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Conserved domains on  [gi|442620116|ref|NP_001262771|]
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Leucine-rich repeat kinase, isoform C [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
1710-2004 2.26e-150

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: 467.48  E-value: 2.26e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVrgarsfKPVAMKMLQPVPPGARAKESALMAFkvavgkwDRDPLQHSCKAYCTARQELAVLLTL 1789
Cdd:cd14000     1 LLGDGGFGSVYRASYKG------EPVAVKIFNKHTSSNFANVPADTML-------RHLRATDAMKNFRLLRQELTVLSHL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVWE 1869
Cdd:cd14000    68 HHPSIVYLLGIGIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 LPQPhtedsprNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNgeEEYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd14000   148 LYPN-------SAIIIKIADYGISRQCCRMGAKGSEGTPGFRAPEIARGN--VIYNEKVDVFSFGMLLYEILSGGAPMVG 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1950 HESIKEC--ILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSILSAP 2004
Cdd:cd14000   219 HLKFPNEfdIHGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVSILNSP 275
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
902-1120 6.63e-32

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd09914:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 161  Bit Score: 123.22  E-value: 6.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  902 RMKLMVVGVAGIGKSTLLDLLRqgagsgssssshrsrasenhWAKRMGHarstsrshrhssassaNISTVGVDIGTWice 981
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLI--------------------GEKFDGD----------------ESSTHGINVQDW--- 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  982 krKRAPGSHGPVVFRTWDFGGQKEYYATHQYFLSKRSLYLVLWRISDGHKGLAeLLQWLGNIQARAPNSPVIIVGTHFDA 1061
Cdd:cd09914    42 --KIPAPERKKIRLNVWDFGGQEIYHATHQFFLTSRSLYLLVFDLRTGDEVSR-VPYWLRQIKAFGGVSPVILVGTHIDE 118
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1062 vgesispQKAEQ-LQQLIREKFiaipdaekigLPRVIDSIEISCRTLHNIHLLANIIYDT 1120
Cdd:cd09914   119 -------SCDEDiLKKALNKKF----------PAIINDIHFVSCKNGKGIAELKKAIAKE 161
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
453-677 4.21e-29

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 122.73  E-value: 4.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  453 LTAITRIDFSHNVLTSIPQELFHLVSLRYLNVAQNKITDLPAPIGQtygCPVLDELFLQDNQLTTLPAAIFHLPALSILD 532
Cdd:COG4886   112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGN---LTNLKSLDLSNNQLTDLPEELGNLTNLKELD 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  533 VSNNKLQQLPFDLWRAPKLRELNVAFNLLRDLPVPpmqtsssllsldklnLQSFeeppsnkprnvtqQRLTHrnlwsatL 612
Cdd:COG4886   189 LSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEP---------------LANL-------------TNLET-------L 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116  613 DITDNDMKwqheqDLgdgktAGVGS-SQLSSLNIANNLFTSIP--AALPclavNLTRLNMSYNSLRSM 677
Cdd:COG4886   234 DLSNNQLT-----DL-----PELGNlTNLEELDLSNNQLTDLPplANLT----NLKTLDLSNNQLTDL 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-369 7.42e-18

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 7.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   35 LLAALGTERQIIVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDHFPELI 114
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  115 QQPTVERWLPLHAACINGHIKLLELLISYsypdylyqtyrdeegqwewrlPFDANAHDVTGQTSLYIASILGNKQLVGVL 194
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA---------------------GADVNARDKDGETPLHLAAYNGNLEIVKLL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  195 LKwqlhcrrtlgdsassvstpitptrkrisfgiqaimsklhiSGesegpddlasqestecqrcpINVNLlCGAARETALL 274
Cdd:COG0666   140 LE----------------------------------------AG--------------------ADVNA-QDNDGNTPLH 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  275 AAVRGGHLDVVQSLLQHGANPNIVAKpvedhndpkcceeiYGLSnvPIAEACKQRSLAMLDLLLKHGA----RDDNG-TA 349
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDN--------------DGET--PLHLAAENGHLEIVKLLLEAGAdvnaKDNDGkTA 222
                         330       340
                  ....*....|....*....|
gi 442620116  350 IGMAITCGDEAILSRLLARR 369
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAG 242
COR super family cl24610
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
1139-1302 6.23e-16

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


The actual alignment was detected with superfamily member pfam16095:

Pssm-ID: 406489  Cd Length: 196  Bit Score: 78.44  E-value: 6.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1139 PASYIALEDIvnviacnLRAAGRD-PVLDGEQYKRLVTEQmrlhnykSFRDAAELQQATTWCHENGVLLHY-DDATLRDY 1216
Cdd:pfam16095    1 PKSWLAVREA-------LEKERQKkPYISYEEYRKICAEN-------GIDDEEDQDTLLEFLHDLGVLLYFqDDPGLRDI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1217 YFLDPQWLCDMLAHVVTVREINpfAPTGVMKLDDLQMLFRSVQVQGNgNRSYIVSLLNKFEVALT---WDSRTLLIPSLL 1293
Cdd:pfam16095   67 VILNPQWLTNAVYRVLDSKHVL--NNNGILTHEDLEQIWKDPGYPRE-LHPYLLRLMEKFELCYElpgDEEGTYLVPQLL 143

                   ....*....
gi 442620116  1294 PSQEAATPN 1302
Cdd:pfam16095  144 PENPPELYD 152
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
809-850 1.56e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


:

Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 41.08  E-value: 1.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 442620116   809 PNLSMLDMTNNCLKEIPAsLHELSSLSVLNISGNVNITELPP 850
Cdd:pfam12799    1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNKITDLSD 41
LRR_8 pfam13855
Leucine rich repeat;
764-842 3.13e-04

Leucine rich repeat;


:

Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   764 LRTLILADNLLTRIqlstdDATTLFNesedadwsvvgvnrskviFPNLSMLDMTNNCLKEI-PASLHELSSLSVLNISGN 842
Cdd:pfam13855    3 LRSLDLSNNRLTSL-----DDGAFKG------------------LSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGN 59
 
Name Accession Description Interval E-value
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
1710-2004 2.26e-150

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: 467.48  E-value: 2.26e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVrgarsfKPVAMKMLQPVPPGARAKESALMAFkvavgkwDRDPLQHSCKAYCTARQELAVLLTL 1789
Cdd:cd14000     1 LLGDGGFGSVYRASYKG------EPVAVKIFNKHTSSNFANVPADTML-------RHLRATDAMKNFRLLRQELTVLSHL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVWE 1869
Cdd:cd14000    68 HHPSIVYLLGIGIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 LPQPhtedsprNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNgeEEYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd14000   148 LYPN-------SAIIIKIADYGISRQCCRMGAKGSEGTPGFRAPEIARGN--VIYNEKVDVFSFGMLLYEILSGGAPMVG 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1950 HESIKEC--ILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSILSAP 2004
Cdd:cd14000   219 HLKFPNEfdIHGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVSILNSP 275
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1705-2001 7.51e-50

