 132 DFGLAtvKTRWSGSQQFEQPTG--SILWMAPEVIRMqdeNPYSFQSDVYAFGIVLYELLT--GQLPYSHINN-------- 199
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 803 effRDQ-----GRqTYLpQPAI------CPDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14062 200 ---RDQilfmvGR-GYL-RPDLskvrsdTPKALRRLMEDCIKFQRDERPLFPQILASL 252
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
567-782 1.26e-22

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: 98.09  E-value: 1.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKdfaldvsanqpvLVAVKMLradaNKNARND-----FLKEIKIMSRLKDPNIIHLL 641
Cdd:cd14002   7 ELIGEGSFGKVY----KGRRKYTGQ------------VVALKFI----PKRGKSEkelrnLRQEIEILRKLNHPNIIEML 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMEnGDLNQFLSrheppnssssDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14002  67 DSFETKKEFVVVTEYAQ-GELFQILE----------DDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKG 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 722 YTIKIADFGMSRNLYSGDYY--RIQGRavlPIrWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14002 136 GVVKLCDFGFARAMSCNTLVltSIKGT---PL-YMAPELVQEQPYDHTADLWSLGCILYELFV 194
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
569-779 2.34e-22

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: 97.20  E-value: 2.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegMEKFKDKDFALdvsanqpvlvavKMLRADA--NKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05123   1 LGKGSFGKVLLV----RKKDTGKLYAM------------KVLRKKEiiKRKEVEHTLNERNILERVNHPFIVKLHYAFQT 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05123  65 EEKLYLVLDYVPGGELFSHLSKE----------GRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKL 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 727 ADFGMSRNLYSG-----------DYyriqgravlpirwMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05123 135 TDFGLAKELSSDgdrtytfcgtpEY-------------LAPEVLLGKGYGKAVDWWSLGVLLYE 185
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
568-782 7.56e-22

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: 96.80  E-value: 7.56e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEVegmekfKDKDfaldvsanqpvlVAVKMLRA---DANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14158  22 KLGEGGFGVVFKGYI------NDKN------------VAVKKLAAmvdISTEDLTKQFEQEIQVMAKCQHENLVELLGYS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLS--RHEPPnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd14158  84 CDGPQLCLVYTYMPNGSLLDRLAclNDTPP---------LSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETF 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESiLLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14158 155 VPKISDFGLARASEKFSQTIMTERIVGTTAYMAPEA-LRGEITPKSDIFSFGVVLLEIIT 213
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
604-851 3.90e-21

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: 93.81  E-value: 3.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrtVS 683
Cdd:cd06623  28 IYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSLADLLKKVGK----------IP 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 684 YTNLKFMATQIASGMKYL-SSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRI--QGRAVlpirWMSWESIL 760
Cdd:cd06623  98 EPVLAYIARQILKGLDYLhTKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQCNtfVGTVT----YMSPERIQ 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 761 LGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIENTGEFfrdQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRP 840
Cdd:cd06623 174 GESYSYAADIWSLGLTLLECAL--GKFPFLPPGQPSFFELMQAI---CDGPPPSLPAEEFSPEFRDFISACLQKDPKKRP 248
                       250
                ....*....|.
gi 62420884 841 SFQEihllLLQ 851
Cdd:cd06623 249 SAAE----LLQ 255
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
569-845 7.32e-21

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: 93.16  E-value: 7.32e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfkdkdfaldVSANQPVLVAVKMLR-ADANKNARNDFLKEIKIMSRLKDPNIIHLLAvCITD 647
Cdd:cd14069   9 LGEGAFGEVFLA----------------VNRNTEEAVAVKFVDmKRAPGDCPENIKKEVCIQKMLSHKNVVRFYG-HRRE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLC-MITEYMENGDLnqfLSRHEPPNSSSSDVrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd14069  72 GEFQyLFLEYASGGEL---FDKIEPDVGMPEDV-------AQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYYRIQGRAVLPIRWMSWEsILLGKFTTAS--DVWAFGVTLWETFTfcqeqpySQLSDEQVIENTGEF 804
Cdd:cd14069 142 SDFGLATVFRYKGKERLLNKMCGTLPYVAPE-LLAKKKYRAEpvDVWSCGIVLFAMLA-------GELPWDQPSDSCQEY 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 805 --FRDQGRQTYLPQPAICPDsVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14069 214 sdWKENKKTYLTPWKKIDTA-ALSLLRKILTENPNKRITIEDI 255
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
565-789 9.75e-21

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: 93.05  E-value: 9.75e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVlvAVKML-RADANKNARNDFLK-EIKIMSRLKDPNIIHLLA 642
Cdd:cd05581   5 FGKPLGEGSYSTVVL--------------AKEKETGKEY--AIKVLdKRHIIKEKKVKYVTiEKEVLSRLAHPGIVKLYY 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05581  69 TFQDESKLYFVLEYAPNGDLLEYIRKY----------GSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDM 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGmSRNLYSGDYYRIQGRAVL--PIRWM--------------SWESILLGKFTTASDVWAFGVTLWETFT---- 782
Cdd:cd05581 139 HIKITDFG-TAKVLGPDSSPESTKGDAdsQIAYNqaraasfvgtaeyvSPELLNEKPAGKSSDLWALGCIIYQMLTgkpp 217

                ....*..
gi 62420884 783 FCQEQPY 789
Cdd:cd05581 218 FRGSNEY 224
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
565-739 1.09e-20

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: 92.45  E-value: 1.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLceveGMEKFKDKdfaldvsanqpvLVAVKMLRADANKNA--RNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd14073   5 LLETLGKGTYGKVKL----AIERATGR------------EVAIKSIKKDKIEDEqdMVRIRREIEIMSSLNHPHIIRIYE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLS-RHEPPnssSSDVRTVsytnlkFmaTQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14073  69 VFENKDKIVIVMEYASGGELYDYISeRRRLP---EREARRI------F--RQIVSAVHYCHKNGVVHRDLKLENILLDQN 137
                       170
                ....*....|....*...
gi 62420884 722 YTIKIADFGMSrNLYSGD 739
Cdd:cd14073 138 GNAKIADFGLS-NLYSKD 154
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
566-845 1.90e-20

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: 91.70  E-value: 1.90e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHlcevegmeKFKDKDfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd08529   5 LNKLGKGSFGVVY--------KVVRKV-------DGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPpnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd08529  70 DKGKLNIVMEYAENGDLHSLIKSQRG--------RPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNLysGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcqEQPYSqlsdeqvIENTGEFF 805
Cdd:cd08529 142 IGDLGVAKIL--SDTTNFAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTG--KHPFE-------AQNQGALI 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 62420884 806 RDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd08529 211 LKIVRGKYPPISASYSQDLSQLIDSCLTKDYRQRPDTTEL 250
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
557-845 2.16e-20

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: 92.05  E-value: 2.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLTFKEKLGEGQFGEVHLCEVEGMekfkdkdfaldvsanqpvlVAVKMLRADA-NKNARNDFLKEIKIMSRLKDP 635
Cdd:cd14151   4 EIPDGQITVGQRIGSGSFGTVYKGKWHGD-------------------VAVKMLNVTApTPQQLQAFKNEVGVLRKTRHV 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCiTDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd14151  65 NILLFMGYS-TKPQLAIVTQWCEGSSLYHHLHIIET---------KFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNN 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMS--RNLYSGDYYRIQGRAvlPIRWMSWESILL---GKFTTASDVWAFGVTLWETFTfcQEQPYS 790
Cdd:cd14151 135 IFLHEDLTVKIGDFGLAtvKSRWSGSHQFEQLSG--SILWMAPEVIRMqdkNPYSFQSDVYAFGIVLYELMT--GQLPYS 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 791 QLSD-EQVIENTGEFFRDQGRQTYLPQpaiCPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14151 211 NINNrDQIIFMVGRGYLSPDLSKVRSN---CPKAMKRLMAECLKKKRDERPLFPQI 263
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
569-845 2.42e-20

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: 91.64  E-value: 2.42e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdfaldvsanqpvlVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd06605   9 LGEGNGGVVSKVRHRPSGQI----------------MAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRheppnssssdVRTVSYTNLKFMATQIASGMKYL-SSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd06605  73 DISICMEYMDGGSLDKILKE----------VGRIPERILGKIAVAVVKGLIYLhEKHKIIHRDVKPSNILVNSRGQVKLC 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMSRNL-------YSGDYYriqgravlpirWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQlsdEQVIEN 800
Cdd:cd06605 143 DFGVSGQLvdslaktFVGTRS-----------YMAPERISGGKYTVKSDIWSLGLSLVELAT--GRFPYPP---PNAKPS 206
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 801 TGEFfrDQGRQTYLPQPAICPDSVYKLMLS-----CWRRDTKNRPSFQEI 845
Cdd:cd06605 207 MMIF--ELLSYIVDEPPPLLPSGKFSPDFQdfvsqCLQKDPTERPSYKEL 254
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
569-845 2.56e-20

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: 91.60  E-value: 2.56e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfKDKDFAldvsanQPVLVAVKMLRADANKNARNDF----LKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd13994   1 IGKGATSVVRIV--------TKKNPR------SGVLYAVKEYRRRDDESKRKDYvkrlTSEYIISSKLHHPNIVKVLDLC 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDP-LCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd13994  67 QDLHGkWCLVMEYCPGGDLFTLIEKA----------DSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 IKIADFGMSRNL-YSGDYY-RIQGRAVLPIRWMSWESILLGKFT-TASDVWAFGVTLWEtfTFCQEQPYSQLSDEqviEN 800
Cdd:cd13994 137 LKLTDFGTAEVFgMPAEKEsPMSAGLCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFA--LFTGRFPWRSAKKS---DS 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 62420884 801 TGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWR---RDTKNRPSFQEI 845
Cdd:cd13994 212 AYKAYEKSGDFTNGPYEPIENLLPSECRRLIYRmlhPDPEKRITIDEA 259
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
563-851 3.70e-20

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: 91.26  E-value: 3.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGMekfkdkdfaldvsanqpvlVAVKMLRADA-NKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd14063   2 LEIKEVIGKGRFGRVHRGRWHGD-------------------VAIKLLNIDYlNEEQLEAFKEEVAAYKNTRHDNLVLFM 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLsrHEPPNssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14063  63 GACMDPPHLAIVTSLCKGRTLYSLI--HERKE-------KFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENG 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIkIADFGMSRNLYSGDYYRIQGRAVLPIRWMS-------------WESILLGKFTTASDVWAFGVTLWEtfTFCQEQP 788
Cdd:cd14063 134 RVV-ITDFGLFSLSGLLQPGRREDTLVIPNGWLCylapeiiralspdLDFEESLPFTKASDVYAFGTVWYE--LLAGRWP 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 789 YSQLSDEQVIENTGeffrdQGRQTYLPQPAIcPDSVYKLMLSCWRRDTKNRPSFQEIHLLLLQ 851
Cdd:cd14063 211 FKEQPAESIIWQVG-----CGKKQSLSQLDI-GREVKDILMQCWAYDPEKRPTFSDLLRMLER 267
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
568-845 3.70e-20

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: 90.95  E-value: 3.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEvegmEKFKDKDFALDVSANQPVlvavkmlrADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd08222   7 KLGSGNFGTVYLVS----DLKATADEELKVLKEISV--------GELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYtnlkFMatQIASGMKYLSSLNFVHRDLATRNCLVgKNYTIKIA 727
Cdd:cd08222  75 ESFCIVTEYCEGGDLDDKISEYKKSGTTIDENQILDW----FI--QLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMSRNL---------YSGDYYriqgravlpirWMSWESILLGKFTTASDVWAFGVTLWETFTFCQE-QPYSQLS-DEQ 796
Cdd:cd08222 148 DFGISRILmgtsdlattFTGTPY-----------YMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAfDGQNLLSvMYK 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 797 VIEntGEffrdqgrqtyLPQ-PAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd08222 217 IVE--GE----------TPSlPDKYSKELNAIYSRMLNKDPALRPSAAEI 254
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
564-782 6.18e-20

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: 91.82  E-value: 6.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVhlCEvegmekfkdkdfALDVSANQPVlvAVKMLRA------DAnKNArndfLKEIKIMSRLKDPNI 637
Cdd:cd07834   3 ELLKPIGSGAYGVV--CS------------AYDKRTGRKV--AIKKISNvfddliDA-KRI----LREIKILRHLKHENI 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCM-----ITEYMENgDLNQFLSRHEPpnSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLA 712
Cdd:cd07834  62 IGLLDILRPPSPEEFndvyiVTELMET-DLHKVIKSPQP--LTDDHIQYFLY--------QILRGLKYLHSAGVIHRDLK 130
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 713 TRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLpIRWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07834 131 PSNILVNSNCDLKICDFGLARGVDPDEDKGFLTEYVV-TRWYRAPELLLSskKYTKAIDIWSVGCIFAELLT 201
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
569-845 6.60e-20

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: 90.11  E-value: 6.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmekfkDKDFALDVsanqpvlvAVKMLRADA-NKNARND---FLKEIKIMSRLKDPNIIHLLAvC 644
Cdd:cd06625   8 LGQGAFGQVYLCY--------DADTGREL--------AVKQVEIDPiNTEASKEvkaLECEIQLLKNLQHERIVQYYG-C 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDD-PLCMITEYMENGDLNQFLSRHeppnSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd06625  71 LQDEkSLSIFMEYMPGGSVKDEIKAY----GALTENVTRKYTR------QILEGLAYLHSNMIVHRDIKGANILRDSNGN 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 IKIADFGMSRnlysgdyyRIQ-------GRAVL--PiRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLsd 794
Cdd:cd06625 141 VKLGDFGASK--------RLQticsstgMKSVTgtP-YWMSPEVINGEGYGRKADIWSVGCTVVEMLT--TKPPWAEF-- 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 795 eqviENTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06625 208 ----EPMAAIFKIATQPTNPQLPPHVSEDARDFLSLIFVRNKKQRPSAEEL 254
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
572-800 8.15e-20

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: 90.35  E-value: 8.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 572 GQFGEVHLCEvegmeKFKDKDfaldvsanqpvLVAVKMLRAD--ANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDP 649
Cdd:cd05579   4 GAYGRVYLAK-----KKSTGD-----------LYAIKVIKKRdmIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQGKKN 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 650 LCMITEYMENGDLNQFLSrheppNSSSSDVRTVsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADF 729
Cdd:cd05579  68 LYLVMEYLPGGDLYSLLE-----NVGALDEDVA-----RIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDF 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 730 GMSR---NLYSGDYYRIQGRAVLPIR----------WMSWESILLGKFTTASDVWAFGVTLWETFT----FCQEQPysql 792
Cdd:cd05579 138 GLSKvglVRRQIKLSIQKKSNGAPEKedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVgippFHAETP---- 213

                ....*...
gi 62420884 793 sdEQVIEN 800
Cdd:cd05579 214 --EEIFQN 219
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
567-782 8.89e-20

Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 90.45  E-value: 8.89e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegmekfKDKDfaldvsanQPVLVAVK-MLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd07833   7 GVVGEGAYGVVLKC--------RNKA--------TGEIVAIKkFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENgDLNQFLSRHepPNSSSSD-VRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd07833  71 RKGRLYLVFEYVER-TLLELLEAS--PGGLPPDaVRSYIW--------QLLQAIAYCHSHNIIHRDIKPENILVSESGVL 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 725 KIADFGMSRNLYSG------DYyriqgravLPIRWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07833 140 KLCDFGFARALTARpaspltDY--------VATRWYRAPELLVGdtNYGKPVDVWAIGCIMAELLD 197
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
565-841 2.17e-19

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: 88.98  E-value: 2.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCEVEGmekfkdkdfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAV- 643
Cdd:cd13979   7 LQEPLGSGGFGSVYKATYKG------------------ETVAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVLAAe 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 -CITDDPLCMIT-EYMENGDLNQFLSRHEPPNSSSSDVRtvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd13979  69 tGTDFASLGLIImEYCGNGTLQQLIYEGSEPLPLAHRIL---------ISLDIARALRFCHSHGIVHLDVKPANILISEQ 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFGMSRNLYSGD-----YYRIQGravlPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSqlSDEQ 796
Cdd:cd13979 140 GVCKLCDFGCSVKLGEGNevgtpRSHIGG----TYTYRAPELLKGERVTPKADIYSFGITLWQMLT--RELPYA--GLRQ 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 797 VI-----------ENTGEFFRDQGrQTYlpqpaicpDSVYKlmlSCWRRDTKNRPS 841
Cdd:cd13979 212 HVlyavvakdlrpDLSGLEDSEFG-QRL--------RSLIS---RCWSAQPAERPN 255
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
623-845 3.81e-19

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: 88.22  E-value: 3.81e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 623 LKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSssdvrtvsytNLKF-MATQIASGMKYL 701
Cdd:cd13992  44 LQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNREIKMDW----------MFKSsFIKDIVKGMNYL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 702 -SSLNFVHRDLATRNCLVGKNYTIKIADFGMsRNLYSGDYYRIQGRAVLPIR--WMSWE----SILLGKFTTASDVWAFG 774
Cdd:cd13992 114 hSSSIGYHGRLKSSNCLVDSRWVVKLTDFGL-RNLLEEQTNHQLDEDAQHKKllWTAPEllrgSLLEVRGTQKGDVYSFA 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 775 VTLWEtfTFCQEQPYSQLSDEQVIENTgeffRDQGRQTYLPQPAI----CPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd13992 193 IILYE--ILFRSDPFALEREVAIVEKV----ISGGNKPFRPELAVlldeFPPRLVLLVKQCWAENPEKRPSFKQI 261
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
565-778 3.92e-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: 88.09  E-value: 3.92e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVhlcevegmEKFKDKdfaldvsanQPVLVAVKMLRADANKNARN--DFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd14161   7 FLETLGKGTYGRV--------KKARDS---------SGRLVAIKSIRKDRIKDEQDllHIRREIEIMSSLNHPHIISVYE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd14161  70 VFENSSKIVIVMEYASRGDLYDYISERQR----------LSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANG 139
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 723 TIKIADFGMSrNLYSGDYYrIQGRAVLPIrWMSWEsILLGKFTTASDV--WAFGVTLW 778
Cdd:cd14161 140 NIKIADFGLS-NLYNQDKF-LQTYCGSPL-YASPE-IVNGRPYIGPEVdsWSLGVLLY 193
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
569-776 4.16e-19

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: 87.71  E-value: 4.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFAldvsanqpvlvaVKMLRADANKnaRNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd14006   1 LGRGRFGVVKRCI----EKATGREFA------------AKFIPKRDKK--KEAVLREISILNQLQHPRIIQLHEAYESPT 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEppNSSSSDVRTvsytnlkFMaTQIASGMKYLSSLNFVHRDLATRNCLV--GKNYTIKI 726
Cdd:cd14006  63 ELVLILELCSGGELLDRLAERG--SLSEEEVRT-------YM-RQLLEGLQYLHNHHILHLDLKPENILLadRPSPQIKI 132
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 727 ADFGMSRNLYSGDYYR-IQGRAvlpiRWMSWESILLGKFTTASDVWAFGVT 776
Cdd:cd14006 133 IDFGLARKLNPGEELKeIFGTP----EFVAPEIVNGEPVSLATDMWSIGVL 179
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
569-841 5.66e-19

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: 88.05  E-value: 5.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEG----MEKFKDKDFAldVSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14000   2 LGDGGFGSVYRASYKGepvaVKIFNKHTSS--NFANVPADTMLRHLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ItdDPLCMITEYMENGDLNQFLSrhEPPNSSSSDVRTVSYTnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT- 723
Cdd:cd14000  80 I--HPLMLVLELAPLGSLDHLLQ--QDSRSFASLGRTLQQR----IALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPn 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 ----IKIADFGMSRNLYSGDYYRIQG----RAVLPIRWMSwesillgKFTTASDVWAFGVTLWETFTFcqEQPYSQLSDE 795
Cdd:cd14000 152 saiiIKIADYGISRQCCRMGAKGSEGtpgfRAPEIARGNV-------IYNEKVDVFSFGMLLYEILSG--GAPMVGHLKF 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 62420884 796 QVIENTGEFFRDQGRQTYLPQPAICPDsvykLMLSCWRRDTKNRPS 841
Cdd:cd14000 223 PNEFDIHGGLRPPLKQYECAPWPEVEV----LMKKCWKENPQQRPT 264
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
598-778 6.40e-19

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: 87.35  E-value: 6.40e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 598 SANQPVLVAVKMLradANKNARNDFL-----KEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHepp 672
Cdd:cd14162  21 STKHKCKVAIKIV---SKKKAPEDYLqkflpREIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDLLDYIRKN--- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 673 nSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDyyriQGRAVL--- 749
Cdd:cd14162  95 -GALPEPQARRWFR------QLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARGVMKTK----DGKPKLset 163
                       170       180       190
                ....*....|....*....|....*....|....
gi 62420884 750 ---PIRWMSWEsILLGKF--TTASDVWAFGVTLW 778
Cdd:cd14162 164 ycgSYAYASPE-ILRGIPydPFLSDIWSMGVVLY 196
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
559-846 6.53e-19

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: 87.88  E-value: 6.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEkLGEGQFGEVHLCEVEGMEKFkdkdfaldvsanqpvlVAVKMLRADANKNARNDFLKEIKIMSRLKDPNII 638
Cdd:cd06620   4 NQDLETLKD-LGAGNGGSVSKVLHIPTGTI----------------MAKKVIHIDAKSSVRKQILRELQILHECHSPYIV 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDP-LCMITEYMENGDLNQFLSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYL-SSLNFVHRDLATRNC 716
Cdd:cd06620  67 SFYGAFLNENNnIIICMEYMDCGSLDKILKKKGP----------FPEEVLGKIAVAVLEGLTYLyNVHRIIHRDIKPSNI 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVlpirWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQ 796
Cdd:cd06620 137 LVNSKGQIKLCDFGVSGELINSIADTFVGTST----YMSPERIQGGKYSVKSDVWSLGLSIIELAL--GEFPFAGSNDDD 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 797 VIENTGEFFRDQGRQTY------LPQPAICPDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd06620 211 DGYNGPMGILDLLQRIVneppprLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLLL 266
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
567-782 9.56e-19

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: 87.56  E-value: 9.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevegmeKFKDKDFAldvsanqpVLVAVKMLRADAN-KNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd07860   6 EKIGEGTYGVVY--------KARNKLTG--------EVVALKKIRLDTEtEGVPSTAIREISLLKELNHPNIVKLLDVIH 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMeNGDLNQFLSRHEPPNSSSSDVRtvSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd07860  70 TENKLYLVFEFL-HQDLKKFMDASALTGIPLPLIK--SYLF------QLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIK 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 726 IADFGMSRNLysGDYYRIQGRAVLPIrWMSWESILLGK--FTTASDVWAFGVTLWETFT 782
Cdd:cd07860 141 LADFGLARAF--GVPVRTYTHEVVTL-WYRAPEILLGCkyYSTAVDIWSLGCIFAEMVT 196
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
563-774 2.82e-18

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: 86.02  E-value: 2.82e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKmlRADANKNARNdflKEIKIMSRLKDPNIIHLLA 642
Cdd:cd14137   6 YTIEKVIGSGSFGVVYQAKLLETGE----------------VVAIK--KVLQDKRYKN---RELQIMRRLKHPNIVKLKY 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDP------LCMITEYMENgDLNQFL-----SRHEPPNSsssDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDL 711
Cdd:cd14137  65 FFYSSGEkkdevyLNLVMEYMPE-TLYRVIrhyskNKQTIPII---YVKLYSY--------QLFRGLAYLHSLGICHRDI 132
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 712 ATRNCLV-GKNYTIKIADFGMSRNLYSGD---------YYriqgRAvlPirwmswESIlLG--KFTTASDVWAFG 774
Cdd:cd14137 133 KPQNLLVdPETGVLKLCDFGSAKRLVPGEpnvsyicsrYY----RA--P------ELI-FGatDYTTAIDIWSAG 194
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
567-782 3.14e-18

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: 86.00  E-value: 3.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekFKDKdfaldvSANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd07836   6 EKLGEGTYATV----------YKGR------NRTTGEIVALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENgDLNQFLSRHEppNSSSSDVRTVSYtnlkFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd07836  70 ENKLMLVFEYMDK-DLKKYMDTHG--VRGALDPNTVKS----FT-YQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 727 ADFGMSR------NLYSGDYYRIqgravlpirWMSWESILLGK--FTTASDVWAFGVTLWETFT 782
Cdd:cd07836 142 ADFGLARafgipvNTFSNEVVTL---------WYRAPDVLLGSrtYSTSIDIWSVGCIMAEMIT 196
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
569-845 4.05e-18

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: 85.56  E-value: 4.05e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfkdkdfaldVSANQPVLVAVKMLRADANKNArNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd06611  13 LGDGAFGKVYKA----------------QHKETGLFAAAKIIQIESEEEL-EDFMVEIDILSECKHPNIVGLYEAYFYEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEPPnSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd06611  76 KLWILIEFCDGGALDSIMLELERG-LTEPQIRYVCR--------QMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLAD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 729 FGMSRNLYSgdyyRIQGRAVL---PiRWMSWESILLGKFTTA-----SDVWAFGVTLWEtftFCQ-EQPYSQLSDEQVIe 799
Cdd:cd06611 147 FGVSAKNKS----TLQKRDTFigtP-YWMAPEVVACETFKDNpydykADIWSLGITLIE---LAQmEPPHHELNPMRVL- 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 62420884 800 ntgeFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06611 218 ----LKILKSEPPTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAEL 259
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
561-792 4.33e-18

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: 85.37  E-value: 4.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 561 KLLTFKEKLGEGQFGEVhlcevegmekFKdkdfALDVSANQPVlvAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHL 640
Cdd:cd06609   1 ELFTLLERIGKGSFGEV----------YK----GIDKRTNQVV--AIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKY 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 LAVCITDDPLCMITEYMENGDLNQFLsrheppNSSSSDVRTVSytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd06609  65 YGSFLKGSKLWIIMEYCGGGSVLDLL------KPGPLDETYIA-----FILREVLLGLEYLHSEGKIHRDIKAANILLSE 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 NYTIKIADFGMS---------RNLYSGDYYriqgravlpirWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQ 791
Cdd:cd06609 134 EGDVKLADFGVSgqltstmskRNTFVGTPF-----------WMAPEVIKQSGYDEKADIWSLGITAIELAK--GEPPLSD 200

                .
gi 62420884 792 L 792
Cdd:cd06609 201 L 201
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
561-799 5.51e-18

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: 84.91  E-value: 5.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 561 KLLTFKEKLGEGQFGEVhlceVEGMEKFKDKDFAL-DVSANQPVLVAVKMLRadanknarndflKEIKIMSRLKDPNIIH 639
Cdd:cd14097   1 KIYTFGRKLGQGSFGVV----IEATHKETQTKWAIkKINREKAGSSAVKLLE------------REVDILKHVNHAHIIH 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLSRHEppNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLVG 719
Cdd:cd14097  65 LEEVFETPKRMYLVMELCEDGELKELLLRKG--FFSENETRHI--------IQSLASAVAYLHKNDIVHRDLKLENILVK 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 720 KN-------YTIKIADFGMSRNLYSGDYYRIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLWetFTFCQEQPYSQL 792
Cdd:cd14097 135 SSiidnndkLNIKVTDFGLSVQKYGLGEDMLQETCGTPI-YMAPEVISAHGYSQQCDIWSIGVIMY--MLLCGEPPFVAK 211

                ....*..
gi 62420884 793 SDEQVIE 799
Cdd:cd14097 212 SEEKLFE 218
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
565-845 6.19e-18

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: 84.37  E-value: 6.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKE--KLGEGQFGEVHLCEVEGMEKFkdkdFALDVsANQPVLvavkmlradaNKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd08530   2 FKVlkKLGKGSYGSVYKVKRLSDNQV----YALKE-VNLGSL----------SQKEREDSVNEIRLLASVNHPNIIRYKE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRheppnssSSDVRTVSYTNLKF-MATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd08530  67 AFLDGNRLCIVMEYAPFGDLSKLISK-------RKKKRRLFPEDDIWrIFIQMLRGLKALHDQKILHRDLKSANILLSAG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFGMSRNLYSGDYYRIQGRavlPIrWMSWESILLGKFTTASDVWAFGVTLWETFTFcqEQPYSQlsdeqviENT 801
Cdd:cd08530 140 DLVKIGDLGISKVLKKNLAKTQIGT---PL-YAAPEVWKGRPYDYKSDIWSLGCLLYEMATF--RPPFEA-------RTM 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 62420884 802 GEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd08530 207 QELRYKVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKL 250
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
556-845 6.60e-18

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: 84.75  E-value: 6.60e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 556 EEFPRKLLTFKeKLGEGQFGEVHLceveGMEKFKDKDFALDVSANQpvlvAVKMLRADANKNARNdFLKEIKIMSRLKDP 635
Cdd:cd14084   2 KELRKKYIMSR-TLGSGACGEVKL----AYDKSTCKKVAIKIINKR----KFTIGSRREINKPRN-IETEIEILKKLSHP 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQflsrheppnssssdvRTVSYTNL-----KFMATQIASGMKYLSSLNFVHRD 710
Cdd:cd14084  72 CIIKIEDFFDAEDDYYIVLELMEGGELFD---------------RVVSNKRLkeaicKLYFYQMLLAVKYLHSNGIIHRD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 711 LATRNCLVGKN--YT-IKIADFGMSRNLysGDYYRIQGRAVLPIrWMSWESILLG---KFTTASDVWAFGVTLWetFTFC 784
Cdd:cd14084 137 LKPENVLLSSQeeEClIKITDFGLSKIL--GETSLMKTLCGTPT-YLAPEVLRSFgteGYTRAVDCWSLGVILF--ICLS 211
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 785 QEQPYSQlsdeqviENTGEFFRDQ---GRQTYLPQ-------PAIcpdSVYKLMLSCwrrDTKNRPSFQEI 845
Cdd:cd14084 212 GYPPFSE-------EYTQMSLKEQilsGKYTFIPKawknvseEAK---DLVKKMLVV---DPSRRPSIEEA 269
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
605-844 6.84e-18

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


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 84.34  E-value: 6.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLrADANKNARNDFL-KEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVS 683
Cdd:cd14120  22 VAIKCI-TKKNLSKSQNLLgKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLADYLQAK----------GTLS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 684 YTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY---------TIKIADFGMSRNLYSGDYyriqgRAVL---PI 751
Cdd:cd14120  91 EDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFARFLQDGMM-----AATLcgsPM 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 752 rWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYsQLSDEQVIENtgefFRDQGRQTYLPQPAICPDSVYKLMLSC 831
Cdd:cd14120 166 -YMAPEVIMSLQYDAKADLWSIGTIVYQCLT--GKAPF-QAQTPQELKA----FYEKNANLRPNIPSGTSPALKDLLLGL 237
                       250
                ....*....|...
gi 62420884 832 WRRDTKNRPSFQE 844
Cdd:cd14120 238 LKRNPKDRIDFED 250
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
605-739 7.20e-18

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: 83.98  E-value: 7.20e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKML---RADANkNARNDFlKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEppNSSSSDVRT 681
Cdd:cd14071  28 VAIKIIdksQLDEE-NLKKIY-REVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIFDYLAQHG--RMSEKEARK 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 682 vsytnlKFMatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSrNLYSGD 739
Cdd:cd14071 104 ------KFW--QILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFS-NFFKPG 152
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
568-841 7.40e-18

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: 84.28  E-value: 7.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCevegmekfkdkdfaldVSANQPVLVAVKMLR-ADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd06626   7 KIGEGTFGKVYTA----------------VNLDTGELMAMKEIRfQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFL--SRHEPpnssssDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd06626  71 REEVYIFMEYCQEGTLEELLrhGRILD------EAVIRVYTL------QLLEGLAYLHENGIVHRDIKPANIFLDSNGLI 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSG----DYYRIQGRAVLPIrWMSWESILLGKFT---TASDVWAFGVTLWETFTfcQEQPYSQLSDE-Q 796
Cdd:cd06626 139 KLGDFGSAVKLKNNtttmAPGEVNSLVGTPA-YMAPEVITGNKGEghgRAADIWSLGCVVLEMAT--GKRPWSELDNEwA 215
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62420884 797 VIENTGeffrdQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPS 841
Cdd:cd06626 216 IMYHVG-----MGHKPPIPDSLQLSPEGKDFLSRCLESDPKKRPT 255
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
567-845 9.00e-18

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 84.22  E-value: 9.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKDFALDVSANQPVLVAVKMLRAdANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05077   5 EHLGRGTRTQIY----AGILNYKDDDEDEGYSYEKEIKVILKVLDP-SHRDISLAFFETASMMRQVSHKHIVLLYGVCVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRheppnssSSDVRTVSYtnlKF-MATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT-- 723
Cdd:cd05077  80 DVENIMVEEFVEFGPLDLFMHR-------KSDVLTTPW---KFkVAKQLASALSYLEDKDLVHGNVCTKNILLAREGIdg 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 -----IKIADFGMSRNLYSgdyyriQGRAVLPIRWMSWESILLGK-FTTASDVWAFGVTLWEtFTFCQEQPysqLSDEQV 797
Cdd:cd05077 150 ecgpfIKLSDPGIPITVLS------RQECVERIPWIAPECVEDSKnLSIAADKWSFGTTLWE-ICYNGEIP---LKDKTL 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 62420884 798 IENTgeffRDQGRQTYLPQPAiCpDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05077 220 AEKE----RFYEGQCMLVTPS-C-KELADLMTHCMNYDPNQRPFFRAI 261
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
568-846 9.87e-18

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: 83.86  E-value: 9.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHL--CEVEGmekfkdkdfaldvsanqpVLVAVKMLRAD--ANKNARNDFLKEIKIMSRLKDPNIIHLLAV 643
Cdd:cd08224   7 KIGKGQFSVVYRarCLLDG------------------RLVALKKVQIFemMDAKARQDCLKEIDLLQQLNHPNIIKYLAS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLsRHEPPNSSSSDVRTV-SYtnlkFMatQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd08224  69 FIENNELNIVLELADAGDLSRLI-KHFKKQKRLIPERTIwKY----FV--QLCSALEHMHSKRIMHRDIKPANVFITANG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGD----------YYriqgravlpirwMSWESILLGKFTTASDVWAFGVTLWETFT----FCQEQp 788
Cdd:cd08224 142 VVKLGDLGLGRFFSSKTtaahslvgtpYY------------MSPERIREQGYDFKSDIWSLGCLLYEMAAlqspFYGEK- 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 789 YSQLSDEQVIENtGEffrdqgrqtYLPQPAIC-PDSVYKLMLSCWRRDTKNRPSFQEIH 846
Cdd:cd08224 209 MNLYSLCKKIEK-CE---------YPPLPADLySQELRDLVAACIQPDPEKRPDISYVL 257
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
567-826 1.04e-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: 84.68  E-value: 1.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlceVEGMEKFKDKdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd07871  11 DKLGEGTYATV----FKGRSKLTEN------------LVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENgDLNQFLSrheppNSSSsdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd07871  75 ERCLTLVFEYLDS-DLKQYLD-----NCGN----LMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSR------NLYSGDYYRIqgravlpirWMSWESILLG--KFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVI 798
Cdd:cd07871 145 ADFGLARaksvptKTYSNEVVTL---------WYRPPDVLLGstEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHL 215
                       250       260
                ....*....|....*....|....*...
gi 62420884 799 entgeFFRDQGRQTYLPQPAICPDSVYK 826
Cdd:cd07871 216 -----IFRLLGTPTEETWPGVTSNEEFR 238
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
557-844 1.04e-17

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: 83.91  E-value: 1.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 557 EFPRKLLtfkekLGEGQFGEVhlceVEGMEKFKdkdfaldvsanQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPN 636
Cdd:cd14202   3 EFSRKDL-----IGHGAFAVV----FKGRHKEK-----------HDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHEN 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSrheppnssssDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNC 716
Cdd:cd14202  63 IVALYDFQEIANSVYLVMEYCNGGDLADYLH----------TMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNI 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVG---------KNYTIKIADFGMSRNLYSGdyyriQGRAVL---PIrWMSWESILLGKFTTASDVWAFGVTLWETFTfc 784
Cdd:cd14202 133 LLSysggrksnpNNIRIKIADFGFARYLQNN-----MMAATLcgsPM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-- 204
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 785 QEQPYsQLSDEQVIENTGEffRDQGRQTYLPQPAICPdsVYKLMLSCWRRDTKNRPSFQE 844
Cdd:cd14202 205 GKAPF-QASSPQDLRLFYE--KNKSLSPNIPRETSSH--LRQLLLGLLQRNQKDRMDFDE 259
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
559-792 1.33e-17

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: 83.47  E-value: 1.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVhlcevegmekFKdkdfALDVSANQPVlvAVKMLRadaNKNARNDFLKEIKIMSRLKDPNII 638
Cdd:cd06612   1 PEEVFDILEKLGEGSYGSV----------YK----AIHKETGQVV--AIKVVP---VEEDLQEIIKEISILKQCDSPYIV 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENG---DLNQFLSRheppNSSSSDVRTVSYTNLKfmatqiasGMKYLSSLNFVHRDLATRN 715
Cdd:cd06612  62 KYYGSYFKNTDLWIVMEYCGAGsvsDIMKITNK----TLTEEEIAAILYQTLK--------GLEYLHSNKKIHRDIKAGN 129
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 716 CLVGKNYTIKIADFGMSRNLysGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcqEQPYSQL 792
Cdd:cd06612 130 ILLNEEGQAKLADFGVSGQL--TDTMAKRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEG--KPPYSDI 202
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
565-790 1.36e-17

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: 83.43  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVH--LCEVEGMEkfkdkdfaldVSANQPVLvavkmlrADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd13983   5 FNEVLGRGSFKTVYraFDTEEGIE----------VAWNEIKL-------RKLPKAERQRFKQEIEILKSLKHPNIIKFYD 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCM--ITEYMENGDLNQFLSRHEPPNSSssdvrtvsytNLKFMATQIASGMKYLSSLN--FVHRDLATRNCLV 718
Cdd:cd13983  68 SWESKSKKEVifITELMTSGTLKQYLKRFKRLKLK----------VIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFI 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 719 -GKNYTIKIADFGMSRNLYSGDYYRIQGRavlPiRWMSWEsILLGKFTTASDVWAFGVTLWETFTFcqEQPYS 790
Cdd:cd13983 138 nGNTGEVKIGDLGLATLLRQSFAKSVIGT---P-EFMAPE-MYEEHYDEKVDIYAFGMCLLEMATG--EYPYS 203
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
569-774 1.58e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 84.81  E-value: 1.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  569 LGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLRADANKNARNDF-------------LKEIKIMSRLKDP 635
Cdd:PTZ00024  17 LGEGTYGKVEK--------------AYDTLTGK--IVAIKKVKIIEISNDVTKDrqlvgmcgihfttLRELKIMNEIKHE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  636 NIIHLLAVCITDDPLCMITEYMEnGDLNQFLSRHeppnssssdVRtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:PTZ00024  81 NIMGLVDVYVEGDFINLVMDIMA-SDLKKVVDRK---------IR-LTESQVKCILLQILNGLNVLHKWYFMHRDLSPAN 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884  716 CLVGKNYTIKIADFGMSR----NLYSGDYYRIQGRA--------VLPIrWMSWESILLG--KFTTASDVWAFG 774
Cdd:PTZ00024 150 IFINSKGICKIADFGLARrygyPPYSDTLSKDETMQrreemtskVVTL-WYRAPELLMGaeKYHFAVDMWSVG 221
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
568-845 1.81e-17