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: 178.51  E-value: 7.51e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1705 IIKGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPVppgarAKESALMAFkvavgkwdrdplqhsckayctaRQELA 1784
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGKGDGKEVEVAVKTLKED-----ASEQQIEEF----------------------LREAR 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1785 VLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:smart00221   54 IMRKLDHPNIVKLLGVCTEeePLMIVMEYMPGGDLLDYLR--KNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAA 131
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1863 ENVLVwelpqphTEDsprnlVHIKIADYGISRQTAPSGAKGFGGTEG---FMAPEIIRYNgeeEYTEKVDCFSFGMFIYE 1939
Cdd:smart00221  132 RNCLV-------GEN-----LVVKISDFGLSRDLYDDDYYKVKGGKLpirWMAPESLKEG---KFTSKSDVWSFGVLLWE 196
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116   1940 NISL-RQPFEG--HESIKECILEGSRPaltQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:smart00221  197 IFTLgEEPYPGmsNAEVLEYLKKGYRL---PKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1705-2001 1.17e-47

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: 171.91  E-value: 1.17e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1705 IIKGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPvppgaRAKESALMAFkvavgkwdrdplqhsckayctaRQELA 1784
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEGENTKIKVAVKTLKE-----GADEEEREDF----------------------LEEAS 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1785 VLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhyrRSGAHMgphTFQTLV---LQAARAIEYLHRRRIIYRD 1859
Cdd:pfam07714   54 IMKKLDHPNIVKLLGVCTQgePLYIVTEYMPGGDLLDFLR---KHKRKL---TLKDLLsmaLQIAKGMEYLESKNFVHRD 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1860 LKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGAKGFGGTEGF----MAPEIIRYNgeeEYTEKVDCFSFGM 1935
Cdd:pfam07714  128 LAARNCLV---------SENL---VVKISDFGLSRDIYDDDYYRKRGGGKLpikwMAPESLKDG---KFTSKSDVWSFGV 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116  1936 FIYENISL-RQPFEGH--ESIKECILEGSRPAltqretQFPTCCL---DLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:pfam07714  193 LLWEIFTLgEQPYPGMsnEEVLEFLEDGYRLP------QPENCPDelyDLMKQCWAYDPEDRPTFSELVEDL 258
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
902-1120 6.63e-32

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 123.22  E-value: 6.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  902 RMKLMVVGVAGIGKSTLLDLLRqgagsgssssshrsrasenhWAKRMGHarstsrshrhssassaNISTVGVDIGTWice 981
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLI--------------------GEKFDGD----------------ESSTHGINVQDW--- 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  982 krKRAPGSHGPVVFRTWDFGGQKEYYATHQYFLSKRSLYLVLWRISDGHKGLAeLLQWLGNIQARAPNSPVIIVGTHFDA 1061
Cdd:cd09914    42 --KIPAPERKKIRLNVWDFGGQEIYHATHQFFLTSRSLYLLVFDLRTGDEVSR-VPYWLRQIKAFGGVSPVILVGTHIDE 118
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1062 vgesispQKAEQ-LQQLIREKFiaipdaekigLPRVIDSIEISCRTLHNIHLLANIIYDT 1120
Cdd:cd09914   119 -------SCDEDiLKKALNKKF----------PAIINDIHFVSCKNGKGIAELKKAIAKE 161
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1709-2003 6.60e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 129.36  E-value: 6.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvPPGARAKESALMAFkvavgkwdrdplqhsckayctaRQELAVLLT 1788
Cdd:COG0515    13 RLLGRGGMGVVYLARDLRLG----RPVALKVL---RPELAADPEARERF----------------------RREARALAR 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPL--VGICIKPLALVLELapLGGLDalLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:COG0515    64 LNHPNIVRVydVGEEDGRPYLVMEY--VEGES--LADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphTEDSprnlvHIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYENISL 1943
Cdd:COG0515   140 L-------TPDG-----RVKLIDFGIARALGGATLTQTGtvvGTPGYMAPEQARG---EPVDPRSDVYSLGVTLYELLTG 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1944 RQPFEGHE--SIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRP-TASQIVSILSA 2003
Cdd:COG0515   205 RPPFDGDSpaELLRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEERYqSAAELAAALRA 267
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
453-677 4.21e-29

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 122.73  E-value: 4.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  453 LTAITRIDFSHNVLTSIPQELFHLVSLRYLNVAQNKITDLPAPIGQtygCPVLDELFLQDNQLTTLPAAIFHLPALSILD 532
Cdd:COG4886   112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGN---LTNLKSLDLSNNQLTDLPEELGNLTNLKELD 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  533 VSNNKLQQLPFDLWRAPKLRELNVAFNLLRDLPVPpmqtsssllsldklnLQSFeeppsnkprnvtqQRLTHrnlwsatL 612
Cdd:COG4886   189 LSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEP---------------LANL-------------TNLET-------L 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116  613 DITDNDMKwqheqDLgdgktAGVGS-SQLSSLNIANNLFTSIP--AALPclavNLTRLNMSYNSLRSM 677
Cdd:COG4886   234 DLSNNQLT-----DL-----PELGNlTNLEELDLSNNQLTDLPplANLT----NLKTLDLSNNQLTDL 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-369 7.42e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 7.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   35 LLAALGTERQIIVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDHFPELI 114
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  115 QQPTVERWLPLHAACINGHIKLLELLISYsypdylyqtyrdeegqwewrlPFDANAHDVTGQTSLYIASILGNKQLVGVL 194
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA---------------------GADVNARDKDGETPLHLAAYNGNLEIVKLL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  195 LKwqlhcrrtlgdsassvstpitptrkrisfgiqaimsklhiSGesegpddlasqestecqrcpINVNLlCGAARETALL 274
Cdd:COG0666   140 LE----------------------------------------AG--------------------ADVNA-QDNDGNTPLH 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  275 AAVRGGHLDVVQSLLQHGANPNIVAKpvedhndpkcceeiYGLSnvPIAEACKQRSLAMLDLLLKHGA----RDDNG-TA 349
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDN--------------DGET--PLHLAAENGHLEIVKLLLEAGAdvnaKDNDGkTA 222
                         330       340
                  ....*....|....*....|
gi 442620116  350 IGMAITCGDEAILSRLLARR 369
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAG 242
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
968-1060 3.69e-17

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 79.47  E-value: 3.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   968 ISTVGVDIGTWICEKRkraPGSHGPVVFRTWDFGGQKEYYATHQYFLSKRSLYLVLWRISDGHKglaeLLQWLGNIQARA 1047
Cdd:pfam08477   29 KSTIGVDFKTKTVLEN---DDNGKKIKLNIWDTAGQERFRSLHPFYYRGAAAALLVYDSRTFSN----LKYWLRELKKYA 101
                           90
                   ....*....|...
gi 442620116  1048 PNSPVIIVGTHFD 1060
Cdd:pfam08477  102 GNSPVILVGNKID 114
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
1805-2006 5.67e-17

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 86.85  E-value: 5.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedSPRNLVh 1884
Cdd:PTZ00283  114 IALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILL----------CSNGLV- 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1885 iKIADYGISRQTAPSGA----KGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEGhESIKECI--- 1957
Cdd:PTZ00283  183 -KLGDFGFSKMYAATVSddvgRTFCGTPYYVAPEIWR---RKPYSKKADMFSLGVLLYELLTLKRPFDG-ENMEEVMhkt 257
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1958 LEGS---RPALTQRETQfptcclDLMVLCWHEQPRRRPTASQivsILSAPEC 2006
Cdd:PTZ00283  258 LAGRydpLPPSISPEMQ------EIVTALLSSDPKRRPSSSK---LLNMPIC 300
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
1139-1302 6.23e-16

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


Pssm-ID: 406489  Cd Length: 196  Bit Score: 78.44  E-value: 6.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1139 PASYIALEDIvnviacnLRAAGRD-PVLDGEQYKRLVTEQmrlhnykSFRDAAELQQATTWCHENGVLLHY-DDATLRDY 1216
Cdd:pfam16095    1 PKSWLAVREA-------LEKERQKkPYISYEEYRKICAEN-------GIDDEEDQDTLLEFLHDLGVLLYFqDDPGLRDI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1217 YFLDPQWLCDMLAHVVTVREINpfAPTGVMKLDDLQMLFRSVQVQGNgNRSYIVSLLNKFEVALT---WDSRTLLIPSLL 1293
Cdd:pfam16095   67 VILNPQWLTNAVYRVLDSKHVL--NNNGILTHEDLEQIWKDPGYPRE-LHPYLLRLMEKFELCYElpgDEEGTYLVPQLL 143

                   ....*....
gi 442620116  1294 PSQEAATPN 1302
Cdd:pfam16095  144 PENPPELYD 152
Ank_2 pfam12796
Ankyrin repeats (3 copies);
58-143 6.97e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 6.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116    58 LFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDHFpelIQQPTVERWLPLHAACINGHIKLL 137
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIV 77

                   ....*.
gi 442620116   138 ELLISY 143
Cdd:pfam12796   78 KLLLEK 83
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
454-565 2.82e-12

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 72.42  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  454 TAITRIDFSHNVLTSIPQELFHlvSLRYLNVAQNKITDLPA--PIGQTygcpvldELFLQDNQLTTLPA----------- 520
Cdd:PRK15370  262 SALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAhlPSGIT-------HLNVQSNSLTALPEtlppglktlea 332
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442620116  521 ---AIFHL-----PALSILDVSNNKLQQLPFDLwrAPKLRELNVAFNLLRDLP 565
Cdd:PRK15370  333 genALTSLpaslpPELQVLDVSKNQITVLPETL--PPTITTLDVSRNALTNLP 383
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
904-1083 1.45e-10

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 62.31  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  904 KLMVVGVAGIGKSTLLD-LLRQGAGSGSSSsshrsrasenhwakrmgharstsrshrhssassaniSTVGVDIgtwiceK 982
Cdd:COG1100     5 KIVVVGTGGVGKTSLVNrLVGDIFSLEKYL------------------------------------STNGVTI------D 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  983 RKRAPGSHGPVVFRTWDFGGQKEYYATHQYF---LSKRSLYLVLWrisDGH--KGLAELLQWLGNIQARAPNSPVIIVGT 1057
Cdd:COG1100    43 KKELKLDGLDVDLVIWDTPGQDEFRETRQFYarqLTGASLYLFVV---DGTreETLQSLYELLESLRRLGKKSPIILVLN 119
                         170       180
                  ....*....|....*....|....*.
gi 442620116 1058 HFDAVGEsISPQKAEQLQQLIREKFI 1083
Cdd:COG1100   120 KIDLYDE-EEIEDEERLKEALSEDNI 144
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
1789-1949 1.78e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 62.89  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIV---------PLVGIcikplalVLELAPlgGLDalLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:NF033483   64 LSHPNIVsvydvgedgGIPYI-------VMEYVD--GRT--LKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphTEDSprnlvHIKIADYGISR--------QTApsgakGFGGTEGFMAPEIIRYngeEEYTEKVDCF 1931
Cdd:NF033483  133 IKPQNILI-------TKDG-----RVKVTDFGIARalssttmtQTN-----SVLGTVHYLSPEQARG---GTVDARSDIY 192
                         170
                  ....*....|....*...
gi 442620116 1932 SFGMFIYENISLRQPFEG 1949
Cdd:NF033483  193 SLGIVLYEMLTGRPPFDG 210
LRR_8 pfam13855
Leucine rich repeat;
478-538 4.58e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 48.67  E-value: 4.58e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116   478 SLRYLNVAQNKITDLPApiGQTYGCPVLDELFLQDNQLTTL-PAAIFHLPALSILDVSNNKL 538
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDD--GAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PHA02875 PHA02875
ankyrin repeat protein; Provisional
61-300 3.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   61 ACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDH--FPElIQQPTVERwlPLHAACINGHIKLLE 138
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHgaIPD-VKYPDIES--ELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  139 -LLISYSYPDYLYqtYRDeegqwewrlpfdanahdvtGQTSLYIASILGNKQLVGVLLKWQlhcrrtlgdsassvSTPIT 217
Cdd:PHA02875   86 eLLDLGKFADDVF--YKD-------------------GMTPLHLATILKKLDIMKLLIARG--------------ADPDI 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  218 PTRKRISFGIQAIMSKlhisgesegpdDLASQESTECQRCPINVNLLCGAareTALLAAVRGGHLDVVQSLLQHGANPNI 297
Cdd:PHA02875  131 PNTDKFSPLHLAVMMG-----------DIKGIELLIDHKACLDIEDCCGC---TPLIIAMAKGDIAICKMLLDSGANIDY 196

                  ...
gi 442620116  298 VAK 300
Cdd:PHA02875  197 FGK 199
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
452-564 1.98e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 48.24  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  452 ALTAITRIDFSHNVLTSIpQELFHLVSLRYLNVAQNKIT---DLpapigqtYGCPVLDELFLQDNQL---TTL---PAAI 522
Cdd:cd21340    44 FLTNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISvveGL-------ENLTNLEELHIENQRLppgEKLtfdPRSL 115
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 442620116  523 FHL-PALSILDVSNNKLQQLPfDLWRAPKLRELNVAFNLLRDL 564
Cdd:cd21340   116 AALsNSLRVLNISGNNIDSLE-PLAPLRNLEQLDASNNQISDL 157
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
809-850 1.56e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 41.08  E-value: 1.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 442620116   809 PNLSMLDMTNNCLKEIPAsLHELSSLSVLNISGNVNITELPP 850
Cdd:pfam12799    1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNKITDLSD 41
LRR_8 pfam13855
Leucine rich repeat;
764-842 3.13e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   764 LRTLILADNLLTRIqlstdDATTLFNesedadwsvvgvnrskviFPNLSMLDMTNNCLKEI-PASLHELSSLSVLNISGN 842
Cdd:pfam13855    3 LRSLDLSNNRLTSL-----DDGAFKG------------------LSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGN 59
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
809-858 5.29e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.61  E-value: 5.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442620116  809 PNLSMLDMTNNCLK-EIPASLHELSSLSVLNISGNVNITELPPHLGLLSRL 858
Cdd:PLN00113  140 PNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSL 190
 
Name Accession Description Interval E-value
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
1710-2004 2.26e-150