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: 83.54  E-value: 1.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEVEGMekfkdkdfaldvsanqpvlVAVKMLR-ADANKNARNDFLKEIKIMSRLKDPNIIHLLAVcIT 646
Cdd:cd14149  19 RIGSGSFGTVYKGKWHGD-------------------VAVKILKvVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGY-MT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPpnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd14149  79 KDNLAIVTQWCEGSSLYKHLHVQET---------KFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMS--RNLYSGDYYRIQGRAvlPIRWMSWESILL---GKFTTASDVWAFGVTLWETFTfcQEQPYSQLSD-EQVIEN 800
Cdd:cd14149 150 GDFGLAtvKSRWSGSQQVEQPTG--SILWMAPEVIRMqdnNPFSFQSDVYSYGIVLYELMT--GELPYSHINNrDQIIFM 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62420884 801 TGEFFRDQGRQTYLPQpaiCPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14149 226 VGRGYASPDLSKLYKN---CPKAMKRLVADCIKKVKEERPLFPQI 267
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
605-845 1.90e-17

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: 83.14  E-value: 1.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLR-ADANKNARNDFLKEIKIMSRLKDPNIIHLLAVcITDDPLCMITEYMENGDLnqflSRHEPPNSSSSDVrtvs 683
Cdd:cd14150  25 VAVKILKvTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGF-MTRPNFAIITQWCEGSSL----YRHLHVTETRFDT---- 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 684 yTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMS--RNLYSGDYYRIQGRAvlPIRWMSWESILL 761
Cdd:cd14150  96 -MQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvKTRWSGSQQVEQPSG--SILWMAPEVIRM 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 762 ---GKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDeqvientgeffRDQ-----GRQTYLPQ----PAICPDSVYKLML 829
Cdd:cd14150 173 qdtNPYSFQSDVYAYGVVLYELMS--GTLPYSNINN-----------RDQiifmvGRGYLSPDlsklSSNCPKAMKRLLI 239
                       250
                ....*....|....*.
gi 62420884 830 SCWRRDTKNRPSFQEI 845
Cdd:cd14150 240 DCLKFKREERPLFPQI 255
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
564-792 2.24e-17

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: 83.70  E-value: 2.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHlcevegmeKFKDKDFAldvsanqpVLVAVKMLRADankNARNDF----LKEIKIMSRLKDPNIIH 639
Cdd:cd07864  10 DIIGIIGEGTYGQVY--------KAKDKDTG--------ELVALKKVRLD---NEKEGFpitaIREIKILRQLNHRSVVN 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVcITDDPLCM-----------ITEYMENgDLNQFLSrheppnsssSDVRTVSYTNLKFMATQIASGMKYLSSLNFVH 708
Cdd:cd07864  71 LKEI-VTDKQDALdfkkdkgafylVFEYMDH-DLMGLLE---------SGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLH 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 709 RDLATRNCLVGKNYTIKIADFGMSRnLYSGDYYRIQGRAVLPIrWMSWESILLG--KFTTASDVWAFGVTLWETFT---- 782
Cdd:cd07864 140 RDIKCSNILLNNKGQIKLADFGLAR-LYNSEESRPYTNKVITL-WYRPPELLLGeeRYGPAIDVWSCGCILGELFTkkpi 217
                       250
                ....*....|
gi 62420884 783 FCQEQPYSQL 792
Cdd:cd07864 218 FQANQELAQL 227
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
567-845 2.34e-17

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: 82.43  E-value: 2.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmEKFKDKDFAldvsanqpVLVAVKMLRADANknaRNDFLKEIKIMSRLKD-PNIIHLLAVCI 645
Cdd:cd13997   6 EQIGSGSFSEVFKVR----SKVDGCLYA--------VKKSKKPFRGPKE---RARALREVEAHAALGQhPNIVRYYSSWE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRhEPPNSSSSDVRtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd13997  71 EGGHLYIQMELCENGSLQDALEE-LSPISKLSEAE------VWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNLYSGDYYRiQGRAvlpiRWMSWEsILLGKFT--TASDVWAFGVTLWETFTfCQEQPYSQLSDEQVientge 803
Cdd:cd13997 144 IGDFGLATRLETSGDVE-EGDS----RYLAPE-LLNENYThlPKADIFSLGVTVYEAAT-GEPLPRNGQQWQQL------ 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 62420884 804 ffrdqgRQTYLPQP--AICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd13997 211 ------RQGKLPLPpgLVLSQELTRLLKVMLDPDPTRRPTADQL 248
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
567-774 4.14e-17

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: 82.76  E-value: 4.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekFKdkdfALDVSANQPVLVAvKMLRADANKNARNDFLKEIKIMSRLKD-PNIIHLLAVCI 645
Cdd:cd07832   6 GRIGEGAHGIV----------FK----AKDRETGETVALK-KVALRKLEGGIPNQALREIKALQACQGhPYVVKLRDVFP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMEnGDLNQFLsRHEPPNSSSSDVRtvsytnlKFMAtQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd07832  71 HGTGFVLVFEYML-SSLSEVL-RDEERPLTEAQVK-------RYMR-MLLKGVAYMHANRIMHRDLKPANLLISSTGVLK 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 726 IADFGMSRnLYSGDYYRIQGRAVlPIRWMSWESILLG--KFTTASDVWAFG 774
Cdd:cd07832 141 IADFGLAR-LFSEEDPRLYSHQV-ATRWYRAPELLYGsrKYDEGVDLWAVG 189
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
569-730 5.23e-17

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: 78.25  E-value: 5.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGmekfkdkdfaldvsanQPVLVAVKMLRaDANKNARNDFLKEIKIMSRLK--DPNIIHLLAVCIT 646
Cdd:cd13968   1 MGEGASAKVFWAEGEC----------------TTIGVAVKIGD-DVNNEEGEDLESEMDILRRLKglELNIPKVLVTEDV 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEppnSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd13968  64 DGPNILLMELVKGGTLIAYTQEEE---LDEKDVESIMY--------QLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKL 132

                ....
gi 62420884 727 ADFG 730
Cdd:cd13968 133 IDFG 136
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
569-845 8.56e-17

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: 80.93  E-value: 8.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfKDKDFALDVSANQpvlVAVKMLRADANKNARNdflkEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd08220   8 VGRGAYGTVYLC--------RRKDDNKLVIIKQ---IPVEQMTKEERQAALN----EVKVLSMLHHPNIIEYYESFLEDK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHeppNSSSSDVRTVsytnLKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI-KIA 727
Cdd:cd08220  73 ALMIVMEYAPGGTLFEYIQQR---KGSLLSEEEI----LHFF-VQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIG 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMSRNLYS-GDYYRIQGRAVlpirWMSWEsILLGK-FTTASDVWAFGVTLWEtftfcqeqpYSQLSDEQVIENTGEFF 805
Cdd:cd08220 145 DFGISKILSSkSKAYTVVGTPC----YISPE-LCEGKpYNQKSDIWALGCVLYE---------LASLKRAFEAANLPALV 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 62420884 806 RDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd08220 211 LKIMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEI 250
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
565-800 8.61e-17

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 81.45  E-value: 8.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCevegMEKFKDKDFALDVsanqpvlVAVKMLRADANKnarndflKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14104   4 IAEELGRGQFGIVHRC----VETSSKKTYMAKF-------VKVKGADQVLVK-------KEISILNIARHRNILRLHESF 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHeppNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRN--CLVGKNY 722
Cdd:cd14104  66 ESHEELVMIFEFISGVDIFERITTA---RFELNEREIVSYVR------QVCEALEFLHSKNIGHFDIRPENiiYCTRRGS 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 723 TIKIADFGMSRNLYSGDYYRIQGRAVlpiRWMSWESILLGKFTTASDVWAFGVTLWetFTFCQEQPYSQLSDEQVIEN 800
Cdd:cd14104 137 YIKIIEFGQSRQLKPGDKFRLQYTSA---EFYAPEVHQHESVSTATDMWSLGCLVY--VLLSGINPFEAETNQQTIEN 209
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
567-845 8.75e-17

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: 81.72  E-value: 8.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLRADANKNARNDflKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd13998   1 EVIGKGRFGEVWKASLKNEP------------------VAVKIFSSRDKQSWFRE--KEIYRTPMLKHENILQFIAADER 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCM----ITEYMENGDLNQFLSRHeppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNF---------VHRDLAT 713
Cdd:cd13998  61 DTALRTelwlVTAFHPNGSL*DYLSLH-----------TIDWVSLCRLALSVARGLAHLHSEIPgctqgkpaiAHRDLKS 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMSRNLYSGDYY---RIQGRaVLPIRWMSWE----SILLGKFTT--ASDVWAFGVTLWETFTFC 784
Cdd:cd13998 130 KNILVKNDGTCCIADFGLAVRLSPSTGEednANNGQ-VGTKRYMAPEvlegAINLRDFESfkRVDIYAMGLVLWEMASRC 208
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 785 QE--------QP--YSQLSDEQVIENTGEFF-RDQGRQT----YLPQPAIcpDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd13998 209 TDlfgiveeyKPpfYSEVPNHPSFEDMQEVVvRDKQRPNipnrWLSHPGL--QSLAETIEECWDHDAEARLTAQCI 282
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
556-798 1.14e-16

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: 81.27  E-value: 1.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 556 EEFPRKLltfkEKLGEGQFGEVhlcevegmekFKDKDFAldvsaNQPVlVAVKMLRADANKNARNDFLKEIKIMSRLKDP 635
Cdd:cd06641   3 EELFTKL----EKIGKGSFGEV----------FKGIDNR-----TQKV-VAIKIIDLEEAEDEIEDIQQEITVLSQCDSP 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLsrhEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd06641  63 YVTKYYGSYLKDTKLWIIMEYLGGGSALDLL---EPGPLDETQIATI--------LREILKGLDYLHSEKKIHRDIKAAN 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDE 795
Cdd:cd06641 132 VLLSEHGEVKLADFGVAGQLTDTQIKR--N*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELAR--GEPPHSELHPM 207

                ...
gi 62420884 796 QVI 798
Cdd:cd06641 208 KVL 210
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
555-774 1.20e-16

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: 81.50  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 555 VEEFpRKLltfkEKLGEGQFGEVhlcevegmekFKdkdfALDVSANQpvLVAVKMLRADankNARNDF----LKEIKIMS 630
Cdd:cd07843   4 VDEY-EKL----NRIEEGTYGVV----------YR----ARDKKTGE--IVALKKLKME---KEKEGFpitsLREINILL 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 631 RLKDPNIIHL--LAVCITDDPLCMITEYMENgDLNQFLSRHEPPNSSSSdvrtvsytnLKFMATQIASGMKYLSSLNFVH 708
Cdd:cd07843  60 KLQHPNIVTVkeVVVGSNLDKIYMVMEYVEH-DLKSLMETMKQPFLQSE---------VKCLMLQLLSGVAHLHDNWILH 129
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 709 RDLATRNCLVGKNYTIKIADFGMSRnlYSGDYYRIQGRAVLPIrWMSWESILLG--KFTTASDVWAFG 774
Cdd:cd07843 130 RDLKTSNLLLNNRGILKICDFGLAR--EYGSPLKPYTQLVVTL-WYRAPELLLGakEYSTAIDMWSVG 194
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
568-796 1.41e-16

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: 81.65  E-value: 1.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVhlcevegmekFKDKDfaldvsANQPVLVAVKMLRADankNARNDF----LKEIKIMSRLKDPNIIHLLAV 643
Cdd:cd07865  19 KIGQGTFGEV----------FKARH------RKTGQIVALKKVLME---NEKEGFpitaLREIKILQLLKHENVVNLIEI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDdplcmitEYMENGDLNQF-----LSRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd07865  80 CRTK-------ATPYNRYKGSIylvfeFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 GKNYTIKIADFGMSRNLY---SGDYYRIQGRAVlpIRWMSWESILLGK--FTTASDVWAFGVTLWETFTfcqEQPYSQLS 793
Cdd:cd07865 153 TKDGVLKLADFGLARAFSlakNSQPNRYTNRVV--TLWYRPPELLLGErdYGPPIDMWGAGCIMAEMWT---RSPIMQGN 227

                ...
gi 62420884 794 DEQ 796
Cdd:cd07865 228 TEQ 230
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
569-781 1.66e-16

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: 80.78  E-value: 1.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVhlcevegmekFKDKDfaldvsANQPVLVAVKMLRADANKNARNDF-LKEIKIMSRLKD---PNIIHLLAVC 644
Cdd:cd07838   7 IGEGAYGTV----------YKARD------LQDGRFVALKKVRVPLSEEGIPLStIREIALLKQLESfehPNVVRLLDVC 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDD-----PLCMITEYMENgDLNQFLSRHEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVG 719
Cdd:cd07838  71 HGPRtdrelKLTLVFEHVDQ-DLATYLDKCPKPGLPPETIKDLMR--------QLLRGLDFLHSHRIVHRDLKPQNILVT 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 720 KNYTIKIADFGMSRnLYSgdyYRIQGRAVLPIRWMSWESILLGK-FTTASDVWAFGVTLWETF 781
Cdd:cd07838 142 SDGQVKLADFGLAR-IYS---FEMALTSVVVTLWYRAPEVLLQSsYATPVDMWSVGCIFAELF 200
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
567-779 1.86e-16

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: 81.64  E-value: 1.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlCEvegmekfkdkdfALDVSANQPVLVAvKMLRADAN-KNARNDfLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd07855  11 ETIGSGAYGVV--CS------------AIDTKSGQKVAIK-KIPNAFDVvTTAKRT-LRELKILRHFKHDNIIAIRDILR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLC------MITEYMENgDLNQFLSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVG 719
Cdd:cd07855  75 PKVPYAdfkdvyVVLDLMES-DLHHIIHSDQP----------LTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVN 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 720 KNYTIKIADFGMSRNLYSGD----YYRIQGRAVLPIRwmSWESIL-LGKFTTASDVWAFGVTLWE 779
Cdd:cd07855 144 ENCELKIGDFGMARGLCTSPeehkYFMTEYVATRWYR--APELMLsLPEYTQAIDMWSVGCIFAE 206
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
569-799 1.87e-16

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: 80.21  E-value: 1.87e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLC-EVEGMEKFKDKdfaldvsanqpVLVAVKMLRADANKNArndFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd14098   8 LGSGTFAEVKKAvEVETGKMRAIK-----------QIVKRKVAGNDKNLQL---FQREINILKSLEHPGIVRLIDWYEDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN--YTIK 725
Cdd:cd14098  74 QHIYLVMEYVEGGDLMDFIMAWG----------AIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDdpVIVK 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 726 IADFGMSRNLYSGDYYRI---QGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIE 799
Cdd:cd14098 144 ISDFGLAKVIHTGTFLVTfcgTMAYLAPEILMSKEQNLQGGYSNLVDMWSVGCLVYVMLT--GALPFDGSSQLPVEK 218
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
566-793 1.99e-16

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: 80.00  E-value: 1.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCevegmekfkdkdfaldVSANQPVLVAVKMLRadaNKNARNDF-LKEIKIMSRL--KDP----NII 638
Cdd:cd14133   4 LEVLGKGTFGQVVKC----------------YDLLTGEEVALKIIK---NNKDYLDQsLDEIRLLELLnkKDKadkyHIV 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENgDLNQFLSRHEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd14133  65 RLKDVFYFKNHLCIVFELLSQ-NLYEFLKQNKFQYLSLPRIRKI--------AQQILEALVFLHSLGLIHCDLKPENILL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 gKNY---TIKIADFGMSRNLYSGDYYRIQGRAvlpirWMSWESILLGKFTTASDVWAFGVTLWETFT----FCQEQPYSQ 791
Cdd:cd14133 136 -ASYsrcQIKIIDFGSSCFLTQRLYSYIQSRY-----YRAPEVILGLPYDEKIDMWSLGCILAELYTgeplFPGASEVDQ 209

                ..
gi 62420884 792 LS 793
Cdd:cd14133 210 LA 211
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
566-841 2.20e-16

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: 80.35  E-value: 2.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCevegMEKFKDKDFAldvsanqpvlvAVKMLRADANKNARNDFLKEIKIMSRLK-DPNIIHLLAVC 644
Cdd:cd14198  13 SKELGRGKFAVVRQC----ISKSTGQEYA-----------AKFLKKRRRGQDCRAEILHEIAVLELAKsNPRVVNLHEVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY-- 722
Cdd:cd14198  78 ETTSEIILILEYAAGGEIFNLCVPDLAEMVSENDIIR--------LIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYpl 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 -TIKIADFGMSRNL-YSGDYYRIQGRAvlpiRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIEN 800
Cdd:cd14198 150 gDIKIVDFGMSRKIgHACELREIMGTP----EYLAPEILNYDPITTATDMWNIGVIAYMLLT--HESPFVGEDNQETFLN 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 62420884 801 TGEFFRDQGRQTY--LPQPAIcpDSVYKLMLscwrRDTKNRPS 841
Cdd:cd14198 224 ISQVNVDYSEETFssVSQLAT--DFIQKLLV----KNPEKRPT 260
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
569-845 2.32e-16

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: 79.89  E-value: 2.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLceveGMEKFKDKDFALdvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd06628   8 IGSGSFGSVYL----GMNASSGELMAV----KQVELPSVSAENKDRKKSMLDALQREIALLRELQHENIVQYLGSSSDAN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHEPPNSSSsdvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd06628  80 HLNIFLEYVPGGSVATLLNNYGAFEESL----------VRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 729 FGMSRNL--------YSGDYYRIQGRavlpIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIEN 800
Cdd:cd06628 150 FGISKKLeanslstkNNGARPSLQGS----VFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT--GTHPFPDCTQMQAIFK 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 62420884 801 TGEFFRdqgrqtylPQ-PAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06628 224 IGENAS--------PTiPSNISSEARDFLEKTFEIDHNKRPTADEL 261
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
569-849 3.23e-16

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: 80.25  E-value: 3.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLRADANKN---ARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14159   1 IGEGGFGCVYQAVMRNTE------------------YAVKRLKEDSELDwsvVKNSFLTEVEKLSRFRHPNIVDLAGYSA 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHE--PPNSSSSDVRTVSYTnlkfmatqiASGMKYLSSLN--FVHRDLATRNCLVGKN 721
Cdd:cd14159  63 QQGNYCLIYVYLPNGSLEDRLHCQVscPCLSWSQRLHVLLGT---------ARAIQYLHSDSpsLIHGDVKSSNILLDAA 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFGM---SRNLYSGDYYRIQGR--------AVLPirwmsWESILLGKFTTASDVWAFGVTLWETFT-------- 782
Cdd:cd14159 134 LNPKLGDFGLarfSRRPKQPGMSSTLARtqtvrgtlAYLP-----EEYVKTGTLSVEIDVYSFGVVLLELLTgrramevd 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 783 -----FCQEQPYSQLSDEQVIENTGEFFRD--------QGRQTYL-PQPAICPDSVyKLMLS-----CWRRDTKNRPSFQ 843
Cdd:cd14159 209 scsptKYLKDLVKEEEEAQHTPTTMTHSAEaqaaqlatSICQKHLdPQAGPCPPEL-GIEISqlacrCLHRRAKKRPPMT 287

                ....*.
gi 62420884 844 EIHLLL 849
Cdd:cd14159 288 EVFQEL 293
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
567-774 3.66e-16

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: 79.64  E-value: 3.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekFKdkdfALDVSANQpvLVAVKMLRADANKNA-RNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd07835   5 EKIGEGTYGVV----------YK----ARDKLTGE--IVALKKIRLETEDEGvPSTAIREISLLKELNHPNIVRLLDVVH 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMeNGDLNQFLSRHepPNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd07835  69 SENKLYLVFEFL-DLDLKKYMDSS--PLTGLDPPLIKSYLY------QLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALK 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 726 IADFGMSrnlysgdyyriqgRAV-LPIR---------WMSWESILLG--KFTTASDVWAFG 774
Cdd:cd07835 140 LADFGLA-------------RAFgVPVRtythevvtlWYRAPEILLGskHYSTPVDIWSVG 187
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
567-844 3.97e-16

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: 80.04  E-value: 3.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd07872  12 EKLGEGTYATVF----KGRSKLTEN------------LVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENgDLNQFLSrheppnssssDVRTV-SYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd07872  76 DKSLTLVFEYLDK-DLKQYMD----------DCGNImSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELK 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSR------NLYSGDYYRIqgravlpirWMSWESILLG--KFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQV 797
Cdd:cd07872 145 LADFGLARaksvptKTYSNEVVTL---------WYRPPDVLLGssEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELH 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 798 I----------EN-----TGEFFRDQGRQTYLPQPAI--CP--DSV-YKLMLSCWRRDTKNRPSFQE 844
Cdd:cd07872 216 LifrllgtpteETwpgisSNDEFKNYNFPKYKPQPLInhAPrlDTEgIELLTKFLQYESKKRISAEE 282
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
567-839 4.08e-16

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: 79.73  E-value: 4.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVegmekFKDkdfaldvSANQPVLVAVKMLRADANKNARNDflKEIKIMSRLKDPNIIHLLAVCI- 645
Cdd:cd14055   1 KLVGKGRFAEVWKAKL-----KQN-------ASGQYETVAVKIFPYEEYASWKNE--KDIFTDASLKHENILQFLTAEEr 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 ---TDDPLCMITEYMENGDLNQFLSRHeppnssssdvrTVSYTNLKFMATQIASGMKYLSS---------LNFVHRDLAT 713
Cdd:cd14055  67 gvgLDRQYWLITAYHENGSLQDYLTRH-----------ILSWEDLCKMAGSLARGLAHLHSdrtpcgrpkIPIAHRDLKS 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMSRNL---YSGDYYRIQGRAVLPiRWMSWEsILLGKFTTAS-------DVWAFGVTLWETFTF 783
Cdd:cd14055 136 SNILVKNDGTCVLADFGLALRLdpsLSVDELANSGQVGTA-RYMAPE-ALESRVNLEDlesfkqiDVYSMALVLWEMASR 213
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 784 CQ--------EQPY-SQLSDEQVIENT-GEFFRDQGR----QTYLPQPAICpdSVYKLMLSCWRRDTKNR 839
Cdd:cd14055 214 CEasgevkpyELPFgSKVRERPCVESMkDLVLRDRGRpeipDSWLTHQGMC--VLCDTITECWDHDPEAR 281
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
566-830 5.06e-16

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 78.92  E-value: 5.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVH--LCEVEgmekfkdkdfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAV 643
Cdd:cd08228   7 EKKIGRGQFSEVYraTCLLD----------------RKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLsRHEPPNSSSSDVRTVsytnLKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd08228  71 FIEDNELNIVLELADAGDLSQMI-KYFKKQKRLIPERTV----WKYF-VQLCSAVEHMHSRRVMHRDIKPANVFITATGV 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 IKIADFGMSRnLYSGDYYRIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLWET--------------FTFCQ--EQ 787
Cdd:cd08228 145 VKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMaalqspfygdkmnlFSLCQkiEQ 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 62420884 788 -PYSQLSDEQVIENtgefFRDQGRQTYLPQPAICPDSVYKLMLS 830
Cdd:cd08228 223 cDYPPLPTEHYSEK----LRELVSMCIYPDPDQRPDIGYVHQIA 262
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
563-779 6.13e-16

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: 79.16  E-value: 6.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVlvaVKMLRADANKNarndflkEIKIMSRLKDPNIIHLLA 642
Cdd:cd05580   3 FEFLKTLGTGSFGRVRLVKHKDSGKY----YALKILKKAKI---IKLKQVEHVLN-------EKRILSEVRHPFIVNLLG 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSR-HEPPNSSSsdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd05580  69 SFQDDRNLYMVMEYVPGGELFSLLRRsGRFPNDVA-----------KFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSD 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 722 YTIKIADFGMSRNLySGDYYRIQGRAvlpiRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05580 138 GHIKITDFGFAKRV-KDRTYTLCGTP----EYLAPEIILSKGHGKAVDWWALGILIYE 190
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
569-779 6.41e-16

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: 79.11  E-value: 6.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARND--FLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05577   1 LGRGGFGEVCACQVKATGK----------------MYACKKLDKKRIKKKKGEtmALNEKIILEKVSSPFIVSLAYAFET 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05577  65 KDKLCLVLTLMNGGDLKYHIYNVGTRGFSEARAI--------FYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRI 136
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 727 ADFGMSRNLYSGDyyRIQGRAVLPiRWMSWEsILLGK--FTTASDVWAFGVTLWE 779
Cdd:cd05577 137 SDLGLAVEFKGGK--KIKGRVGTH-GYMAPE-VLQKEvaYDFSVDWFALGCMLYE 187
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
569-778 7.83e-16

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: 78.56  E-value: 7.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEgmekFKDKDFALDVsanqpvLVAVKMLR-------------ADANKNARNDF---LKEIKIMSRL 632
Cdd:cd14118   2 IGKGSYGIVKLAYNE----EDNTLYAMKI------LSKKKLLKqagffrrppprrkPGALGKPLDPLdrvYREIAILKKL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 633 KDPNIIHLLAVciTDDP----LCMITEYMENGDLNQflsrhEPPNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVH 708
Cdd:cd14118  72 DHPNVVKLVEV--LDDPnednLYMVFELVDKGAVME-----VPTDNPLSEETARSYFR------DIVLGIEYLHYQKIIH 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 709 RDLATRNCLVGKNYTIKIADFGMSrNLYSGDYYRIQGRAVLPIrWMSWESILLGKFT---TASDVWAFGVTLW 778
Cdd:cd14118 139 RDIKPSNLLLGDDGHVKIADFGVS-NEFEGDDALLSSTAGTPA-FMAPEALSESRKKfsgKALDIWAMGVTLY 209
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
567-782 8.37e-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: 78.89  E-value: 8.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd07873   8 DKLGEGTYATVY----KGRSKLTDN------------LVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHT 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENgDLNQFLSrhEPPNSsssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd07873  72 EKSLTLVFEYLDK-DLKQYLD--DCGNS-------INMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 727 ADFGMSR------NLYSGDYYRIqgravlpirWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07873 142 ADFGLARaksiptKTYSNEVVTL---------WYRPPDILLGstDYSTQIDMWGVGCIFYEMST 196
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
563-845 9.09e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 78.07  E-value: 9.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVhlcevegmekFKDKDFAL-DVSANQPVLVAVKMLRaDANKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd05078   1 LIFNESLGQGTFTKI----------FKGIRREVgDYGQLHETEVLLKVLD-KAHRNYSESFFEAASMMSQLSHKHLVLNY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV--- 718
Cdd:cd05078  70 GVCVCGDENILVQEYVKFGSLDTYLKKNK---------NCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLire 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 -----GKNYTIKIADFGMSrnlysgdyYRIQGRAVL--PIRWMSWESILLGK-FTTASDVWAFGVTLWETFTfCQEQPYS 790
Cdd:cd05078 141 edrktGNPPFIKLSDPGIS--------ITVLPKDILleRIPWVPPECIENPKnLSLATDKWSFGTTLWEICS-GGDKPLS 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 791 QLSDEQVIentgEFFRDQGRqtyLPQPAICpdSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05078 212 ALDSQRKL----QFYEDRHQ---LPAPKWT--ELANLINNCMDYEPDHRPSFRAI 257
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
623-782 1.08e-15

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 79.27  E-value: 1.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 623 LKEIKIMSRLKDPNIIHLLAVCITDDPLCM-----ITEYMENgDLNQFLSrheppnssssdVRTVSYTNLKFMATQIASG 697
Cdd:cd07849  51 LREIKILLRFKHENIIGILDIQRPPTFESFkdvyiVQELMET-DLYKLIK-----------TQHLSNDHIQYFLYQILRG 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 698 MKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLG--KFTTASDVWAFGV 775
Cdd:cd07849 119 LKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNskGYTKAIDIWSVGC 198

                ....*..
gi 62420884 776 TLWETFT 782
Cdd:cd07849 199 ILAEMLS 205
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
604-792 1.18e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 78.47  E-value: 1.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRADANKNARN-DFLKEIKIMSRLKD---PNIIHLLAVCIT-----DDPLCMITEYMENgDLNQFLSRHEPPNS 674
Cdd:cd07863  27 FVALKSVRVQTNEDGLPlSTVREVALLKRLEAfdhPNIVRLMDVCATsrtdrETKVTLVFEHVDQ-DLRTYLDKVPPPGL 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 675 SSSDVRTvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRnLYSgdYYRIQGRAVLPIRWM 754
Cdd:cd07863 106 PAETIKD--------LMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLAR-IYS--CQMALTPVVVTLWYR 174
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 62420884 755 SWESILLGKFTTASDVWAFGVTLWETFT----FCQEQPYSQL 792
Cdd:cd07863 175 APEVLLQSTYATPVDMWSVGCIFAEMFRrkplFCGNSEADQL 216
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
567-742 1.58e-15

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: 77.31  E-value: 1.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVlvAVKMLRADANKNARND--FLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14079   8 KTLGVGSFGKVKL--------------AEHELTGHKV--AVKILNRQKIKSLDMEekIRREIQILKLFRHPHIIRLYEVI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEppNSSSSDVRtvsytnlKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd14079  72 ETPTDIFMVMEYVSGGELFDYIVQKG--RLSEDEAR-------RFF-QQIISGVEYCHRHMVVHRDLKPENLLLDSNMNV 141
                       170
                ....*....|....*...
gi 62420884 725 KIADFGMSRNLYSGDYYR 742
Cdd:cd14079 142 KIADFGLSNIMRDGEFLK 159
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
567-788 1.60e-15

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: 77.85  E-value: 1.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCiT 646
Cdd:cd06621   7 SSLGEGAGGSVTKCRLRNTKT----------------IFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAF-L 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMIT---EYMENGDLNQFLSRheppnSSSSDVRTVSYTNLKfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd06621  70 DEQDSSIGiamEYCEGGSLDSIYKK-----VKKKGGRIGEKVLGK-IAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 724 IKIADFGMSRNL-------YSGDYYriqgravlpirWMSWESILLGKFTTASDVWAFGVTLWET----FTFCQEQP 788
Cdd:cd06621 144 VKLCDFGVSGELvnslagtFTGTSY-----------YMAPERIQGGPYSITSDVWSLGLTLLEVaqnrFPFPPEGE 208
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
604-788 2.06e-15

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 77.75  E-value: 2.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRAdANKNArndFLKEIKIMS--RLKDPNIIHLLAV----CITDDPLCMITEYMENGDLNQFLSrheppnssss 677
Cdd:cd14053  20 LVAVKIFPL-QEKQS---WLTEREIYSlpGMKHENILQFIGAekhgESLEAEYWLITEFHERGSLCDYLK---------- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 678 dVRTVSYTNLKFMATQIASGMKYL----SSLN------FVHRDLATRNCLVGKNYTIKIADFGMSRNLysgDYYRIQGRA 747
Cdd:cd14053  86 -GNVISWNELCKIAESMARGLAYLhediPATNgghkpsIAHRDFKSKNVLLKSDLTACIADFGLALKF---EPGKSCGDT 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 748 VLPI---RWMSWEsILLG--KFTTAS----DVWAFGVTLWETFTFCQEQP 788
Cdd:cd14053 162 HGQVgtrRYMAPE-VLEGaiNFTRDAflriDMYAMGLVLWELLSRCSVHD 210
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
605-845 2.31e-15

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


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 77.01  E-value: 2.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLsRHEPPNSSSSDVRTVsy 684
Cdd:cd06610  29 VAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLDIM-KSSYPRGGLDEAIIA-- 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 685 TNLKfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVL---PIrWMSWESILL 761
Cdd:cd06610 106 TVLK----EVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRTRKVRKTFvgtPC-WMAPEVMEQ 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 762 GK-FTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIENTgeffrdqgRQTYLPQPAICPD-----SVYKLMLS-CWRR 834
Cdd:cd06610 181 VRgYDFKADIWSFGITAIELAT--GAAPYSKYPPMKVLMLT--------LQNDPPSLETGADykkysKSFRKMISlCLQK 250
                       250
                ....*....|.
gi 62420884 835 DTKNRPSFQEI 845
Cdd:cd06610 251 DPSKRPTAEEL 261
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
567-782 2.47e-15

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


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 77.79  E-value: 2.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKL---GEGQFGEVHlcevegmeKFKDKdfaldVSANQpvlVAVKMLRADankNARNDF----LKEIKIMSRLKDPNIIH 639
Cdd:cd07845  10 EKLnriGEGTYGIVY--------RARDT-----TSGEI---VALKKVRMD---NERDGIpissLREITLLLNLRHPNIVE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITD--DPLCMITEYMENgDLNQFLSRHEPPNSSSSdvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCL 717
Cdd:cd07845  71 LKEVVVGKhlDSIFLVMEYCEQ-DLASLLDNMPTPFSESQ---------VKCLMLQLLRGLQYLHENFIIHRDLKVSNLL 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 718 VGKNYTIKIADFGMSRNLysGDYYRIQGRAVLPIrWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07845 141 LTDKGCLKIADFGLARTY--GLPAKPMTPKVVTL-WYRAPELLLGctTYTTAIDMWAVGCILAELLA 204
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
604-839 2.53e-15

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: 77.40  E-value: 2.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRAdankNARNDFLKEIKIMS--RLKDPNIIHLLAVC--ITDDPL---CMITEYMENGDLNQFLSRHeppnsss 676
Cdd:cd14054  20 PVAVKVFPA----RHRQNFQNEKDIYElpLMEHSNILRFIGADerPTADGRmeyLLVLEYAPKGSLCSYLREN------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 677 sdvrTVSYTNLKFMATQIASGMKYLSSL---------NFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRA 747
Cdd:cd14054  89 ----TLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSLVRGRPGA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 748 --------VLPIRWMS------------WESILLgkfttASDVWAFGVTLWETFTFC------QEQPYSQLSDEQVIENT 801
Cdd:cd14054 165 aenasiseVGTLRYMApevlegavnlrdCESALK-----QVDVYALGLVLWEIAMRCsdlypgESVPPYQMPYEAELGNH 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 62420884 802 GEFFRDQ------GRQTYLPQP----AICPDSVYKLMLSCWRRDTKNR 839
Cdd:cd14054 240 PTFEDMQllvsreKARPKFPDAwkenSLAVRSLKETIEDCWDQDAEAR 287
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
568-731 2.89e-15

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: 76.60  E-value: 2.89e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCevegMEKFKDKDFALDVSANQPVLVAVKMLRadanknarndflKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd14095   7 VIGDGNFAVVKEC----RDKATDKEYALKIIDKAKCKGKEHMIE------------NEVAILRRVKHPNIVQLIEEYDTD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSrheppnssssdvRTVSYT--NLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN---- 721
Cdd:cd14095  71 TELYLVMELVKGGDLFDAIT------------SSTKFTerDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHedgs 138
                       170
                ....*....|
gi 62420884 722 YTIKIADFGM 731
Cdd:cd14095 139 KSLKLADFGL 148
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
567-835 2.91e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 77.07  E-value: 2.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevegmeKFKDKdfaldvSANQpvLVAVKMLRADA-NKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd07861   6 EKIGEGTYGVVY--------KGRNK------KTGQ--IVAMKKIRLESeEEGVPSTAIREISLLKELQHPNIVCLEDVLM 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENgDLNQFLSrhEPPNSSSSDVRTV-SYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd07861  70 QENRLYLVFEFLSM-DLKKYLD--SLPKGKYMDAELVkSYLY------QILQGILFCHSRRVLHRDLKPQNLLIDNKGVI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLysGDYYRIQGRAVLPIrWMSWESILLG--KFTTASDVWAFGVTLWETFTfcqEQPYSQLSDEqvIENTG 802
Cdd:cd07861 141 KLADFGLARAF--GIPVRVYTHEVVTL-WYRAPEVLLGspRYSTPVDIWSIGTIFAEMAT---KKPLFHGDSE--IDQLF 212
                       250       260       270
                ....*....|....*....|....*....|...
gi 62420884 803 EFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRD 835
Cdd:cd07861 213 RIFRILGTPTEDIWPGVTSLPDYKNTFPKWKKG 245
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
567-782 4.12e-15

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: 76.69  E-value: 4.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegmekfKDKDfaldvsANQpvLVAVK-MLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd07846   7 GLVGEGSYGMVMKC--------RHKE------TGQ--IVAIKkFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFlsRHEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd07846  71 RKKRWYLVFEFVDHTVLDDL--EKYPNGLDESRVRKYLF--------QILRGIDFCHSHNIIHRDIKPENILVSQSGVVK 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 726 IADFGMSRNLYSG-----DYyriqgravLPIRWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07846 141 LCDFGFARTLAAPgevytDY--------VATRWYRAPELLVGdtKYGKAVDVWAVGCLVTEMLT 196
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
567-779 4.24e-15

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 76.70  E-value: 4.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekFKDKDfaldvsANQPVLVAVKMLRAD-ANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd07839   6 EKIGEGTYGTV----------FKAKN------RETHEIVALKRVRLDdDDEGVPSSALREICLLKELKHKNIVRLYDVLH 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENgDLNQFLS--RHEPpnssssDVRTVSytnlKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd07839  70 SDKKLTLVFEYCDQ-DLKKYFDscNGDI------DPEIVK----SFM-FQLLKGLAFCHSHNVLHRDLKPQNLLINKNGE 137
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 724 IKIADFGMSRNlysgdyYRIqgravlPIRWMSWE---------SILLGK--FTTASDVWAFGVTLWE 779
Cdd:cd07839 138 LKLADFGLARA------FGI------PVRCYSAEvvtlwyrppDVLFGAklYSTSIDMWSAGCIFAE 192
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
603-782 6.10e-15

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: 75.99  E-value: 6.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 603 VLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLsRHEPPNSSSSDVRTV 682
Cdd:cd14664  18 TLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLGELL-HSRPESQPPLDWETR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 SYtnlkfMATQIASGMKYL---SSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYY---RIQGRavlpIRWMSW 756
Cdd:cd14664  97 QR-----IALGSARGLAYLhhdCSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHvmsSVAGS----YGYIAP 167
                       170       180
                ....*....|....*....|....*.
gi 62420884 757 ESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14664 168 EYAYTGKVSEKSDVYSYGVVLLELIT 193
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
605-789 6.76e-15

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 75.59  E-value: 6.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRadaNKNARNDFL-----KEIKIMSRLKDPNIIHLLAVCITDD-PLCMITEYMENGDLNQFLSRHEPPNSSSSd 678
Cdd:cd14165  29 VAIKIID---KKKAPDDFVekflpRELEILARLNHKSIIKTYEIFETSDgKVYIVMELGVQGDLLEFIKLRGALPEDVA- 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 679 vrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDyyriQGRAVLPIRW----- 753
Cdd:cd14165 105 ---------RKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLRDE----NGRIVLSKTFcgsaa 171
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 62420884 754 MSWESILLGKF--TTASDVWAFGVTLWetFTFCQEQPY 789
Cdd:cd14165 172 YAAPEVLQGIPydPRIYDIWSLGVILY--IMVCGSMPY 207
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
552-779 7.42e-15

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: 76.61  E-value: 7.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 552 DVAVEEFPRKLLTFKEKLGEGQFGEVHlcevegmekfkdkdFALDVSANQpvLVAVKMLRADANKNAR--NDFLKEIKIM 629
Cdd:cd06633  12 DLFYKDDPEEIFVDLHEIGHGSFGAVY--------------FATNSHTNE--VVAIKKMSYSGKQTNEkwQDIIKEVKFL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 630 SRLKDPNIIHLLAVCITDDPLCMITEYMEnGDLNQFLSRHEPPnssssdVRTVSYTNLKFMATQiasGMKYLSSLNFVHR 709
Cdd:cd06633  76 QQLKHPNTIEYKGCYLKDHTAWLVMEYCL-GSASDLLEVHKKP------LQEVEIAAITHGALQ---GLAYLHSHNMIHR 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 710 DLATRNCLVGKNYTIKIADFGMSR-----NLYSGDYYriqgravlpirWMSWESILL---GKFTTASDVWAFGVTLWE 779
Cdd:cd06633 146 DIKAGNILLTEPGQVKLADFGSASiaspaNSFVGTPY-----------WMAPEVILAmdeGQYDGKVDIWSLGITCIE 212
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
567-782 7.81e-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: 75.87  E-value: 7.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegmekfKDKDfaldvsANQpvLVAVK-MLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd07847   7 SKIGEGSYGVVFKC--------RNRE------TGQ--IVAIKkFVESEDDPVIKKIALREIRMLKQLKHPNLVNLIEVFR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQfLSRHepPNSSSSD-VRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd07847  71 RKRKLHLVFEYCDHTVLNE-LEKN--PRGVPEHlIKKIIW--------QTLQAVNFCHKHNCIHRDVKPENILITKQGQI 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGDYYRIQGRAVlpiRWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07847 140 KLCDFGFARILTGPGDDYTDYVAT---RWYRAPELLVGdtQYGPPVDVWAIGCVFAELLT 196
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
565-779 8.20e-15