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: 467.48  E-value: 2.26e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVrgarsfKPVAMKMLQPVPPGARAKESALMAFkvavgkwDRDPLQHSCKAYCTARQELAVLLTL 1789
Cdd:cd14000     1 LLGDGGFGSVYRASYKG------EPVAVKIFNKHTSSNFANVPADTML-------RHLRATDAMKNFRLLRQELTVLSHL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVWE 1869
Cdd:cd14000    68 HHPSIVYLLGIGIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 LPQPhtedsprNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNgeEEYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd14000   148 LYPN-------SAIIIKIADYGISRQCCRMGAKGSEGTPGFRAPEIARGN--VIYNEKVDVFSFGMLLYEILSGGAPMVG 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1950 HESIKEC--ILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSILSAP 2004
Cdd:cd14000   219 HLKFPNEfdIHGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTVVSILNSP 275
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
1711-2001 1.90e-53

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: 188.13  E-value: 1.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCkvRGarsfKPVAMKMLQPVPPGARAKEsalmAFkvavgkwdrdplqhsckayctaRQELAVLLTLK 1790
Cdd:cd13999     1 IGSGSFGEVYKGKW--RG----TDVAIKKLKVEDDNDELLK----EF----------------------RREVSILSKLR 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPLGGLDALLrhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd13999    49 HPNIVQFIGACLSPppLCIVTEYMPGGSLYDLL---HKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILL- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphteDSPrnlVHIKIADYGISR--QTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd13999   125 --------DEN---FTVKIADFGLSRikNSTTEKMTGVVGTPRWMAPEVLR---GEPYTEKADVYSFGIVLWELLTGEVP 190
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1947 FEGHES---IKECILEGSRPALtqretqfPTCC----LDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd13999   191 FKELSPiqiAAAVVQKGLRPPI-------PPDCppelSKLIKRCWNEDPEKRPSFSEIVKRL 245
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
1711-2004 1.36e-50

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: 181.32  E-value: 1.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFkanckVRGARSFKPVAMKMLQPVPPGARAKESAlmafkvavgkwdRDPLQH-----SCKAYCTARQELAV 1785
Cdd:cd14067     1 LGQGGSGTVI-----YRARYQGQPVAVKRFHIKKCKKRTDGSA------------DTMLKHlraadAMKNFSEFRQEASM 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSGAHM--GPHTFQTLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14067    64 LHSLQHPCIVYLIGISIHPLCFALELAPLGSLNTVLEENHKGSSFMplGHMLTFKIAYQIAAGLAYLHKKNIIFCDLKSD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVWELPQphtedspRNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIiryNGEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd14067   144 NILVWSLDV-------QEHINIKLSDYGISRQSFHEGALGVEGTPGYQAPEI---RPRIVYDEKVDMFSYGMVLYELLSG 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1944 RQPFEGHE--SIKECILEGSRPALTQ-RETQFpTCCLDLMVLCWHEQPRRRPTASQIVSILSAP 2004
Cdd:cd14067   214 QRPSLGHHqlQIAKKLSKGIRPVLGQpEEVQF-FRLQALMMECWDTKPEKRPLACSVVEQMKDP 276
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
1705-2001 7.51e-50

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: 178.51  E-value: 7.51e-50
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1705 IIKGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPVppgarAKESALMAFkvavgkwdrdplqhsckayctaRQELA 1784
Cdd:smart00221    1 LTLGKKLGEGAFGEVYKGTLKGKGDGKEVEVAVKTLKED-----ASEQQIEEF----------------------LREAR 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1785 VLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:smart00221   54 IMRKLDHPNIVKLLGVCTEeePLMIVMEYMPGGDLLDYLR--KNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAA 131
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1863 ENVLVwelpqphTEDsprnlVHIKIADYGISRQTAPSGAKGFGGTEG---FMAPEIIRYNgeeEYTEKVDCFSFGMFIYE 1939
Cdd:smart00221  132 RNCLV-------GEN-----LVVKISDFGLSRDLYDDDYYKVKGGKLpirWMAPESLKEG---KFTSKSDVWSFGVLLWE 196
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116   1940 NISL-RQPFEG--HESIKECILEGSRPaltQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:smart00221  197 IFTLgEEPYPGmsNAEVLEYLKKGYRL---PKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1707-1997 1.13e-48

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 175.03  E-value: 1.13e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1707 KGSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvppgarakesalmafkvavgkwdrdPLQHSCKAYCTARQELAVL 1786
Cdd:smart00220    3 ILEKLGEGSFGKVYLARDKKTG----KLVAIKVI---------------------------KKKKIKKDRERILREIKIL 51
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1787 LTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:smart00220   52 KKLKHPNIVRLYDVFEDEdkLYLVMEYCEGGDLFDLLKKRGR----LSEDEARFYLRQILSALEYLHSKGIVHRDLKPEN 127
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1865 VLVwelpqphTEDSprnlvHIKIADYGISRQTAPSG-AKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISL 1943
Cdd:smart00220  128 ILL-------DEDG-----HVKLADFGLARQLDPGEkLTTFVGTPEYMAPEVLLGKG---YGKAVDIWSLGVILYELLTG 192
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116   1944 RQPFEGHESIKE--CILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:smart00220  193 KPPFPGDDQLLElfKKIGKPKPPFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEA 248
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
1705-2001 1.88e-48

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 174.26  E-value: 1.88e-48
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1705 IIKGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPVppgarAKESALMAFkvavgkwdrdplqhsckayctaRQELA 1784
Cdd:smart00219    1 LTLGKKLGEGAFGEVYKGKLKGKGGKKKVEVAVKTLKED-----ASEQQIEEF----------------------LREAR 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1785 VLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhyrRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:smart00219   54 IMRKLDHPNVVKLLGVCTEeePLYIVMEYMEGGDLLSYLR---KNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAA 130
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   1863 ENVLVwelpqphTEDsprnlVHIKIADYGISRQTAPSGAKGFGGTEG---FMAPEIIRYNgeeEYTEKVDCFSFGMFIYE 1939
Cdd:smart00219  131 RNCLV-------GEN-----LVVKISDFGLSRDLYDDDYYRKRGGKLpirWMAPESLKEG---KFTSKSDVWSFGVLLWE 195
                           250       260       270       280       290       300
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116   1940 NISL-RQPFEG--HESIKECILEGSRPaltQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:smart00219  196 IFTLgEQPYPGmsNEEVLEYLKNGYRL---PQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
1705-2001 1.17e-47

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: 171.91  E-value: 1.17e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1705 IIKGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPvppgaRAKESALMAFkvavgkwdrdplqhsckayctaRQELA 1784
Cdd:pfam07714    1 LTLGEKLGEGAFGEVYKGTLKGEGENTKIKVAVKTLKE-----GADEEEREDF----------------------LEEAS 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1785 VLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhyrRSGAHMgphTFQTLV---LQAARAIEYLHRRRIIYRD 1859
Cdd:pfam07714   54 IMKKLDHPNIVKLLGVCTQgePLYIVTEYMPGGDLLDFLR---KHKRKL---TLKDLLsmaLQIAKGMEYLESKNFVHRD 127
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1860 LKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGAKGFGGTEGF----MAPEIIRYNgeeEYTEKVDCFSFGM 1935
Cdd:pfam07714  128 LAARNCLV---------SENL---VVKISDFGLSRDIYDDDYYRKRGGGKLpikwMAPESLKDG---KFTSKSDVWSFGV 192
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116  1936 FIYENISL-RQPFEGH--ESIKECILEGSRPAltqretQFPTCCL---DLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:pfam07714  193 LLWEIFTLgEQPYPGMsnEEVLEFLEDGYRLP------QPENCPDelyDLMKQCWAYDPEDRPTFSELVEDL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1711-2001 2.22e-47

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: 171.57  E-value: 2.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSfKPVAMKMLQPvppgaRAKESALMAFkvavgkwdrdplqhsckayctaRQELAVLLTLK 1790
Cdd:cd00192     3 LGEGAFGEVYKGKLKGGDGKT-VDVAVKTLKE-----DASESERKDF----------------------LKEARVMKKLG 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVL-----QAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd00192    55 HPNVVRLLGVCTEeePLYLVMEYMEGGDLLDFLRKSRPVFPSPEPSTLSLKDLlsfaiQIAKGMEYLASKKFVHRDLAAR 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphTEDsprnlVHIKIADYGISRQTAPSGAKGFGGTEGF----MAPEIIRYNgeeEYTEKVDCFSFGMFIYE 1939
Cdd:cd00192   135 NCLV-------GED-----LVVKISDFGLSRDIYDDDYYRKKTGGKLpirwMAPESLKDG---IFTSKSDVWSFGVLLWE 199
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1940 NISL-RQPFEG---HEsIKECILEGSRPAltqretqFPTCCLD----LMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd00192   200 IFTLgATPYPGlsnEE-VLEYLRKGYRLP-------KPENCPDelyeLMLSCWQLDPEDRPTFSELVERL 261
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
1711-2001 6.30e-39

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 145.49  E-value: 6.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVPPGARAKEsalmafkvavgkwdrdplqhsckayctARQELAVLLTLK 1790
Cdd:cd00180     1 LGKGSFGKVYKARDKETG----KKVAVKVIPKEKLKKLLEE---------------------------LLREIEILKKLN 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRsgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVW 1868
Cdd:cd00180    50 HPNIVKLYDVFETEnfLYLVMEYCEGGSLKDLLKENKG---PLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLD 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 ELPqphtedsprnlvHIKIADYGISRQTAPSGAK----GFGGTEGFMAPEIIrynGEEEYTEKVDCFSFGMFIYEnislr 1944
Cdd:cd00180   127 SDG------------TVKLADFGLAKDLDSDDSLlkttGGTTPPYYAPPELL---GGRYYGPKVDIWSLGVILYE----- 186
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1945 qpfeghesIKECIlegsrpaltqretqfptcclDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd00180   187 --------LEELK--------------------DLIRRMLQYDPKKRPSAKELLEHL 215
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
1780-2003 9.34e-35

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: 134.69  E-value: 9.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHtfqTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd14068    35 RQELVVLSHLHHPSLVALLAAGTAPRMLVMELAPKGSLDALLQQDNASLTRTLQH---RIALHVADGLRYLHSAMIIYRD 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVWELpqphtedSPRNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYE 1939
Cdd:cd14068   112 LKPHNVLLFTL-------YPNCAIIAKIADYGIAQYCCRMGIKTSEGTPGFRAPEVAR--GNVIYNQQADVYSFGLLLYD 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1940 NIS--------LRQPFEghesIKECILEGSRPALTQRETQFPTCCLD-LMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd14068   183 ILTcgerivegLKFPNE----FDELAIQGKLPDPVKEYGCAPWPGVEaLIKDCLKENPQCRPTSAQVFDILNS 251
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
1707-2002 3.09e-34

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: 134.08  E-value: 3.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQpvppgaraKESALMAFKVAVgkwdrdplqhsckayctarQELAVL 1786
Cdd:cd05057    11 KGKVLGSGAFGTVYKGVWIPEGEKVKIPVAIKVLR--------EETGPKANEEIL-------------------DEAYVM 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIKP-LALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd05057    64 ASVDHPHLVRLLGICLSSqVQLITQLMPLG---CLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwELPQphtedsprnlvHIKIADYGISRqTAPSGAKGFGGTEG-----FMAPEIIRYNgeeEYTEKVDCFSFGMFIYEN 1940
Cdd:cd05057   141 LV-KTPN-----------HVKITDFGLAK-LLDVDEKEYHAEGGkvpikWMALESIQYR---IYTHKSDVWSYGVTVWEL 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1941 ISL-RQPFEGHES--IKECILEGsrpaltQRETQFPTCCLD---LMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05057   205 MTFgAKPYEGIPAveIPDLLEKG------ERLPQPPICTIDvymVLVKCWMIDAESRPTFKELANEFS 266
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
1709-1994 4.49e-32

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 127.32  E-value: 4.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQPvppGARAKESALMAFkvavgkwdrdplqhsckayctaRQELAVLLT 1788
Cdd:cd14014     6 RLLGRGGMGEVYRARDTLLG----RPVAIKVLRP---ELAEDEEFRERF----------------------LREARALAR 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPL--VGICIKPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14014    57 LSHPNIVRVydVGEDDGRPYIVMEYVEGGSLADLLRERGP----LPPREALRILAQIADALAAAHRAGIVHRDIKPANIL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphTEDSprnlvHIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd14014   133 L-------TEDG-----RVKLTDFGIARALGDSGLTQTGsvlGTPAYMAPEQAR---GGPVDPRSDIYSLGVVLYELLTG 197
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1944 RQPFEGH--ESIKECILEGSRPALTQRETQFPTcCLDLMVL-CWHEQPRRRPTA 1994
Cdd:cd14014   198 RPPFDGDspAAVLAKHLQEAPPPPSPLNPDVPP-ALDAIILrALAKDPEERPQS 250
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
902-1120 6.63e-32

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 123.22  E-value: 6.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  902 RMKLMVVGVAGIGKSTLLDLLRqgagsgssssshrsrasenhWAKRMGHarstsrshrhssassaNISTVGVDIGTWice 981
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLI--------------------GEKFDGD----------------ESSTHGINVQDW--- 41
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  982 krKRAPGSHGPVVFRTWDFGGQKEYYATHQYFLSKRSLYLVLWRISDGHKGLAeLLQWLGNIQARAPNSPVIIVGTHFDA 1061
Cdd:cd09914    42 --KIPAPERKKIRLNVWDFGGQEIYHATHQFFLTSRSLYLLVFDLRTGDEVSR-VPYWLRQIKAFGGVSPVILVGTHIDE 118
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1062 vgesispQKAEQ-LQQLIREKFiaipdaekigLPRVIDSIEISCRTLHNIHLLANIIYDT 1120
Cdd:cd09914   119 -------SCDEDiLKKALNKKF----------PAIINDIHFVSCKNGKGIAELKKAIAKE 161
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
1711-2002 1.40e-31