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: 75.42  E-value: 8.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVhlcevegmekFKDKDFALDVsanqpvLVAVKMLRADAnKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd06613   4 LIQRIGSGTYGDV----------YKARNIATGE------LAAVKVIKLEP-GDDFEIIQQEISMLKECRHPNIVAYFGSY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd06613  67 LRRDKLWIVMEYCGGGSLQDIYQVTGP----------LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDV 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 725 KIADFGMS---------RNLYSGDYYriqgravlpirWMSWESILL---GKFTTASDVWAFGVTLWE 779
Cdd:cd06613 137 KLADFGVSaqltatiakRKSFIGTPY-----------WMAPEVAAVerkGGYDGKCDIWALGITAIE 192
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
562-845 1.04e-14

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: 75.14  E-value: 1.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 562 LLTFKEKLGEGQFGEVHLCE-VEGMEKfkdkdfaldvsanqpvlVAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd14074   4 LYDLEETLGRGHFAVVKLARhVFTGEK-----------------VAVKVIdKTKLDDVSKAHLFQEVRCMKLVQHPNVVR 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLSRHEppNSSSSDVRTVSYtnlkfmaTQIASGMKYLSSLNFVHRDLATRNCLV- 718
Cdd:cd14074  67 LYEVIDTQTKLYLILELGDGGDMYDYIMKHE--NGLNEDLARKYF-------RQIVSAISYCHKLHVVHRDLKPENVVFf 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 GKNYTIKIADFGMSRNLYSGDYYRIQGRAVLpirwMSWESILLGKF--TTASDVWAFGVTLWetFTFCQEQPYSQLSDEQ 796
Cdd:cd14074 138 EKQGLVKLTDFGFSNKFQPGEKLETSCGSLA----YSAPEILLGDEydAPAVDIWSLGVILY--MLVCGQPPFQEANDSE 211
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 62420884 797 VIENTGEffrdqGRQTYlpqPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14074 212 TLTMIMD-----CKYTV---PAHVSPECKDLIRRMLIRDPKKRASLEEI 252
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
569-733 1.08e-14

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: 74.57  E-value: 1.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFAldvsanqpvlvaVKMLRADANKNaRNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd14103   1 LGRGKFGTVYRCV----EKATGKELA------------AKFIKCRKAKD-REDVRNEIEIMNQLRHPRLLQLYDAFETPR 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLnqfLSRHEPPNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRN--CLVGKNYTIKI 726
Cdd:cd14103  64 EMVLVMEYVAGGEL---FERVVDDDFELTERDCILFMR------QICEGVQYMHKQGILHLDLKPENilCVSRTGNQIKI 134

                ....*..
gi 62420884 727 ADFGMSR 733
Cdd:cd14103 135 IDFGLAR 141
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
560-779 1.09e-14

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: 75.02  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKE--KLGEGQFGEVHLCEvegmEKFKDkdfaldvsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNI 637
Cdd:cd13996   3 RYLNDFEEieLLGSGGFGSVYKVR----NKVDG------------VTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMENGDLNQFLSRhepPNSSSSDVRTVsYTNLkfmATQIASGMKYLSSLNFVHRDLATRNCL 717
Cdd:cd13996  67 VRYYTAWVEEPPLYIQMELCEGGTLRDWIDR---RNSSSKNDRKL-ALEL---FKQILKGVSYIHSKGIVHRDLKPSNIF 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 718 V-GKNYTIKIADFGMSRNLYSGDyyRIQGRAVLP--------------IRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd13996 140 LdNDDLQVKIGDFGLATSIGNQK--RELNNLNNNnngntsnnsvgigtPLYASPEQLDGENYNEKADIYSLGIILFE 214
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
569-784 1.10e-14

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 75.05  E-value: 1.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmekfkdkdfalDVSANQPVlvAVKMLRADANKNArnDFLKEIKIMSRLKD-PNIIHLLAVCI-T 646
Cdd:cd13987   1 LGEGTYGKVLLAV--------------HKGSGTKM--ALKFVPKPSTKLK--DFLREYNISLELSVhPHIIKTYDVAFeT 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLsrhePPNSSSSDVRTvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLV-GKNYT-I 724
Cdd:cd13987  63 EDYYVFAQEYAPYGDLFSII----PPQVGLPEERV------KRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDCRrV 132
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 725 KIADFGMSRnlysgdyyriqgRAVLPIRWMSW----------ESILLGKFT--TASDVWAFGVTLwetftFC 784
Cdd:cd13987 133 KLCDFGLTR------------RVGSTVKRVSGtipytapevcEAKKNEGFVvdPSIDVWAFGVLL-----FC 187
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
605-738 1.26e-14

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: 74.48  E-value: 1.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVrtvs 683
Cdd:cd14072  28 VAIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARA---- 103
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 684 ytnlKFmaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSG 738
Cdd:cd14072 104 ----KF--RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPG 152
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
552-779 1.30e-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: 75.86  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 552 DVAVEEFPRKLLTFKEKLGEGQFGEVHlcevegmekfkdkdFALDVSANQPVLVAvKMLRADANKNAR-NDFLKEIKIMS 630
Cdd:cd06635  16 ELFFKEDPEKLFSDLREIGHGSFGAVY--------------FARDVRTSEVVAIK-KMSYSGKQSNEKwQDIIKEVKFLQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 631 RLKDPNIIHLLAVCITDDPLCMITEYMEnGDLNQFLSRHEPPnssssdVRTVSYTNLKFMATQiasGMKYLSSLNFVHRD 710
Cdd:cd06635  81 RIKHPNSIEYKGCYLREHTAWLVMEYCL-GSASDLLEVHKKP------LQEIEIAAITHGALQ---GLAYLHSHNMIHRD 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 711 LATRNCLVGKNYTIKIADFGMSR-----NLYSGDYYriqgravlpirWMSWESILL---GKFTTASDVWAFGVTLWE 779
Cdd:cd06635 151 IKAGNILLTEPGQVKLADFGSASiaspaNSFVGTPY-----------WMAPEVILAmdeGQYDGKVDVWSLGITCIE 216
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
569-782 1.37e-14

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: 75.18  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdfaldvsanqpvlVAVKMLRADANKNARND--FLKEIKIMSRLKDPNII-------H 639
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEY----------------VAIKKCRQELSPSDKNRerWCLEVQIMKKLNHPNVVsardvppE 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDP-LCMitEYMENGDLNQFLSRhePPNSS---SSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd13989  65 LEKLSPNDLPlLAM--EYCSGGDLRKVLNQ--PENCCglkESEVRTL--------LSDISSAISYLHENRIIHRDLKPEN 132
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CL---VGKNYTIKIADFGMSRNLysgDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd13989 133 IVlqqGGGRVIYKLIDLGYAKEL---DQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECIT 199
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
568-841 1.38e-14

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: 75.07  E-value: 1.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVhlcevegmekFKDKDFAldvsaNQPVLVAVKMLRADANKNARN-DFLKEIKIMSRLKD---PNIIHLLAV 643
Cdd:cd07862   8 EIGEGAYGKV----------FKARDLK-----NGGRFVALKRVRVQTGEEGMPlSTIREVAVLRHLETfehPNVVRLFDV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CIT-----DDPLCMITEYMENgDLNQFLSRHEPPNssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd07862  73 CTVsrtdrETKLTLVFEHVDQ-DLTTYLDKVPEPG--------VPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 GKNYTIKIADFGMSRnLYSgdyYRIQGRAVLPIRWMSWESILL-GKFTTASDVWAFGVTLWETFtfcQEQPYSQLSDEqv 797
Cdd:cd07862 144 TSSGQIKLADFGLAR-IYS---FQMALTSVVVTLWYRAPEVLLqSSYATPVDLWSVGCIFAEMF---RRKPLFRGSSD-- 214
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 798 IENTGEFF--------RDQGRQTYLPQPAICP-------------DSVYK-LMLSCWRRDTKNRPS 841
Cdd:cd07862 215 VDQLGKILdviglpgeEDWPRDVALPRQAFHSksaqpiekfvtdiDELGKdLLLKCLTFNPAKRIS 280
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
569-732 1.45e-14

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: 74.36  E-value: 1.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevegmekfkdkdFALDVSANQPVlvAVKMLraDANKNARNDFLK----EIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14663   8 LGEGTFAKVK--------------FARNTKTGESV--AIKII--DKEQVAREGMVEqikrEIAIMKLLRHPNIVELHEVM 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd14663  70 ATKTKIFFVMELVTGGELFSKIAKNGRLKEDKA----------RKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNL 139

                ....*...
gi 62420884 725 KIADFGMS 732
Cdd:cd14663 140 KISDFGLS 147
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
564-784 1.65e-14

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: 74.51  E-value: 1.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLCevegmekfkdkdfaldVSANQPVLVAVKML-RADANKNARNDFL-KEIKIMSRLKDPNIIHLL 641
Cdd:cd14164   3 TLGTTIGEGSFSKVKLA----------------TSQKYCCKVAIKIVdRRRASPDFVQKFLpRELSILRRVNHPNIVQMF 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVC-ITDDPLCMITEYMENgDLNQFLSR-HEPPNSSSSDvrtvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLV- 718
Cdd:cd14164  67 ECIeVANGRLYIVMEAAAT-DLLQKIQEvHHIPKDLARD-----------MFAQMVGAVNYLHDMNIVHRDLKCENILLs 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 719 GKNYTIKIADFGMSRNLYsgDYYRIQGRAVLPIRWMSWESILLGKFTTAS-DVWAFGVTLWETFTFC 784
Cdd:cd14164 135 ADDRKIKIADFGFARFVE--DYPELSTTFCGSRAYTPPEVILGTPYDPKKyDVWSLGVVLYVMVTGT 199
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
567-788 1.87e-14

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: 74.61  E-value: 1.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd07870   6 EKLGEGSYATVY----KGISRINGQ------------LVALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENgDLNQFLSRHePPNSSSSDVRTvsytnlkFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd07870  70 KETLTFVFEYMHT-DLAQYMIQH-PGGLHPYNVRL-------FM-FQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKL 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSR------NLYSGDYYRIqgravlpirWMSWESILLG--KFTTASDVWAFGVTLWETFtfcQEQP 788
Cdd:cd07870 140 ADFGLARaksipsQTYSSEVVTL---------WYRPPDVLLGatDYSSALDIWGAGCIFIEML---QGQP 197
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
569-796 1.92e-14

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: 74.18  E-value: 1.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVegmeKFKDKDFALdvsanqpvlvavKMLRADA--NKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05572   1 LGVGGFGRVELVQL----KSKGRTFAL------------KCVKKRHivQTRQQEHIFSEKEILEECNSPFIVKLYRTFKD 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05572  65 KKYLYMLMEYCLGGELWTILRDRGLFDEYTA----------RFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKL 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 727 ADFGMSRNLYSGDY-YRIQGRavlPiRWMSWEsILLGK-FTTASDVWAFGVTLWEtfTFCQEQPYSQLSDEQ 796
Cdd:cd05572 135 VDFGFAKKLGSGRKtWTFCGT---P-EYVAPE-IILNKgYDFSVDYWSLGILLYE--LLTGRPPFGGDDEDP 199
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
559-845 2.20e-14

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: 74.32  E-value: 2.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHlcevEGMEKFKDKdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNII 638
Cdd:cd06642   2 PEELFTKLERIGKGSFGEVY----KGIDNRTKE------------VVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYIT 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENGDLNQFLsrhEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd06642  66 RYYGSYLKGTKLWIIMEYLGGGSALDLL---KPGPLEETYIATI--------LREILKGLDYLHSERKIHRDIKAANVLL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 GKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVI 798
Cdd:cd06642 135 SEQGDVKLADFGVAGQLTDTQIKR--NTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAK--GEPPNSDLHPMRVL 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 799 ----ENTGEFFRDQGRQTYlpqpaicpdsvYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06642 211 flipKNSPPTLEGQHSKPF-----------KEFVEACLNKDPRFRPTAKEL 250
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
569-730 2.54e-14

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: 74.06  E-value: 2.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegmekfkdkDFALDVSANQ-PVLVAVKMLRADANKNARND--FLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14076   9 LGEGEFGKVKL------------GWPLPKANHRsGVQVAIKLIRRDTQQENCQTskIMREINILKGLTHPNIVRLLDVLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd14076  77 TKKYIGIVLEFVSGGELFDYILARRRLKDSVA----------CRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLV 146

                ....*
gi 62420884 726 IADFG 730
Cdd:cd14076 147 ITDFG 151
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
569-841 3.27e-14

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: 73.47  E-value: 3.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHL-CEVEGMEKFKDKDFALDVSANqpvlvavkmlradANKNARndflKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd08219   8 VGEGSFGRALLvQHVNSDQKYAMKEIRLPKSSS-------------AVEDSR----KEAVLLAKMKHPNIVAFKESFEAD 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSrheppnssssDVRTVSYTNLKFMA--TQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd08219  71 GHLYIVMEYCDGGDLMQKIK----------LQRGKLFPEDTILQwfVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNL---------YSGDYYRIQGRAvlpirwmsWESIllgKFTTASDVWAFGVTLWETFTFcqEQPYSQLSDEQ 796
Cdd:cd08219 141 LGDFGSARLLtspgayactYVGTPYYVPPEI--------WENM---PYNNKSDIWSLGCILYELCTL--KHPFQANSWKN 207
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62420884 797 VIENTGeffrdQGrqTYLPQPAICPDSVYKLMLSCWRRDTKNRPS 841
Cdd:cd08219 208 LILKVC-----QG--SYKPLPSHYSYELRSLIKQMFKRNPRSRPS 245
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
568-733 3.35e-14

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: 73.44  E-value: 3.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLC--EVEGmekfkdkdfaldvsanqpVLVAVKML--RADANKNARNDFLKEIKIMSRLKDPNIIHLLAV 643
Cdd:cd14081   8 TLGKGQTGLVKLAkhCVTG------------------QKVAIKIVnkEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDV 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnLKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd14081  70 YENKKYLYLVLEYVSGGELFDYLVKKGRLTEKEA---------RKFF-RQIISALDYCHSHSICHRDLKPENLLLDEKNN 139
                       170
                ....*....|
gi 62420884 724 IKIADFGMSR 733
Cdd:cd14081 140 IKIADFGMAS 149
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
569-779 3.40e-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: 73.98  E-value: 3.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVlvaVKMLRADANKNarndflkEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd14209   9 LGTGSFGRVMLVRHKETGNY----YAMKILDKQKV---VKLKQVEHTLN-------EKRILQAINFPFLVKLEYSFKDNS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRheppnssssdVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd14209  75 NLYMVMEYVPGGEMFSHLRR----------IGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTD 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 729 FGMSRnlysgdyyRIQGRAVL----PiRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd14209 145 FGFAK--------RVKGRTWTlcgtP-EYLAPEIILSKGYNKAVDWWALGVLIYE 190
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
604-854 3.41e-14

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: 73.76  E-value: 3.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPnssssdvrtvs 683
Cdd:cd06619  28 ILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSLDVYRKIPEHV----------- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 684 ytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGdyyrIQGRAVLPIRWMSWESILLGK 763
Cdd:cd06619  97 ---LGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNS----IAKTYVGTNAYMAPERISGEQ 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 764 FTTASDVWAFGVTLWETFTfcQEQPYSQLSdeqviENTGEFFRDQGRQTYLPQ-PAICPDSVYK-----LMLSCWRRDTK 837
Cdd:cd06619 170 YGIHSDVWSLGISFMELAL--GRFPYPQIQ-----KNQGSLMPLQLLQCIVDEdPPVLPVGQFSekfvhFITQCMRKQPK 242
                       250
                ....*....|....*....
gi 62420884 838 NRPSFQEI--HLLLLQQGD 854
Cdd:cd06619 243 ERPAPENLmdHPFIVQYND 261
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
564-853 4.15e-14

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: 73.90  E-value: 4.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEK--LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARND--FLKEIKIMSRLKDPNIIH 639
Cdd:cd05630   1 TFRQYrvLGKGGFGEVCACQVRATGK----------------MYACKKLEKKRIKKRKGEamALNEKQILEKVNSRFVVS 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLnQFLSRHEPpNSSSSDVRTVsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVG 719
Cdd:cd05630  65 LAYAYETKDALCLVLTLMNGGDL-KFHIYHMG-QAGFPEARAV------FYAAEICCGLEDLHRERIVYRDLKPENILLD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 720 KNYTIKIADFGMSRNLYSGDyyRIQGRaVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQlSDEQVIE 799
Cdd:cd05630 137 DHGHIRISDLGLAVHVPEGQ--TIKGR-VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA--GQSPFQQ-RKKKIKR 210
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 800 NTGEFFRDQGRQTYLPQPAICPDSVYKLM--------LSCW---RRDTKNRPSFQEIHLLLLQQG 853
Cdd:cd05630 211 EEVERLVKEVPEEYSEKFSPQARSLCSMLlckdpaerLGCRgggAREVKEHPLFKKLNFKRLGAG 275
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
594-782 4.45e-14

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: 73.23  E-value: 4.45e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 594 ALDVSANqpVLVAVKMLRADANKNARND-----FLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSR 668
Cdd:cd06630  19 ARDVKTG--TLMAVKQVSFCRNSSSEQEevveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLLSK 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 669 HEPpnssSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYT-IKIADFGMSRNLYS-----GDYyr 742
Cdd:cd06630  97 YGA----FSENVIINYTL------QILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLASkgtgaGEF-- 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 62420884 743 iQGRAVLPIRWMSWEsILLGK-FTTASDVWAFGVTLWETFT 782
Cdd:cd06630 165 -QGQLLGTIAFMAPE-VLRGEqYGRSCDVWSVGCVIIEMAT 203
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
563-845 4.88e-14

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 73.41  E-value: 4.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVH---LCEVEGMEKFKDKDFALDVSANQPVLVAVKMLRAdANKNARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd05076   1 ITQLSHLGQGTRTNIYegrLLVEGSGEPEEDKELVPGRDRGQELRVVLKVLDP-SHHDIALAFFETASLMSQVSHTHLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKF-MATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd05076  80 VHGVCVRGSENIMVEEFVEHGPLDVWLRKE----------KGHVPMAWKFvVARQLASALSYLENKNLVHGNVCAKNILL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 -------GKNYTIKIADFGMSRNLYSGDyyriqgRAVLPIRWMSWESILLG-KFTTASDVWAFGVTLWEtFTFCQEQPYS 790
Cdd:cd05076 150 arlgleeGTSPFIKLSDPGVGLGVLSRE------ERVERIPWIAPECVPGGnSLSTAADKWGFGATLLE-ICFNGEAPLQ 222
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 791 qlsdEQVIENTGEFFRDQGRqtyLPQPAiCPDsVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd05076 223 ----SRTPSEKERFYQRQHR---LPEPS-CPE-LATLISQCLTYEPTQRPSFRTI 268
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
560-804 5.91e-14

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 72.75  E-value: 5.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd14167   2 RDIYDFREVLGTGAFSEVVLAEEKRTQK----------------LVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLsrheppnssssdVRTVSYT--NLKFMATQIASGMKYLSSLNFVHRDLATRNCL 717
Cdd:cd14167  66 LDDIYESGGHLYLIMQLVSGGELFDRI------------VEKGFYTerDASKLIFQILDAVKYLHDMGIVHRDLKPENLL 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 718 ---VGKNYTIKIADFGMSRNLYSGDyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWetFTFCQEQPYSQLSD 794
Cdd:cd14167 134 yysLDEDSKIMISDFGLSKIEGSGS---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY--ILLCGYPPFYDEND 208
                       250
                ....*....|....
gi 62420884 795 ----EQVIENTGEF 804
Cdd:cd14167 209 aklfEQILKAEYEF 222
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
625-782 6.62e-14

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: 73.75  E-value: 6.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 625 EIKIMSRLKD-PNIIHLLAV--CITDDPLCMITEYMEngdlnqflsrheppnsssSDVRTVSYTNL------KFMATQIA 695
Cdd:cd07852  56 EIMFLQELNDhPNIIKLLNVirAENDKDIYLVFEYME------------------TDLHAVIRANIledihkQYIMYQLL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 696 SGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYriQGRAVL----PIRWMSWESILLG--KFTTASD 769
Cdd:cd07852 118 KALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEED--DENPVLtdyvATRWYRAPEILLGstRYTKGVD 195
                       170
                ....*....|...
gi 62420884 770 VWAFGVTLWETFT 782
Cdd:cd07852 196 MWSVGCILGEMLL 208
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
566-732 6.78e-14

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


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 72.59  E-value: 6.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHlcEVEGMEKfkDKDFALDVsanqpvlVAVKMLradANKNARNDFLKEIKIMSRLKDPNIIHLLAvCI 645
Cdd:cd14099   6 GKFLGKGGFAKCY--EVTDMST--GKVYAGKV-------VPKSSL---TKPKQREKLKSEIKIHRSLKHPNIVKFHD-CF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLC-MITEYMENGDLNQFLSR----HEPpnssssdvrTVSYtnlkFMaTQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd14099  71 EDEENVyILLELCSNGSLMELLKRrkalTEP---------EVRY----FM-RQILSGVKYLHSNRIIHRDLKLGNLFLDE 136
                       170
                ....*....|..
gi 62420884 721 NYTIKIADFGMS 732
Cdd:cd14099 137 NMNVKIGDFGLA 148
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
567-817 6.78e-14

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 72.91  E-value: 6.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmEKFKDKDFALDvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd14105  11 EELGSGQFAVVKKCR----EKSTGLEYAAK-------FIKKRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEppnsSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNC-LVGKN---Y 722
Cdd:cd14105  80 KTDVVLILELVAGGELFDFLAEKE----SLSEEEATEFLK------QILDGVNYLHTKNIAHFDLKPENImLLDKNvpiP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGDYYR-IQG--RAVLPiRWMSWESILLgkfttASDVWAFGV---------------TLWETFTFC 784
Cdd:cd14105 150 RIKLIDFGLAHKIEDGNEFKnIFGtpEFVAP-EIVNYEPLGL-----EADMWSIGVityillsgaspflgdTKQETLANI 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 62420884 785 QEQPYSqlSDEQVIENTGEFFRDQGRQTYLPQP 817
Cdd:cd14105 224 TAVNYD--FDDEYFSNTSELAKDFIRQLLVKDP 254
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
605-798 6.92e-14

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: 72.89  E-value: 6.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADANKNARNDFLKEIKIMSRLKD---PNIIHLLAVCITDDPLCMITEYMENGDLNQfLSRHEPpnssssdvrt 681
Cdd:cd06917  29 VALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEGGSIRT-LMRAGP---------- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 682 VSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQgrAVLPIRWMSWESILL 761
Cdd:cd06917  98 IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSKRST--FVGTPYWMAPEVITE 175
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 62420884 762 GK-FTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVI 798
Cdd:cd06917 176 GKyYDTKADIWSLGITTYEMAT--GNPPYSDVDALRAV 211
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
567-840 6.94e-14

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 73.18  E-value: 6.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd07844   6 DKLGEGSYATVY----KGRSKLTGQ------------LVALKEIRLEHEEGAPFTAIREASLLKDLKHANIVTLHDIIHT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENgDLNQFLSRHepPNSsssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd07844  70 KKTLTLVFEYLDT-DLKQYMDDC--GGG-------LSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSR------NLYSGDyyriqgraVLPIrWMSWESILLG--KFTTASDVWAFGVTLWETFTFCQEQPYSQLSDEQVi 798
Cdd:cd07844 140 ADFGLARaksvpsKTYSNE--------VVTL-WYRPPDVLLGstEYSTSLDMWGVGCIFYEMATGRPLFPGSTDVEDQL- 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 62420884 799 entGEFFRDQGRQTYLPQPAICPDSVYKlmlSCWRRDTKNRP 840
Cdd:cd07844 210 ---HKIFRVLGTPTEETWPGVSSNPEFK---PYSFPFYPPRP 245
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
565-778 7.30e-14

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: 72.48  E-value: 7.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLC-EVEGMEKFKDKDFALDVSANQPVlVAVKMLRADANKNARNdfLKEIKIMSRLKDPNIIHLLAV 643
Cdd:cd14077   5 FVKTIGAGSMGKVKLAkHIRTGEKCAIKIIPRASNAGLKK-EREKRLEKEISRDIRT--IREAALSSLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDvrtvsytnlKFmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd14077  82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQAR---------KF-ARQIASALDYLHRNSIVHRDLKIENILISKSGN 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 724 IKIADFGMSrNLYSgdyYRIQGRAVLPIRWMSWESILLGKFTTAS--DVWAFGVTLW 778
Cdd:cd14077 152 IKIIDFGLS-NLYD---PRRLLRTFCGSLYFAAPELLQAQPYTGPevDVWSFGVVLY 204
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
569-800 7.64e-14

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: 73.80  E-value: 7.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVL----VAVKMLradanknarndflkEIKIMSRLKD-PNIIHLLAV 643
Cdd:cd05619  13 LGKGSFGKVFLAELKGTNQF----FAIKALKKDVVLmdddVECTMV--------------EKRVLSLAWEhPFLTHLFCT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLN---QFLSRHEPPNSSssdvrtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd05619  75 FQTKENLFFVMEYLNGGDLMfhiQSCHKFDLPRAT-------------FYAAEIICGLQFLHSKGIVYRDLKLDNILLDK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 NYTIKIADFGMSRNLYSGDyYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIEN 800
Cdd:cd05619 142 DGHIKIADFGMCKENMLGD-AKTSTFCGTP-DYIAPEILLGQKYNTSVDWWSFGVLLYEMLI--GQSPFHGQDEEELFQS 217
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
569-853 7.79e-14

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: 72.77  E-value: 7.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARNDF--LKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05605   8 LGKGGFGEVCACQVRATGK----------------MYACKKLEKKRIKKRKGEAmaLNEKQILEKVNSRFVVSLAYAYET 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05605  72 KDALCLVLTIMNGGDLKFHIYNMGNPGFEEERAV--------FYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDyyRIQGRaVLPIRWMSWESILLGKFTTASDVWAFGVTLWET------FTFCQEQPYSQLSDEQVIEN 800
Cdd:cd05605 144 SDLGLAVEIPEGE--TIRGR-VGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMiegqapFRARKEKVKREEVDRRVKED 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 801 TGEF---FRDQGRQtylpqpaICP---DSVYKLMLSCWR---RDTKNRPSFQEIHLLLLQQG 853
Cdd:cd05605 221 QEEYsekFSEEAKS-------ICSqllQKDPKTRLGCRGegaEDVKSHPFFKSINFKRLEAG 275
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
569-799 8.66e-14

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: 73.50  E-value: 8.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVsANQPVLVAvkmlradanKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd05595   3 LGKGTFGKVILVR----EKATGRYYAMKI-LRKEVIIA---------KDEVAHTVTESRVLQNTRHPFLTALKYAFQTHD 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd05595  69 RLCFVMEYANGGELFFHLSRE----------RVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITD 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 729 FGMSRNLYSgDYYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWEtfTFCQEQPYSQLSDEQVIE 799
Cdd:cd05595 139 FGLCKEGIT-DGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYE--MMCGRLPFYNQDHERLFE 205
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
567-779 8.66e-14

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: 73.19  E-value: 8.66e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd07869  11 EKLGEGSYATVY----KGKSKVNGK------------LVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENgDLNQFLSRHepPNSSSSDvrtvsytNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd07869  75 KETLTLVFEYVHT-DLCQYMDKH--PGGLHPE-------NVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKL 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 727 ADFGMSR------NLYSGDYYRIqgravlpirWMSWESILLG--KFTTASDVWAFGVTLWE 779
Cdd:cd07869 145 ADFGLARaksvpsHTYSNEVVTL---------WYRPPDVLLGstEYSTCLDMWGVGCIFVE 196
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
566-742 8.69e-14

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: 72.39  E-value: 8.69e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCevegMEKFKDKDFA---LDVSANQPVLVAVKMLRadanknarNDFLKEIKIMSRL-KDPNIIHLL 641
Cdd:cd14093   8 KEILGRGVSSTVRRC----IEKETGQEFAvkiIDITGEKSSENEAEELR--------EATRREIEILRQVsGHPNIIELH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSrheppnssssDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14093  76 DVFESPTFIFLVFELCRKGELFDYLT----------EVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDN 145
                       170       180
                ....*....|....*....|.
gi 62420884 722 YTIKIADFGMSRNLYSGDYYR 742
Cdd:cd14093 146 LNVKISDFGFATRLDEGEKLR 166
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
567-845 9.85e-14

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 72.08  E-value: 9.85e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLceveGMekfkdkdfaldvsANQPVLVAVKMLRADAN--KNARNDFLK---EIKIMSRLKDPNIIHLL 641
Cdd:cd06631   7 NVLGKGAYGTVYC----GL-------------TSTGQLIAVKQVELDTSdkEKAEKEYEKlqeEVDLLKTLKHVNIVGYL 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHEPpnssSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd06631  70 GTCLEDNVVSIFMEFVPGGSIASILARFGA----LEEPVFCRYTK------QILEGVAYLHNNNVIHRDIKGNNIMLMPN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFGMSRNLYSGDYYRIQGRAVLPIR----WMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQV 797
Cdd:cd06631 140 GVIKLIDFGCAKRLCINLSSGSQSQLLKSMRgtpyWMAPEVINETGHGRKSDIWSIGCTVFEMAT--GKPPWADMNPMAA 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 62420884 798 IENTGEffrDQGRQTYLPQPAiCPDSVyKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06631 218 IFAIGS---GRKPVPRLPDKF-SPEAR-DFVHACLTRDQDERPSAEQL 260
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
604-849 1.13e-13

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. 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 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-A/B 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: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 72.24  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKML---RADANKNArndfLKEIKIMSRLKDPNIIHLLAVCItdDP--LCMITEYMENGDLNQFLSRHEppnssssd 678
Cdd:cd14042  32 LVAIKKVnkkRIDLTREV----LKELKHMRDLQHDNLTRFIGACV--DPpnICILTEYCPKGSLQDILENED-------- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 679 vrtvsyTNLKFM-----ATQIASGMKYL-SSLNFVHRDLATRNCLVGKNYTIKIADFGMSRnLYSGDYYRIQGRAVLPIR 752
Cdd:cd14042  98 ------IKLDWMfryslIHDIVKGMHYLhDSEIKSHGNLKSSNCVVDSRFVLKITDFGLHS-FRSGQEPPDDSHAYYAKL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 753 -WMSWESILLGKF----TTASDVWAFGVTLWETFTfcQEQPYSQ----LSDEQVIENTgeffRDQGRQTYL-P--QPAIC 820
Cdd:cd14042 171 lWTAPELLRDPNPpppgTQKGDVYSFGIILQEIAT--RQGPFYEegpdLSPKEIIKKK----VRNGEKPPFrPslDELEC 244
                       250       260
                ....*....|....*....|....*....
gi 62420884 821 PDSVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14042 245 PDEVLSLMQRCWAEDPEERPDFSTLRNKL 273
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
605-800 1.14e-13

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: 71.94  E-value: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLradaNKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLS--RHEPPNSsssdVRtv 682
Cdd:cd14010  28 VAIKCV----DKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETLLRqdGNLPESS----VR-- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 sytnlKFmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR----------NLYSGDYYRIQGRAVLPIR 752
Cdd:cd14010  98 -----KF-GRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelfGQFSDEGNVNKVSKKQAKR 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 62420884 753 ----WMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIEN 800
Cdd:cd14010 172 gtpyYMAPELFQGGVHSFASDLWALGCVLYEMFT--GKPPFVAESFTELVEK 221
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
567-797 1.15e-13

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: 72.03  E-value: 1.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegmekfkdkdfaldVSANQPVLVAVKMLRADANKNARNDFLK---------EIKIMSRLKDPNI 637
Cdd:cd06629   7 ELIGKGTYGRVYLA----------------MNATTGEMLAVKQVELPKTSSDRADSRQktvvdalksEIDTLKDLDHPNI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPpnsSSSDVrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCL 717
Cdd:cd06629  71 VQYLGFEETEDYFSIFLEYVPGGSIGSCLRKYGK---FEEDL-------VRFFTRQILDGLAYLHSKGILHRDLKADNIL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 718 VGKNYTIKIADFGMSR---NLYSGDY-YRIQGRavlpIRWMSWESI-LLGKFTTAS-DVWAFGVTLWETFTfcQEQPYSQ 791
Cdd:cd06629 141 VDLEGICKISDFGISKksdDIYGNNGaTSMQGS----VFWMAPEVIhSQGQGYSAKvDIWSLGCVVLEMLA--GRRPWSD 214

                ....*.
gi 62420884 792 lsDEQV 797
Cdd:cd06629 215 --DEAI 218
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
569-845 1.22e-13

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


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 71.90  E-value: 1.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVhlcevegmekfkdKDfALDVSANQpvLVAVKMLRADANK---NARNDFLKEIKIMSRLKDPNIIHLLAVcI 645
Cdd:cd14119   1 LGEGSYGKV-------------KE-VLDTETLC--RRAVKILKKRKLRripNGEANVKREIQILRRLNHRNVIKLVDV-L 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDD---PLCMITEYMeNGDLNQFLSrheppnsSSSDVR-TVSYTNLKFmaTQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14119  64 YNEekqKLYMVMEYC-VGGLQEMLD-------SAPDKRlPIWQAHGYF--VQLIDGLEYLHSQGIIHKDIKPGNLLLTTD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFGMSRNL--YSGDY--YRIQGR-AVLPIRWMSWESILLGKfttASDVWAFGVTLWETFTfcQEQPYSQlsdeq 796
Cdd:cd14119 134 GTLKISDFGVAEALdlFAEDDtcTTSQGSpAFQPPEIANGQDSFSGF---KVDIWSAGVTLYNMTT--GKYPFEG----- 203
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 62420884 797 viENTGEFFRDQGRQTYLpQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14119 204 --DNIYKLFENIGKGEYT-IPDDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
568-798 1.39e-13

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 72.37  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHlcevegmeKFKDKDFAldvsanqpVLVAVKMLRADaNKNARNDFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd06644  19 ELGDGAFGKVY--------KAKNKETG--------ALAAAKVIETK-SEEELEDYMVEIEILATCNHPYIVKLLGAFYWD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd06644  82 GKLWIMIEFCPGGAVDAIMLELD---------RGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMS---------RNLYSGDYYriqgravlpirWMSWESILL-----GKFTTASDVWAFGVTLWETFTFcqEQPYSQLS 793
Cdd:cd06644 153 DFGVSaknvktlqrRDSFIGTPY-----------WMAPEVVMCetmkdTPYDYKADIWSLGITLIEMAQI--EPPHHELN 219

                ....*
gi 62420884 794 DEQVI 798
Cdd:cd06644 220 PMRVL 224
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
569-779 1.39e-13

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: 72.08  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVSANQPVlvaVKMLRADANKNARNdflkeikIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd05612   9 IGTGTFGRVHLVR----DRISEHYYALKVMAIPEV---IRLKQEQHVHNEKR-------VLKEVSHPFIIRLFWTEHDQR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSrheppnssssDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd05612  75 FLYMLMEYVPGGELFSYLR----------NSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTD 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 729 FGMSRNLySGDYYRIQGRAvlpiRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05612 145 FGFAKKL-RDRTWTLCGTP----EYLAPEVIQSKGHNKAVDWWALGILIYE 190
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
567-845 1.57e-13

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: 71.26  E-value: 1.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEK-------FKDKdFALDVSANQPVLVAVKMlradanknarndflkEIKIMSRLKD---PN 636
Cdd:cd14004   6 KEMGEGAYGQVNLAIYKSKGKevvikfiFKER-ILVDTWVRDRKLGTVPL---------------EIHILDTLNKrshPN 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENG-DLNQFLSRHepPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd14004  70 IVKLLDFFEDDEFYYLVMEKHGSGmDLFDFIERK--PNMDEKEAKYIFR--------QVADAVKHLHDQGIVHRDIKDEN 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLVGKNYTIKIADFGMSRNLYSGDYYRIQGravlPIRWMSWEsILLGKFTTAS--DVWAFGVTLWeTFTFcQEQPYSQLs 793
Cdd:cd14004 140 VILDGNGTIKLIDFGSAAYIKSGPFDTFVG----TIDYAAPE-VLRGNPYGGKeqDIWALGVLLY-TLVF-KENPFYNI- 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 62420884 794 deqvientgeffrDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14004 212 -------------EEILEADLRIPYAVSEDLIDLISRMLNRDVGDRPTIEEL 250
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
564-785 1.57e-13

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: 71.92  E-value: 1.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVLVAVKMLRADANKNAR-------------NDFLKEIKIMS 630
Cdd:cd14199   5 KLKDEIGKGSYGVVKLAYNEDDNTY----YAMKVLSKKKLMRQAGFPRRPPPRGARaapegctqprgpiERVYQEIAILK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 631 RLKDPNIIHLLAVciTDDP----LCMITEYMENGdlnqflsrhepPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNF 706
Cdd:cd14199  81 KLDHPNVVKLVEV--LDDPsedhLYMVFELVKQG-----------PVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKI 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 707 VHRDLATRNCLVGKNYTIKIADFGMSrNLYSGDYYRIQGRAVLPIrWMSWES------ILLGKfttASDVWAFGVTLWeT 780
Cdd:cd14199 148 IHRDVKPSNLLVGEDGHIKIADFGVS-NEFEGSDALLTNTVGTPA-FMAPETlsetrkIFSGK---ALDVWAMGVTLY-C 221

                ....*
gi 62420884 781 FTFCQ 785
Cdd:cd14199 222 FVFGQ 226
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
569-775 1.83e-13

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: 71.22  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegMEKFKDKDFALDVsanqpvlvavkmlrADANKNARNDFL--KEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd14184   9 IGDGNFAVVKEC----VERSTGKEFALKI--------------IDKAKCCGKEHLieNEVSILRRVKHPNIIMLIEEMDT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSrheppNSSSSDVRTVSYtnlkfMATQIASGMKYLSSLNFVHRDLATRNCLV----GKNY 722
Cdd:cd14184  71 PAELYLVMELVKGGDLFDAIT-----SSTKYTERDASA-----MVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTK 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 723 TIKIADFGMSrNLYSGDYYRIQGRAVlpirWMSWESILLGKFTTASDVWAFGV 775
Cdd:cd14184 141 SLKLGDFGLA-TVVEGPLYTVCGTPT----YVAPEIIAETGYGLKVDIWAAGV 188
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
559-845 1.85e-13

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: 71.62  E-value: 1.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVhlcevegmekFKDKDfaldvSANQPVlVAVKMLRADANKNARNDFLKEIKIMSRLKDPNII 638
Cdd:cd06640   2 PEELFTKLERIGKGSFGEV----------FKGID-----NRTQQV-VAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVT 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENGDLNQFLsRHEPPNSsssdvrtvsyTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd06640  66 KYYGSYLKGTKLWIIMEYLGGGSALDLL-RAGPFDE----------FQIATMLKEILKGLDYLHSEKKIHRDIKAANVLL 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 GKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVI 798
Cdd:cd06640 135 SEQGDVKLADFGVAGQLTDTQIKR--NTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAK--GEPPNSDMHPMRVL 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 799 ENTGEFfrdqgrqtylPQPAICPD---SVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06640 211 FLIPKN----------NPPTLVGDfskPFKEFIDACLNKDPSFRPTAKEL 250
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
624-843 1.89e-13