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: 125.63  E-value: 1.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAncKVRGarsfKPVAMKMLQpvppgaraKESALMAFKVAVgkwdrdplqhsckayctaRQelavLLTLK 1790
Cdd:cd14058     1 VGRGSFGVVCKA--RWRN----QIVAVKIIE--------SESEKKAFEVEV------------------RQ----LSRVD 44
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICI--KPLALVLELAPLGGLDALLrHYRRSGAHMGPHTFQTLVLQAARAIEYLHR---RRIIYRDLKSENV 1865
Cdd:cd14058    45 HPNIIKLYGACSnqKPVCLVMEYAEGGSLYNVL-HGKEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LvweLPQPHTEdsprnlvhIKIADYGIS--RQTAPSGAKgfgGTEGFMAPEIIRYNgeeEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd14058   124 L---LTNGGTV--------LKICDFGTAcdISTHMTNNK---GSAAWMAPEVFEGS---KYSEKCDVFSWGIILWEVITR 186
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1944 RQPFEGHE----SIKECILEGSRPALtqrETQFPTCCLDLMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd14058   187 RKPFDHIGgpafRIMWAVHNGERPPL---IKNCPKPIESLMTRCWSKDPEKRPSMKEIVKIMS 246
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
1705-1996 3.00e-31

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: 124.56  E-value: 3.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1705 IIKGSLLGRGAFGFVFKANCKVRGARsfkpVAMKMLQpVPPGARAKESALMafkvavgkwdrdplqhsckayctarQELA 1784
Cdd:cd06606     2 WKKGELLGKGSFGSVYLALNLDTGEL----MAVKEVE-LSGDSEEELEALE-------------------------REIR 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd06606    52 ILSSLKHPNIVRYLGTERTEntLNIFLEYVPGGSLASLLKKFGK----LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKG 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphTEDSprnlvHIKIADYGISRQ----TAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIY 1938
Cdd:cd06606   128 ANILV-------DSDG-----VVKLADFGCAKRlaeiATGEGTKSLRGTPYWMAPEVIR---GEGYGRAADIWSLGCTVI 192
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1939 ENISLRQPFEGHESIKECILegsRPALTQRETQFPTC----CLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd06606   193 EMATGKPPWSELGNPVAALF---KIGSSGEPPPIPEHlseeAKDFLRKCLQRDPKKRPTADE 251
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
1709-2003 6.60e-31

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 129.36  E-value: 6.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvPPGARAKESALMAFkvavgkwdrdplqhsckayctaRQELAVLLT 1788
Cdd:COG0515    13 RLLGRGGMGVVYLARDLRLG----RPVALKVL---RPELAADPEARERF----------------------RREARALAR 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPL--VGICIKPLALVLELapLGGLDalLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:COG0515    64 LNHPNIVRVydVGEEDGRPYLVMEY--VEGES--LADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphTEDSprnlvHIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYENISL 1943
Cdd:COG0515   140 L-------TPDG-----RVKLIDFGIARALGGATLTQTGtvvGTPGYMAPEQARG---EPVDPRSDVYSLGVTLYELLTG 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1944 RQPFEGHE--SIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRP-TASQIVSILSA 2003
Cdd:COG0515   205 RPPFDGDSpaELLRAHLREPPPPPSELRPDLPPALDAIVLRALAKDPEERYqSAAELAAALRA 267
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
1758-2003 1.19e-30

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: 123.61  E-value: 1.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWDRDPLQHSCKAYCTARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLrhyrrSGAHMGPHT 1835
Cdd:cd14145    31 EVAVKAARHDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEpnLCLVMEFARGGPLNRVL-----SGKRIPPDI 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1836 FQTLVLQAARAIEYLHRRRI---IYRDLKSENVLVWELpqphTEDSPRNLVHIKIADYGISRQTAPSGAKGFGGTEGFMA 1912
Cdd:cd14145   106 LVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEK----VENGDLSNKILKITDFGLAREWHRTTKMSAAGTYAWMA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1913 PEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIkeCILEGSrpALTQRETQFPTCCLD----LMVLCWHEQP 1988
Cdd:cd14145   182 PEVIR---SSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGL--AVAYGV--AMNKLSLPIPSTCPEpfarLMEDCWNPDP 254
                         250
                  ....*....|....*
gi 442620116 1989 RRRPTASQIVSILSA 2003
Cdd:cd14145   255 HSRPPFTNILDQLTA 269
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
1780-2001 1.99e-30

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: 122.77  E-value: 1.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSgahmGPHTFQTLV---LQAARAIEYLH--- 1851
Cdd:cd14066    38 LTELEMLGRLRHPNLVRLLGYCLESdeKLLVYEYMPNGSLEDRLHCHKGS----PPLPWPQRLkiaKGIARGLEYLHeec 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVWELPQPhtedsprnlvhiKIADYGISRQTAPSGAK----GFGGTEGFMAPEIIRYNgeeEYTEK 1927
Cdd:cd14066   114 PPPIIHGDIKSSNILLDEDFEP------------KLTDFGLARLIPPSESVsktsAVKGTIGYLAPEYIRTG---RVSTK 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1928 VDCFSFGMFIYENISLRQPF------------------EGHESIKECILEGSRPALTQRETQFpTCCLDLMVLCWHEQPR 1989
Cdd:cd14066   179 SDVYSFGVVLLELLTGKPAVdenrenasrkdlvewvesKGKEELEDILDKRLVDDDGVEEEEV-EALLRLALLCTRSDPS 257
                         250
                  ....*....|..
gi 442620116 1990 RRPTASQIVSIL 2001
Cdd:cd14066   258 LRPSMKEVVQML 269
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
1705-2000 2.22e-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: 122.19  E-value: 2.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1705 IIKgsLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELA 1784
Cdd:cd08215     4 KIR--VIGKGSFGSAYLVRRKSDG----KLYVLKEIDLSNMSEKEREEAL--------------------------NEVK 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVG-------ICIkplalVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd08215    52 LLSKLKHPNIVKYYEsfeengkLCI-----VMEYADGGDLAQKIKKQKKKGQPFPEEQILDWFVQICLALKYLHSRKILH 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGM 1935
Cdd:cd08215   127 RDLKTQNIFL-------TKDG-----VVKLGDFGISKVLESTTdlAKTVVGTPYYLSPELCE---NKPYNYKSDIWALGC 191
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1936 FIYENISLRQPFEGhESIKEC---ILEGSRPALtqrETQFPTCCLDLMVLCWHEQPRRRPTASQIVSI 2000
Cdd:cd08215   192 VLYELCTLKHPFEA-NNLPALvykIVKGQYPPI---PSQYSSELRDLVNSMLQKDPEKRPSANEILSS 255
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
1711-1993 2.29e-30

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: 122.18  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckvRGARSFKPVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd13978     1 LGSGGFGTVSKA----RHVSWFGMVAIKCLHSSPNCIEERKALL--------------------------KEAEKMERAR 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPLGGLDALLRhyRRSGAHMGPHTFQtLVLQAARAIEYLH--RRRIIYRDLKSENVL 1866
Cdd:cd13978    51 HSYVLPLLGVCVERrsLGLVMEYMENGSLKSLLE--REIQDVPWSLRFR-IIHEIALGMNFLHnmDPPLLHHDLKPENIL 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphtedspRNLVHIKIADYGISR-------QTAPSGAKGFGGTEGFMAPEIIRyNGEEEYTEKVDCFSFGMFIYE 1939
Cdd:cd13978   128 L------------DNHFHVKISDFGLSKlgmksisANRRRGTENLGGTPIYMAPEAFD-DFNKKPTSKSDVYSFAIVIWA 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1940 NISLRQPFEGHES---IKECILEGSRPALTQ----RETQFPTCCLDLMVLCWHEQPRRRPT 1993
Cdd:cd13978   195 VLTRKEPFENAINpllIMQIVSKGDRPSLDDigrlKQIENVQELISLMIRCWDGNPDARPT 255
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
1759-2004 4.83e-30

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: 121.35  E-value: 4.83e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1759 VAVGKWDRDPLQHSCKAYCTARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLrhyrrSGAHMGPHTF 1836
Cdd:cd14061    20 VAVKAARQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPpnLCLVMEYARGGALNRVL-----AGRKIPPHVL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1837 QTLVLQAARAIEYLHRRR---IIYRDLKSENVLvweLPQPHTEDSPRNLVhIKIADYGISRQTAPSGAKGFGGTEGFMAP 1913
Cdd:cd14061    95 VDWAIQIARGMNYLHNEApvpIIHRDLKSSNIL---ILEAIENEDLENKT-LKITDFGLAREWHKTTRMSAAGTYAWMAP 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1914 EIIRYNgeeEYTEKVDCFSFGMFIYENISLRQPFEGhesiKECILEGSRPALTQRETQFPTCCLD----LMVLCWHEQPR 1989
Cdd:cd14061   171 EVIKSS---TFSKASDVWSYGVLLWELLTGEVPYKG----IDGLAVAYGVAVNKLTLPIPSTCPEpfaqLMKDCWQPDPH 243
                         250
                  ....*....|....*
gi 442620116 1990 RRPTASQIVSILSAP 2004
Cdd:cd14061   244 DRPSFADILKQLENI 258
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
1708-1999 1.69e-29

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: 119.50  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKvrgaRSFKPVAMKMLQpvppgaraKESaLMAFKVAVGkwdrdplqhsckayctARQELAVLL 1787
Cdd:cd14007     5 GKPLGKGKFGNVYLAREK----KSGFIVALKVIS--------KSQ-LQKSGLEHQ----------------LRREIEIQS 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14007    56 HLRHPNILRLYGYFEdkKRIYLILEYAPNGELYKELKKQKR----FDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENI 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqpHTEDsprnlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd14007   132 LL------GSNG------ELKLADFGWSVHAPSNRRKTFCGTLDYLPPEMVE---GKEYDYKVDIWSLGVLCYELLVGKP 196
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1946 PFEG--HESIKECILEGsrpaltqrETQFP----TCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14007   197 PFESksHQETYKRIQNV--------DIKFPssvsPEAKDLISKLLQKDPSKRLSLEQVLN 248
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
453-677 4.21e-29

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 122.73  E-value: 4.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  453 LTAITRIDFSHNVLTSIPQELFHLVSLRYLNVAQNKITDLPAPIGQtygCPVLDELFLQDNQLTTLPAAIFHLPALSILD 532
Cdd:COG4886   112 LTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGN---LTNLKSLDLSNNQLTDLPEELGNLTNLKELD 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  533 VSNNKLQQLPFDLWRAPKLRELNVAFNLLRDLPVPpmqtsssllsldklnLQSFeeppsnkprnvtqQRLTHrnlwsatL 612
Cdd:COG4886   189 LSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEP---------------LANL-------------TNLET-------L 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116  613 DITDNDMKwqheqDLgdgktAGVGS-SQLSSLNIANNLFTSIP--AALPclavNLTRLNMSYNSLRSM 677
Cdd:COG4886   234 DLSNNQLT-----DL-----PELGNlTNLEELDLSNNQLTDLPplANLT----NLKTLDLSNNQLTDL 287
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
1759-2003 5.55e-29

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: 118.59  E-value: 5.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1759 VAVGKWDRDPLQHSCKAYCTARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLrhyrrSGAHMGPHTF 1836
Cdd:cd14147    29 VAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEpnLCLVMEYAAGGPLSRAL-----AGRRVPPHVL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1837 QTLVLQAARAIEYLHRRRI---IYRDLKSENVLvweLPQPHTEDSPRNLVhIKIADYGISRQTAPSGAKGFGGTEGFMAP 1913
Cdd:cd14147   104 VNWAVQIARGMHYLHCEALvpvIHRDLKSNNIL---LLQPIENDDMEHKT-LKITDFGLAREWHKTTQMSAAGTYAWMAP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1914 EIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEGhesiKECILEGSRPALTQRETQFPTCCLD----LMVLCWHEQPR 1989
Cdd:cd14147   180 EVIK---ASTFSKGSDVWSFGVLLWELLTGEVPYRG----IDCLAVAYGVAVNKLTLPIPSTCPEpfaqLMADCWAQDPH 252
                         250
                  ....*....|....
gi 442620116 1990 RRPTASQIVSILSA 2003
Cdd:cd14147   253 RRPDFASILQQLEA 266
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
1710-2003 7.97e-29

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: 118.22  E-value: 7.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRgarsfkpvamkmlqpvppgarakesalmafKVAVGKWDRDPLQHSCKAYCTARQELAVLLTL 1789
Cdd:cd14146     1 IIGVGGFGKVYRATWKGQ------------------------------EVAVKAARQDPDEDIKATAESVRQEAKLFSML 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP--LALVLELAPLGGLDALL-----RHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRR---IIYRD 1859
Cdd:cd14146    51 RHPNIIKLEGVCLEEpnLCLVMEFARGGTLNRALaaanaAPGPRRARRIPPHILVNWAVQIARGMLYLHEEAvvpILHRD 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVWELPQpHTEDSPRNLvhiKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYE 1939
Cdd:cd14146   131 LKSSNILLLEKIE-HDDICNKTL---KITDFGLAREWHRTTKMSAAGTYAWMAPEVIK---SSLFSKGSDIWSYGVLLWE 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1940 NISLRQPFEGHESIkeCILEGSrpALTQRETQFPTCCLD----LMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd14146   204 LLTGEVPYRGIDGL--AVAYGV--AVNKLTLPIPSTCPEpfakLMKECWEQDPHIRPSFALILEQLTA 267
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
1786-2001 9.90e-29

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: 116.83  E-value: 9.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14059    35 LRKLNHPNIIKFKGVCTQApcYCILMEYCPYGQLYEVLR----AGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSP 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqpHTEDSprnlvhIKIADYGISRQTAPSGAK-GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENIS 1942
Cdd:cd14059   111 NVLV------TYNDV------LKISDFGTSKELSEKSTKmSFAGTVAWMAPEVIR---NEPCSEKVDIWSFGVVLWELLT 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1943 LRQPFEGHESikECILEGSRPALTQreTQFPTCCLD----LMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14059   176 GEIPYKDVDS--SAIIWGVGSNSLQ--LPVPSTCPDgfklLMKQCWNSKPRNRPSFRQILMHL 234
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
1711-1997 1.19e-28