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: 71.58  E-value: 1.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 624 KEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSS 703
Cdd:cd14201  54 KEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNGGDLADYLQAKG----------TLSEDTIRVFLQQIAAAMRILHS 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 704 LNFVHRDLATRNCLVG---------KNYTIKIADFGMSRNLYSGdyyriQGRAVL---PIrWMSWESILLGKFTTASDVW 771
Cdd:cd14201 124 KGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYLQSN-----MMAATLcgsPM-YMAPEVIMSQHYDAKADLW 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 772 AFGVTLWETFTfcQEQPYSQLSDEQVientgEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQ 843
Cdd:cd14201 198 SIGTVIYQCLV--GKPPFQANSPQDL-----RMFYEKNKNLQPSIPRETSPYLADLLLGLLQRNQKDRMDFE 262
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
559-779 2.08e-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: 71.98  E-value: 2.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHlcevegmekfkdkdFALDVSANQPVLVAvKMLRADANKNAR-NDFLKEIKIMSRLKDPNI 637
Cdd:cd06634  13 PEKLFSDLREIGHGSFGAVY--------------FARDVRNNEVVAIK-KMSYSGKQSNEKwQDIIKEVKFLQKLRHPNT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMEnGDLNQFLSRHEPPnSSSSDVRTVSYTNLKfmatqiasGMKYLSSLNFVHRDLATRNCL 717
Cdd:cd06634  78 IEYRGCYLREHTAWLVMEYCL-GSASDLLEVHKKP-LQEVEIAAITHGALQ--------GLAYLHSHNMIHRDVKAGNIL 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 718 VGKNYTIKIADFGMSR-----NLYSGDYYriqgravlpirWMSWESILL---GKFTTASDVWAFGVTLWE 779
Cdd:cd06634 148 LTEPGLVKLGDFGSASimapaNSFVGTPY-----------WMAPEVILAmdeGQYDGKVDVWSLGITCIE 206
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
552-799 2.11e-13

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 72.42  E-value: 2.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 552 DVAVEEFPRKLLT---FKEKLGEGQFGEVHLCEvegmEKFKDKDFALDVSANQPVL----VAVKMLRADANKNARNDFLK 624
Cdd:cd05593   3 DASTTHHKRKTMNdfdYLKLLGKGTFGKVILVR----EKASGKYYAMKILKKEVIIakdeVAHTLTESRVLKNTRHPFLT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 625 EIKIMSRlkdpniihllavciTDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSL 704
Cdd:cd05593  79 SLKYSFQ--------------TKDRLCFVMEYVNGGELFFHLSRE----------RVFSEDRTRFYGAEIVSALDYLHSG 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 705 NFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSgDYYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWEtfTFC 784
Cdd:cd05593 135 KIVYRDLKLENLMLDKDGHIKITDFGLCKEGIT-DAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYE--MMC 210
                       250
                ....*....|....*
gi 62420884 785 QEQPYSQLSDEQVIE 799
Cdd:cd05593 211 GRLPFYNQDHEKLFE 225
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
563-793 2.19e-13

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: 71.42  E-value: 2.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHlcevegmekfkdKDFaldvsaNQP--VLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHL 640
Cdd:cd06622   3 IEVLDELGKGNYGSVY------------KVL------HRPtgVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDF 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 LAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVrtvsytnLKFMATQIASGMKYL-SSLNFVHRDLATRNCLVG 719
Cdd:cd06622  65 YGAFFIEGAVYMCMEYMDAGSLDKLYAGGVATEGIPEDV-------LRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVN 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 720 KNYTIKIADFGMSRNLYSGdyyrIQGRAVLPIRWMSWESILLG------KFTTASDVWAFGVTLWETFTFCQEQP----- 788
Cdd:cd06622 138 GNGQVKLCDFGVSGNLVAS----LAKTNIGCQSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEMALGRYPYPpetya 213

                ....*..
gi 62420884 789 --YSQLS 793
Cdd:cd06622 214 niFAQLS 220
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
567-732 2.83e-13

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: 70.91  E-value: 2.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmekfkdkdfaldvSANQPVLV-AVKMLRADANK-NARNDFLKEIKIMSRLKD---PNIIHLL 641
Cdd:cd14052   6 ELIGSGEFSQVYKVS----------------ERVPTGKVyAVKKLKPNYAGaKDRLRRLEEVSILRELTLdghDNIVQLI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHeppnsssSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14052  70 DSWEYHGHLYIQTELCENGSLDVFLSEL-------GLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFE 142
                       170
                ....*....|.
gi 62420884 722 YTIKIADFGMS 732
Cdd:cd14052 143 GTLKIGDFGMA 153
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
566-775 3.02e-13

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: 70.72  E-value: 3.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCevegMEKfkdkdfaldvsaNQPVLVAVKMLRADANKNaRNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14190   9 KEVLGGGKFGKVHTC----TEK------------RTGLKLAAKVINKQNSKD-KEMVLLEIQVMNQLNHRNLIQLYEAIE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLnqfLSRHEPPNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRN--CLVGKNYT 723
Cdd:cd14190  72 TPNEIVLFMEYVEGGEL---FERIVDEDYHLTEVDAMVFVR------QICEGIQFMHQMRVLHLDLKPENilCVNRTGHQ 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 724 IKIADFGMSRnlysgdyyRIQGRAVLPI-----RWMSWESILLGKFTTASDVWAFGV 775
Cdd:cd14190 143 VKIIDFGLAR--------RYNPREKLKVnfgtpEFLSPEVVNYDQVSFPTDMWSMGV 191
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
559-779 3.12e-13

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: 70.55  E-value: 3.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLraDANKNARNDFL-KEIKIMSRLKDPNI 637
Cdd:cd06648   5 PRSDLDNFVKIGEGSTGIVCI--------------ATDKSTGR--QVAVKKM--DLRKQQRRELLfNEVVIMRDYQHPNI 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMENGDLNQFLSR---HEPpnssssDVRTVSYTNLKFMAtqiasgmkYLSSLNFVHRDLATR 714
Cdd:cd06648  67 VEMYSSYLVGDELWVVMEFLEGGALTDIVTHtrmNEE------QIATVCRAVLKALS--------FLHSQGVIHRDIKSD 132
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLySGDYYRIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd06648 133 SILLTSDGRVKLSDFGFCAQV-SKEVPRRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIE 195
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
567-845 3.29e-13

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: 70.61  E-value: 3.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegmekfKDKDfaldvSANQPVLVAVKMLRAdaNKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd08218   6 KKIGEGSFGKALLV--------KSKE-----DGKQYVIKEINISKM--SPKEREESRKEVAVLSKMKHPNIVQYQESFEE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMA--TQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd08218  71 NGNLYIVMDYCDGGDLYKRINAQ----------RGVLFPEDQILDwfVQLCLALKHVHDRKILHRDIKSQNIFLTKDGII 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYS---------GDYYriqgravlpirWMSWESILLGKFTTASDVWAFGVTLWETFTFcqEQPYSQLSDE 795
Cdd:cd08218 141 KLGDFGIARVLNStvelartciGTPY-----------YLSPEICENKPYNNKSDIWALGCVLYEMCTL--KHAFEAGNMK 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 796 QVIENTgeffrdqGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd08218 208 NLVLKI-------IRGSYPPVPSRYSYDLRSLVSQLFKRNPRDRPSINSI 250
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
605-782 3.38e-13

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: 71.73  E-value: 3.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVK---MLRADANKNArndfLKEIKIMSRLKDPNII---HLLAVCITDDP-----------LCMITEYMENgDLNQFLS 667
Cdd:cd07854  33 VAVKkivLTDPQSVKHA----LREIKIIRRLDHDNIVkvyEVLGPSGSDLTedvgsltelnsVYIVQEYMET-DLANVLE 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 668 RHeppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVG-KNYTIKIADFGMSRNL---YSGDYYRI 743
Cdd:cd07854 108 QG-----------PLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLARIVdphYSHKGYLS 176
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 62420884 744 QGravLPIRWMSWESILLG--KFTTASDVWAFGVTLWETFT 782
Cdd:cd07854 177 EG---LVTKWYRSPRLLLSpnNYTKAIDMWAAGCIFAEMLT 214
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
597-778 4.32e-13

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: 70.27  E-value: 4.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 597 VSANQPVLVAVKMLRADANKNA--RNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPns 674
Cdd:cd14186  21 RSLHTGLEVAIKMIDKKAMQKAgmVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMSRYLKNRKKP-- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 675 sssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGD--YYRIQGRAvlpiR 752
Cdd:cd14186  99 -------FTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHekHFTMCGTP----N 167
                       170       180
                ....*....|....*....|....*.
gi 62420884 753 WMSWESILLGKFTTASDVWAFGVTLW 778
Cdd:cd14186 168 YISPEIATRSAHGLESDVWSLGCMFY 193
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
568-779 4.48e-13

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: 71.28  E-value: 4.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVhlCEVEgmekfkdkdfalDVSANQPVLVAVKML-RADANKNARNDFLKEIKIMSRLKD-PNIIHLLAVCI 645
Cdd:cd07857   7 ELGQGAYGIV--CSAR------------NAETSEEETVAIKKItNVFSKKILAKRALRELKLLRHFRGhKNITCLYDMDI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 -TDDPLCMITEYME--NGDLNQFLSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd07857  73 vFPGNFNELYLYEElmEADLHQIIRSGQP----------LTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADC 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 723 TIKIADFGMSRNlYSGDYYRIQGRAV--LPIRWMSWESILLG--KFTTASDVWAFGVTLWE 779
Cdd:cd07857 143 ELKICDFGLARG-FSENPGENAGFMTeyVATRWYRAPEIMLSfqSYTKAIDVWSVGCILAE 202
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
568-774 4.63e-13

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: 71.16  E-value: 4.63e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHlcevegmeKFKDKDfaldvsANQPVLVAVKMLRADANK-------NARndflkEIKIMSRLKDPNIIHL 640
Cdd:cd07842   7 CIGRGTYGRVY--------KAKRKN------GKDGKEYAIKKFKGDKEQytgisqsACR-----EIALLRELKHENVVSL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 LAVCI--TDDPLCMITEYMENgDLNQFLSRHEPPNSSSSDVRTVsytnlKFMATQIASGMKYLSSlNFV-HRDLATRNCL 717
Cdd:cd07842  68 VEVFLehADKSVYLLFDYAEH-DLWQIIKFHRQAKRVSIPPSMV-----KSLLWQILNGIHYLHS-NWVlHRDLKPANIL 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 718 V-GKNY---TIKIADFGMSR-------NLYSGDyyriqgRAVLPIrWMSWESILLGK--FTTASDVWAFG 774
Cdd:cd07842 141 VmGEGPergVVKIGDLGLARlfnaplkPLADLD------PVVVTI-WYRAPELLLGArhYTKAIDIWAIG 203
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
567-845 5.68e-13

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: 69.94  E-value: 5.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLcevegmekfkdkdfALDvSANQpvLVAVKMLR-ADANKNARNDFLKEIKIMSRLKD-PNIIHLLAVC 644
Cdd:cd14131   7 KQLGKGGSSKVYK--------------VLN-PKKK--IYALKRVDlEGADEQTLQSYKNEIELLKKLKGsDRIIQLYDYE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDP--LCMITEYMEnGDLNQFLSRHEPPNSSSSDVRtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNy 722
Cdd:cd14131  70 VTDEDdyLYMVMECGE-IDLATILKKKRPKPIDPNFIR--------YYWKQMLEAVHTIHEEGIVHSDLKPANFLLVKG- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRnlysgdyyRIQGRAVLPIR--------WMSWESILLGKFTT----------ASDVWAFGVTLWEtFTFc 784
Cdd:cd14131 140 RLKLIDFGIAK--------AIQNDTTSIVRdsqvgtlnYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQ-MVY- 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 785 QEQPYSQLSDE----QVIENTGeffrdqgrqTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14131 210 GKTPFQHITNPiaklQAIIDPN---------HEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPEL 265
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
569-796 5.97e-13

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: 70.02  E-value: 5.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegMEKFKDKDFALdvsanqpvlvavKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd14183  14 IGDGNFAVVKEC----VERSTGREYAL------------KIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPT 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRheppnssssdvrTVSYT--NLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY---- 722
Cdd:cd14183  78 ELYLVMELVKGGDLFDAITS------------TNKYTerDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQdgsk 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 723 TIKIADFGMSrNLYSGDYYRIQGRAVlpirWMSWESILLGKFTTASDVWAFGVTLWetFTFCQEQPYSQLSDEQ 796
Cdd:cd14183 146 SLKLGDFGLA-TVVDGPLYTVCGTPT----YVAPEIIAETGYGLKVDIWAAGVITY--ILLCGFPPFRGSGDDQ 212
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
569-779 6.27e-13

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: 69.79  E-value: 6.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevegmekfkdkdFALDVSANQpvLVAVKMLRADANKNAR--NDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd06607   9 IGHGSFGAVY--------------YARNKRTSE--VVAIKKMSYSGKQSTEkwQDIIKEVKFLRQLRHPNTIEYKGCYLR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMEngdlnqflsrheppnSSSSDVRTVSYTNLKfmATQIAS-------GMKYLSSLNFVHRDLATRNCLVG 719
Cdd:cd06607  73 EHTAWLVMEYCL---------------GSASDIVEVHKKPLQ--EVEIAAichgalqGLAYLHSHNRIHRDVKAGNILLT 135
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 720 KNYTIKIADFGMSR-----NLYSGDYYriqgravlpirWMSWESILL---GKFTTASDVWAFGVTLWE 779
Cdd:cd06607 136 EPGTVKLADFGSASlvcpaNSFVGTPY-----------WMAPEVILAmdeGQYDGKVDVWSLGITCIE 192
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
569-779 6.30e-13

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: 70.02  E-value: 6.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLC------EVEGMEKFKDkdfaldvsanqpvlvavkmlrADANKNARNDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:cd07848   9 VGEGAYGVVLKCrhketkEIVAIKKFKD---------------------SEENEEVKETTLRELKMLRTLKQENIVELKE 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLnQFLSRHepPNSSSSD-VRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd07848  68 AFRRRGKLYLVFEYVEKNML-ELLEEM--PNGVPPEkVRSYIY--------QLIKAIHWCHKNDIVHRDIKPENLLISHN 136
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 722 YTIKIADFGMSRNLYSGDyyRIQGRAVLPIRWMSWESILLGK-FTTASDVWAFGVTLWE 779
Cdd:cd07848 137 DVLKLCDFGFARNLSEGS--NANYTEYVATRWYRSPELLLGApYGKAVDMWSVGCILGE 193
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
606-841 6.74e-13

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 70.12  E-value: 6.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 606 AVKMLRADANKNARNDFLK----EIKIMSRLKDPNIIHLLAVC-ITDDPLCMIteyMENGDLNQFlSRHEPPNSSSSDVR 680
Cdd:cd14001  32 AVKKINSKCDKGQRSLYQErlkeEAKILKSLNHPNIVGFRAFTkSEDGSLCLA---MEYGGKSLN-DLIEERYEAGLGPF 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 681 TVSyTNLKfMATQIASGMKYL-SSLNFVHRDLATRNCLVGKNY-TIKIADFGMSRNLY---------SGDYYRIQGravl 749
Cdd:cd14001 108 PAA-TILK-VALSIARALEYLhNEKKILHGDIKSGNVLIKGDFeSVKLCDFGVSLPLTenlevdsdpKAQYVGTEP---- 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 750 pirWMSWESILLGK-FTTASDVWAFGVTLWETFTFcqEQPYSQLSDEQVIENTGEFFRDQ-GRQTYL----PQPAI---C 820
Cdd:cd14001 182 ---WKAKEALEEGGvITDKADIFAYGLVLWEMMTL--SVPHLNLLDIEDDDEDESFDEDEeDEEAYYgtlgTRPALnlgE 256
                       250       260
                ....*....|....*....|....*
gi 62420884 821 PDSVYKLMLS----CWRRDTKNRPS 841
Cdd:cd14001 257 LDDSYQKVIElfyaCTQEDPKDRPS 281
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
605-849 7.36e-13

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 69.50  E-value: 7.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADA---NKNARndflKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPnssssdvrt 681
Cdd:cd14045  33 VAIKKIAKKSftlSKRIR----KEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNEDIP--------- 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 682 vsyTNLKF---MATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSrnLYSGD-------YYRIQGRAVlpi 751
Cdd:cd14045 100 ---LNWGFrfsFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLT--TYRKEdgsenasGYQQRLMQV--- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 752 rWMSWE--SILLGKFTTASDVWAFGVTLWETFT---FCQEQPYSqlSDEQVIENTGEFFRDQGRQTylpqpAICPDSVYK 826
Cdd:cd14045 172 -YLPPEnhSNTDTEPTQATDVYSYAIILLEIATrndPVPEDDYS--LDEAWCPPLPELISGKTENS-----CPCPADYVE 243
                       250       260
                ....*....|....*....|...
gi 62420884 827 LMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14045 244 LIRRCRKNNPAQRPTFEQIKKTL 266
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
563-779 8.07e-13

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: 70.41  E-value: 8.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANknARNDFLKEIKIMSRL-----KDPNI 637
Cdd:cd05616   2 FNFLMVLGKGSFGKVMLAERKGTDE----------------LYAVKILKKDVV--IQDDDVECTMVEKRVlalsgKPPFL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMENGDLN---QFLSRHEPPNSSssdvrtvsytnlkFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05616  64 TQLHSCFQTMDRLYFVMEYVNGGDLMyhiQQVGRFKEPHAV-------------FYAAEIAIGLFFLQSKGIIYRDLKLD 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 715 NCLVGKNYTIKIADFGMSR-NLYSGdyYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05616 131 NVMLDSEGHIKIADFGMCKeNIWDG--VTTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYE 193
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
567-735 8.21e-13

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: 70.34  E-value: 8.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVLVAVKMLRAdanknarndfLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05574   7 KLLGKGDVGRVYLVRLKGTGKL----FAMKVLDKEEMIKRNKVKRV----------LTEREILATLDHPFLPTLYASFQT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRhEPPNSSSSDVrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05574  73 STHLCFVMDYCPGGELFRLLQK-QPGKRLPEEV-------ARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIML 144

                ....*....
gi 62420884 727 ADFGMSRNL 735
Cdd:cd05574 145 TDFDLSKQS 153
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
559-853 8.83e-13

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: 70.01  E-value: 8.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLCEvegmEKFkdkdfaldvSANQpvlVAVKMLraDANKNARNDFL-KEIKIMSRLKDPNI 637
Cdd:cd06659  19 PRQLLENYVKIGEGSTGVVCIAR----EKH---------SGRQ---VAVKMM--DLRKQQRRELLfNEVVIMRDYQHPNV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMENGDLNQFLSRhepPNSSSSDVRTVSYTNLKFMAtqiasgmkYLSSLNFVHRDLATRNCL 717
Cdd:cd06659  81 VEMYKSYLVGEELWVLMEYLQGGALTDIVSQ---TRLNEEQIATVCEAVLQALA--------YLHSQGVIHRDIKSDSIL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 718 VGKNYTIKIADFGMSRNLySGDYYRIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQV 797
Cdd:cd06659 150 LTLDGRVKLSDFGFCAQI-SKDVPKRKSLVGTPY-WMAPEVISRCPYGTEVDIWSLGIMVIEMVD--GEPPYFSDSPVQA 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 798 IENtgefFRDQGRQTYLPQPAICP---DSVYKLMLscwrRDTKNRPSFQEI--HLLLLQQG 853
Cdd:cd06659 226 MKR----LRDSPPPKLKNSHKASPvlrDFLERMLV----RDPQERATAQELldHPFLLQTG 278
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
569-804 1.08e-12

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: 69.64  E-value: 1.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARND--FLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05631   8 LGKGGFGEVCACQVRATGK----------------MYACKKLEKKRIKKRKGEamALNEKRILEKVNSRFVVSLAYAYET 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLsrHEPPNSSSSDVRTVsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05631  72 KDALCLVLTIMNGGDLKFHI--YNMGNPGFDEQRAI------FYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRI 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDyyRIQGRaVLPIRWMSWESILLGKFTTASDVWAFGVTLWET------FTFCQEQPYSQLSDEQVIEN 800
Cdd:cd05631 144 SDLGLAVQIPEGE--TVRGR-VGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMiqgqspFRKRKERVKREEVDRRVKED 220

                ....
gi 62420884 801 TGEF 804
Cdd:cd05631 221 QEEY 224
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
567-849 1.53e-12

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: 68.84  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMekfkdkdfaldvsanqpvlVAVKMLRADA-NKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14152   6 ELIGQGRWGKVHRGRWHGE-------------------VAIRLLEIDGnNQDHLKLFKKEVMNYRQTRHENVVLFMGACM 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLsrHEPPNSsssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIk 725
Cdd:cd14152  67 HPPHLAIITSFCKGRTLYSFV--RDPKTS-------LDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVV- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IAD---FGMSRNLYSGdyyRIQGRAVLPIRWMSW------ESILLGK------FTTASDVWAFGvTLWETFTfCQEQPYS 790
Cdd:cd14152 137 ITDfglFGISGVVQEG---RRENELKLPHDWLCYlapeivREMTPGKdedclpFSKAADVYAFG-TIWYELQ-ARDWPLK 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 791 QLSDEQVIENTGEffrDQGRQTYLPQPAICPDsVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14152 212 NQPAEALIWQIGS---GEGMKQVLTTISLGKE-VTEILSACWAFDLEERPSFTLLMDML 266
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
564-732 1.55e-12

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: 68.52  E-value: 1.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLceveGMEKF-KDKdfaldvsanqpvlVAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd14075   5 RIRGELGSGNFSQVKL----GIHQLtKEK-------------VAIKILdKTKLDQKTQRLLSREISSMEKLHHPNIIRLY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14075  68 EVVETLSKLHLVMEYASGGELYTKISTEGKLSESEA----------KPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN 137
                       170
                ....*....|.
gi 62420884 722 YTIKIADFGMS 732
Cdd:cd14075 138 NCVKVGDFGFS 148
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
559-789 1.58e-12

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: 68.98  E-value: 1.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVLVAVKMLRADANKNArndFLKEIKIMSRLKDPNII 638
Cdd:cd06654  18 PKKKYTRFEKIGQGASGTVYT--------------AMDVATGQEVAIRQMNLQQQPKKEL---IINEILVMRENKNPNIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENGDLNQFLSRheppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd06654  81 NYLDSYLVGDELWVVMEYLAGGSLTDVVTE-----------TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 719 GKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPY 789
Cdd:cd06654 150 GMDGSVKLTDFGFCAQITPEQSKR--STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIE--GEPPY 216
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
567-844 1.61e-12

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: 68.51  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmEKFKDKDFALDVsanqpvlvaVKMLRADANKN--ARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14194  11 EELGSGQFAVVKKCR----EKSTGLQYAAKF---------IKKRRTKSSRRgvSREDIEREVSILKEIQHPNVITLHEVY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHEppnSSSSDVRTvsytnlKFMaTQIASGMKYLSSLNFVHRDLATRNC-LVGKNYT 723
Cdd:cd14194  78 ENKTDVILILELVAGGELFDFLAEKE---SLTEEEAT------EFL-KQILNGVYYLHSLQIAHFDLKPENImLLDRNVP 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 ---IKIADFGMSRNLYSG-DYYRIQGRA--VLPiRWMSWESILLgkfttASDVWAFGVTLWetFTFCQEQPYSQLSDEQV 797
Cdd:cd14194 148 kprIKIIDFGLAHKIDFGnEFKNIFGTPefVAP-EIVNYEPLGL-----EADMWSIGVITY--ILLSGASPFLGDTKQET 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 62420884 798 IENTGEFFRDQGRQTYLPQPAICPDSVYKLMLscwrRDTKNRPSFQE 844
Cdd:cd14194 220 LANVSAVNYEFEDEYFSNTSALAKDFIRRLLV----KDPKKRMTIQD 262
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
568-798 2.04e-12

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: 68.51  E-value: 2.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHlcevegmeKFKDKDFAldvsanqpVLVAVKMLRADANKNARnDFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd06643  12 ELGDGAFGKVY--------KAQNKETG--------ILAAAKVIDTKSEEELE-DYMVEIDILASCDHPNIVKLLDAFYYE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd06643  75 NNLWILIEFCAGGAVDAVMLELE---------RPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMS---------RNLYSGDYYriqgravlpirWMSWESILLGK-----FTTASDVWAFGVTLWETFTFcqEQPYSQLS 793
Cdd:cd06643 146 DFGVSakntrtlqrRDSFIGTPY-----------WMAPEVVMCETskdrpYDYKADVWSLGVTLIEMAQI--EPPHHELN 212

                ....*
gi 62420884 794 DEQVI 798
Cdd:cd06643 213 PMRVL 217
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
559-789 2.12e-12

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: 68.60  E-value: 2.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVLVAVKMLRADANKNArndFLKEIKIMSRLKDPNII 638
Cdd:cd06655  17 PKKKYTRYEKIGQGASGTVFT--------------AIDVATGQEVAIKQINLQKQPKKEL---IINEILVMKELKNPNIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENGDLNQFLSRheppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd06655  80 NFLDSFLVGDELFVVMEYLAGGSLTDVVTE-----------TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLL 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 719 GKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPY 789
Cdd:cd06655 149 GMDGSVKLTDFGFCAQITPEQSKR--STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE--GEPPY 215
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
559-789 2.29e-12

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: 68.59  E-value: 2.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVLVAVKMLRADANKNArndFLKEIKIMSRLKDPNII 638
Cdd:cd06656  17 PKKKYTRFEKIGQGASGTVYT--------------AIDIATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENGDLNQFLSRheppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd06656  80 NYLDSYLVGDELWVVMEYLAGGSLTDVVTE-----------TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 719 GKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPY 789
Cdd:cd06656 149 GMDGSVKLTDFGFCAQITPEQSKR--STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE--GEPPY 215
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
567-798 2.39e-12

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: 68.06  E-value: 2.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegmekfKDKdfaldVSANQPVLVAVKMLRADANKNARNDflKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd08225   6 KKIGEGSFGKIYLA--------KAK-----SDSEHCVIKEIDLTKMPVKEKEASK--KEVILLAKMKHPNIVTFFASFQE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMA--TQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd08225  71 NGRLFIVMEYCDGGDLMKRINRQ----------RGVLFSEDQILSwfVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMV 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 725 -KIADFGMSRNLysGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcqEQPYSQLSDEQVI 798
Cdd:cd08225 141 aKLGDFGIARQL--NDSMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTL--KHPFEGNNLHQLV 211
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
564-853 2.48e-12

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: 68.84  E-value: 2.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEK--LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARND--FLKEIKIMSRLKDPNIIH 639
Cdd:cd05632   3 TFRQYrvLGKGGFGEVCACQVRATGK----------------MYACKRLEKKRIKKRKGEsmALNEKQILEKVNSQFVVN 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLsrHEPPNSSSSDVRTVsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVG 719
Cdd:cd05632  67 LAYAYETKDALCLVLTIMNGGDLKFHI--YNMGNPGFEEERAL------FYAAEILCGLEDLHRENTVYRDLKPENILLD 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 720 KNYTIKIADFGMSRNLYSGDyyRIQGRaVLPIRWMSWESILLGKFTTASDVWAFGVTLWET------FTFCQEQPYSQLS 793
Cdd:cd05632 139 DYGHIRISDLGLAVKIPEGE--SIRGR-VGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMiegqspFRGRKEKVKREEV 215
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 794 DEQVIENTGEF---FRDQGRQtyLPQPAICPDSvyKLMLSCWRR---DTKNRPSFQEIHLLLLQQG 853
Cdd:cd05632 216 DRRVLETEEVYsakFSEEAKS--ICKMLLTKDP--KQRLGCQEEgagEVKRHPFFRNMNFKRLEAG 277
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
565-845 2.72e-12

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: 67.95  E-value: 2.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHlcevegmeKFKDKdfaldvsANQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNI------I 638
Cdd:cd08217   4 VLETIGKGSFGTVR--------KVRRK-------SDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIvryydrI 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCItddpLCMITEYMENGDLNQFLSRHEPPNSSSSDvRTVsytnLKFMaTQIASGMKYLSSLN-----FVHRDLAT 713
Cdd:cd08217  69 VDRANTT----LYIVMEYCEGGDLAQLIKKCKKENQYIPE-EFI----WKIF-TQLLLALYECHNRSvgggkILHRDLKP 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMSRNLYSGD----------YYriqgravlpirwMSWESILLGKFTTASDVWAFGVTLWEtftF 783
Cdd:cd08217 139 ANIFLDSDNNVKLGDFGLARVLSHDSsfaktyvgtpYY------------MSPELLNEQSYDEKSDIWSLGCLIYE---L 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 784 CQEQP----YSQLSDEQVIeNTGEFfrdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd08217 204 CALHPpfqaANQLELAKKI-KEGKF---------PRIPSRYSSELNEVIKSMLNVDPDKRPSVEEL 259
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
565-778 2.74e-12

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: 68.05  E-value: 2.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCEVEGmekfKDKDFALDVSANQPVLVAVKMLR---ADANKNARNDFLK----------EIKIMSR 631
Cdd:cd14200   4 LQSEIGKGSYGVVKLAYNES----DDKYYAMKVLSKKKLLKQYGFPRrppPRGSKAAQGEQAKplaplervyqEIAILKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 632 LKDPNIIHLLAVciTDDP----LCMITEYMENGDLNQFlsrhePPNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFV 707
Cdd:cd14200  80 LDHVNIVKLIEV--LDDPaednLYMVFDLLRKGPVMEV-----PSDKPFSEDQARLYFR------DIVLGIEYLHYQKIV 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 708 HRDLATRNCLVGKNYTIKIADFGMSrNLYSGDYYRIQGRAVLPIrWMSWESI------LLGKfttASDVWAFGVTLW 778
Cdd:cd14200 147 HRDIKPSNLLLGDDGHVKIADFGVS-NQFEGNDALLSSTAGTPA-FMAPETLsdsgqsFSGK---ALDVWAMGVTLY 218
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
567-778 3.73e-12

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: 67.85  E-value: 3.73e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVhlcevegmekFKdkdfALDVSANQPVlVAVKMLR-ADAN-----KNARNDFLKEIKIMSRLKDPNIIHL 640
Cdd:cd14096   7 NKIGEGAFSNV----------YK----AVPLRNTGKP-VAIKVVRkADLSsdnlkGSSRANILKEVQIMKRLSHPNIVKL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 LAVCITDDPLCMITEYMENGDL-NQF---------LSRHeppnssssdvrtvsytnlkfMATQIASGMKYLSSLNFVHRD 710
Cdd:cd14096  72 LDFQESDEYYYIVLELADGGEIfHQIvrltyfsedLSRH--------------------VITQVASAVKYLHEIGVVHRD 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 711 LATRNCL------------------------------------VGKnytIKIADFGMSRNLYSGDyyriqgrAVLP---I 751
Cdd:cd14096 132 IKPENLLfepipfipsivklrkadddetkvdegefipgvggggIGI---VKLADFGLSKQVWDSN-------TKTPcgtV 201
                       250       260
                ....*....|....*....|....*..
gi 62420884 752 RWMSWESILLGKFTTASDVWAFGVTLW 778
Cdd:cd14096 202 GYTAPEVVKDERYSKKVDMWALGCVLY 228
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
564-845 3.81e-12

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: 67.33  E-value: 3.81e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVhlcevegmekFKDKdfaldvSANQPVLVAVKMLRA-DANKNARNDFLKEIKIMSRLKD-PNIIHLL 641
Cdd:cd14050   4 TILSKLGEGSFGEV----------FKVR------SREDGKLYAVKRSRSrFRGEKDRKRKLEEVERHEKLGEhPNCVRFI 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMEnGDLNQFLSRHeppnSSSSDVRTVSYTnlkfmaTQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14050  68 KAWEEKGILYIQTELCD-TSLQQYCEET----HSLPESEVWNIL------LDLLKGLKHLHDHGLIHLDIKPANIFLSKD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFGMSRNLYSGDYYRIQ-GRAvlpiRWMSWEsILLGKFTTASDVWAFGVTLWETFTfcqeqpysqlsDEQVIEN 800
Cdd:cd14050 137 GVCKLGDFGLVVELDKEDIHDAQeGDP----RYMAPE-LLQGSFTKAADIFSLGITILELAC-----------NLELPSG 200
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 801 tGEFFRdQGRQTYLPQP---AICPD--SVYKLMLScwrRDTKNRPSFQEI 845
Cdd:cd14050 201 -GDGWH-QLRQGYLPEEftaGLSPElrSIIKLMMD---PDPERRPTAEDL 245
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
625-804 3.89e-12

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: 67.28  E-value: 3.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 625 EIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLsrheppnssssdVRTVSYT--NLKFMATQIASGMKYLS 702
Cdd:cd14185  48 EILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFDAI------------IESVKFTehDAALMIIDLCEALVYIH 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 703 SLNFVHRDLATRNCLVGKN----YTIKIADFGMSRnLYSGDYYRIQGRA--VLPirwmsweSILLGK-FTTASDVWAFGV 775
Cdd:cd14185 116 SKHIVHRDLKPENLLVQHNpdksTTLKLADFGLAK-YVTGPIFTVCGTPtyVAP-------EILSEKgYGLEVDMWAAGV 187
                       170       180       190
                ....*....|....*....|....*....|....
gi 62420884 776 TLWetFTFCQEQPY-SQLSDE----QVIEnTGEF 804
Cdd:cd14185 188 ILY--ILLCGFPPFrSPERDQeelfQIIQ-LGHY 218
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
569-779 4.32e-12

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: 67.29  E-value: 4.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvEGMEKFKdkdFALDVsanqpvLVAVKMLRADANKNARndflKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd14116  13 LGKGKFGNVYLAR-EKQSKFI---LALKV------LFKAQLEKAGVEHQLR----REVEIQSHLRHPNILRLYGYFHDAT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHeppnSSSSDVRTVSYTnlkfmaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIAD 728
Cdd:cd14116  79 RVYLILEYAPLGTVYRELQKL----SKFDEQRTATYI------TELANALSYCHSKRVIHRDIKPENLLLGSAGELKIAD 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 62420884 729 FGMSRNLYSGDYYRIQGravlPIRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd14116 149 FGWSVHAPSSRRTTLCG----TLDYLPPEMIEGRMHDEKVDLWSLGVLCYE 195
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
566-779 5.08e-12

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: 67.75  E-value: 5.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVH--LCEVEGmekfkdkdfaldvsanqpVLVAVKMLR----ADANknARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd08229  29 EKKIGRGQFSEVYraTCLLDG------------------VPVALKKVQifdlMDAK--ARADCIKEIDLLKQLNHPNVIK 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLNQFLsRHEPPNSSSSDVRTVsytnLKFMaTQIASGMKYLSSLNFVHRDLATRNCLVG 719
Cdd:cd08229  89 YYASFIEDNELNIVLELADAGDLSRMI-KHFKKQKRLIPEKTV----WKYF-VQLCSALEHMHSRRVMHRDIKPANVFIT 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 720 KNYTIKIADFGMSRnLYSGDYYRIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd08229 163 ATGVVKLGDLGLGR-FFSSKTTAAHSLVGTPY-YMSPERIHENGYNFKSDIWSLGCLLYE 220
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
563-845 5.20e-12

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks 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 Jak3 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: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 66.85  E-value: 5.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHlcevEGMEKFKDKDFALDVsanqPVLVAVkmlrADAN-KNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd14208   1 LTFMESLGKGSFTKIY----RGLRTDEEDDERCET----EVLLKV----MDPThGNCQESFLEAASIMSQISHKHLVLLH 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLcMITEYMENGDLNQFLSR--HEPPNSSSSDVRTVSytnlkfmatQIASGMKYLSSLNFVHRDLATRNCLV- 718
Cdd:cd14208  69 GVCVGKDSI-MVQEFVCHGALDLYLKKqqQKGPVAISWKLQVVK---------QLAYALNYLEDKQLVHGNVSAKKVLLs 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 -----GKNYTIKIADFGMSRNLYSGDYYriqgraVLPIRWMSWESILLGK-FTTASDVWAFGVTLWETFT-----FCQEQ 787
Cdd:cd14208 139 regdkGSPPFIKLSDPGVSIKVLDEELL------AERIPWVAPECLSDPQnLALEADKWGFGATLWEIFSgghmpLSALD 212
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 788 PYSQLsdeqvientgEFFRDqgRQTyLPQPAICpdSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14208 213 PSKKL----------QFYND--RKQ-LPAPHWI--ELASLIQQCMSYNPLLRPSFRAI 255
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
569-779 5.23e-12

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: 67.80  E-value: 5.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVL----VAVKMLradanknarndflkEIKIMS-RLKDPNIIHLLAV 643
Cdd:cd05592   3 LGKGSFGKVMLAELKGTNQY----FAIKALKKDVVLedddVECTMI--------------ERRVLAlASQHPFLTHLFCT 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLnQFlsrHEPPNSSSSDVRTvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd05592  65 FQTESHLFFVMEYLNGGDL-MF---HIQQSGRFDEDRA------RFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGH 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 724 IKIADFGMSR-NLYSG----------DYyriqgravlpirwMSWEsILLG-KFTTASDVWAFGVTLWE 779
Cdd:cd05592 135 IKIADFGMCKeNIYGEnkastfcgtpDY-------------IAPE-ILKGqKYNQSVDWWSFGVLLYE 188
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
566-775 5.34e-12

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: 66.99  E-value: 5.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCevegMEKFKDKDFAldvsanqpvlvaVKMLRA-DANKNARNDFLKEIKIMSRLKD-PNIIHLLAV 643
Cdd:cd14106  13 STPLGRGKFAVVRKC----IHKETGKEYA------------AKFLRKrRRGQDCRNEILHEIAVLELCKDcPRVVNLHEV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLSRHEPPnsSSSDVRtvsytnlKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd14106  77 YETRSELILILELAAGGELQTLLDEEECL--TEADVR-------RLM-RQILEGVQYLHERNIVHLDLKPQNILLTSEFP 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 724 ---IKIADFGMSRNLYSG-DYYRIQGRA--VLPiRWMSWESIllgkfTTASDVWAFGV 775
Cdd:cd14106 147 lgdIKLCDFGISRVIGEGeEIREILGTPdyVAP-EILSYEPI-----SLATDMWSIGV 198
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
569-779 5.46e-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: 67.66  E-value: 5.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdfaldvsanqpvlVAVKMLRADA---NKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05620   3 LGKGSFGKVLLAELKGKGEY----------------FAVKALKKDVvliDDDVECTMVEKRVLALAWENPFLTHLYCTFQ 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSrheppnssssDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05620  67 TKEHLFFVMEFLNGGDLMFHIQ----------DKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIK 136
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 726 IADFGMSRNLYSGDyYRIQGRAVLPiRWMSWEsILLG-KFTTASDVWAFGVTLWE 779
Cdd:cd05620 137 IADFGMCKENVFGD-NRASTFCGTP-DYIAPE-ILQGlKYTFSVDWWSFGVLLYE 188
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
569-731 6.06e-12

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: 67.77  E-value: 6.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKdfaldvsanqpvLVAVKMLRADA--NKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05571   3 LGKGTFGKVILCR----EKATGE------------LYAIKILKKEViiAKDEVAHTLTENRVLQNTRHPFLTSLKYSFQT 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05571  67 NDRLCFVMEYVNGGELFFHLSRE----------RVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKI 136

                ....*
gi 62420884 727 ADFGM 731
Cdd:cd05571 137 TDFGL 141
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
568-783 6.08e-12

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: 67.30  E-value: 6.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEvegmeKFKDKDFaldvsanqpvlVAVKMLRADANKNARNDFLKEIKIMSRLKD-PNIIHLLAVcIT 646
Cdd:cd07831   6 KIGEGTFSEVLKAQ-----SRKTGKY-----------YAIKCMKKHFKSLEQVNNLREIQALRRLSPhPNILRLIEV-LF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDP---LCMITEYMengDLNQF---LSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVgK 720
Cdd:cd07831  69 DRKtgrLALVFELM---DMNLYeliKGRKRP----------LPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-K 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 721 NYTIKIADFGMSRNLYSGDYYRIqgraVLPIRWMSWESILL--GKFTTASDVWAFGVTLWETFTF 783
Cdd:cd07831 135 DDILKLADFGSCRGIYSKPPYTE----YISTRWYRAPECLLtdGYYGPKMDIWAVGCVFFEILSL 195
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
563-845 6.29e-12

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: 67.06  E-value: 6.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVhlcevegmEKFKDKdfaldvsaNQPVLVAVKMLRADANKNARNDFLKEIKIMSRLKD-PNIIHLL 641
Cdd:cd06617   3 LEVIEELGRGAYGVV--------DKMRHV--------PTGTIMAVKRIRATVNSQEQKRLLMDLDISMRSVDcPYTVTFY 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCIT--DDPLCMitEYMENGdLNQFLSR-HEPPNSSSSDVrtvsytnLKFMATQIASGMKYL-SSLNFVHRDLATRNCL 717
Cdd:cd06617  67 GALFRegDVWICM--EVMDTS-LDKFYKKvYDKGLTIPEDI-------LGKIAVSIVKALEYLhSKLSVIHRDVKPSNVL 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 718 VGKNYTIKIADFGMSRNLYSgDYYRIQGRAVLPirWMSWESI----LLGKFTTASDVWAFGVTLWE--TFTFCQEQ---P 788
Cdd:cd06617 137 INRNGQVKLCDFGISGYLVD-SVAKTIDAGCKP--YMAPERInpelNQKGYDVKSDVWSLGITMIElaTGRFPYDSwktP 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 789 YSQLsdEQVIEntgeffrdqGRQTYLPQPAICPDSVYkLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06617 214 FQQL--KQVVE---------EPSPQLPAEKFSPEFQD-FVNKCLKKNYKERPNYPEL 258
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
567-780 7.00e-12

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: 66.91  E-value: 7.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLradankNARND--FLKEIKIMSR--LKDPNIIHLLA 642
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRGEK------------------VAVKIF------SSRDEdsWFRETEIYQTvmLRHENILGFIA 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLC----MITEYMENGDLNQFLSRHEppnssssdVRTVSYTNLkfmATQIASGMKYL--------SSLNFVHRD 710
Cdd:cd14056  57 ADIKSTGSWtqlwLITEYHEHGSLYDYLQRNT--------LDTEEALRL---AYSAASGLAHLhteivgtqGKPAIAHRD 125
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 711 LATRNCLVGKNYTIKIADFGMSRNLYSgdyyriqGRAVLPI---------RWMSWEsILLGKFTT-------ASDVWAFG 774
Cdd:cd14056 126 LKSKNILVKRDGTCCIADLGLAVRYDS-------DTNTIDIppnprvgtkRYMAPE-VLDDSINPksfesfkMADIYSFG 197

                ....*.
gi 62420884 775 VTLWET 780
Cdd:cd14056 198 LVLWEI 203
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
567-733 7.12e-12

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: 66.48  E-value: 7.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmekfkDKDFALDVSAnqpvlvavKMLRADANKNaRNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd14193  10 EILGGGRFGQVHKCE--------EKSSGLKLAA--------KIIKARSQKE-KEEVKNEIEVMNQLNHANLIQLYDAFES 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLnqfLSRHEPPNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRN--CLVGKNYTI 724
Cdd:cd14193  73 RNDIVLVMEYVDGGEL---FDRIIDENYNLTELDTILFIK------QICEGIQYMHQMYILHLDLKPENilCVSREANQV 143

                ....*....
gi 62420884 725 KIADFGMSR 733
Cdd:cd14193 144 KIIDFGLAR 152
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
564-797 7.45e-12

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: 66.84  E-value: 7.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAV 643
Cdd:cd14169   6 ELKEKLGEGAFSEVVLAQERGSQR----------------LVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDL-NQFLSRHEPPNSSSSDVrtvsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLVG--- 719
Cdd:cd14169  70 YESPTHLYLAMELVTGGELfDRIIERGSYTEKDASQL-----------IGQVLQAVKYLHQLGIVHRDLKPENLLYAtpf 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 720 KNYTIKIADFGMSRNLYSGdyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWetFTFCQEQPYSQLSDEQV 797
Cdd:cd14169 139 EDSKIMISDFGLSKIEAQG----MLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISY--ILLCGYPPFYDENDSEL 210
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
569-804 7.98e-12

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: 66.57  E-value: 7.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegmekfkdkdfALDVSANQPVLVAVKMLRADANKNARNDFLK----EIKIMSRLKDPNIIHLLAVC 644
Cdd:cd13990   8 LGKGGFSEVYK--------------AFDLVEQRYVACKIHQLNKDWSEEKKQNYIKhalrEYEIHKSLDHPRIVKLYDVF 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 -ITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLN--FVHRDLATRNCLVGKN 721
Cdd:cd13990  74 eIDTDSFCTVLEYCDGNDLDFYLKQH----------KSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YT---IKIADFGMSRnLYSGDYYRIQGravlpirwMSWESILLG-----------------KFTTASDVWAFGVTLWETF 781
Cdd:cd13990 144 NVsgeIKITDFGLSK-IMDDESYNSDG--------MELTSQGAGtywylppecfvvgktppKISSKVDVWSVGVIFYQML 214
                       250       260
                ....*....|....*....|....*....
gi 62420884 782 ----TFCQEQPYSQLSDEQVIEN--TGEF 804
Cdd:cd13990 215 ygrkPFGHNQSQEAILEENTILKatEVEF 243
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
605-782 8.17e-12

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 66.91  E-value: 8.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADANKNARNDFLKEIKIMSRLKDPNII-------HLLAVCITDDPLcMITEYMENGDLNQFLSRHEppnsSSS 677
Cdd:cd14038  22 VAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVaardvpeGLQKLAPNDLPL-LAMEYCQGGDLRKYLNQFE----NCC 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 678 DVRTVSYTNLkfmATQIASGMKYLSSLNFVHRDLATRNCLV--GKNYTI-KIADFGMSRNLYSGDyyrIQGRAVLPIRWM 754
Cdd:cd14038  97 GLREGAILTL---LSDISSALRYLHENRIIHRDLKPENIVLqqGEQRLIhKIIDLGYAKELDQGS---LCTSFVGTLQYL 170
                       170       180
                ....*....|....*....|....*...
gi 62420884 755 SWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14038 171 APELLEQQKYTVTVDYWSFGTLAFECIT 198
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
614-785 9.75e-12

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: 65.91  E-value: 9.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 614 ANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYtnlkfmatQ 693
Cdd:cd08221  38 LSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQLFPEEVVLWYLY--------Q 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 694 IASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSgdYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAF 773
Cdd:cd08221 110 IVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDS--ESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAV 187
                       170
                ....*....|..
gi 62420884 774 GVTLWETFTFCQ 785
Cdd:cd08221 188 GCVLYELLTLKR 199
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
569-779 1.08e-11

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: 66.44  E-value: 1.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNaRNDF---LKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05608   9 LGKGGFGEVSACQMRATGK----------------LYACKKLNKKRLKK-RKGYegaMVEKRILAKVHSRFIVSLAYAFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTnlkfmaTQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05608  72 TKTDLCLVMTIMNGGDLRYHIYNVDEENPGFQEPRACFYT------AQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVR 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 62420884 726 IADFGMSRNLYSGDyYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05608 146 ISDLGLAVELKDGQ-TKTKGYAGTP-GFMAPELLLGEEYDYSVDYFTLGVTLYE 197
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
567-782 1.10e-11

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: 66.80  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegmekfkdkdfaLDVSANQpvLVAVKMLRadaN-KNARNDFLKEIKIMSRLKD------PNIIH 639
Cdd:cd14210  19 SVLGKGSFGQVVKC--------------LDHKTGQ--LVAIKIIR---NkKRFHQQALVEVKILKHLNDndpddkHNIVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEyMENGDLNQFLSRHEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRN---C 716
Cdd:cd14210  80 YKDSFIFRGHLCIVFE-LLSINLYELLKSNNFQGLSLSLIRKF--------AKQILQALQFLHKLNIIHCDLKPENillK 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 717 LVGKNyTIKIADFGMS----RNLYSgdYyrIQGRAvlpirWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14210 151 QPSKS-SIKVIDFGSScfegEKVYT--Y--IQSRF-----YRAPEVILGLPYDTAIDMWSLGCILAELYT 210
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
606-779 1.18e-11

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: 65.96  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 606 AVKMLRA---DANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLnqflsrheppnssSSDVRTV 682
Cdd:cd05611  25 AIKVLKKsdmIAKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDC-------------ASLIKTL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 SYTNLKFMATQIAS---GMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGdyyRIQGRAVLPIRWMSWESI 759
Cdd:cd05611  92 GGLPEDWAKQYIAEvvlGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEK---RHNKKFVGTPDYLAPETI 168
                       170       180
                ....*....|....*....|
gi 62420884 760 LLGKFTTASDVWAFGVTLWE 779
Cdd:cd05611 169 LGVGDDKMSDWWSLGCVIFE 188
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
623-774 1.44e-11

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 67.08  E-value: 1.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 623 LKEIKIMSRLKDPNIIHLLAVCITDDPLC-----MITEYMENgDLNQFLSRhePPNSSSSDVRTVSYtnlkfmatQIASG 697
Cdd:cd07853  47 FRELKMLCFFKHDNVLSALDILQPPHIDPfeeiyVVTELMQS-DLHKIIVS--PQPLSSDHVKVFLY--------QILRG 115
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 698 MKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRnLYSGDYYRIQGRAVLPIRWMSWEsILLG--KFTTASDVWAFG 774
Cdd:cd07853 116 LKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLAR-VEEPDESKHMTQEVVTQYYRAPE-ILMGsrHYTSAVDIWSVG 192
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
569-779 1.45e-11

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: 66.09  E-value: 1.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegmekFKDKDFALdvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAV----- 643
Cdd:cd14039   1 LGTGGFGNVCL--------YQNQETGE--------KIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVpeemn 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 -CITDDPLcMITEYMENGDLNQFLSRhePPNSSSsdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCL---VG 719
Cdd:cd14039  65 fLVNDVPL-LAMEYCSGGDLRKLLNK--PENCCG-----LKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVlqeIN 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 720 KNYTIKIADFGMSRNLYSGDyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd14039 137 GKIVHKIIDLGYAKDLDQGS---LCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
604-779 1.54e-11

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 66.77  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  604 LVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPpnsSSSDVrtvs 683
Cdd:PLN00034 101 LYALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLEGTHIADEQ---FLADV---- 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  684 ytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLysGDYYRIQGRAVLPIRWMSWESILL-- 761
Cdd:PLN00034 174 -------ARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL--AQTMDPCNSSVGTIAYMSPERINTdl 244
                        170       180
                 ....*....|....*....|.
gi 62420884  762 --GKFT-TASDVWAFGVTLWE 779
Cdd:PLN00034 245 nhGAYDgYAGDIWSLGVSILE 265
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
624-845 1.57e-11

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: 65.46  E-value: 1.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 624 KEIKIMSRLKDPNIIHLLAVCIT--DDP----LCMITEYMENGDLNQFLSRheppnssssdVRTVSYTNLKFMATQIASG 697
Cdd:cd14012  47 KELESLKKLRHPNLVSYLAFSIErrGRSdgwkVYLLTEYAPGGSLSELLDS----------VGSVPLDTARRWTLQLLEA 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 698 MKYLSSLNFVHRDLATRNCLVGKN---YTIKIADFGMSRNLYSGDYYRIQgRAVLPIRWMSWESILLGK-FTTASDVWAF 773
Cdd:cd14012 117 LEYLHRNGVVHKSLHAGNVLLDRDagtGIVKLTDYSLGKTLLDMCSRGSL-DEFKQTYWLPPELAQGSKsPTRKTDVWDL 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 774 GVTLWET-FTFCQEQPYSQLSDeqvientgeffrdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14012 196 GLLFLQMlFGLDVLEKYTSPNP-------------------VLVSLDLSASLQDFLSKCLSLDPKKRPTALEL 249
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
566-778 1.61e-11

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: 65.91  E-value: 1.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCevegMEKFKDKDFALDVsanqpvlVAVKMLRA-DANKNARndflkEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14086   6 KEELGKGAFSVVRRC----VQKSTGQEFAAKI-------INTKKLSArDHQKLER-----EARICRLLKHPNIVRLHDSI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDL-NQFLSRHEPPNSSSSdvrtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVG---K 720
Cdd:cd14086  70 SEEGFHYLVFDLVTGGELfEDIVAREFYSEADAS-----------HCIQQILESVNHCHQNGIVHRDLKPENLLLAsksK 138
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 721 NYTIKIADFGMSRNLySGDYYRIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLW 778
Cdd:cd14086 139 GAAVKLADFGLAIEV-QGDQQAWFGFAGTPG-YLSPEVLRKDPYGKPVDIWACGVILY 194
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
569-845 1.61e-11

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: 65.87  E-value: 1.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfKDKDFALDVSANQpvlVAVKMLRADANKNArNDFLKEIKIMSRLKDPNIIHLLAvCITD- 647
Cdd:cd06651  15 LGQGAFGRVYLC--------YDVDTGRELAAKQ---VQFDPESPETSKEV-SALECEIQLLKNLQHERIVQYYG-CLRDr 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 --DPLCMITEYMENGDLNQFLSRHeppnSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd06651  82 aeKTLTIFMEYMPGGSVKDQLKAY----GALTESVTRKYTR------QILEGMSYLHSNMIVHRDIKGANILRDSAGNVK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNLYSGDYYRIQGRAVLPI-RWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLsdeqviENTGEF 804
Cdd:cd06651 152 LGDFGASKRLQTICMSGTGIRSVTGTpYWMSPEVISGEGYGRKADVWSLGCTVVEMLT--EKPPWAEY------EAMAAI 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 62420884 805 FRDQGRQTYLPQPAICPDSVyKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06651 224 FKIATQPTNPQLPSHISEHA-RDFLGCIFVEARHRPSAEEL 263
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
569-782 1.63e-11

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: 66.27  E-value: 1.63e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegMEKFKDKDfaldvsANQpvLVAVKMLRaDANKNARNDFLK--EIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05582   3 LGQGSFGKVFL-----VRKITGPD------AGT--LYAMKVLK-KATLKVRDRVRTkmERDILADVNHPFIVKLHYAFQT 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHeppnssssdvrtVSYT--NLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd05582  69 EGKLYLILDFLRGGDLFTRLSKE------------VMFTeeDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHI 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 725 KIADFGMSRNLYSGD--YYRIQGravlPIRWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd05582 137 KLTDFGLSKESIDHEkkAYSFCG----TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT 192
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
569-849 1.82e-11

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 65.36  E-value: 1.82e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLradaNKNARNDFLK-EIKIMSRLKDPNIIHLLAVCITd 647
Cdd:cd14068   2 LGDGGFGSVYRAVYRGED------------------VAVKIF----NKHTSFRLLRqELVVLSHLHHPSLVALLAAGTA- 58
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 dPLCMITEYMENGDLNQFLsRHEppnsSSSDVRTVSYTnlkfMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT---- 723
Cdd:cd14068  59 -PRMLVMELAPKGSLDALL-QQD----NASLTRTLQHR----IALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPncai 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 -IKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILlgkFTTASDVWAFGVTLWETFTfCQEqpysQLSDEQVIENTG 802
Cdd:cd14068 129 iAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVARGNVI---YNQQADVYSFGLLLYDILT-CGE----RIVEGLKFPNEF 200
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 803 EFFRDQGRqtyLPQP------AICPDsVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14068 201 DELAIQGK---LPDPvkeygcAPWPG-VEALIKDCLKENPQCRPTSAQVFDIL 249
pknD PRK13184
serine/threonine-protein kinase PknD;
568-803 1.82e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 67.87  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  568 KLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVlvAVKMLRADANKNA--RNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:PRK13184   9 LIGKGGMGEVYL--------------AYDPVCSRRV--ALKKIREDLSENPllKKRFLREAKIAADLIHPGIVPVYSICS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  646 TDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDV--RTVSYTNLKFMATqIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:PRK13184  73 DGDPVYYTMPYIEGYTLKSLLKSVWQKESLSKELaeKTSVGAFLSIFHK-ICATIEYVHSKGVLHRDLKPDNILLGLFGE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  724 IKIADFG------------------MSRNLYSGdyYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTFcq 785
Cdd:PRK13184 152 VVILDWGaaifkkleeedlldidvdERNICYSS--MTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTL-- 227
                        250       260
                 ....*....|....*....|...
gi 62420884  786 EQPY-----SQLSDEQVIENTGE 803
Cdd:PRK13184 228 SFPYrrkkgRKISYRDVILSPIE 250
PHA02988 PHA02988
hypothetical protein; Provisional
622-845 2.27e-11

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 65.53  E-value: 2.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  622 FLKEIKIMSRLKDPNIIHLLAVCI-TDDPLC---MITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASG 697
Cdd:PHA02988  65 TENEIKNLRRIDSNNILKIYGFIIdIVDDLPrlsLILEYCTRGYLREVLDKE----------KDLSFKTKLDMAIDCCKG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  698 MKYL-SSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSwesILLGKFTTASDVWAFGVT 776
Cdd:PHA02988 135 LYNLyKYTNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKNVNFMVYFSYKMLN---DIFSEYTIKDDIYSLGVV 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884  777 LWETFTFCqeQPYSQLSDEQ----VIENTGEffrdqgrqtyLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:PHA02988 212 LWEIFTGK--IPFENLTTKEiydlIINKNNS----------LKLPLDCPLEIKCIVEACTSHDSIKRPNIKEI 272
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
605-845 3.13e-11

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


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 64.43  E-value: 3.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRA-DANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLsrHEPPNSSSSDVRTVS 683
Cdd:cd14057  21 IVAKILKVrDVTTRISRDFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSLYNVL--HEGTGVVVDQSQAVK 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 684 YtnlkfmATQIASGMKYLSSLN--FVHRDLATRNCLVGKNYTIKI--ADFGMSrnlysgdyYRIQGRAVLPIrWMSWESI 759
Cdd:cd14057  99 F------ALDIARGMAFLHTLEplIPRHHLNSKHVMIDEDMTARInmADVKFS--------FQEPGKMYNPA-WMAPEAL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 760 LLGKFTT---ASDVWAFGVTLWETFTfcQEQPYSQLSDEQVientGEFFRDQGRQTYLPqPAICPdSVYKLMLSCWRRDT 836
Cdd:cd14057 164 QKKPEDInrrSADMWSFAILLWELVT--REVPFADLSNMEI----GMKIALEGLRVTIP-PGISP-HMCKLMKICMNEDP 235

                ....*....
gi 62420884 837 KNRPSFQEI 845
Cdd:cd14057 236 GKRPKFDMI 244
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
569-845 3.59e-11

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: 64.68  E-value: 3.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfkdkdfaLDVSANQPVLVAVKMLRADANKNAR--NDFLKEIKIMSRLKDPNIIHLLAvCIT 646
Cdd:cd06652  10 LGQGAFGRVYLC--------------YDADTGRELAVKQVQFDPESPETSKevNALECEIQLLKNLLHERIVQYYG-CLR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDP---LCMITEYMENGDLNQFLSRHeppnSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd06652  75 DPQertLSIFMEYMPGGSIKDQLKSY----GALTENVTRKYTR------QILEGVHYLHSNMIVHRDIKGANILRDSVGN 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 IKIADFGMSRNLYSgdyYRIQGRAVLPIR----WMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLsdeqviE 799
Cdd:cd06652 145 VKLGDFGASKRLQT---ICLSGTGMKSVTgtpyWMSPEVISGEGYGRKADIWSVGCTVVEMLT--EKPPWAEF------E 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 62420884 800 NTGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWrRDTKNRPSFQEI 845
Cdd:cd06652 214 AMAAIFKIATQPTNPQLPAHVSDHCRDFLKRIF-VEAKLRPSADEL 258
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
569-791 4.37e-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: 64.28  E-value: 4.37e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfKDKDFALDVSANQ-PvlvavkmLRADANKNAR--NDFLKEIKIMSRLKDPNIIHLLAvCI 645
Cdd:cd06653  10 LGRGAFGEVYLC--------YDADTGRELAVKQvP-------FDPDSQETSKevNALECEIQLLKNLRHDRIVQYYG-CL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TD---DPLCMITEYMENGDLNQFLSRHeppnSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd06653  74 RDpeeKKLSIFVEYMPGGSVKDQLKAY----GALTENVTRRYTR------QILQGVSYLHSNMIVHRDIKGANILRDSAG 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 723 TIKIADFGMSRnlysgdyyRIQ-----GRAVLPIR----WMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQ 791
Cdd:cd06653 144 NVKLGDFGASK--------RIQticmsGTGIKSVTgtpyWMSPEVISGEGYGRKADVWSVACTVVEMLT--EKPPWAE 211
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
560-803 4.46e-11

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: 64.63  E-value: 4.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEvegmEKFKDKDFALDvsanqpvlvAVKMLRADANKNARNdflkEIKIMSRLKDPNIIH 639
Cdd:cd14166   2 RETFIFMEVLGSGAFSEVYLVK----QRSTGKLYALK---------CIKKSPLSRDSSLEN----EIAVLKRIKHENIVT 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDL-NQFLSRHEPPNSSSSDVrtvsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd14166  65 LEDIYESTTHYYLVMQLVSGGELfDRILERGVYTEKDASRV-----------INQVLSAVKYLHENGIVHRDLKPENLLY 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 ---GKNYTIKIADFGMSRNLYSGdyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWetFTFCQEQPYSQLSDE 795
Cdd:cd14166 134 ltpDENSKIMITDFGLSKMEQNG----IMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITY--ILLCGYPPFYEETES 207

                ....*...
gi 62420884 796 QVIENTGE 803
Cdd:cd14166 208 RLFEKIKE 215
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
559-789 4.72e-11

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: 64.18  E-value: 4.72e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVLVAVKMLRADANKNArndFLKEIKIMSRLKDPNII 638
Cdd:cd06647   5 PKKKYTRFEKIGQGASGTVYT--------------AIDVATGQEVAIKQMNLQQQPKKEL---IINEILVMRENKNPNIV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDDPLCMITEYMENGDLnqflsrheppnsssSDVRTVSYTNLKFMAT---QIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd06647  68 NYLDSYLVGDELWVVMEYLAGGSL--------------TDVVTETCMDEGQIAAvcrECLQALEFLHSNQVIHRDIKSDN 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 716 CLVGKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPY 789
Cdd:cd06647 134 ILLGMDGSVKLTDFGFCAQITPEQSKR--STMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVE--GEPPY 203
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
555-802 6.22e-11

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: 65.01  E-value: 6.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 555 VEEFPRKLlTFKEKLGEGQFGEVhlCevegmekfkdkdFALDVSANQPVlvAVKMLRA--DANKNARNDFlKEIKIMSRL 632
Cdd:cd07851  10 VWEVPDRY-QNLSPVGSGAYGQV--C------------SAFDTKTGRKV--AIKKLSRpfQSAIHAKRTY-RELRLLKHM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 633 KDPNIIHLLAVCITDDPL------CMITEYMeNGDLNQFLSRheppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNF 706
Cdd:cd07851  72 KHENVIGLLDVFTPASSLedfqdvYLVTHLM-GADLNNIVKC-----------QKLSDDHIQFLVYQILRGLKYIHSAGI 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 707 VHRDLATRNCLVGKNYTIKIADFGMSRNLYSgdyyRIQGRAVlpIRWMSWESILL--GKFTTASDVWAFGVTLWETFT-- 782
Cdd:cd07851 140 IHRDLKPSNLAVNEDCELKILDFGLARHTDD----EMTGYVA--TRWYRAPEIMLnwMHYNQTVDIWSVGCIMAELLTgk 213
                       250       260
                ....*....|....*....|..
gi 62420884 783 --FCQEQPYSQLSdeQVIENTG 802
Cdd:cd07851 214 tlFPGSDHIDQLK--RIMNLVG 233
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
567-733 6.67e-11

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: 63.83  E-value: 6.67e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmekfkdkdfalDVSANQPVlvAVKMLRADANKNaRNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd14192  10 EVLGGGRFGQVHKCT--------------ELSTGLTL--AAKIIKVKGAKE-REEVKNEINIMNQLNHVNLIQLYDAFES 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLnqfLSRHEPPNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRN--CLVGKNYTI 724
Cdd:cd14192  73 KTNLTLIMEYVDGGEL---FDRITDESYQLTELDAILFTR------QICEGVHYLHQHYILHLDLKPENilCVNSTGNQI 143

                ....*....
gi 62420884 725 KIADFGMSR 733
Cdd:cd14192 144 KIIDFGLAR 152
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
569-845 6.85e-11

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: 63.58  E-value: 6.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegmekfkdkdfALDVSANqpVLVAVKMLradANKNARN--DFLKEIKIMSRLKDPNIIHLLAvCIT 646
Cdd:cd06624  16 LGKGTFGVVYA--------------ARDLSTQ--VRIAIKEI---PERDSREvqPLHEEIALHSRLSHKNIVQYLG-SVS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMIteYMEngdlnqflsrHEPPNSSSSDVRT------VSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVgK 720
Cdd:cd06624  76 EDGFFKI--FME----------QVPGGSLSALLRSkwgplkDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLV-N 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 NYT--IKIADFGMSRNL---------YSGDyyriqgravlpIRWMSWESILLGK--FTTASDVWAFGVTLWETFTfcQEQ 787
Cdd:cd06624 143 TYSgvVKISDFGTSKRLaginpctetFTGT-----------LQYMAPEVIDKGQrgYGPPADIWSLGCTIIEMAT--GKP 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 788 PYSQLSDEQvientGEFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06624 210 PFIELGEPQ-----AAMFKVGMFKIHPEIPESLSEEAKSFILRCFEPDPDKRATASDL 262
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
567-779 7.06e-11

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: 64.09  E-value: 7.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevegmeKFKDKdfaldvsaNQPVLVAVKMLRADANKNA-RNDFLKEIKIMSRL-KDPNIIHLLAVC 644
Cdd:cd07837   7 EKIGEGTYGKVY--------KARDK--------NTGKLVALKKTRLEMEEEGvPSTALREVSLLQMLsQSIYIVRLLDVE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDP----LCMITEYMENgDLNQFLSRHEPPNSSSSDVRTVSytnlKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd07837  71 HVEENgkplLYLVFEYLDT-DLKKFIDSYGRGPHNPLPAKTIQ----SFM-YQLCKGVAHCHSHGVMHRDLKPQNLLVDK 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 721 NY-TIKIADFGMSRNLysgdyyriqgraVLPIR---------WMSWESILLG--KFTTASDVWAFGVTLWE 779
Cdd:cd07837 145 QKgLLKIADLGLGRAF------------TIPIKsytheivtlWYRAPEVLLGstHYSTPVDMWSVGCIFAE 203
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
569-799 8.41e-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: 64.67  E-value: 8.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVSANQpVLVAvkmlradanKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd05594  33 LGKGTFGKVILVK----EKATGRYYAMKILKKE-VIVA---------KDEVAHTLTENRVLQNSRHPFLTALKYSFQTHD 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 PLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYL-SSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd05594  99 RLCFVMEYANGGELFFHLSRE----------RVFSEDRARFYGAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKIT 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 728 DFGMSRNLYSgDYYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWEtfTFCQEQPYSQLSDEQVIE 799
Cdd:cd05594 169 DFGLCKEGIK-DGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYE--MMCGRLPFYNQDHEKLFE 236
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
606-775 8.92e-11

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: 63.32  E-value: 8.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 606 AVKMLraDANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDL-NQFLSRHeppNSSSSDVRTVsy 684
Cdd:cd14087  30 AIKMI--ETKCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELfDRIIAKG---SFTERDATRV-- 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 685 tnLKFMATqiasGMKYLSSLNFVHRDLATRNCLV---GKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPiRWMSWESILL 761
Cdd:cd14087 103 --LQMVLD----GVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKKGPNCLMKTTCGTP-EYIAPEILLR 175
                       170
                ....*....|....
gi 62420884 762 GKFTTASDVWAFGV 775
Cdd:cd14087 176 KPYTQSVDMWAVGV 189
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
569-823 9.32e-11

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: 63.93  E-value: 9.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegmekfkdkdfALDVSANQPVLVAVKML----RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14041  14 LGRGGFSEVYK--------------AFDLTEQRYVAVKIHQLnknwRDEKKENYHKHACREYRIHKELDHPRIVKLYDYF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITD-DPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLN--FVHRDLATRNCLVGKN 721
Cdd:cd14041  80 SLDtDSFCTVLEYCEGNDLDFYLKQH----------KLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YT---IKIADFGMSRNLYSGDYYRIQGRAVLP-----IRWMSWESILLG----KFTTASDVWAFGVTLWETFTfcQEQPY 789
Cdd:cd14041 150 TAcgeIKITDFGLSKIMDDDSYNSVDGMELTSqgagtYWYLPPECFVVGkeppKISNKVDVWSVGVIFYQCLY--GRKPF 227
                       250       260       270
                ....*....|....*....|....*....|....
gi 62420884 790 SQLSDEQVIENTGEFFRDQGRQtYLPQPAICPDS 823
Cdd:cd14041 228 GHNQSQQDILQENTILKATEVQ-FPPKPVVTPEA 260
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
560-804 1.09e-10

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: 63.16  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd14083   2 RDKYEFKEVLGTGAFSEVVLAEDKATGK----------------LVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAvcITDDP--LCMITEYMENGDLNQFLsrheppnssssdVRTVSYT--NLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd14083  66 LLD--IYESKshLYLVMELVTGGELFDRI------------VEKGSYTekDASHLIRQVLEAVDYLHSLGIVHRDLKPEN 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 716 CLV---GKNYTIKIADFGMSRNLYSGdyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWetFTFCQEQPYSQL 792
Cdd:cd14083 132 LLYyspDEDSKIMISDFGLSKMEDSG----VMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISY--ILLCGYPPFYDE 205
                       250
                ....*....|....*.
gi 62420884 793 SD----EQVIENTGEF 804
Cdd:cd14083 206 NDsklfAQILKAEYEF 221
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
697-846 1.11e-10

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. 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 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-2D 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: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 63.19  E-value: 1.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 697 GMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMsrnlysGDYYRIQgRAVLPIR------WMSWESI----LLGKFTT 766
Cdd:cd14043 109 GMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGY------NEILEAQ-NLPLPEPapeellWTAPELLrdprLERRGTF 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 767 ASDVWAFGVTLWEtfTFCQEQPY--SQLSDEQVIENTgeffrdqGRQTYLPQPAICPDS----VYKLMLSCWRRDTKNRP 840
Cdd:cd14043 182 PGDVFSFAIIMQE--VIVRGAPYcmLGLSPEEIIEKV-------RSPPPLCRPSVSMDQapleCIQLMKQCWSEAPERRP 252

                ....*.
gi 62420884 841 SFQEIH 846
Cdd:cd14043 253 TFDQIF 258
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
569-848 1.20e-10

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: 63.12  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegmekfkdkdfALDVSANQpVLVAVKMLRADANKNarNDFLKEIKIMSRL-KDPNIIHLLAVCITD 647
Cdd:cd13985   8 LGEGGFSYVYL--------------AHDVNTGR-RYALKRMYFNDEEQL--RVAIKEIEIMKRLcGHPNIVQYYDSAILS 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DP----LCMITEYMEnGDLNQFLSRHEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLN--FVHRDLATRNCLVGKN 721
Cdd:cd13985  71 SEgrkeVLLLMEYCP-GSLVDILEKSPPSPLSEEEVLRIFY--------QICQAVGHLHSQSppIIHRDIKIENILFSNT 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YTIKIADFG-MSRNLYSgdYYRIQGRAVLPIRWMSW--------ESI-LLGKF--TTASDVWAFGVTLWETFTFcqEQPY 789
Cdd:cd13985 142 GRFKLCDFGsATTEHYP--LERAEEVNIIEEEIQKNttpmyrapEMIdLYSKKpiGEKADIWALGCLLYKLCFF--KLPF 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 790 sqlsDEQVIentgefFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPS-FQEIHLL 848
Cdd:cd13985 218 ----DESSK------LAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAERPDiFQVINII 267
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
567-817 1.25e-10

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: 63.10  E-value: 1.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEvegmEKFKDKDFALDvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd14195  11 EELGSGQFAIVRKCR----EKGTGKEYAAK-------FIKKRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFEN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEppnSSSSDVRTvsytnlKFMaTQIASGMKYLSSLNFVHRDLATRNCLV----GKNY 722
Cdd:cd14195  80 KTDVVLILELVSGGELFDFLAEKE---SLTEEEAT------QFL-KQILDGVHYLHSKRIAHFDLKPENIMLldknVPNP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGDYYR-IQGRAvlpiRWMSWESILLGKFTTASDVWAFGVTLWETFT----FCQEQPYSQLS---- 793
Cdd:cd14195 150 RIKLIDFGIAHKIEAGNEFKnIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLSgaspFLGETKQETLTnisa 225
                       250       260
                ....*....|....*....|....*....
gi 62420884 794 -----DEQVIENTGEFFRDQGRQTYLPQP 817
Cdd:cd14195 226 vnydfDEEYFSNTSELAKDFIRRLLVKDP 254
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
564-782 1.27e-10

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: 62.84  E-value: 1.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLCEvegmEKFKDKDFALDvsanqpvlvavKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAV 643
Cdd:cd08223   3 QFLRVIGKGSYGEVWLVR----HKRDRKQYVIK-----------KLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKES 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMIT-EYMENGDLNQFLSRHEPPNSSSSDVrtVSYtnlkFMatQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd08223  68 FEGEDGFLYIVmGFCEGGDLYTRLKEQKGVLLEERQV--VEW----FV--QIAMALQYMHERNILHRDLKTQNIFLTKSN 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSRNLYSGdyYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd08223 140 IIKVGDLGIARVLESS--SDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMAT 197
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
559-775 1.34e-10

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: 62.92  E-value: 1.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLCEVEGMEK-FKDKDFALDVSANQPVLVAVKMLRAdanknarndfLKEIKIMSrlkdpni 637
Cdd:cd14111   1 PQKPYTFLDEKARGRFGVIRRCRENATGKnFPAKIVPYQAEEKQGVLQEYEILKS----------LHHERIMA------- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 ihLLAVCITDDPLCMITEYMENGDLNQFLS---RHeppnsSSSDVrtVSYTnlkfmaTQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd14111  64 --LHEAYITPRYLVLIAEFCSGKELLHSLIdrfRY-----SEDDV--VGYL------VQILQGLEYLHGRRVLHLDIKPD 128
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 715 NCLVGKNYTIKIADFGmSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGV 775
Cdd:cd14111 129 NIMVTNLNAIKIVDFG-SAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGV 188
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
570-779 1.37e-10

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: 62.66  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 570 GEGQFGEVhlCEVEgmEKFKDKDFALDVSANQPVLvavkmlradaNKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDP 649
Cdd:cd05578   9 GKGSFGKV--CIVQ--KKDTKKMFAMKYMNKQKCI----------EKDSVRNVLNELEILQELEHPFLVNLWYSFQDEED 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 650 LCMITEYMENGDLNQFLSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADF 729
Cdd:cd05578  75 MYMVVDLLLGGDLRYHLQQKVK----------FSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDF 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 62420884 730 GMSRNLYSGDYyrIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05578 145 NIATKLTDGTL--ATSTSGTKP-YMAPEVFMRAGYSFAVDWWSLGVTAYE 191
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
564-849 1.56e-10

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: 62.51  E-value: 1.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFK--EKLGEGQFGEVhlCEVEgmEKFKDKDFAldvsanqpvlvaVKMLRADANKNARndflkEIKIMSRLKDPNIIHLL 641
Cdd:cd14047   7 DFKeiELIGSGGFGQV--FKAK--HRIDGKTYA------------IKRVKLNNEKAER-----EVKALAKLDHPNIVRYN 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AvCITDDPLCMIT-----------------EYMENGDLNQFLSRHEppnssssdvrtvSYTNLKFMAT----QIASGMKY 700
Cdd:cd14047  66 G-CWDGFDYDPETsssnssrsktkclfiqmEFCEKGTLESWIEKRN------------GEKLDKVLALeifeQITKGVEY 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 701 LSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLySGDYYRIQGRAVLpiRWMSWESILLGKFTTASDVWAFGVTLWET 780
Cdd:cd14047 133 IHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVTSL-KNDGKRTKSKGTL--SYMSPEQISSQDYGKEVDIYALGLILFEL 209
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 781 FTFCQEqpysqlsdeqvIENTGEFFRDQgRQTYLPqPAICP-----DSVYKLMLScwrRDTKNRPSFQEIHLLL 849
Cdd:cd14047 210 LHVCDS-----------AFEKSKFWTDL-RNGILP-DIFDKrykieKTIIKKMLS---KKPEDRPNASEILRTL 267
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
569-779 1.58e-10

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: 63.46  E-value: 1.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmekfKDKDfaldvsANQpvLVAVKMLRADA--NKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05573   9 IGRGAFGEVWLV--------RDKD------TGQ--VYAMKILRKSDmlKREQIAHVRAERDILADADSPWIVRLHYAFQD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHeppnssssDVRTVSYTnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05573  73 EDHLYLVMEYMPGGDLMNLLIKY--------DVFPEETA--RFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGD---YYRIQGR------AVLPIRW------------------MSWEsILLG-KFTTASDVWAFGVTLW 778
Cdd:cd05573 143 ADFGLCTKMNKSGdreSYLNDSVntlfqdNVLARRRphkqrrvraysavgtpdyIAPE-VLRGtGYGPECDWWSLGVILY 221

                .
gi 62420884 779 E 779
Cdd:cd05573 222 E 222
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
560-799 1.64e-10

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: 63.14  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 560 RKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIH 639
Cdd:cd14168   9 KKIFEFKEVLGTGAFSEVVLAEERATGK----------------LFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLAVCITDDPLCMITEYMENGDLnqFLSRHEPPNSSSSDVRTvsytnlkfMATQIASGMKYLSSLNFVHRDLATRNCLV- 718
Cdd:cd14168  73 LEDIYESPNHLYLVMQLVSGGEL--FDRIVEKGFYTEKDAST--------LIRQVLDAVYYLHRMGIVHRDLKPENLLYf 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 --GKNYTIKIADFGMSRNLYSGDyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWetFTFCQEQPYSQLSDEQ 796
Cdd:cd14168 143 sqDEESKIMISDFGLSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY--ILLCGYPPFYDENDSK 217

                ...
gi 62420884 797 VIE 799
Cdd:cd14168 218 LFE 220
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
594-779 1.76e-10

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 63.36  E-value: 1.76e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 594 ALDVSANQPVLVAVKMLRADANKNARNDFlKEIKIMSRLKDPNIIHLLAVCITD-DPLCMITEYMENgDLNQFLSrhepp 672
Cdd:cd07856  29 ARDQLTGQNVAVKKIMKPFSTPVLAKRTY-RELKLLKHLRHENIISLSDIFISPlEDIYFVTELLGT-DLHRLLT----- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 673 nssssdVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR-------NLYSGDYYRIqg 745
Cdd:cd07856 102 ------SRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARiqdpqmtGYVSTRYYRA-- 173
                       170       180       190
                ....*....|....*....|....*....|....
gi 62420884 746 ravlPIRWMSWEsillgKFTTASDVWAFGVTLWE 779
Cdd:cd07856 174 ----PEIMLTWQ-----KYDVEVDIWSAGCIFAE 198
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
568-782 2.11e-10

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: 62.26  E-value: 2.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCevegMEKFKDKDFAldvsanqpvlvAVKMLRADANKNARNDFLKEIKIMSRLKD-PNIIHLLAVCIT 646
Cdd:cd14197  16 ELGRGKFAVVRKC----VEKDSGKEFA-----------AKFMRKRRKGQDCRMEIIHEIAVLELAQAnPWVINLHEVYET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDL-NQFLSRHEppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT-- 723
Cdd:cd14197  81 ASEMILVLEYAAGGEIfNQCVADRE---------EAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPlg 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 724 -IKIADFGMSRNLYSGDYYR-IQG--RAVLPiRWMSWESIllgkfTTASDVWAFGVTLWETFT 782
Cdd:cd14197 152 dIKIVDFGLSRILKNSEELReIMGtpEYVAP-EILSYEPI-----STATDMWSIGVLAYVMLT 208
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
605-782 2.15e-10

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: 63.26  E-value: 2.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLR------ADANKnarndFLKEIKIMSRLKDPNIIHLLAVCITDDP-----LCMITEYMENgDLNQFLSrheppn 673
Cdd:cd07859  28 VAIKKINdvfehvSDATR-----ILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdIYVVFELMES-DLHQVIK------ 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 674 sSSSDVRTVSYtnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRW 753
Cdd:cd07859  96 -ANDDLTPEHH---QFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAIFWTDYVATRW 171
                       170       180       190
                ....*....|....*....|....*....|..
gi 62420884 754 MSWESI---LLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd07859 172 YRAPELcgsFFSKYTPAIDIWSIGCIFAEVLT 203
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
603-779 2.51e-10

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: 62.45  E-value: 2.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 603 VLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRheppnssssdVRTV 682
Cdd:cd06615  27 LIMARKLIHLEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKK----------AGRI 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 SYTNLKFMATQIASGMKYL-SSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLysgdyyrIQGRA---VLPIRWMSWES 758
Cdd:cd06615  97 PENILGKISIAVLRGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQL-------IDSMAnsfVGTRSYMSPER 169
                       170       180
                ....*....|....*....|.
gi 62420884 759 ILLGKFTTASDVWAFGVTLWE 779
Cdd:cd06615 170 LQGTHYTVQSDIWSLGLSLVE 190
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
567-733 2.77e-10

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 63.66  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  567 EKLGEGqfgevhlceveGM-EKFKDKDFALDVsanqpvLVAVKMLRAD--ANKNARNDFLKEIKIMSRLKDPNIihllaV 643
Cdd:NF033483  13 ERIGRG-----------GMaEVYLAKDTRLDR------DVAVKVLRPDlaRDPEFVARFRREAQSAASLSHPNI-----V 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  644 CITD----DP---LCMitEYMENGDLNQFLSRHEP-PNSsssdvRTVSYTnlkfmaTQIASGMKYLSSLNFVHRDLATRN 715
Cdd:NF033483  71 SVYDvgedGGipyIVM--EYVDGRTLKDYIREHGPlSPE-----EAVEIM------IQILSALEHAHRNGIVHRDIKPQN 137
                        170
                 ....*....|....*...
gi 62420884  716 CLVGKNYTIKIADFGMSR 733
Cdd:NF033483 138 ILITKDGRVKVTDFGIAR 155
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
561-845 2.98e-10

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: 61.94  E-value: 2.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 561 KLLTFKEKLGEGQFGEVHlcevEGMekfkDKDFALDVSANQpvLVAVKMLRADanknaRNDFLKEIKIMSRLKDPNIIHL 640
Cdd:cd14033   1 RFLKFNIEIGRGSFKTVY----RGL----DTETTVEVAWCE--LQTRKLSKGE-----RQRFSEEVEMLKGLQHPNIVRF 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 L---------AVCITddplcMITEYMENGDLNQFLSRheppnssssdVRTVSYTNLKFMATQIASGMKYLSSLN--FVHR 709
Cdd:cd14033  66 YdswkstvrgHKCII-----LVTELMTSGTLKTYLKR----------FREMKLKLLQRWSRQILKGLHFLHSRCppILHR 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 710 DLATRNCLV-GKNYTIKIADFGMSrNLYSGDYyriqGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQP 788
Cdd:cd14033 131 DLKCDNIFItGPTGSVKIGDLGLA-TLKRASF----AKSVIGTPEFMAPEMYEEKYDEAVDVYAFGMCILEMAT--SEYP 203
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 789 YSQlsdeqvIENTGEFFRD--QGRQtylpqpaicPDSVYKLML--------SCWRRDTKNRPSFQEI 845
Cdd:cd14033 204 YSE------CQNAAQIYRKvtSGIK---------PDSFYKVKVpelkeiieGCIRTDKDERFTIQDL 255
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
568-782 3.13e-10

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: 61.76  E-value: 3.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHlcevEGMEKFKDKDFALDVsanqpvlVAVKMLRADA--NKNARndflKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14070   9 KLGEGSFAKVR----EGLHAVTGEKVAIKV-------IDKKKAKKDSyvTKNLR----REGRIQQMIRHPNITQLLDILE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDL-NQFLSRHEppnSSSSDVRtvSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd14070  74 TENSYYLVMELCPGGNLmHRIYDKKR---LEEREAR--RYIR------QLVSAVEHLHRAGVVHRDLKIENLLLDENDNI 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 725 KIADFGMSRNL----YSGDYYRIQGRAVlpirWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14070 143 KLIDFGLSNCAgilgYSDPFSTQCGSPA----YAAPELLARKKYGPKVDVWSIGVNMYAMLT 200
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
563-779 3.20e-10

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 62.53  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  563 LTFKEKLGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVLvavKMLRADanknarnDFLKEIKIMSRLKDPNIIHLLA 642
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEY----YAIKCLKKREIL---KMKQVQ-------HVAQEKSILMELSHPFIVNMMC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  643 VCITDDPLCMITEYMENGDLNQFL-SRHEPPNssssDVRtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:PTZ00263  86 SFQDENRVYFLLEFVVGGELFTHLrKAGRFPN----DVA-------KFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884  722 YTIKIADFGMSRNLySGDYYRIQGRAvlpiRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:PTZ00263 155 GHVKVTDFGFAKKV-PDRTFTLCGTP----EYLAPEVIQSKGHGKAVDWWTMGVLLYE 207
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
569-779 3.78e-10

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: 62.23  E-value: 3.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANknARNDFLKEIKIMSRL-----KDPNIIHLLAV 643
Cdd:cd05570   3 LGKGSFGKVMLAERKKTDE----------------LYAIKVLKKEVI--IEDDDVECTMTEKRVlalanRHPFLTGLHAC 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLSRheppnssssdVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd05570  65 FQTEDRLYFVMEYVNGGDLMFHIQR----------ARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGH 134
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 724 IKIADFGMSR-NLYSG----------DYyriqgravlpirwMSWEsILLGK-FTTASDVWAFGVTLWE 779
Cdd:cd05570 135 IKIADFGMCKeGIWGGnttstfcgtpDY-------------IAPE-ILREQdYGFSVDWWALGVLLYE 188
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
565-735 5.03e-10

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: 61.50  E-value: 5.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCevegMEKFKDKDFAldvsanqpvlvaVKMLRadanKNARnDFLKEIKIMSRL-KDPNIIHLLAV 643
Cdd:cd14091   4 IKEEIGKGSYSVCKRC----IHKATGKEYA------------VKIID----KSKR-DPSEEIEILLRYgQHPNIITLRDV 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDL------NQFLSRHEppnssSSDVrtvsytnlkfMATqIASGMKYLSSLNFVHRDLATRNCL 717
Cdd:cd14091  63 YDDGNSVYLVTELLRGGELldrilrQKFFSERE-----ASAV----------MKT-LTKTVEYLHSQGVVHRDLKPSNIL 126
                       170       180
                ....*....|....*....|..
gi 62420884 718 V----GKNYTIKIADFGMSRNL 735
Cdd:cd14091 127 YadesGDPESLRICDFGFAKQL 148
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
569-736 6.71e-10

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 60.75  E-value: 6.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFKDKDFALDVSANQPVLVAVKMLR----ADANKNArNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14067   1 LGQGGSGTVIYRARYQGQPVAVKRFHIKKCKKRTDGSADTMLKhlraADAMKNF-SEFRQEASMLHSLQHPCIVYLIGIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ItdDPLCMITEYMENGDLNQFLSRheppNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV-----G 719
Cdd:cd14067  80 I--HPLCFALELAPLGSLNTVLEE----NHKGSSFMPLGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSDNILVwsldvQ 153
                       170
                ....*....|....*..
gi 62420884 720 KNYTIKIADFGMSRNLY 736
Cdd:cd14067 154 EHINIKLSDYGISRQSF 170
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
690-840 7.35e-10

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: 60.58  E-value: 7.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 690 MATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR--NLYSGDyyrIQGRavlPIRwMSWEsILLGKFTTA 767
Cdd:cd13975 107 IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKpeAMMSGS---IVGT---PIH-MAPE-LFSGKYDNS 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 768 SDVWAFGVTLW----------ETFTFCQEQpysqlsdeqviENTGEFFRDQGRQTYLPQpaiCPDSVYKLMLSCWRRDTK 837
Cdd:cd13975 179 VDVYAFGILFWylcaghvklpEAFEQCASK-----------DHLWNNVRKGVRPERLPV---FDEECWNLMEACWSGDPS 244

                ...
gi 62420884 838 NRP 840
Cdd:cd13975 245 QRP 247
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
623-782 7.37e-10

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: 61.62  E-value: 7.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 623 LKEIKIMSRLKDPNIIHLLAVCItddPLCM--------ITEYMENgDLNQFLSrheppnssSSdvRTVSYTNLKFMATQI 694
Cdd:cd07858  52 LREIKLLRHLDHENVIAIKDIMP---PPHReafndvyiVYELMDT-DLHQIIR--------SS--QTLSDDHCQYFLYQL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 695 ASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR-NLYSGDY---YRIqgravlpIRWMSWESILL--GKFTTAS 768
Cdd:cd07858 118 LRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARtTSEKGDFmteYVV-------TRWYRAPELLLncSEYTTAI 190
                       170
                ....*....|....
gi 62420884 769 DVWAFGVTLWETFT 782
Cdd:cd07858 191 DVWSVGCIFAELLG 204
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
569-730 9.89e-10

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: 61.55  E-value: 9.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVsanqpvLVAVKMLRadanknaRND---FLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05621  60 IGRGAFGEVQLVR----HKASQKVYAMKL------LSKFEMIK-------RSDsafFWEERDIMAFANSPWVVQLFCAFQ 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNSSSsdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05621 123 DDKYLYMVMEYMPGGDLVNLMSNYDVPEKWA-----------KFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLK 191

                ....*
gi 62420884 726 IADFG 730
Cdd:cd05621 192 LADFG 196
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
605-779 1.02e-09

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 60.53  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLradankNARND--FLKEIKIMSR--LKDPNIIHLLAVCIT----DDPLCMITEYMENGDLNQFLSRHeppnsss 676
Cdd:cd14142  31 VAVKIF------SSRDEksWFRETEIYNTvlLRHENILGFIASDMTsrnsCTQLWLITHYHENGSLYDYLQRT------- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 677 sdvrTVSYTNLKFMATQIASGMKYLSSLNF--------VHRDLATRNCLVGKNYTIKIADFGM-------SRNLYSGDYY 741
Cdd:cd14142  98 ----TLDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILVKSNGQCCIADLGLavthsqeTNQLDVGNNP 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 62420884 742 RIQGRavlpiRWMS----WESILLGKFTT--ASDVWAFGVTLWE 779
Cdd:cd14142 174 RVGTK-----RYMApevlDETINTDCFESykRVDIYAFGLVLWE 212
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
624-782 1.05e-09

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 61.12  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 624 KEIKIMSRLKDPNIIHLLAVCITDDPLCMITEY-----MENGDLNQfLSRHEppnssssdvrTVSYTNLKFMATQIASGM 698
Cdd:cd07880  63 RELRLLKHMKHENVIGLLDVFTPDLSLDRFHDFylvmpFMGTDLGK-LMKHE----------KLSEDRIQFLVYQMLKGL 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 699 KYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSgdyyRIQGRAVlpIRWMSWESILLG--KFTTASDVWAFGVT 776
Cdd:cd07880 132 KYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDS----EMTGYVV--TRWYRAPEVILNwmHYTQTVDIWSVGCI 205

                ....*.
gi 62420884 777 LWETFT 782
Cdd:cd07880 206 MAEMLT 211
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
563-849 1.20e-09

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: 60.02  E-value: 1.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGMekfkdkdfaldvsanqpvlVAVKMLRADA-NKNARNDFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd14153   2 LEIGELIGKGRFGQVYHGRWHGE-------------------VAIRLIDIERdNEEQLKAFKREVMAYRQTRHENVVLFM 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEymengdlnqfLSRHEPPNSSSSDVRTVSYTN-LKFMATQIASGMKYLSSLNFVHRDLATRNCLVgK 720
Cdd:cd14153  63 GACMSPPHLAIITS----------LCKGRTLYSVVRDAKVVLDVNkTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-D 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 NYTIKIADFGM---SRNLYSG---DYYRIQG-----RAVLPIRWMSWESILLG-KFTTASDVWAFGvTLWETFtFCQEQP 788
Cdd:cd14153 132 NGKVVITDFGLftiSGVLQAGrreDKLRIQSgwlchLAPEIIRQLSPETEEDKlPFSKHSDVFAFG-TIWYEL-HAREWP 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 789 YSQLSDEQVIENTGeffrdQGRQTYLPQPAICPDsVYKLMLSCWRRDTKNRPSFQEIHLLL 849
Cdd:cd14153 210 FKTQPAEAIIWQVG-----SGMKPNLSQIGMGKE-ISDILLFCWAYEQEERPTFSKLMEML 264
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
605-783 1.40e-09

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


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 60.65  E-value: 1.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADANKNARNDfLKEIKIMSRLKD--PNIIHL-------------------------------LAVCITDDPLC 651
Cdd:cd13977  28 VAVKKIRCNAPENVELA-LREFWALSSIQRqhPNVIQLeecvlqrdglaqrmshgssksdlylllvetsLKGERCFDPRS 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 652 -----MITEYMENGDLNQFLSRHEPPNSsssdvrtvsyTNLKFMaTQIASGMKYLSSLNFVHRDLATRNCLVGKNY---T 723
Cdd:cd13977 107 acylwFVMEFCDGGDMNEYLLSRRPDRQ----------TNTSFM-LQLSSALAFLHRNQIVHRDLKPDNILISHKRgepI 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 724 IKIADFGMSRnLYSGDYYRIQGRAVLPIRWMS-------------WEsillGKFTTASDVWAFGVTLW---ETFTF 783
Cdd:cd13977 176 LKVADFGLSK-VCSGSGLNPEEPANVNKHFLSsacgsdfymapevWE----GHYTAKADIFALGIIIWamvERITF 246
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
616-849 1.59e-09

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. 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 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-C 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: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 59.90  E-value: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 616 KNARNDFLKEIKI----MSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRheppnssssdvrTVSYTNLKFMA 691
Cdd:cd14044  40 KNNEGNFTEKQKIelnkLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLND------------KISYPDGTFMD 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 692 TQ--------IASGMKYLSSLNF-VHRDLATRNCLVGKNYTIKIADFGmsrnlysgdyyriqGRAVLPIR---WMSWESI 759
Cdd:cd14044 108 WEfkisvmydIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVKITDFG--------------CNSILPPSkdlWTAPEHL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 760 LLGKFTTASDVWAFGVTLWETFtFCQEQPYSqlsdEQVIENTGEFFRDQGRQTYLP-QPAICPDS-------VYKLMLSC 831
Cdd:cd14044 174 RQAGTSQKGDVYSYGIIAQEII-LRKETFYT----AACSDRKEKIYRVQNPKGMKPfRPDLNLESagerereVYGLVKNC 248
                       250
                ....*....|....*...
gi 62420884 832 WRRDTKNRPSFQEIHLLL 849
Cdd:cd14044 249 WEEDPEKRPDFKKIENTL 266
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
567-735 1.63e-09

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


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 59.52  E-value: 1.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegMEKFKDKDFALDVsANQPVLVAVKMLRadanknarndflKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd14114   8 EELGTGAFGVVHRC----TERATGNNFAAKF-IMTPHESDKETVR------------KEIQIMNQLHHPKLINLHDAFED 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLnqfLSRHEPPNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRN--CLVGKNYTI 724
Cdd:cd14114  71 DNEMVLILEFLSGGEL---FERIAAEHYKMSEAEVINYMR------QVCEGLCHMHENNIVHLDIKPENimCTTKRSNEV 141
                       170
                ....*....|.
gi 62420884 725 KIADFGMSRNL 735
Cdd:cd14114 142 KLIDFGLATHL 152
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
624-782 1.83e-09

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 60.44  E-value: 1.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 624 KEIKIMSRLKDPNIIHLLAVCITDDPL------CMITEYMeNGDLNQFLSrheppnssssdVRTVSYTNLKFMATQIASG 697
Cdd:cd07877  65 RELRLLKHMKHENVIGLLDVFTPARSLeefndvYLVTHLM-GADLNNIVK-----------CQKLTDDHVQFLIYQILRG 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 698 MKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRnlYSGDyyriQGRAVLPIRWMSWESILLG--KFTTASDVWAFGV 775
Cdd:cd07877 133 LKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR--HTDD----EMTGYVATRWYRAPEIMLNwmHYNQTVDIWSVGC 206

                ....*..
gi 62420884 776 TLWETFT 782
Cdd:cd07877 207 IMAELLT 213
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
569-779 1.91e-09

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: 60.10  E-value: 1.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANknARNDFLKEIKIMSRL-----KDPNIIHLLAV 643
Cdd:cd05587   4 LGKGSFGKVMLAERKGTDE----------------LYAIKILKKDVI--IQDDDVECTMVEKRVlalsgKPPFLTQLHSC 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLN---QFLSRHEPPNSSssdvrtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd05587  66 FQTMDRLYFVMEYVNGGDLMyhiQQVGKFKEPVAV-------------FYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDA 132
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 721 NYTIKIADFGMSRNLYSG-----------DYyriqgraVLPirwmswESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05587 133 EGHIKIADFGMCKEGIFGgkttrtfcgtpDY-------IAP------EIIAYQPYGKSVDWWAYGVLLYE 189
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
616-784 1.95e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 59.73  E-value: 1.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 616 KNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEP-PnssssdvrtVSYTNLKFMATQI 694
Cdd:cd05609  41 RNQIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDCATLLKNIGPlP---------VDMARMYFAETVL 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 695 AsgMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR--------NLYSG----DYYRIQGRAVL--PiRWMSWESIL 760
Cdd:cd05609 112 A--LEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiglmslttNLYEGhiekDTREFLDKQVCgtP-EYIAPEVIL 188
                       170       180
                ....*....|....*....|....
gi 62420884 761 LGKFTTASDVWAFGVTLWETFTFC 784
Cdd:cd05609 189 RQGYGKPVDWWAMGIILYEFLVGC 212
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
569-779 2.06e-09

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: 60.01  E-value: 2.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADA--NKNARNDFLKEIKIMSRLKDPNIIHLLAVCI- 645
Cdd:cd05615  18 LGKGSFGKVMLAERKGSDE----------------LYAIKILKKDVviQDDDVECTMVEKRVLALQDKPPFLTQLHSCFq 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLN---QFLSRHEPPNSSssdvrtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05615  82 TVDRLYFVMEYVNGGDLMyhiQQVGKFKEPQAV-------------FYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEG 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 723 TIKIADFGMSR-NLYSGdyyrIQGRAVLPI-RWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05615 149 HIKIADFGMCKeHMVEG----VTTRTFCGTpDYIAPEIIAYQPYGRSVDWWAYGVLLYE 203
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
567-832 2.07e-09

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 59.76  E-value: 2.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLradANKNARNDFLK-EIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGED------------------VAVKIF---SSREERSWFREaEIYQTVMLRHENILGFIAADN 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDD----PLCMITEYMENGDLNQFLSRHeppnssssdvrTVSYTNLKFMATQIASGMKYL--------SSLNFVHRDLAT 713
Cdd:cd14143  60 KDNgtwtQLWLVSDYHEHGSLFDYLNRY-----------TVTVEGMIKLALSIASGLAHLhmeivgtqGKPAIAHRDLKS 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMS-RNLYSGDYYRI-QGRAVLPIRWMSWE----SILLGKFTT--ASDVWAFGVTLWETFTFCQ 785
Cdd:cd14143 129 KNILVKKNGTCCIADLGLAvRHDSATDTIDIaPNHRVGTKRYMAPEvlddTINMKHFESfkRADIYALGLVFWEIARRCS 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 786 --------EQPYSQL-SDEQVIENTGEFFRDQGRQTYLP---QPAICPDSVYKLMLSCW 832
Cdd:cd14143 209 iggihedyQLPYYDLvPSDPSIEEMRKVVCEQKLRPNIPnrwQSCEALRVMAKIMRECW 267
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
603-779 2.44e-09

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: 59.68  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 603 VLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRheppnssssdVRTV 682
Cdd:cd06650  31 LVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKK----------AGRI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 SYTNLKFMATQIASGMKYLSSLN-FVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGdyyrIQGRAVLPIRWMSWESILL 761
Cdd:cd06650 101 PEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS----MANSFVGTRSYMSPERLQG 176
                       170
                ....*....|....*...
gi 62420884 762 GKFTTASDVWAFGVTLWE 779
Cdd:cd06650 177 THYSVQSDIWSMGLSLVE 194
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
569-779 2.51e-09

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: 60.40  E-value: 2.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVsanqpvLVAVKMLRadanknaRND---FLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05622  81 IGRGAFGEVQLVR----HKSTRKVYAMKL------LSKFEMIK-------RSDsafFWEERDIMAFANSPWVVQLFYAFQ 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNSSSsdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05622 144 DDRYLYMVMEYMPGGDLVNLMSNYDVPEKWA-----------RFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLK 212
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 726 IADFGMSRNLYSGDYYRIQGRAVLPiRWMSWESILL----GKFTTASDVWAFGVTLWE 779
Cdd:cd05622 213 LADFGTCMKMNKEGMVRCDTAVGTP-DYISPEVLKSqggdGYYGRECDWWSVGVFLYE 269
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
569-732 2.53e-09

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: 59.11  E-value: 2.53e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmeKFKDKDFaldvsanqpvLVAVKML-RADANKNA-RNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd14117  14 LGKGKFGNVYLA------REKQSKF----------IVALKVLfKSQIEKEGvEHQLRREIEIQSHLRHPNILRLYNYFHD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSRHEppnsSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd14117  78 RKRIYLILEYAPRGELYKELQKHG----RFDEQRTATFME------ELADALHYCHEKKVIHRDIKPENLLMGYKGELKI 147

                ....*.
gi 62420884 727 ADFGMS 732
Cdd:cd14117 148 ADFGWS 153
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
603-779 2.68e-09

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 59.68  E-value: 2.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 603 VLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSrheppnssssDVRTV 682
Cdd:cd06649  31 LIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLK----------EAKRI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 SYTNLKFMATQIASGMKYLSSLN-FVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGdyyrIQGRAVLPIRWMSWESILL 761
Cdd:cd06649 101 PEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS----MANSFVGTRSYMSPERLQG 176
                       170
                ....*....|....*...
gi 62420884 762 GKFTTASDVWAFGVTLWE 779
Cdd:cd06649 177 THYSVQSDIWSMGLSLVE 194
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
567-779 2.68e-09

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 59.45  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  567 EKLGEGQFGEVHlcevegmeKFKDKdfaldvSANQpvLVAVKMLRADA-NKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:PLN00009   8 EKIGEGTYGVVY--------KARDR------VTNE--TIALKKIRLEQeDEGVPSTAIREISLLKEMQHGNIVRLQDVVH 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  646 TDDPLCMITEYMENgDLNQFLSRHEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGK-NYTI 724
Cdd:PLN00009  72 SEKRLYLVFEYLDL-DLKKHMDSSPDFAKNPRLIKTYLY--------QILRGIAYCHSHRVLHRDLKPQNLLIDRrTNAL 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884  725 KIADFGMSRNLysGDYYRIQGRAVLPIrWMSWESILLGK--FTTASDVWAFGVTLWE 779
Cdd:PLN00009 143 KLADFGLARAF--GIPVRTFTHEVVTL-WYRAPEILLGSrhYSTPVDIWSVGCIFAE 196
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
565-733 2.75e-09

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: 59.65  E-value: 2.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVLvavKMLRADANKNARNDFLKEIKimsrlkDPNIIHLLAVC 644
Cdd:cd05602  11 FLKVIGKGSFGKVLLARHKSDEKF----YAVKVLQKKAIL---KKKEEKHIMSERNVLLKNVK------HPFLVGLHFSF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 724
Cdd:cd05602  78 QTTDKLYFVLDYINGGELFYHLQRE----------RCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHI 147

                ....*....
gi 62420884 725 KIADFGMSR 733
Cdd:cd05602 148 VLTDFGLCK 156
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
566-778 2.92e-09

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: 58.55  E-value: 2.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQPVlvAVKMLradaNKNARNDFL----KEIKIMSRLKDPNIIHLL 641
Cdd:cd14078   8 HETIGSGGFAKVKL--------------ATHILTGEKV--AIKIM----DKKALGDDLprvkTEIEALKNLSHQHICRLY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSRHEppNSSSSDVRTVsytnlkFmaTQIASGMKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14078  68 HVIETDNKIFMVLEYCPGGELFDYIVAKD--RLSEDEARVF------F--RQIVSAVAYVHSQGYAHRDLKPENLLLDED 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 722 YTIKIADFGMSRNLYSGDYYRIQGRAVLPIrWMSWESIlLGK--FTTASDVWAFGVTLW 778
Cdd:cd14078 138 QNLKLIDFGLCAKPKGGMDHHLETCCGSPA-YAAPELI-QGKpyIGSEADVWSMGVLLY 194
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
563-784 3.19e-09

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 59.61  E-value: 3.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  563 LTFKEKLGEGQFGEVHLCevegmeKFKDKDFaldvsanqPVLVAVKMLRADANKNARNDFL-KEIKIMSRLKDPNIIHLL 641
Cdd:PTZ00426  32 FNFIRTLGTGSFGRVILA------TYKNEDF--------PPVAIKRFEKSKIIKQKQVDHVfSERKILNYINHPFCVNLY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  642 AVCITDDPLCMITEYMENGDLNQFLSRHEP-PNSSSSdvrtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:PTZ00426  98 GSFKDESYLYLVLEFVIGGEFFTFLRRNKRfPNDVGC-----------FYAAQIVLIFEYLQSLNIVYRDLKPENLLLDK 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884  721 NYTIKIADFGMSRnLYSGDYYRIQGRAvlpiRWMSWESILLGKFTTASDVWAFGVTLWETFTFC 784
Cdd:PTZ00426 167 DGFIKMTDFGFAK-VVDTRTYTLCGTP----EYIAPEILLNVGHGKAADWWTLGIFIYEILVGC 225
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
555-779 4.18e-09

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: 59.29  E-value: 4.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 555 VEEFPRKLLTFKeKLGEGQFGEVhlCEvegmekfkdkdfALDVSANQPVlvAVKMLRADANK--NARNDFlKEIKIMSRL 632
Cdd:cd07878  10 VWEVPERYQNLT-PVGSGAYGSV--CS------------AYDTRLRQKV--AVKKLSRPFQSliHARRTY-RELRLLKHM 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 633 KDPNIIHLL-----AVCITD-DPLCMITEYMeNGDLNQFLSrheppnssssdVRTVSYTNLKFMATQIASGMKYLSSLNF 706
Cdd:cd07878  72 KHENVIGLLdvftpATSIENfNEVYLVTNLM-GADLNNIVK-----------CQKLSDEHVQFLIYQLLRGLKYIHSAGI 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 707 VHRDLATRNCLVGKNYTIKIADFGMSRNlySGDyyriQGRAVLPIRWMSWESILLG--KFTTASDVWAFGVTLWE 779
Cdd:cd07878 140 IHRDLKPSNVAVNEDCELRILDFGLARQ--ADD----EMTGYVATRWYRAPEIMLNwmHYNQTVDIWSVGCIMAE 208
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
566-813 6.28e-09

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: 58.42  E-value: 6.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCEVEgmekfKDKDFaldvsanqpvlVAVKMLRadaNKNAR-NDFLKEIKIMSRLK---DP----NI 637
Cdd:cd14212   4 LDLLGQGTFGQVVKCQDL-----KTNKL-----------VAVKVLK---NKPAYfRQAMLEIAILTLLNtkyDPedkhHI 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEyMENGDLNQFLSRHEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCL 717
Cdd:cd14212  65 VRLLDHFMHHGHLCIVFE-LLGVNLYELLKQNQFRGLSLQLIRKF--------LQQLLDALSVLKDARIIHCDLKPENIL 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 718 VGKNYT--IKIADFGMS----RNLYSgdYyrIQGRavlpiRWMSWEsILLG-KFTTASDVWAFGVTLWETF----TFCQE 786
Cdd:cd14212 136 LVNLDSpeIKLIDFGSAcfenYTLYT--Y--IQSR-----FYRSPE-VLLGlPYSTAIDMWSLGCIAAELFlglpLFPGN 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62420884 787 QPYSQLSdeQVIE--------------NTGEFFR----DQGRQTY 813
Cdd:cd14212 206 SEYNQLS--RIIEmlgmppdwmlekgkNTNKFFKkvakSGGRSTY 248
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
605-834 7.43e-09

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 57.74  E-value: 7.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADANKNARNDFlkEIKIMSRLKDPNIIHLLAV----CITDDPLCMITEYMENGDLNQFLSrheppnssssdVR 680
Cdd:cd14141  21 VAVKIFPIQDKLSWQNEY--EIYSLPGMKHENILQFIGAekrgTNLDVDLWLITAFHEKGSLTDYLK-----------AN 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 681 TVSYTNLKFMATQIASGMKYLSS----------LNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVLP 750
Cdd:cd14141  88 VVSWNELCHIAQTMARGLAYLHEdipglkdghkPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGT 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 751 IRWMSWEsILLGKFTTAS------DVWAFGVTLWETFTFCQEqpysqlSDEQVIENTGEFFRDQGRQTYLP--QPAICPD 822
Cdd:cd14141 168 RRYMAPE-VLEGAINFQRdaflriDMYAMGLVLWELASRCTA------SDGPVDEYMLPFEEEVGQHPSLEdmQEVVVHK 240
                       250
                ....*....|..
gi 62420884 823 SVYKLMLSCWRR 834
Cdd:cd14141 241 KKRPVLRECWQK 252
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
567-788 8.10e-09

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: 57.51  E-value: 8.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevegmeKFKDKDfaldvsaNQPVLVAVK---MLRADANKNARN------DFLKEIKIM-SRLKDPN 636
Cdd:cd08528   6 ELLGSGAFGCVY--------KVRKKS-------NGQTLLALKeinMTNPAFGRTEQErdksvgDIISEVNIIkEQLRHPN 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 637 IIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRtvsytnLKFMATQIASGMKYL-SSLNFVHRDLATRN 715
Cdd:cd08528  71 IVRYYKTFLENDRLYIVMELIEGAPLGEHFSSLKEKNEHFTEDR------IWNIFVQMVLALRYLhKEKQIVHRDLKPNN 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 716 CLVGKNYTIKIADFGMSRNLYSGDYYRIQgrAVLPIRWMSWESILLGKFTTASDVWAFGVTLWEtftFCQEQP 788
Cdd:cd08528 145 IMLGEDDKVTITDFGLAKQKGPESSKMTS--VVGTILYSCPEIVQNEPYGEKADIWALGCILYQ---MCTLQP 212
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
566-738 1.28e-08

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: 57.71  E-value: 1.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCEvegmEKFKDKDFALDVsanqpvLVAVKMLRADANKNarndFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05601   6 KNVIGRGHFGEVQVVK----EKATGDIYAMKV------LKKSETLAQEEVSF----FEEERDIMAKANSPWITKLQYAFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05601  72 DSENLYLVMEYHPGGDLLSLLSRYDDIFEESM---------ARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIK 142
                       170
                ....*....|...
gi 62420884 726 IADFGMSRNLYSG 738
Cdd:cd05601 143 LADFGSAAKLSSD 155
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
567-787 1.44e-08

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: 56.65  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHlcevEGMEKFKDKDFALDVsanqpvlvaVKMLRADANKNARndfLK-EIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14082   9 EVLGSGQFGIVY----GGKHRKTGRDVAIKV---------IDKLRFPTKQESQ---LRnEVAILQQLSHPGVVNLECMFE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMeNGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY--- 722
Cdd:cd14082  73 TPERVFVVMEKL-HGDMLEMIL--------SSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfp 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 723 TIKIADFGMSRNLYSGDYYRiqgRAVLPIRWMSWESILLGKFTTASDVWAFG----VTLWETFTFCQEQ 787
Cdd:cd14082 144 QVKLCDFGFARIIGEKSFRR---SVVGTPAYLAPEVLRNKGYNRSLDMWSVGviiyVSLSGTFPFNEDE 209
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
565-742 1.77e-08

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 56.31  E-value: 1.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCEvegmekfkdkdfalDVSANQPVlvAVKMlraDANKNARNDFLKEIKIMSRLKD-PNIIHLLAv 643
Cdd:cd14016   4 LVKKIGSGSFGEVYLGI--------------DLKTGEEV--AIKI---EKKDSKHPQLEYEAKVYKLLQGgPGIPRLYW- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPL-CMITEYMenG-DLNQFLSRHEppnssssdvRTVSytnLK--FM-ATQIASGMKYLSSLNFVHRDLATRNCLV 718
Cdd:cd14016  64 FGQEGDYnVMVMDLL--GpSLEDLFNKCG---------RKFS---LKtvLMlADQMISRLEYLHSKGYIHRDIKPENFLM 129
                       170       180
                ....*....|....*....|....*..
gi 62420884 719 GKNYTIK---IADFGMSRnlysgdYYR 742
Cdd:cd14016 130 GLGKNSNkvyLIDFGLAK------KYR 150
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
568-799 1.78e-08

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: 56.52  E-value: 1.78e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKnaRNDFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd14113  14 ELGRGRFSVVKKCDQRGTKR----------------AVATKFVNKKLMK--RDQVTHELGVLQSLQHPQLVGLLDTFETP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLsrheppnssssdvrtVSYTNL-----KFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd14113  76 TSYILVLEMADQGRLLDYV---------------VRWGNLteekiRFYLREILEALQYLHNCRIAHLDLKPENILVDQSL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 ---TIKIADFGMSRNLYSGDY-YRIQGRAvlpiRWMSWESILLGKFTTASDVWAFGVtlwetFTFCQEQPYSQLSDEQVI 798
Cdd:cd14113 141 skpTIKLADFGDAVQLNTTYYiHQLLGSP----EFAAPEIILGNPVSLTSDLWSIGV-----LTYVLLSGVSPFLDESVE 211

                .
gi 62420884 799 E 799
Cdd:cd14113 212 E 212
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
569-845 1.83e-08

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. 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 (a pseudokinase in the case of IRAK3), 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. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 56.43  E-value: 1.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEkfkdkdfaldvsanqpvlVAVKMLRADAN---KNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14160   1 IGEGEIFEVYRVRIGNRS------------------YAVKLFKQEKKmqwKKHWKRFLSELEVLLLFQHPNILELAAYFT 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVsytnlkfMATQIASGMKYLSSLN---FVHRDLATRNCLVGKNY 722
Cdd:cd14160  63 ETEKFCLVYPYMQNGTLFDRLQCHGVTKPLSWHERIN-------ILIGIAKAIHYLHNSQpctVICGNISSANILLDDQM 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 723 TIKIADFGMSR------------NLYSGDYYRIQgravlpirWMSWESILLGKFTTASDVWAFGVTLWETFTFC---QEQ 787
Cdd:cd14160 136 QPKLTDFALAHfrphledqsctiNMTTALHKHLW--------YMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCkvvLDD 207
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 788 P-YSQLSD--EQVIENTGE----FFRDQGRQTYLPQPAICpdsVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14160 208 PkHLQLRDllHELMEKRGLdsclSFLDLKFPPCPRNFSAK---LFRLAGRCTATKAKLRPDMDEV 269
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
565-778 2.05e-08

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: 56.15  E-value: 2.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLcevegMEKFKDKDfaldvsanqpvLVAVKMLraDANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14665   4 LVKDIGSGNFGVARL-----MRDKQTKE-----------LVAVKYI--ERGEKIDENVQREIINHRSLRHPNIVRFKEVI 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSrheppnssssDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT- 723
Cdd:cd14665  66 LTPTHLAIVMEYAAGGELFERIC----------NAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAp 135
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 724 -IKIADFGMSRN--LYSGDYYRIQGRAvlpirWMSWESILLGKFT-TASDVWAFGVTLW 778
Cdd:cd14665 136 rLKICDFGYSKSsvLHSQPKSTVGTPA-----YIAPEVLLKKEYDgKIADVWSCGVTLY 189
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
569-779 2.44e-08

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 57.35  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  569 LGEGQFGEVHlcevegmekfkdKDFALDVSANqpvlVAVKMLRADANKNARndflkEIKIMSRLKDPNIIHLLAVcitdd 648
Cdd:PTZ00036  74 IGNGSFGVVY------------EAICIDTSEK----VAIKKVLQDPQYKNR-----ELLIMKNLNHINIIFLKDY----- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  649 plcMITEYMENGDLNQFL---------SRHEPPNSSSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVG 719
Cdd:PTZ00036 128 ---YYTECFKKNEKNIFLnvvmefipqTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLID 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884  720 KN-YTIKIADFGMSRNLYSGDyyriqgRAVLPI--RWMSWESILLG--KFTTASDVWAFGVTLWE 779
Cdd:PTZ00036 205 PNtHTLKLCDFGSAKNLLAGQ------RSVSYIcsRFYRAPELMLGatNYTTHIDLWSLGCIIAE 263
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
569-801 2.90e-08

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: 56.22  E-value: 2.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLcevegmekfkdkdfALDVSANQPVLVAVKML----RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVC 644
Cdd:cd14040  14 LGRGGFSEVYK--------------AFDLYEQRYAAVKIHQLnkswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITD-DPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLN--FVHRDLATRNCLVGKN 721
Cdd:cd14040  80 SLDtDTFCTVLEYCEGNDLDFYLKQH----------KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 722 YT---IKIADFGMSRnLYSGDYYRIQG-----RAVLPIRWMSWESILLG----KFTTASDVWAFGVTLWETFTfcQEQPY 789
Cdd:cd14040 150 TAcgeIKITDFGLSK-IMDDDSYGVDGmdltsQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLY--GRKPF 226
                       250
                ....*....|....
gi 62420884 790 SQLSDEQVI--ENT 801
Cdd:cd14040 227 GHNQSQQDIlqENT 240
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
559-789 2.97e-08

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: 56.18  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKmlRADANKNARNDFL-KEIKIMSRLKDPNI 637
Cdd:cd06657  18 PRTYLDNFIKIGEGSTGIVCIATVKSSGK----------------LVAVK--KMDLRKQQRRELLfNEVVIMRDYQHENV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMENGDLnqflsrheppnsssSDVRTVSYTNLKFMATQIASGMKYLSSLN---FVHRDLATR 714
Cdd:cd06657  80 VEMYNSYLVGDELWVVMEFLEGGAL--------------TDIVTHTRMNEEQIAAVCLAVLKALSVLHaqgVIHRDIKSD 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLySGDYYRIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPY 789
Cdd:cd06657 146 SILLTHDGRVKLSDFGFCAQV-SKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIEMVD--GEPPY 216
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
568-733 3.39e-08

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: 56.58  E-value: 3.39e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCevegmekfKDKDFAldvsanqpVLVAVKMLRADANK--NARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05600  18 QVGQGGYGSVFLA--------RKKDTG--------EICALKIMKKKVLFklNEVNHVLTERDILTTTNSPWLVKLLYAFQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05600  82 DPENVYLAMEYVPGGDFRTLLNNS----------GILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIK 151

                ....*...
gi 62420884 726 IADFGMSR 733
Cdd:cd05600 152 LTDFGLAS 159
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
638-845 3.47e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 56.95  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  638 IHLLAVCI------------TDDPLCMITEYMENGDLN----QFLSRHEPpnSSSSDVRTVSYtnlkfmatQIASGMKYL 701
Cdd:PTZ00267 116 LHCLAACDhfgivkhfddfkSDDKLLLIMEYGSGGDLNkqikQRLKEHLP--FQEYEVGLLFY--------QIVLALDEV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  702 SSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNL-----------YSGDYYRIQGRAvlpirwmsWESillGKFTTASDV 770
Cdd:PTZ00267 186 HSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYsdsvsldvassFCGTPYYLAPEL--------WER---KRYSKKADM 254
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884  771 WAFGVTLWETFTFcqEQPYSQLSDEQVIENT--GEffrdqgrqtYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:PTZ00267 255 WSLGVILYELLTL--HRPFKGPSQREIMQQVlyGK---------YDPFPCPVSSGMKALLDPLLSKNPALRPTTQQL 320
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
623-795 4.11e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 56.04  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  623 LKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMeNGDLNQFLSRHEPPnssssdvrtVSYTNLKFMATQIASGMKYLS 702
Cdd:PHA03209 105 LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHY-SSDLYTYLTKRSRP---------LPIDQALIIEKQILEGLRYLH 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  703 SLNFVHRDLATRNCLVGKNYTIKIADFGMSR-NLYSGDYYRIQGravlPIRWMSWESILLGKFTTASDVWAFGVTLWETF 781
Cdd:PHA03209 175 AQRIIHRDVKTENIFINDVDQVCIGDLGAAQfPVVAPAFLGLAG----TVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
                        170
                 ....*....|....
gi 62420884  782 TFcqeqPYSQLSDE 795
Cdd:PHA03209 251 AY----PSTIFEDP 260
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
566-779 4.22e-08

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 55.65  E-value: 4.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVhlceVEGMEKFKDKDFAldvsanqpvlvaVKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14048  11 IQCLGRGGFGVV----FEAKNKVDDCNYA------------VKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDP-----------LCMITEYMENGDLNQFLSRheppnSSSSDVRTVSYtnLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd14048  75 ERPPegwqekmdevyLYIQMQLCRKENLKDWMNR-----RCTMESRELFV--CLNIFKQIASAVEYLHSKGLIHRDLKPS 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLYSGD-----------YYRIQGRaVLPIRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd14048 148 NVFFSLDDVVKVGDFGLVTAMDQGEpeqtvltpmpaYAKHTGQ-VGTRLYMSPEQIHGNQYSEKVDIFALGLILFE 222
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
566-739 4.89e-08

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: 55.31  E-value: 4.89e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCevegMEKFKDKDFA---LDVSANQpvlvavkMLRADANKNARNDFLKEIKIMSRLK-DPNIIHLL 641
Cdd:cd14182   8 KEILGRGVSSVVRRC----IHKPTRQEYAvkiIDITGGG-------SFSPEEVQELREATLKEIDILRKVSgHPNIIQLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLNQFLSrhEPPNSSSSDVRTVSYTNLKFMatqiasgmKYLSSLNFVHRDLATRNCLVGKN 721
Cdd:cd14182  77 DTYETNTFFFLVFDLMKKGELFDYLT--EKVTLSEKETRKIMRALLEVI--------CALHKLNIVHRDLKPENILLDDD 146
                       170
                ....*....|....*...
gi 62420884 722 YTIKIADFGMSRNLYSGD 739
Cdd:cd14182 147 MNIKLTDFGFSCQLDPGE 164
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
559-789 5.15e-08

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: 55.43  E-value: 5.15e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLceveGMEKFKDKDfaldvsanqpvlVAVKmlRADANKNARNDFL-KEIKIMSRLKDPNI 637
Cdd:cd06658  20 PREYLDSFIKIGEGSTGIVCI----ATEKHTGKQ------------VAVK--KMDLRKQQRRELLfNEVVIMRDYHHENV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCMITEYMENGDLnqflsrheppnsssSDVRTVSYTNLKFMATQIASGMKYLSSLN---FVHRDLATR 714
Cdd:cd06658  82 VDMYNSYLVGDELWVVMEFLEGGAL--------------TDIVTHTRMNEEQIATVCLSVLRALSYLHnqgVIHRDIKSD 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 715 NCLVGKNYTIKIADFGMSRNLySGDYYRIQGRAVLPIrWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPY 789
Cdd:cd06658 148 SILLTSDGRIKLSDFGFCAQV-SKEVPKRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMID--GEPPY 218
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
558-734 5.45e-08

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: 55.07  E-value: 5.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 558 FPRKLLTFKE--KLGEGQFGEVhlcevegmEKFKDKdfaLDVSanqpvLVAVKMLRADANKNARNDFLKEIKIMSRLKDP 635
Cdd:cd14046   1 FSRYLTDFEElqVLGKGAFGQV--------VKVRNK---LDGR-----YYAIKKIKLRSESKNNSRILREVMLLSRLNHQ 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRheppNSSSSDVRTVSYTNlkfmatQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd14046  65 HVVRYYQAWIERANLYIQMEYCEKSTLRDLIDS----GLFQDTDRLWRLFR------QILEGLAYIHSQGIIHRDLKPVN 134
                       170
                ....*....|....*....
gi 62420884 716 CLVGKNYTIKIADFGMSRN 734
Cdd:cd14046 135 IFLDSNGNVKIGDFGLATS 153
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
559-779 5.51e-08

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: 55.05  E-value: 5.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLRADANKnarnDF---LKEIKIMSRLKDP 635
Cdd:cd06645   9 PQEDFELIQRIGSGTYGDVYK--------------ARNVNTGE--LAAIKVIKLEPGE----DFavvQQEIIMMKDCKHS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd06645  69 NIVAYFGSYLRRDKLWICMEFCGGGSLQDIYHVTGP----------LSESQIAYVSRETLQGLYYLHSKGKMHRDIKGAN 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 716 CLVGKNYTIKIADFGMSRNLySGDYYRIQGRAVLPIrWMSWESILL---GKFTTASDVWAFGVTLWE 779
Cdd:cd06645 139 ILLTDNGHVKLADFGVSAQI-TATIAKRKSFIGTPY-WMAPEVAAVerkGGYNQLCDIWAVGITAIE 203
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
569-779 6.23e-08

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: 54.91  E-value: 6.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVhlCEVEgmekfkdkdfaldvSANQPVLVAVKML--RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCIT 646
Cdd:cd05607  10 LGKGGFGEV--CAVQ--------------VKNTGQMYACKKLdkKRLKKKSGEKMALLEKEILEKVNSPFIVSLAYAFET 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 DDPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05607  74 KTHLCLVMSLMNGGDLKYHIY--------NVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRL 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 62420884 727 ADFGMSRNLYSGDyyRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05607 146 SDLGLAVEVKEGK--PITQRAGTN-GYMAPEILKEESYSYPVDWFAMGCSIYE 195
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
553-788 6.33e-08

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: 54.98  E-value: 6.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 553 VAVEEFPRKLlTFKEKLGEGQFGEVHLCevegMEKFKDKDFALDVsanqpVLVAVKMLRADANKNARNDFLKEIKIMSRL 632
Cdd:cd14181   3 AGAKEFYQKY-DPKEVIGRGVSSVVRRC----VHRHTGQEFAVKI-----IEVTAERLSPEQLEEVRSSTLKEIHILRQV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 633 KD-PNIIHLLAVCITDDPLCMITEYMENGDLNQFLSrheppnssssDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDL 711
Cdd:cd14181  73 SGhPSIITLIDSYESSTFIFLVFDLMRRGELFDYLT----------EKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 712 ATRNCLVGKNYTIKIADFGMSRNLYSGDYYR----IQGRAVLPIRWMSWESILLGkFTTASDVWAFGVTLwetFTFCQEQ 787
Cdd:cd14181 143 KPENILLDDQLHIKLSDFGFSCHLEPGEKLRelcgTPGYLAPEILKCSMDETHPG-YGKEVDLWACGVIL---FTLLAGS 218

                .
gi 62420884 788 P 788
Cdd:cd14181 219 P 219
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
569-730 1.02e-07

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: 55.08  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVsanqpvLVAVKMLRadanknaRND---FLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05596  34 IGRGAFGEVQLVR----HKSTKKVYAMKL------LSKFEMIK-------RSDsafFWEERDIMAHANSEWIVQLHYAFQ 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNSSSsdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05596  97 DDKYLYMVMDYMPGGDLVNLMSNYDVPEKWA-----------RFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLK 165

                ....*
gi 62420884 726 IADFG 730
Cdd:cd05596 166 LADFG 170
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
568-832 1.07e-07

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: 54.40  E-value: 1.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHlcevegMEKFKDKDfaldvsanqpvlVAVKMLRADANKNarndFLKEIKIMSR--LKDPNIIHLLAVCI 645
Cdd:cd14144   2 SVGKGRYGEVW------KGKWRGEK------------VAVKIFFTTEEAS----WFRETEIYQTvlMRHENILGFIAADI 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDD----PLCMITEYMENGDLNQFLSRHeppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNF--------VHRDLAT 713
Cdd:cd14144  60 KGTgswtQLYLITDYHENGSLYDFLRGN-----------TLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKS 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMS-RNLYSGDYYRI-QGRAVLPIRWMSWE----SILLGKFTT--ASDVWAFGVTLWE------ 779
Cdd:cd14144 129 KNILVKKNGTCCIADLGLAvKFISETNEVDLpPNTRVGTKRYMAPEvldeSLNRNHFDAykMADMYSFGLVLWEiarrci 208
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 780 TFTFCQE-QP--YSQLSDEQVIENTGEFFRDQGRQTYLP---QPAICPDSVYKLMLSCW 832
Cdd:cd14144 209 SGGIVEEyQLpyYDAVPSDPSYEDMRRVVCVERRRPSIPnrwSSDEVLRTMSKLMSECW 267
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
562-733 1.30e-07

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: 54.06  E-value: 1.30e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 562 LLTFKEKLGEGQFGEVHLCEVEGmekfkdkdfaldvsANQPVlvAVKMLRADANKNArndFLKEIKIMSRLKDPNIIHLL 641
Cdd:cd14085   4 FFEIESELGRGATSVVYRCRQKG--------------TQKPY--AVKKLKKTVDKKI---VRTEIGVLLRLSHPNIIKLK 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENGDLnqFLSRHEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLV--- 718
Cdd:cd14085  65 EIFETPTEISLVLELVTGGEL--FDRIVEKGYYSERDAADA--------VKQILEAVAYLHENGIVHRDLKPENLLYatp 134
                       170
                ....*....|....*
gi 62420884 719 GKNYTIKIADFGMSR 733
Cdd:cd14085 135 APDAPLKIADFGLSK 149
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
559-776 1.72e-07

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: 53.46  E-value: 1.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHlcevegmeKFKDKDfaldvsANQpvLVAVKMLraDANKNARNDFLKEIKIMSRLKD-PNI 637
Cdd:cd06608   4 PAGIFELVEVIGEGTYGKVY--------KARHKK------TGQ--LAAIKIM--DIIEDEEEEIKLEINILRKFSNhPNI 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCITDDPLCM------ITEYMENG---DLNQFLsrHEPPNSSSSDVrtVSYtnlkfMATQIASGMKYLSSLNFVH 708
Cdd:cd06608  66 ATFYGAFIKKDPPGGddqlwlVMEYCGGGsvtDLVKGL--RKKGKRLKEEW--IAY-----ILRETLRGLAYLHENKVIH 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 709 RDLATRNCLVGKNYTIKIADFGMS---------RNLYSGDYYriqgravlpirWMSWESILLGKFTTA-----SDVWAFG 774
Cdd:cd06608 137 RDIKGQNILLTEEAEVKLVDFGVSaqldstlgrRNTFIGTPY-----------WMAPEVIACDQQPDAsydarCDVWSLG 205

                ..
gi 62420884 775 VT 776
Cdd:cd06608 206 IT 207
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
606-782 1.94e-07

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: 53.87  E-value: 1.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 606 AVKMLradanKNARNDFLKEIKIMSRL-KDPNIIHLLAVCITDDPLCMITEYMENGDL------NQFLSRHEppnsSSSD 678
Cdd:cd14176  48 AVKII-----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELldkilrQKFFSERE----ASAV 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 679 VRTVSYTnlkfmatqiasgMKYLSSLNFVHRDLATRNCLV----GKNYTIKIADFGMSRNLYSGDyyriqGRAVLPI--- 751
Cdd:cd14176 119 LFTITKT------------VEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAEN-----GLLMTPCyta 181
                       170       180       190
                ....*....|....*....|....*....|.
gi 62420884 752 RWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14176 182 NFVAPEVLERQGYDAACDIWSLGVLLYTMLT 212
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
605-740 2.23e-07

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: 53.04  E-value: 2.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADANKNARndflKEIKIMsRLKD--PNIIHLLavCITDDP--------LCMIT--EYMENGDLNQFLSRHEPp 672
Cdd:cd13982  28 VAVKRLLPEFFDFAD----REVQLL-RESDehPNVIRYF--CTEKDRqflyialeLCAASlqDLVESPRESKLFLRPGL- 99
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 673 nssssdvrtvsytNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV-----GKNYTIKIADFGMSRNLYSGDY 740
Cdd:cd13982 100 -------------EPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRAMISDFGLCKKLDVGRS 159
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
564-778 2.26e-07

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: 53.49  E-value: 2.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVHLCevegMEKFKDKDFALDVsanqpvlvavkmlradANKNARnDFLKEIKIMSRL-KDPNIIHLLA 642
Cdd:cd14175   4 VVKETIGVGSYSVCKRC----VHKATNMEYAVKV----------------IDKSKR-DPSEEIEILLRYgQHPNIITLKD 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDL------NQFLSRHEppnsSSSDVRTVSYTnlkfmatqiasgMKYLSSLNFVHRDLATRNC 716
Cdd:cd14175  63 VYDDGKHVYLVTELMRGGELldkilrQKFFSERE----ASSVLHTICKT------------VEYLHSQGVVHRDLKPSNI 126
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 717 LV----GKNYTIKIADFGMSRNLYSGDyyriqGRAVLPI---RWMSWESILLGKFTTASDVWAFGVTLW 778
Cdd:cd14175 127 LYvdesGNPESLRICDFGFAKQLRAEN-----GLLMTPCytaNFVAPEVLKRQGYDEGCDIWSLGILLY 190
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
548-845 2.64e-07

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: 53.09  E-value: 2.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 548 LSGKDVAVEEFPRKLLTFK--EKLGEGQFGEVH--LCEVEGMEkfkdkdfaldvsanqpvlVAVKMLraDANKNARNDFL 623
Cdd:cd06638   3 LSGKTIIFDSFPDPSDTWEiiETIGKGTYGKVFkvLNKKNGSK------------------AAVKIL--DPIHDIDEEIE 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 624 KEIKIMSRLKD-PNIIHLLAV-----CITDDPLCMITEYMENGDLNQ----FLSRHEppnssssdvrTVSYTNLKFMATQ 693
Cdd:cd06638  63 AEYNILKALSDhPNVVKFYGMyykkdVKNGDQLWLVLELCNGGSVTDlvkgFLKRGE----------RMEEPIIAYILHE 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 694 IASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESI-----LLGKFTTAS 768
Cdd:cd06638 133 ALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRLRR--NTSVGTPFWMAPEVIaceqqLDSTYDARC 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 769 DVWAFGVTLWETFTfcQEQPYSQLSDEQVIentgeFFRDQGRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd06638 211 DVWSLGITAIELGD--GDPPLADLHPMRAL-----FKIPRNPPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDL 280
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
604-778 2.69e-07

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: 52.85  E-value: 2.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKML----RADANknarndFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLsrheppnsssSDV 679
Cdd:cd14662  27 LVAVKYIerglKIDEN------VQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGGELFERI----------CNA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 680 RTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT--IKIADFGMSRN--LYSGDYYRIQGRAVLPIRWMS 755
Cdd:cd14662  91 GRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSsvLHSQPKSTVGTPAYIAPEVLS 170
                       170       180
                ....*....|....*....|...
gi 62420884 756 wESILLGKFttaSDVWAFGVTLW 778
Cdd:cd14662 171 -RKEYDGKV---ADVWSCGVTLY 189
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
681-845 2.92e-07

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: 52.62  E-value: 2.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 681 TVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYR--IQGRAvlpiRWMSWES 758
Cdd:cd14189  97 TLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKktICGTP----NYLAPEV 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 759 ILLGKFTTASDVWAFGVTLWEtfTFCQEQPYSQLsdeqvieNTGEFFRDQgRQTYLPQPAICPDSVYKLMLSCWRRDTKN 838
Cdd:cd14189 173 LLRQGHGPESDVWSLGCVMYT--LLCGNPPFETL-------DLKETYRCI-KQVKYTLPASLSLPARHLLAGILKRNPGD 242

                ....*..
gi 62420884 839 RPSFQEI 845
Cdd:cd14189 243 RLTLDQI 249
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
569-782 2.94e-07

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 53.48  E-value: 2.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVhlceVEGMEKFKDKDfaldvsanqpvlVAVKMLRADanKNARNDFLKEIKIMSRL--KDP----NIIHLLA 642
Cdd:cd14226  21 IGKGSFGQV----VKAYDHVEQEW------------VAIKIIKNK--KAFLNQAQIEVRLLELMnkHDTenkyYIVRLKR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENgDLNQFLsRHeppnsssSDVRTVSyTNL--KFmATQIASGMKYLSS--LNFVHRDLATRNCLV 718
Cdd:cd14226  83 HFMFRNHLCLVFELLSY-NLYDLL-RN-------TNFRGVS-LNLtrKF-AQQLCTALLFLSTpeLSIIHCDLKPENILL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 719 --GKNYTIKIADFGMSRNLYSGDYYRIQGRAvlpirWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14226 152 cnPKRSAIKIIDFGSSCQLGQRIYQYIQSRF-----YRSPEVLLGLPYDLAIDMWSLGCILVEMHT 212
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
569-733 3.00e-07

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 53.43  E-value: 3.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdFALDVSANQPVLvavkmlradaNKNARNDFLKEIKIMSR-LKDPNIIHLLAVCITD 647
Cdd:cd05603   3 IGKGSFGKVLLAKRKCDGKF----YAVKVLQKKTIL----------KKKEQNHIMAERNVLLKnLKHPFLVGLHYSFQTS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd05603  69 EKLYFVLDYVNGGELFFHLQRE----------RCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLT 138

                ....*.
gi 62420884 728 DFGMSR 733
Cdd:cd05603 139 DFGLCK 144
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
621-777 3.05e-07

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: 52.93  E-value: 3.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 621 DFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYTNlkfmatQIASGMKY 700
Cdd:cd14094  51 DLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMR------QILEALRY 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 701 LSSLNFVHRDLATRNCLVGKNYT---IKIADFGMSRNLySGDYYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTL 777
Cdd:cd14094 125 CHDNNIIHRDVKPHCVLLASKENsapVKLGGFGVAIQL-GESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVIL 202
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
569-800 3.72e-07

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 53.07  E-value: 3.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRaDANKNARND---FLKEIKIM---SRLKDPNIIHLLA 642
Cdd:cd05589   7 LGRGHFGKVLLAEYKPTGE----------------LFAIKALK-KGDIIARDEvesLMCEKRIFetvNSARHPFLVNLFA 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLnqFLSRHEppnSSSSDVRTVsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05589  70 CFQTPEHVCFVMEYAAGGDL--MMHIHE---DVFSEPRAV------FYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEG 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 723 TIKIADFGMSR-NLYSGDyyRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIEN 800
Cdd:cd05589 139 YVKIADFGLCKeGMGFGD--RTSTFCGTP-EFLAPEVLTDTSYTRAVDWWGLGVLIYEMLV--GESPFPGDDEEEVFDS 212
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
568-782 3.99e-07

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: 52.96  E-value: 3.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEVEGMEKFkdkdfaldvsanqpvlVAVKMLRADanKNARNDFLKEIKIMS--RLKDP------NIIH 639
Cdd:cd14136  17 KLGWGHFSTVWLCWDLQNKRF----------------VALKVVKSA--QHYTEAALDEIKLLKcvREADPkdpgreHVVQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LLavcitDD-----P----LCMITEYMenGDLNQFLSRHeppnsssSDVRTVSYTNLKFMATQIASGMKYL-SSLNFVHR 709
Cdd:cd14136  79 LL-----DDfkhtgPngthVCMVFEVL--GPNLLKLIKR-------YNYRGIPLPLVKKIARQVLQGLDYLhTKCGIIHT 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 710 DLATRNCLVG-KNYTIKIADFGMS---RNLYSGDyyrIQGRavlpiRWMSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14136 145 DIKPENVLLCiSKIEVKIADLGNAcwtDKHFTED---IQTR-----QYRSPEVILGAGYGTPADIWSTACMAFELAT 213
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
569-733 4.58e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 52.66  E-value: 4.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVSANQPVLvavkmlradaNKNARNDFLKEIKIMSR-LKDPNIIHLLAVCITD 647
Cdd:cd05604   4 IGKGSFGKVLLAK----RKRDGKYYAVKVLQKKVIL----------NRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd05604  70 DKLYFVLDFVNGGELFFHLQRE----------RSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLT 139

                ....*.
gi 62420884 728 DFGMSR 733
Cdd:cd05604 140 DFGLCK 145
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
678-841 4.61e-07

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: 52.50  E-value: 4.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 678 DVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT----IKIADFGM-----SRNL---YSGDYYRIQG 745
Cdd:cd14018 131 WVNTPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFDgcpwLVIADFGCcladdSIGLqlpFSSWYVDRGG 210
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 746 RAVLpirwMSWESI--LLGKFT----TASDVWAFGVTLWETFTfcQEQPYSQLSDEQVIENTGeffrdqgRQTYLPQ-PA 818
Cdd:cd14018 211 NACL----MAPEVStaVPGPGVvinySKADAWAVGAIAYEIFG--LSNPFYGLGDTMLESRSY-------QESQLPAlPS 277
                       170       180
                ....*....|....*....|...
gi 62420884 819 ICPDSVYKLMLSCWRRDTKNRPS 841
Cdd:cd14018 278 AVPPDVRQVVKDLLQRDPNKRVS 300
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
548-779 8.93e-07

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: 51.55  E-value: 8.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 548 LSGKDVAVEEFPRKLLTFKEKLGEGQFGEVhlcevegmekFKDKDfaldVSANQpvLVAVKMLraDANKNARNDFLKEIK 627
Cdd:cd06636   3 LDDIDLSALRDPAGIFELVEVVGNGTYGQV----------YKGRH----VKTGQ--LAAIKVM--DVTEDEEEEIKLEIN 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 628 IMSRLKD-PNIIHLLAVCIT------DDPLCMITEYMENGDLNQfLSRHEPPNSSSSDVrtvsytnLKFMATQIASGMKY 700
Cdd:cd06636  65 MLKKYSHhRNIATYYGAFIKksppghDDQLWLVMEFCGAGSVTD-LVKNTKGNALKEDW-------IAYICREILRGLAH 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 701 LSSLNFVHRDLATRNCLVGKNYTIKIADFGMS---------RNLYSGDYYriqgravlpirWMSWESILL-----GKFTT 766
Cdd:cd06636 137 LHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSaqldrtvgrRNTFIGTPY-----------WMAPEVIACdenpdATYDY 205
                       250
                ....*....|...
gi 62420884 767 ASDVWAFGVTLWE 779
Cdd:cd06636 206 RSDIWSLGITAIE 218
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
566-841 9.22e-07

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: 51.04  E-value: 9.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVHLCEVEGmekfkdkdfaldvsanQPVLVAVKMLRADANKNARNdfLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14107   7 KEEIGRGTFGFVKRVTHKG----------------NGECCAAKFIPLRSSTRARA--FQERDILARLSHRRLTCLLDQFE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV--GKNYT 723
Cdd:cd14107  69 TRKTLILILELCSSEELLDRLFLKG----------VVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTRED 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 IKIADFGMSRNLysgDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfCQeQPYSQLSDEQVIENT-- 801
Cdd:cd14107 139 IKICDFGFAQEI---TPSEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLT-CH-SPFAGENDRATLLNVae 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 62420884 802 GEFFRDQGRQTYLPQPAicPDSVYKLMlscwRRDTKNRPS 841
Cdd:cd14107 214 GVVSWDTPEITHLSEDA--KDFIKRVL----QPDPEKRPS 247
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
554-733 1.19e-06

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: 51.42  E-value: 1.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 554 AVEEFprkllTFKEKLGEGQFGEVHLceveGMEKFKDKDFALDVsanqpvlvavkMLRADA-NKNARNDFLKEIKIMSRL 632
Cdd:cd05610   2 SIEEF-----VIVKPISRGAFGKVYL----GRKKNNSKLYAVKV-----------VKKADMiNKNMVHQVQAERDALALS 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 633 KDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRH----EPpnssssdvrtvsyTNLKFMAtQIASGMKYLSSLNFVH 708
Cdd:cd05610  62 KSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYgyfdEE-------------MAVKYIS-EVALALDYLHRHGIIH 127
                       170       180
                ....*....|....*....|....*
gi 62420884 709 RDLATRNCLVGKNYTIKIADFGMSR 733
Cdd:cd05610 128 RDLKPDNMLISNEGHIKLTDFGLSK 152
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
569-845 1.34e-06

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: 51.55  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVegmeKFKDKDFALDVsanqpvLVAVKMLradanKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDD 648
Cdd:cd05623  80 IGRGAFGEVAVVKL----KNADKVFAMKI------LNKWEML-----KRAETACFREERDVLVNGDSQWITTLHYAFQDD 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 649 P-LCMITEYMENGDLNQFLSRHEP--PNSSSsdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05623 145 NnLYLVMDYYVGGDLLTLLSKFEDrlPEDMA-----------RFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIR 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRNLYSgDYYRIQGRAVLPIRWMSWESILL-----GKFTTASDVWAFGVTLWETFTfcQEQPYSQlsdEQVIEN 800
Cdd:cd05623 214 LADFGSCLKLME-DGTVQSSVAVGTPDYISPEILQAmedgkGKYGPECDWWSLGVCMYEMLY--GETPFYA---ESLVET 287
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 801 TGEFFRDQGRQTYLPQPAICPDSVYKLM--LSCWR---------RDTKNRPSFQEI 845
Cdd:cd05623 288 YGKIMNHKERFQFPTQVTDVSENAKDLIrrLICSRehrlgqngiEDFKNHPFFVGI 343
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
614-845 1.40e-06

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: 50.78  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 614 ANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQ 693
Cdd:cd14188  40 SKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKAR----------KVLTEPEVRYYLRQ 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 694 IASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYR--IQGRAvlpiRWMSWESILLGKFTTASDVW 771
Cdd:cd14188 110 IVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRrtICGTP----NYLSPEVLNKQGHGCESDIW 185
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 772 AFGVTLwetFTFCQEQPYSQLSdeqvieNTGEFFRDQgRQTYLPQPAICPDSVYKLMLSCWRRDTKNRPSFQEI 845
Cdd:cd14188 186 ALGCVM---YTMLLGRPPFETT------NLKETYRCI-REARYSLPSSLLAPAKHLIASMLSKNPEDRPSLDEI 249
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
569-799 1.51e-06

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: 51.06  E-value: 1.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADA--NKNARNDFLKEIKIMSRLKDPNIIHLLAVCI- 645
Cdd:cd05590   3 LGKGSFGKVMLARLKESGR----------------LYAVKVLKKDVilQDDDVECTMTEKRILSLARNHPFLTQLYCCFq 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05590  67 TPDRLFFVMEFVNGGDLMFHIQKS----------RRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 726 IADFGMSRN-LYSG----------DYyriqgraVLPirwmswESILLGKFTTASDVWAFGVTLWEtfTFCQEQPYSQLSD 794
Cdd:cd05590 137 LADFGMCKEgIFNGkttstfcgtpDY-------IAP------EILQEMLYGPSVDWWAMGVLLYE--MLCGHAPFEAENE 201

                ....*
gi 62420884 795 EQVIE 799
Cdd:cd05590 202 DDLFE 206
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
605-825 1.62e-06

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: 51.24  E-value: 1.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPL------CMITEYMEnGDLNQFLSRHeppnssss 677
Cdd:cd07874  45 VAIKKLsRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELMD-ANLCQVIQME-------- 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 678 dvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNlySGDYYRIQGRAVlpIRWMSWE 757
Cdd:cd07874 116 ----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART--AGTSFMMTPYVV--TRYYRAP 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 758 SILLGK-FTTASDVWAFGVTLWETFTFCQEQPYSQLSDE--QVIENTG----EFFRD---------QGRQTY--LPQPAI 819
Cdd:cd07874 188 EVILGMgYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQwnKVIEQLGtpcpEFMKKlqptvrnyvENRPKYagLTFPKL 267

                ....*.
gi 62420884 820 CPDSVY 825
Cdd:cd07874 268 FPDSLF 273
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
566-775 1.78e-06

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: 50.39  E-value: 1.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVhlcevegmekfkdkdFALdVSANQPVLVAVKMLRADANKNARNdFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd14191   7 EERLGSGKFGQV---------------FRL-VEKKTKKVWAGKFFKAYSAKEKEN-IRQEISIMNCLHHPKLVQCVDAFE 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLsrheppnsSSSDVRTVSYTNLKFMaTQIASGMKYLSSLNFVHRDLATRN--CLVGKNYT 723
Cdd:cd14191  70 EKANIVMVLEMVSGGELFERI--------IDEDFELTERECIKYM-RQISEGVEYIHKQGIVHLDLKPENimCVNKTGTK 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 724 IKIADFGMSRNLYSGDYYRI---QGRAVLPiRWMSWESIllgkfTTASDVWAFGV 775
Cdd:cd14191 141 IKLIDFGLARRLENAGSLKVlfgTPEFVAP-EVINYEPI-----GYATDMWSIGV 189
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
569-781 2.10e-06

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: 50.80  E-value: 2.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRaDANKNARNDFLkEIKIMSRLKDPNIIHLLAV----C 644
Cdd:cd14229   8 LGRGTFGQVVKCWKRGTNE----------------IVAVKILK-NHPSYARQGQI-EVGILARLSNENADEFNFVrayeC 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITD-DPLCMITEYMENgDLNQFLSRHEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCL----VG 719
Cdd:cd14229  70 FQHrNHTCLVFEMLEQ-NLYDFLKQNKFSPLPLKVIRPI--------LQQVATALKKLKSLGLIHADLKPENIMlvdpVR 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 720 KNYTIKIADFGMSRNLysgdyYRIQGRAVLPIRWMSWESILLG-KFTTASDVWAFGVTLWETF 781
Cdd:cd14229 141 QPYRVKVIDFGSASHV-----SKTVCSTYLQSRYYRAPEIILGlPFCEAIDMWSLGCVIAELF 198
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
568-839 2.16e-06

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


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 50.42  E-value: 2.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 568 KLGEGQFGEVHLCEVEGmekfkdkdfaldvsanQPVLVAVKMLRADANknarndFLKEIKIMSR--LKDPNIIHLLAVCI 645
Cdd:cd14220   2 QIGKGRYGEVWMGKWRG----------------EKVAVKVFFTTEEAS------WFRETEIYQTvlMRHENILGFIAADI 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 ----TDDPLCMITEYMENGDLNQFLsrheppNSSSSDVRTVsytnLKfMATQIASGMKYLSSLNF--------VHRDLAT 713
Cdd:cd14220  60 kgtgSWTQLYLITDYHENGSLYDFL------KCTTLDTRAL----LK-LAYSAACGLCHLHTEIYgtqgkpaiAHRDLKS 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMSRNlYSGDYYRIQgravLPI-------RWMSW----ESILLGKFTT--ASDVWAFGVTLWET 780
Cdd:cd14220 129 KNILIKKNGTCCIADLGLAVK-FNSDTNEVD----VPLntrvgtkRYMAPevldESLNKNHFQAyiMADIYSFGLIIWEM 203
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 781 FTFC---------QEQPYSQLSDEQVIENTGEFFRDQGRQTYLP---QPAICPDSVYKLMLSCWRRDTKNR 839
Cdd:cd14220 204 ARRCvtggiveeyQLPYYDMVPSDPSYEDMREVVCVKRLRPTVSnrwNSDECLRAVLKLMSECWAHNPASR 274
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
559-779 2.84e-06

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: 49.64  E-value: 2.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVHLcevegmekfkdkdfALDVSANQpvLVAVKMLRADANknarNDF---LKEIKIMSRLKDP 635
Cdd:cd06646   7 PQHDYELIQRVGSGTYGDVYK--------------ARNLHTGE--LAAVKIIKLEPG----DDFsliQQEIFMVKECKHC 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 636 NIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPpnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd06646  67 NIVAYFGSYLSREKLWICMEYCGGGSLQDIYHVTGP----------LSELQIAYVCRETLQGLAYLHSKGKMHRDIKGAN 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 716 CLVGKNYTIKIADFGMS---------RNLYSGDYYriqgravlpirWMSWESILL---GKFTTASDVWAFGVTLWE 779
Cdd:cd06646 137 ILLTDNGDVKLADFGVAakitatiakRKSFIGTPY-----------WMAPEVAAVeknGGYNQLCDIWAVGITAIE 201
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
565-733 3.67e-06

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: 49.77  E-value: 3.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 565 FKEKLGEGQFGEVHLCevegMEKFKDKDFALDVSANQPvlvavkmlradankNARNdflkEIKIMSRLKD-PNIIHLLAV 643
Cdd:cd14171  10 WTQKLGTGISGPVRVC----VKKSTGERFALKILLDRP--------------KART----EVRLHMMCSGhPNIVQIYDV 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITD----------DPLCMITEYMENGDLNQFLSRHeppnSSSSDVRTVSYTnlkfmaTQIASGMKYLSSLNFVHRDLAT 713
Cdd:cd14171  68 YANSvqfpgessprARLLIVMELMEGGELFDRISQH----RHFTEKQAAQYT------KQIALAVQHCHSLNIAHRDLKP 137
                       170       180
                ....*....|....*....|...
gi 62420884 714 RNCLVGKN---YTIKIADFGMSR 733
Cdd:cd14171 138 ENLLLKDNsedAPIKLCDFGFAK 160
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
550-841 4.06e-06

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 50.25  E-value: 4.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  550 GKDVAVEEFPRKLLTFKEKLGEGQFGEVhLCevegmekfkdkdfALDVSANQPVLVAV----KMLRADANKNARN----- 620
Cdd:PTZ00283  21 AKDEATAKEQAKKYWISRVLGSGATGTV-LC-------------AKRVSDGEPFAVKVvdmeGMSEADKNRAQAEvccll 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  621 --DFLKEIK-----IMSRLKDPNIIHLLAvcitddplcMITEYMENGDLnqflsRHEPPNSSSSDvRTVSYTNLKFMATQ 693
Cdd:PTZ00283  87 ncDFFSIVKchedfAKKDPRNPENVLMIA---------LVLDYANAGDL-----RQEIKSRAKTN-RTFREHEAGLLFIQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  694 IASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR---NLYSGD---------YYriqgraVLPIRWMSwesill 761
Cdd:PTZ00283 152 VLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKmyaATVSDDvgrtfcgtpYY------VAPEIWRR------ 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  762 GKFTTASDVWAFGVTLWETFTFcqEQPYSQLSDEQVIENTgeffrDQGRQTYLPqPAICPD--SVYKLMLScwrRDTKNR 839
Cdd:PTZ00283 220 KPYSKKADMFSLGVLLYELLTL--KRPFDGENMEEVMHKT-----LAGRYDPLP-PSISPEmqEIVTALLS---SDPKRR 288

                 ..
gi 62420884  840 PS 841
Cdd:PTZ00283 289 PS 290
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
569-732 4.83e-06

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: 49.67  E-value: 4.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmekfkdkdfaldvSANQPVLVAVKMLRADANKNARNDFLK-----EIKIMSRLKDPNIIHLLAV 643
Cdd:cd05633  13 IGRGGFGEVYGCR----------------KADTGKMYAMKCLDKKRIKMKQGETLAlneriMLSLVSTGDCPFIVCMTYA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd05633  77 FHTPDKLCFILDLMNGGDLHYHLSQHG----------VFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGH 146

                ....*....
gi 62420884 724 IKIADFGMS 732
Cdd:cd05633 147 VRISDLGLA 155
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
624-782 5.55e-06

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: 49.52  E-value: 5.55e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 624 KEIKIMSRLKDPNIIHLLAVCITDDPL------CMITEYMENgDLNQFLSRHeppnssssdvrtVSYTNLKFMATQIASG 697
Cdd:cd07879  63 RELTLLKHMQHENVIGLLDVFTSAVSGdefqdfYLVMPYMQT-DLQKIMGHP------------LSEDKVQYLVYQMLCG 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 698 MKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSgdyyRIQGRAVlpIRWMSWESILLG--KFTTASDVWAFGV 775
Cdd:cd07879 130 LKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADA----EMTGYVV--TRWYRAPEVILNwmHYNQTVDIWSVGC 203

                ....*..
gi 62420884 776 TLWETFT 782
Cdd:cd07879 204 IMAEMLT 210
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
563-778 6.60e-06

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: 48.82  E-value: 6.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGmekfkdkdfaldvSANQPVL--VAVKmlradaNKNARNDFLKEIKIMSRLK-DPNIIH 639
Cdd:cd14037   5 VTIEKYLAEGGFAHVYLVKTSN-------------GGNRAALkrVYVN------DEHDLNVCKREIEIMKRLSgHKNIVG 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 640 LL---AVCITDD--PLCMITEYMENGDLNQFLSRHEPPNSSSSDVrtvsytnLKFMaTQIASGMKYLSSLN--FVHRDLA 712
Cdd:cd14037  66 YIdssANRSGNGvyEVLLLMEYCKGGGVIDLMNQRLQTGLTESEI-------LKIF-CDVCEAVAAMHYLKppLIHRDLK 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 713 TRNCLVGKNYTIKIADFGMS-------RNLYSGDYYR--IQGRAVLPIRwmSWESILL--GK-FTTASDVWAFGVTLW 778
Cdd:cd14037 138 VENVLISDSGNYKLCDFGSAttkilppQTKQGVTYVEedIKKYTTLQYR--APEMIDLyrGKpITEKSDIWALGCLLY 213
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
606-782 6.67e-06

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; 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. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 48.68  E-value: 6.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 606 AVKMLRADA---NKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLsRHEPPNSSSSDVRTV 682
Cdd:cd14157  20 VIKRLKETEcesPKSTERFFQTEVQICFRCCHPNILPLLGFCVESDCHCLIYPYMPNGSLQDRL-QQQGGSHPLPWEQRL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 SytnlkfmatqIASGM----KYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMsrNLYSGDY---YRIQGRAVLPIR--W 753
Cdd:cd14157  99 S----------ISLGLlkavQHLHNFGILHGNIKSSNVLLDGNLLPKLGHSGL--RLCPVDKksvYTMMKTKVLQISlaY 166
                       170       180
                ....*....|....*....|....*....
gi 62420884 754 MSWESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd14157 167 LPEDFVRHGQLTEKVDIFSCGVVLAEILT 195
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
605-842 6.92e-06

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: 49.27  E-value: 6.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPL------CMITEYMEnGDLNQFLSRHeppnssss 677
Cdd:cd07875  52 VAIKKLsRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLeefqdvYIVMELMD-ANLCQVIQME-------- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 678 dvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNlySGDYYRIQGRAVlpIRWMSWE 757
Cdd:cd07875 123 ----LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLART--AGTSFMMTPYVV--TRYYRAP 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 758 SILLGK-FTTASDVWAFGVTLWETFTFCQEQPYSQLSDE--QVIENTGeffrdqgrqtylpqpAICPDSVYKLMLSCwRR 834
Cdd:cd07875 195 EVILGMgYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQwnKVIEQLG---------------TPCPEFMKKLQPTV-RT 258

                ....*...
gi 62420884 835 DTKNRPSF 842
Cdd:cd07875 259 YVENRPKY 266
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
569-731 7.20e-06

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: 48.85  E-value: 7.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKFkdkdfaldvsanqpvlVAVKMLRADA--NKNARNDFLKEIKI-MSRLKDPNIIHLLAVCI 645
Cdd:cd05575   3 IGKGSFGKVLLARHKAEGKL----------------YAVKVLQKKAilKRNEVKHIMAERNVlLKNVKHPFLVGLHYSFQ 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05575  67 TKDKLYFVLDYVNGGELFFHLQRE----------RHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVV 136

                ....*.
gi 62420884 726 IADFGM 731
Cdd:cd05575 137 LTDFGL 142
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
569-810 7.33e-06

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: 49.24  E-value: 7.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITD 647
Cdd:cd05624  80 IGRGAFGEVAVVKMKNTER----------------IYAMKILnKWEMLKRAETACFREERNVLVNGDCQWITTLHYAFQD 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DP-LCMITEYMENGDLNQFLSRHE---PPNSSssdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd05624 144 ENyLYLVMDYYVGGDLLTLLSKFEdklPEDMA------------RFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGH 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 724 IKIADFGMSRNLySGDYYRIQGRAVLPIRWMSWEsIL------LGKFTTASDVWAFGVTLWETFTfcQEQPYSQlsdEQV 797
Cdd:cd05624 212 IRLADFGSCLKM-NDDGTVQSSVAVGTPDYISPE-ILqamedgMGKYGPECDWWSLGVCMYEMLY--GETPFYA---ESL 284
                       250
                ....*....|...
gi 62420884 798 IENTGEFFRDQGR 810
Cdd:cd05624 285 VETYGKIMNHEER 297
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
646-732 7.87e-06

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: 48.59  E-value: 7.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05606  69 TPDKLCFILDLMNGGDLHYHLSQHG----------VFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVR 138

                ....*..
gi 62420884 726 IADFGMS 732
Cdd:cd05606 139 ISDLGLA 145
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
605-733 8.64e-06

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: 48.95  E-value: 8.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKML-RADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITE-Y--MENGDLN-----QFLSRHEppnss 675
Cdd:cd07850  28 VAIKKLsRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLEEFQDvYlvMELMDANlcqviQMDLDHE----- 102
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 676 ssdvrtvsytNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR 733
Cdd:cd07850 103 ----------RMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR 150
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
598-822 9.96e-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: 48.09  E-value: 9.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 598 SANQPVLVAV--KMLRADANKNARNDFL----KEIKIMSRLKDPNIIHLLAVCIT-DDPLCMITEY----MENgDLNQFL 666
Cdd:cd14011  19 STKQEVSVFVfeKKQLEEYSKRDREQILellkRGVKQLTRLRHPRILTVQHPLEEsRESLAFATEPvfasLAN-VLGERD 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 667 SRHEPPNSSS----SDVRtVSYTNLkfmatQIASGMKYL-SSLNFVHRDLATRNCLVGKNYTIKIADFGMS------RNL 735
Cdd:cd14011  98 NMPSPPPELQdyklYDVE-IKYGLL-----QISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFDFCisseqaTDQ 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 736 YSGDYYRIQGRAVLPI---RWMSWESILLGKFTTASDVWAFGVTLWETFTFCQ---------------EQPYSQLSdEQV 797
Cdd:cd14011 172 FPYFREYDPNLPPLAQpnlNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKplfdcvnnllsykknSNQLRQLS-LSL 250
                       250       260
                ....*....|....*....|....*
gi 62420884 798 IENTGEFFRDQGRQTYLPQPAICPD 822
Cdd:cd14011 251 LEKVPEELRDHVKTLLNVTPEVRPD 275
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
567-731 1.11e-05

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: 48.18  E-value: 1.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegMEKFKDKDFALDVSANQPvlvavkmlradanKNARNDFLKEIKIMSRLK-DPNIIHLLAVCI 645
Cdd:cd14090   8 ELLGEGAYASVQTC----INLYTGKEYAVKIIEKHP-------------GHSRSRVFREVETLHQCQgHPNILQLIEYFE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPPNS--SSSDVRtvsytnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd14090  71 DDERFYLVFEKMRGGPLLSHIEKRVHFTEqeASLVVR------------DIASALDFLHDKGIAHRDLKPENILCESMDK 138
                       170
                ....*....|.
gi 62420884 724 I---KIADFGM 731
Cdd:cd14090 139 VspvKICDFDL 149
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
561-776 1.16e-05

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 47.99  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 561 KLLTFKEKLGEGQFGEVHLCEvegmEKFKDKDFALDVSANQPvlvavkmlradankNARNDFLKEIKIMSRLKDPNIIHL 640
Cdd:cd14110   3 KTYAFQTEINRGRFSVVRQCE----EKRSGQMLAAKIIPYKP--------------EDKQLVLREYQVLRRLSHPRIAQL 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 LAVCITDDPLCMITEYMENGDLNQFLSrhEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd14110  65 HSAYLSPRHLVLIEELCSGPELLYNLA--ERNSYSEAEVTDYLW--------QILSAVDYLHSRRILHLDLRSENMIITE 134
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 721 NYTIKIADFGmSRNLYSGDYYRIQGRAVLPIRWMSWEsILLGK-FTTASDVWAFGVT 776
Cdd:cd14110 135 KNLLKIVDLG-NAQPFNQGKVLMTDKKGDYVETMAPE-LLEGQgAGPQTDIWAIGVT 189
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
605-841 1.21e-05

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 48.10  E-value: 1.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 605 VAVKMLRADANKNARNDflKEIKIMSRLKDPNIIHLLAV----CITDDPLCMITEYMENGDLNQFLSRHeppnssssdvr 680
Cdd:cd14140  21 VAVKIFPIQDKQSWQSE--REIFSTPGMKHENLLQFIAAekrgSNLEMELWLITAFHDKGSLTDYLKGN----------- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 681 TVSYTNLKFMATQIASGMKYLSS-----------LNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRIQGRAVL 749
Cdd:cd14140  88 IVSWNELCHIAETMARGLSYLHEdvprckgeghkPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPGDTHGQVG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 750 PIRWMSWEsILLG--KFTTAS----DVWAFGVTLWETFTFC-------------------QEQPYSQLSDEQVIENTGEF 804
Cdd:cd14140 168 TRRYMAPE-VLEGaiNFQRDSflriDMYAMGLVLWELVSRCkaadgpvdeymlpfeeeigQHPSLEDLQEVVVHKKMRPV 246
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 62420884 805 FRDQgrqtYLPQPAICPDSVykLMLSCWRRDTKNRPS 841
Cdd:cd14140 247 FKDH----WLKHPGLAQLCV--TIEECWDHDAEARLS 277
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
625-780 1.33e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 48.74  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  625 EIKIMSRLKDPNIIHLLAVCITDDPLCMIT-EYmeNGDLNQFLSRHeppnssssdVRTVSYTNLKFMATQIASGMKYLSS 703
Cdd:PHA03211 210 EARLLRRLSHPAVLALLDVRVVGGLTCLVLpKY--RSDLYTYLGAR---------LRPLGLAQVTAVARQLLSAIDYIHG 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884  704 LNFVHRDLATRNCLVGKNYTIKIADFG---MSRNLYSGD-YYRIQGravlPIRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:PHA03211 279 EGIIHRDIKTENVLVNGPEDICLGDFGaacFARGSWSTPfHYGIAG----TVDTNAPEVLAGDPYTPSVDIWSAGLVIFE 354

                 .
gi 62420884  780 T 780
Cdd:PHA03211 355 A 355
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
615-845 1.39e-05

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


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 47.74  E-value: 1.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 615 NKNARNDFLKEIKIMSRLKDPNIIHLL----AVCITDDPLCMITEYMENGDLNQFLSRheppnssssdVRTVSYTNLKFM 690
Cdd:cd14030  64 SKSERQRFKEEAGMLKGLQHPNIVRFYdsweSTVKGKKCIVLVTELMTSGTLKTYLKR----------FKVMKIKVLRSW 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 691 ATQIASGMKYLSSLN--FVHRDLATRNCLV-GKNYTIKIADFGMSrNLYSGDYyriqGRAVLPIRWMSWESILLGKFTTA 767
Cdd:cd14030 134 CRQILKGLQFLHTRTppIIHRDLKCDNIFItGPTGSVKIGDLGLA-TLKRASF----AKSVIGTPEFMAPEMYEEKYDES 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 768 SDVWAFGVTLWETFTfcQEQPYSQlsdeqvIENTGEFFRdqgRQTYLPQPA----ICPDSVYKLMLSCWRRDTKNRPSFQ 843
Cdd:cd14030 209 VDVYAFGMCMLEMAT--SEYPYSE------CQNAAQIYR---RVTSGVKPAsfdkVAIPEVKEIIEGCIRQNKDERYAIK 277

                ..
gi 62420884 844 EI 845
Cdd:cd14030 278 DL 279
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
594-779 1.40e-05

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: 48.10  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 594 ALDVSANQPVLVAvKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPL------CMITEYMEnGDLNQFLS 667
Cdd:cd07876  40 AFDTVLGINVAVK-KLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELMD-ANLCQVIH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 668 RHeppnssssdvrtVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR----NLYSGDYyri 743
Cdd:cd07876 118 ME------------LDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARtactNFMMTPY--- 182
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 62420884 744 qgraVLPIRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd07876 183 ----VVTRYYRAPEVILGMGYKENVDIWSVGCIMGE 214
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
603-852 1.70e-05

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: 47.75  E-value: 1.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 603 VLVAVKMLRADANKNARNDFLKEIKIMSRLKD-PNIIHLLAVCITDDP--LCMitEYMENGdLNQFLSRHEPPnssssdv 679
Cdd:cd06618  41 HVMAVKQMRRSGNKEENKRILMDLDVVLKSHDcPYIVKCYGYFITDSDvfICM--ELMSTC-LDKLLKRIQGP------- 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 680 rtVSYTNLKFMATQIASGMKYLSSL-NFVHRDLATRNCLVGKNYTIKIADFGMS-RNLYSGDYYRIQGRAVlpirWMSWE 757
Cdd:cd06618 111 --IPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGISgRLVDSKAKTRSAGCAA----YMAPE 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 758 SI---LLGKFTTASDVWAFGVTLWETFTfcQEQPYSqlsdeqviENTGEfFRDQGRQTYLPQPAICPDSVYKLML----- 829
Cdd:cd06618 185 RIdppDNPKYDIRADVWSLGISLVELAT--GQFPYR--------NCKTE-FEVLTKILNEEPPSLPPNEGFSPDFcsfvd 253
                       250       260
                ....*....|....*....|...
gi 62420884 830 SCWRRDTKNRPSFQEihllLLQQ 852
Cdd:cd06618 254 LCLTKDHRYRPKYRE----LLQH 272
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
564-733 1.90e-05

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: 47.25  E-value: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 564 TFKEKLGEGQFGEVhlcevegmekFKdkdfALDVSANQpvLVAVKMLRADANKNArndfLK-EIKIMSRLkdpniihlla 642
Cdd:cd14017   3 KVVKKIGGGGFGEI----------YK----VRDVVDGE--EVAMKVESKSQPKQV----LKmEVAVLKKL---------- 52
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 vcitdDPLCMITEYMENGDLNQF--------------LSRHEPPN--SSSSDVRtvsytnlkfMATQIASGMKYLSSLNF 706
Cdd:cd14017  53 -----QGKPHFCRLIGCGRTERYnyivmtllgpnlaeLRRSQPRGkfSVSTTLR---------LGIQILKAIEDIHEVGF 118
                       170       180       190
                ....*....|....*....|....*....|.
gi 62420884 707 VHRDLATRNCLVGKN----YTIKIADFGMSR 733
Cdd:cd14017 119 LHRDVKPSNFAIGRGpsdeRTVYILDFGLAR 149
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
567-781 2.11e-05

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: 47.78  E-value: 2.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARNDFlkEIKIMSRLK-----DPNIIHLL 641
Cdd:cd14227  21 EFLGRGTFGQVVKCWKRGTNE----------------IVAIKILKNHPSYARQGQI--EVSILARLStesadDYNFVRAY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 AVCITDDPLCMITEYMENgDLNQFLSRHEPPNSSSSDVRTVsytnlkfmATQIASGMKYLSSLNFVHRDLATRNCLV--- 718
Cdd:cd14227  83 ECFQHKNHTCLVFEMLEQ-NLYDFLKQNKFSPLPLKYIRPI--------LQQVATALMKLKSLGLIHADLKPENIMLvdp 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 719 -GKNYTIKIADFGMSRNLysgdyYRIQGRAVLPIRWMSWESILLG-KFTTASDVWAFGVTLWETF 781
Cdd:cd14227 154 sRQPYRVKVIDFGSASHV-----SKAVCSTYLQSRYYRAPEIILGlPFCEAIDMWSLGCVIAELF 213
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
559-779 2.25e-05

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: 47.41  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 559 PRKLLTFKEKLGEGQFGEVhlcevegmekFKDKDfaldVSANQpvLVAVKMLraDANKNARNDFLKEIKIMSRLKD-PNI 637
Cdd:cd06637   4 PAGIFELVELVGNGTYGQV----------YKGRH----VKTGQ--LAAIKVM--DVTGDEEEEIKQEINMLKKYSHhRNI 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 638 IHLLAVCI------TDDPLCMITEYMENGDLNQFLSrheppnssSSDVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDL 711
Cdd:cd06637  66 ATYYGAFIkknppgMDDQLWLVMEFCGAGSVTDLIK--------NTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDI 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 712 ATRNCLVGKNYTIKIADFGMS---------RNLYSGDYYriqgravlpirWMSWESILL-----GKFTTASDVWAFGVTL 777
Cdd:cd06637 138 KGQNVLLTENAEVKLVDFGVSaqldrtvgrRNTFIGTPY-----------WMAPEVIACdenpdATYDFKSDLWSLGITA 206

                ..
gi 62420884 778 WE 779
Cdd:cd06637 207 IE 208
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
569-750 2.60e-05

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: 47.54  E-value: 2.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVsanqpvLVAVKMLRAD--ANKNARNDFLKE------IKIMSRLKDPNIIHL 640
Cdd:cd05629   9 IGKGAFGEVRLVQ----KKDTGKIYAMKT------LLKSEMFKKDqlAHVKAERDVLAEsdspwvVSLYYSFQDAQYLYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 lavcitddplcmITEYMENGDLNQFLSRHEppnSSSSDVRtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd05629  79 ------------IMEFLPGGDLMTMLIKYD---TFSEDVT-------RFYMAECVLAIEAVHKLGFIHRDIKPDNILIDR 136
                       170       180       190
                ....*....|....*....|....*....|....*
gi 62420884 721 NYTIKIADFGMSRNLYSGD---YYR--IQGRAVLP 750
Cdd:cd05629 137 GGHIKLSDFGLSTGFHKQHdsaYYQklLQGKSNKN 171
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
623-789 2.98e-05

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: 46.73  E-value: 2.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 623 LKEIKIMSRLKDPNII--------HLLAVCITDDPLCMITEYMENGDLNQFlSRHEPPNSSSSDVRTVSYTNLKFMatQI 694
Cdd:cd14049  53 LREVKVLAGLQHPNIVgyhtawmeHVQLMLYIQMQLCELSLWDWIVERNKR-PCEEEFKSAPYTPVDVDVTTKILQ--QL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 695 ASGMKYLSSLNFVHRDLATRNCLV-GKNYTIKIADFGMS------RNLYSGDYYRIQG----RAVLPIRWMSWESILLGK 763
Cdd:cd14049 130 LEGVTYIHSMGIVHRDLKPRNIFLhGSDIHVRIGDFGLAcpdilqDGNDSTTMSRLNGlthtSGVGTCLYAAPEQLEGSH 209
                       170       180
                ....*....|....*....|....*.
gi 62420884 764 FTTASDVWAFGVTLWETFtfcqeQPY 789
Cdd:cd14049 210 YDFKSDMYSIGVILLELF-----QPF 230
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
569-733 3.30e-05

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: 46.72  E-value: 3.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANknARNDFL------KEIKIMSRlKDPNIIHLLA 642
Cdd:cd05591   3 LGKGSFGKVMLAERKGTDE----------------VYAIKVLKKDVI--LQDDDVdctmteKRILALAA-KHPFLTALHS 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 643 VCITDDPLCMITEYMENGDLNQFLSRheppnssssdVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05591  64 CFQTKDRLFFVMEYVNGGDLMFQIQR----------ARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEG 133
                       170
                ....*....|.
gi 62420884 723 TIKIADFGMSR 733
Cdd:cd05591 134 HCKLADFGMCK 144
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
566-730 3.73e-05

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: 46.13  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 566 KEKLGEGQFGEVhlceVEGMEKFKDKDFALdvsanqpvlvavKMLRAdaNKNARNdflkEIKIMSRLKD-PNIIHLLAV- 643
Cdd:cd14089   6 KQVLGLGINGKV----LECFHKKTGEKFAL------------KVLRD--NPKARR----EVELHWRASGcPHIVRIIDVy 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 --------CitddpLCMITEYMENGDLNQFLSRHEPPNSSSSDVRTVSYtnlkfmatQIASGMKYLSSLNFVHRDLATRN 715
Cdd:cd14089  64 entyqgrkC-----LLVVMECMEGGELFSRIQERADSAFTEREAAEIMR--------QIGSAVAHLHSMNIAHRDLKPEN 130
                       170
                ....*....|....*...
gi 62420884 716 CLV---GKNYTIKIADFG 730
Cdd:cd14089 131 LLYsskGPNAILKLTDFG 148
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
569-782 3.87e-05

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: 46.53  E-value: 3.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLC-EVEGMEKfkDKDFALDVSANQPVLVAVKMlrADANKNARNdFLKEIKimsrlKDPNIIHLLAVCITD 647
Cdd:cd05613   8 LGTGAYGKVFLVrKVSGHDA--GKLYAMKVLKKATIVQKAKT--AEHTRTERQ-VLEHIR-----QSPFLVTLHYAFQTD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd05613  78 TKLHLILDYINGGELFTHLSQRE----------RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLT 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 728 DFGMSRNLYSGDY---YRIQGravlPIRWMSWESILLGK--FTTASDVWAFGVTLWETFT 782
Cdd:cd05613 148 DFGLSKEFLLDENeraYSFCG----TIEYMAPEIVRGGDsgHDKAVDWWSLGVLMYELLT 203
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
567-720 4.71e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 46.17  E-value: 4.71e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCevegMEKFKDKDFALDVSaNQPVLVAVKmlradaNKNArndfLKEIKIMSRL-KDPNIIHLLAVCI 645
Cdd:cd14138  11 EKIGSGEFGSVFKC----VKRLDGCIYAIKRS-KKPLAGSVD------EQNA----LREVYAHAVLgQHSHVVRYYSAWA 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRheppnssssDVRTVSY---TNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGK 720
Cdd:cd14138  76 EDDHMLIQNEYCNGGSLADAISE---------NYRIMSYftePELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISR 144
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
569-782 4.78e-05

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: 46.33  E-value: 4.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHlcevEGMEKFKDKDFALDVSANqpvlvaVKMLR-ADANKnarndflKEIKIMSRLKDPNIIHLLAV--CI 645
Cdd:cd13988   1 LGQGATANVF----RGRHKKTGDLYAVKVFNN------LSFMRpLDVQM-------REFEVLKKLNHKNIVKLFAIeeEL 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSrhEPPNS---SSSDVRTVSytnlkfmaTQIASGMKYLSSLNFVHRDLATRNCL--VGK 720
Cdd:cd13988  64 TTRHKVLVMELCPCGSLYTVLE--EPSNAyglPESEFLIVL--------RDVVAGMNHLRENGIVHRDIKPGNIMrvIGE 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62420884 721 NYT--IKIADFGMSR---------NLYSGDYY---RIQGRAVLpirwmswESILLGKFTTASDVWAFGVTLWETFT 782
Cdd:cd13988 134 DGQsvYKLTDFGAAReleddeqfvSLYGTEEYlhpDMYERAVL-------RKDHQKKYGATVDLWSIGVTFYHAAT 202
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
563-730 4.99e-05

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: 45.96  E-value: 4.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEKLGEGQFGEVHLCEVEGmekfKDKDFALDvsanqpvlvavKMLRADANKNarNDFLKEIKIMSRLK-DPNIIHLL 641
Cdd:cd14036   2 LRIKRVIAEGGFAFVYEAQDVG----TGKEYALK-----------RLLSNEEEKN--KAIIQEINFMKKLSgHPNIVQFC 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 642 -AVCI---TDDPLC----MITEYMEnGDLNQFLSRHEPPNSSSSDvrtvsyTNLKFMaTQIASGMKYL--SSLNFVHRDL 711
Cdd:cd14036  65 sAASIgkeESDQGQaeylLLTELCK-GQLVDFVKKVEAPGPFSPD------TVLKIF-YQTCRAVQHMhkQSPPIIHRDL 136
                       170
                ....*....|....*....
gi 62420884 712 ATRNCLVGKNYTIKIADFG 730
Cdd:cd14036 137 KIENLLIGNQGQIKLCDFG 155
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
567-781 5.98e-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: 46.24  E-value: 5.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 567 EKLGEGQFGEVHLCEVEGMEKfkdkdfaldvsanqpvLVAVKMLRADANKNARNDFlkEIKIMSRLKDPNIIHLLAV--- 643
Cdd:cd14228  21 EFLGRGTFGQVAKCWKRSTKE----------------IVAIKILKNHPSYARQGQI--EVSILSRLSSENADEYNFVrsy 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 -CIT-DDPLCMITEYMENgDLNQFLSRHEppnssssdVRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCL---- 717
Cdd:cd14228  83 eCFQhKNHTCLVFEMLEQ-NLYDFLKQNK--------FSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMlvdp 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62420884 718 VGKNYTIKIADFGMSRNLysgdyYRIQGRAVLPIRWMSWESILLG-KFTTASDVWAFGVTLWETF 781
Cdd:cd14228 154 VRQPYRVKVIDFGSASHV-----SKAVCSTYLQSRYYRAPEIILGlPFCEAIDMWSLGCVIAELF 213
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
569-782 6.86e-05

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: 46.07  E-value: 6.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLC-EVEGMEKfkDKDFALDVsANQPVLVAvKMLRADANKNARNdFLKEIKimsrlKDPNIIHLLAVCITD 647
Cdd:cd05614   8 LGTGAYGKVFLVrKVSGHDA--NKLYAMKV-LRKAALVQ-KAKTVEHTRTERN-VLEHVR-----QSPFLVTLHYAFQTD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 648 DPLCMITEYMENGDLnqFLSRHEPPNSSSSDVRtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIA 727
Cdd:cd05614  78 AKLHLILDYVSGGEL--FTHLYQRDHFSEDEVR--------FYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLT 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 728 DFGMSRNLYSGDYYRIQGRAVlPIRWMSWEsILLGK--FTTASDVWAFGVTLWETFT 782
Cdd:cd05614 148 DFGLSKEFLTEEKERTYSFCG-TIEYMAPE-IIRGKsgHGKAVDWWSLGILMFELLT 202
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
561-839 8.82e-05

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, 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 BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 45.43  E-value: 8.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 561 KLLTFKEKLGEGQFGEVHLCEVEGmEKfkdkdfaldvsanqpvlVAVKMLRADANKNarndFLKEIKIMSR--LKDPNII 638
Cdd:cd14219   5 KQIQMVKQIGKGRYGEVWMGKWRG-EK-----------------VAVKVFFTTEEAS----WFRETEIYQTvlMRHENIL 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 639 HLLAVCITDD----PLCMITEYMENGDLNQFLSrheppnSSSSDVRTVsytnLKfMATQIASGMKYLSSLNF-------- 706
Cdd:cd14219  63 GFIAADIKGTgswtQLYLITDYHENGSLYDYLK------STTLDTKAM----LK-LAYSSVSGLCHLHTEIFstqgkpai 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 707 VHRDLATRNCLVGKNYTIKIADFGMSRNLYSGD-------YYRIQGRAVLPIRWMSwESILLGKFTT--ASDVWAFGVTL 777
Cdd:cd14219 132 AHRDLKSKNILVKKNGTCCIADLGLAVKFISDTnevdippNTRVGTKRYMPPEVLD-ESLNRNHFQSyiMADMYSFGLIL 210
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 778 WETFTFC--------QEQPYSQL-SDEQVIENTGEFFRDQGRQTYLPQ---PAICPDSVYKLMLSCWRRDTKNR 839
Cdd:cd14219 211 WEVARRCvsggiveeYQLPYHDLvPSDPSYEDMREIVCIKRLRPSFPNrwsSDECLRQMGKLMTECWAHNPASR 284
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
569-732 9.30e-05

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: 45.42  E-value: 9.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmekfkdkdfaldvSANQPVLVAVKMLRADANKNARNDFLK-----EIKIMSRLKDPNIIHLLAV 643
Cdd:cd14223   8 IGRGGFGEVYGCR----------------KADTGKMYAMKCLDKKRIKMKQGETLAlneriMLSLVSTGDCPFIVCMSYA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd14223  72 FHTPDKLSFILDLMNGGDLHYHLSQHG----------VFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGH 141

                ....*....
gi 62420884 724 IKIADFGMS 732
Cdd:cd14223 142 VRISDLGLA 150
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
650-845 1.05e-04

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: 45.42  E-value: 1.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 650 LCMITEYMENGDLNQFLSRHE---PPNSsssdvrtvsytnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05597  76 LYLVMDYYCGGDLLTLLSKFEdrlPEEM------------ARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRL 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 727 ADFGMSRNLYSGDYyrIQGR-AVLPIRWMSWEsIL------LGKFTTASDVWAFGVTLWETFtFCQEQPYSqlsdEQVIE 799
Cdd:cd05597 144 ADFGSCLKLREDGT--VQSSvAVGTPDYISPE-ILqamedgKGRYGPECDWWSLGVCMYEML-YGETPFYA----ESLVE 215
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884 800 NTGEFFRDQGRQTYLPQ----PAICPDSVYKLMLSCWRR-------DTKNRPSFQEI 845
Cdd:cd05597 216 TYGKIMNHKEHFSFPDDeddvSEEAKDLIRRLICSRERRlgqngidDFKKHPFFEGI 272
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
569-786 1.30e-04

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: 45.09  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvEGMEKFKDKDFALDVsanqpvLVAVKMLRADAN----KNARNdflkeikIMSRLKDPNIIHLLAVC 644
Cdd:cd05584   4 LGKGGYGKVFQVR-KTTGSDKGKIFAMKV------LKKASIVRNQKDtahtKAERN-------ILEAVKHPFIVDLHYAF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 645 ITDDPLCMITEYMENGDLNQFLSRHE--PPNSSSsdvrtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNY 722
Cdd:cd05584  70 QTGGKLYLILEYLSGGELFMHLEREGifMEDTAC------------FYLAEITLALGHLHSLGIIYRDLKPENILLDAQG 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62420884 723 TIKIADFGMSRNlysgdyyRIQGRAVL-----PIRWMSWESILLGKFTTASDVWAFGVTLWETFT----FCQE 786
Cdd:cd05584 138 HVKLTDFGLCKE-------SIHDGTVThtfcgTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTgappFTAE 203
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
604-841 1.72e-04

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 44.59  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 604 LVAVKMLRAD-ANKNARNDFLKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNssssdvrtV 682
Cdd:cd08216  27 LVAVKKINLEsDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLKTHFPEG--------L 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 683 SYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDY-------YRIQGRAVLPirWMS 755
Cdd:cd08216  99 PELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHGKrqrvvhdFPKSSEKNLP--WLS 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 756 WESI---LLGkFTTASDVWAFGVT------------------------------LWETFTFCQEQPYSQLSDEQVIENTG 802
Cdd:cd08216 177 PEVLqqnLLG-YNEKSDIYSVGITacelangvvpfsdmpatqmllekvrgttpqLLDCSTYPLEEDSMSQSEDSSTEHPN 255
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 62420884 803 effrdqGRQTY-LPQPAICPDSVYKLMLSCWRRDTKNRPS 841
Cdd:cd08216 256 ------NRDTRdIPYQRTFSEAFHQFVELCLQRDPELRPS 289
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
563-804 1.92e-04

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: 44.26  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 563 LTFKEK-LGEGQFGEVHLCevegmekfkdkdfaLDVSANQPVLVAVKMLRADANKNarndflKEIKIMSRLKD-PNIIHL 640
Cdd:cd14179   8 LDLKDKpLGEGSFSICRKC--------------LHKKTNQEYAVKIVSKRMEANTQ------REIAALKLCEGhPNIVKL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 641 LAVCITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLV-- 718
Cdd:cd14179  68 HEVYHDQLHTFLVMELLKGGELLERIKKK----------QHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtd 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 719 -GKNYTIKIADFGMSRnLYSGDYYRIQgRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTF-----CQEQPYSQL 792
Cdd:cd14179 138 eSDNSEIKIIDFGFAR-LKPPDNQPLK-TPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGqvpfqCHDKSLTCT 215
                       250
                ....*....|....
gi 62420884 793 SDEQVIE--NTGEF 804
Cdd:cd14179 216 SAEEIMKkiKQGDF 229
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
653-779 2.67e-04

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 43.68  E-value: 2.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 653 ITEYMENGDLNQFLSRheppnsSSSDVRTVSYTNLKFMATQIASGMKYLSSLN--FVHRDLATRNCLVGKNYTIKIADFG 730
Cdd:cd13984  77 ITEYMSSGSLKQFLKK------TKKNHKTMNEKSWKRWCTQILSALSYLHSCDppIIHGNLTCDTIFIQHNGLIKIGSVA 150
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 62420884 731 MSRNLYSGDYYRIQGRAvlpIRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd13984 151 PDAIHNHVKTCREEHRN---LHFFAPEYGYLEDVTTAVDIYSFGMCALE 196
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
646-782 3.37e-04

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: 43.54  E-value: 3.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHEPpnSSSSDVRtvsytnlkFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIK 725
Cdd:cd05583  70 TDAKLHLILDYVNGGELFTHLYQREH--FTESEVR--------IYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVV 139
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62420884 726 IADFGMSRNLYSGDYYRIQ---GravlPIRWMSWESILLGK--FTTASDVWAFGVTLWETFT 782
Cdd:cd05583 140 LTDFGLSKEFLPGENDRAYsfcG----TIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELLT 197
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
623-824 4.88e-04

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: 43.33  E-value: 4.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 623 LKEIKIMSRLKDPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnlKFMATQIASGMKYLS 702
Cdd:cd05585  42 LAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGELFHHLQREGRFDLSRA----------RFYTAELLCALECLH 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 703 SLNFVHRDLATRNCLVGKNYTIKIADFGMSR-NLYSGDyyRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWETF 781
Cdd:cd05585 112 KFNVIYRDLKPENILLDYTGHIALCDFGLCKlNMKDDD--KTNTFCGTP-EYLAPELLLGHGYTKAVDWWTLGVLLYEML 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 62420884 782 TFCqeQPYSQlsdeqviENTGEFFRdqgrqTYLPQPAICPDSV 824
Cdd:cd05585 189 TGL--PPFYD-------ENTNEMYR-----KILQEPLRFPDGF 217
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
634-824 4.91e-04

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: 43.47  E-value: 4.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 634 DPNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLAT 713
Cdd:cd05617  75 NPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQ----------RKLPEEHARFYAAEICIALNFLHERGIIYRDLKL 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 714 RNCLVGKNYTIKIADFGMSRN-LYSGDyyrIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETFTfcQEQPYSQL 792
Cdd:cd05617 145 DNVLLDADGHIKLTDYGMCKEgLGPGD---TTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMA--GRSPFDII 219
                       170       180       190
                ....*....|....*....|....*....|..
gi 62420884 793 SDEQVIeNTGEFFrdqgRQTYLPQPAICPDSV 824
Cdd:cd05617 220 TDNPDM-NTEDYL----FQVILEKPIRIPRFL 246
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
570-788 5.71e-04

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: 42.99  E-value: 5.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 570 GEGQFGEVHLC------EVEGMEKFKDKDfaldvsanqpvlvavkMLRADANKNARndflKEIKIMSRLKDPNIIHLLAV 643
Cdd:cd05599  10 GRGAFGEVRLVrkkdtgHVYAMKKLRKSE----------------MLEKEQVAHVR----AERDILAEADNPWVVKLYYS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 644 CITDDPLCMITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd05599  70 FQDEENLYLIMEFLPGGDMMTLLMKKD----------TLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGH 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62420884 724 IKIADFGMSRNL------YSG----DYyriqgraVLPirwmswESILLGKFTTASDVWAFGVTLWETFT----FCQEQP 788
Cdd:cd05599 140 IKLSDFGLCTGLkkshlaYSTvgtpDY-------IAP------EVFLQKGYGKECDWWSLGVIMYEMLIgyppFCSDDP 205
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
569-742 9.06e-04

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 42.69  E-value: 9.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHL-CEVegmekfkdkdfalDVSAnqpvLVAVKMLRAD--ANKNARNDFLKEIKIMSRLKDPNIIHLLAVCI 645
Cdd:cd05626   9 LGIGAFGEVCLaCKV-------------DTHA----LYAMKTLRKKdvLNRNQVAHVKAERDILAEADNEWVVKLYYSFQ 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 646 TDDPLCMITEYMENGDLNQFLSRHE--PPNSSssdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYT 723
Cdd:cd05626  72 DKDNLYFVMDYIPGGDMMSLLIRMEvfPEVLA------------RFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGH 139
                       170       180
                ....*....|....*....|..
gi 62420884 724 IKIADFGMS---RNLYSGDYYR 742
Cdd:cd05626 140 IKLTDFGLCtgfRWTHNSKYYQ 161
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
697-779 1.67e-03

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: 41.52  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 697 GMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSGDYYRiqGRAVLPIRWMSWESILLGK-----FTTASDVW 771
Cdd:cd06639 140 GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSARLRR--NTSVGTPFWMAPEVIACEQqydysYDARCDVW 217

                ....*...
gi 62420884 772 AFGVTLWE 779
Cdd:cd06639 218 SLGITAIE 225
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
624-733 1.91e-03

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: 39.94  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 624 KEIKIMSRLKD-----PNIIhllAVCITDDplCMITEYMENGDLNQFLSRHEPPNssssdvrtvsyTNLKFMATQIASgm 698
Cdd:COG3642   5 REARLLRELREagvpvPKVL---DVDPDDA--DLVMEYIEGETLADLLEEGELPP-----------ELLRELGRLLAR-- 66
                        90       100       110
                ....*....|....*....|....*....|....*
gi 62420884 699 kyLSSLNFVHRDLATRNCLVGKNyTIKIADFGMSR 733
Cdd:COG3642  67 --LHRAGIVHGDLTTSNILVDDG-GVYLIDFGLAR 98
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
623-775 1.93e-03

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: 40.96  E-value: 1.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 623 LKEIKIMSRLKDPNIIHLLAVciTDDPLCMITEYMENGDLNQFLSRHEPPnssSSDVRTvsYTNLKFMATQIASGMKYLS 702
Cdd:cd14109  44 MREVDIHNSLDHPNIVQMHDA--YDDEKLAVTVIDNLASTIELVRDNLLP---GKDYYT--ERQVAVFVRQLLLALKHMH 116
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62420884 703 SLNFVHRDLATRNCLVGKNYtIKIADFGMSRNLYSGDYY-RIQGravLPiRWMSWESILLGKFTTASDVWAFGV 775
Cdd:cd14109 117 DLGIAHLDLRPEDILLQDDK-LKLADFGQSRRLLRGKLTtLIYG---SP-EFVSPEIVNSYPVTLATDMWSVGV 185
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
672-738 2.65e-03

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 41.21  E-value: 2.65e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62420884  672 PNSSSSDVRTVSYtnLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNLYSG 738
Cdd:PLN03224 298 PDNMPQDKRDINV--IKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVDGQVKIIDFGAAVDMCTG 362
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
635-739 3.05e-03

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: 40.79  E-value: 3.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 635 PNIIHLLAVCITDDPLCMITEYMENGDLNQFLSRHeppnssssdvRTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05618  81 PFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQ----------RKLPEEHARFYSAEISLALNYLHERGIIYRDLKLD 150
                        90       100
                ....*....|....*....|....*.
gi 62420884 715 NCLVGKNYTIKIADFGMSRN-LYSGD 739
Cdd:cd05618 151 NVLLDSEGHIKLTDYGMCKEgLRPGD 176
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
680-739 3.85e-03

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: 39.92  E-value: 3.85e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62420884 680 RTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSRNL-YSGD 739
Cdd:cd14187 102 KALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVeYDGE 162
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
569-742 5.04e-03

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: 40.02  E-value: 5.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVSANQPVLVA--VKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLlavcit 646
Cdd:cd05628   9 IGRGAFGEVRLVQ----KKDTGHVYAMKILRKADMLEKeqVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYL------ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 ddplcmITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05628  79 ------IMEFLPGGDMMTLLMKKD----------TLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKL 142
                       170
                ....*....|....*....
gi 62420884 727 ADFGMSRNL---YSGDYYR 742
Cdd:cd05628 143 SDFGLCTGLkkaHRTEFYR 161
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
569-742 6.63e-03

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: 39.66  E-value: 6.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCEvegmEKFKDKDFALDVSANQPVLVA--VKMLRADANKNARNDFLKEIKIMSRLKDPNIIHLlavcit 646
Cdd:cd05627  10 IGRGAFGEVRLVQ----KKDTGHIYAMKILRKADMLEKeqVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYL------ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 647 ddplcmITEYMENGDLNQFLSRHEppnssssdvrTVSYTNLKFMATQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 726
Cdd:cd05627  80 ------IMEFLPGGDMMTLLMKKD----------TLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKL 143
                       170
                ....*....|....*....
gi 62420884 727 ADFGMSRNL---YSGDYYR 742
Cdd:cd05627 144 SDFGLCTGLkkaHRTEFYR 162
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
569-779 8.09e-03

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: 39.22  E-value: 8.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 569 LGEGQFGEVHLCevegmeKFKDKDFaldvsanqpvLVAVKMLR-AD-------ANKNARNDFLKE------IKIMSRLKD 634
Cdd:cd05598   9 IGVGAFGEVSLV------RKKDTNA----------LYAMKTLRkKDvlkrnqvAHVKAERDILAEadnewvVKLYYSFQD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62420884 635 pniihllavcitDDPLCMITEYMENGDLNQFLSRHEPPNSSSSdvrtvsytnlKFMATQIASGMKYLSSLNFVHRDLATR 714
Cdd:cd05598  73 ------------KENLYFVMDYIPGGDLMSLLIKKGIFEEDLA----------RFYIAELVCAIESVHKMGFIHRDIKPD 130
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62420884 715 NCLVGKNYTIKIADFGMS---RNLYSGDYYRIQGRAVLPiRWMSWESILLGKFTTASDVWAFGVTLWE 779
Cdd:cd05598 131 NILIDRDGHIKLTDFGLCtgfRWTHDSKYYLAHSLVGTP-NYIAPEVLLRTGYTQLCDWWSVGVILYE 197
 
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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