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: 117.16  E-value: 1.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARsfkpVAMKMLQ-PVPPGARAKesalmaFkvavgkwdrdplqhsckayctaRQELAVLLTL 1789
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTE----VAVKTCReTLPPDLKRK------F----------------------LQEARILKQY 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIK--PLALVLELAPlGGldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd05041    51 DHPNIVKLIGVCVQkqPIMIVMELVP-GG--SLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLV 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 WElpqphtedspRNLVhiKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYNgeeEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd05041   128 GE----------NNVL--KISDFGMSREEEDGEYTVSDGLKqipiKWTAPEALNYG---RYTSESDVWSFGILLWEIFSL 192
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1944 -RQPFEG--HESIKECILEGSR---PALTqretqfPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd05041   193 gATPYPGmsNQQTREQIESGYRmpaPELC------PEAVYRLMLQCWAYDPENRPSFSEI 246
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
1708-1996 3.99e-28

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: 115.65  E-value: 3.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgaraKESALMAFKVAVgkwdrdplqhsckayctaRQELAVLL 1787
Cdd:cd05117     5 GKVLGRGSFGVVRLAVHKKTG----EEYAVKIID--------KKKLKSEDEEML------------------RREIEILK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICI--KPLALVLELAPlGG--LDALLR--HYRRSGAhmgphtfQTLVLQAARAIEYLHRRRIIYRDLK 1861
Cdd:cd05117    55 RLDHPNIVKLYEVFEddKNLYLVMELCT-GGelFDRIVKkgSFSEREA-------AKIMKQILSAVAYLHSQGIVHRDLK 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphteDSPRNLVHIKIADYGISRQ-TAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYen 1940
Cdd:cd05117   127 PENILL---------ASKDPDSPIKIIDFGLAKIfEEGEKLKTVCGTPYYVAPEVLKGKG---YGKKCDIWSLGVILY-- 192
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1941 ISL--RQPFEG--HESIKECILEGsrpaltqrETQFPT--------CCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd05117   193 ILLcgYPPFYGetEQELFEKILKG--------KYSFDSpewknvseEAKDLIKRLLVVDPKKRLTAAE 252
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1711-1951 4.36e-28

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: 115.31  E-value: 4.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKanckVRGARSFKPVAMKMLQpvppgaraKESALmafkvavgkwDRDPLQHsckayctARQELAVLLTLK 1790
Cdd:cd05123     1 LGKGSFGKVLL----VRKKDTGKLYAMKVLR--------KKEII----------KRKEVEH-------TLNERNILERVN 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd05123    52 HPFIVKLHYAFQTEekLYLVLDYVPGGELFSHLSKEGR----FPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILL- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd05123   127 ------DSDG-----HIKLTDFGLAKELSSDGDRtyTFCGTPEYLAPEVLL---GKGYGKAVDWWSLGVLLYEMLTGKPP 192

                  ....*
gi 442620116 1947 FEGHE 1951
Cdd:cd05123   193 FYAEN 197
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
1758-2003 1.26e-27

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: 114.31  E-value: 1.26e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWDRDPLQHSCKAYCTARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLrhyrrSGAHMGPHT 1835
Cdd:cd14148    19 EVAVKAARQDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPphLCLVMEYARGGALNRAL-----AGKKVPPHV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1836 FQTLVLQAARAIEYLHRRR---IIYRDLKSENVLVWElpqPHTEDSPRNLVhIKIADYGISRQTAPSGAKGFGGTEGFMA 1912
Cdd:cd14148    94 LVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILILE---PIENDDLSGKT-LKITDFGLAREWHKTTKMSAAGTYAWMA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1913 PEIIRYNgeeEYTEKVDCFSFGMFIYENISLRQPFEGHESIkeCILEGSrpALTQRETQFPTCCLD----LMVLCWHEQP 1988
Cdd:cd14148   170 PEVIRLS---LFSKSSDVWSFGVLLWELLTGEVPYREIDAL--AVAYGV--AMNKLTLPIPSTCPEpfarLLEECWDPDP 242
                         250
                  ....*....|....*
gi 442620116 1989 RRRPTASQIVSILSA 2003
Cdd:cd14148   243 HGRPDFGSILKRLED 257
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
1711-2001 1.27e-27

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: 114.03  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckvrgaRSFKPVAMKMLQPVPPGArakeSALMAFKvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd14062     1 IGSGSFGTVYKG-------RWHGDVAVKKLNVTDPTP----SQLQAFK----------------------NEVAVLRKTR 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP-LALVLELAPlgGlDALLRHYrrsgaHMGPHTFQTLVL-----QAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd14062    48 HVNILLFMGYMTKPqLAIVTQWCE--G-SSLYKHL-----HVLETKFEMLQLidiarQTAQGMDYLHAKNIIHRDLKSNN 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphTEDSPrnlvhIKIADYGISR-QTAPSGAKGFGGTEG---FMAPEIIRYNGEEEYTEKVDCFSFGMFIYEN 1940
Cdd:cd14062   120 IFL-------HEDLT-----VKIGDFGLATvKTRWSGSQQFEQPTGsilWMAPEVIRMQDENPYSFQSDVYAFGIVLYEL 187
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1941 ISLRQPFEGHESiKECIL--EGS---RPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14062   188 LTGQLPYSHINN-RDQILfmVGRgylRPDLSKVRSDTPKALRRLMEDCIKFQRDERPLFPQILASL 252
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1711-2003 1.42e-27

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: 113.98  E-value: 1.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSfKPVAMKMLQPVPPGARAKEsaLMAfkvavgkwdrdplqhsckayctarqELAVLLTLK 1790
Cdd:cd05060     3 LGHGNFGSVRKGVYLMKSGKE-VEVAVKTLKQEHEKAGKKE--FLR-------------------------EASVMAQLD 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICI-KPLALVLELAPLGGLDALLRHYRrsgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwe 1869
Cdd:cd05060    55 HPCIVRLIGVCKgEPLMLVMELAPLGPLLKYLKKRR----EIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLL-- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 lpqphtedSPRNLVhiKIADYGISRqtapsgAKGFGGTE-----------GFMAPEIIRYNgeeEYTEKVDCFSFGMFIY 1938
Cdd:cd05060   129 --------VNRHQA--KISDFGMSR------ALGAGSDYyrattagrwplKWYAPECINYG---KFSSKSDVWSYGVTLW 189
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1939 ENISLRQP----FEGHESIKecILEG----SRPALTQRETqfptccLDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05060   190 EAFSYGAKpygeMKGPEVIA--MLESgerlPRPEECPQEI------YSIMLSCWKYRPEDRPTFSELESTFRR 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
1707-1996 1.05e-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: 111.53  E-value: 1.05e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVppgarakesalmafkvavGKWDRDPLQhsckayctarQELAVL 1786
Cdd:cd05122     4 ILEKIGKGGFGVVYKARHKKTG----QIVAIKKINLE------------------SKEKKESIL----------NEIAIL 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVG--ICIKPLALVLELAPLGGLDALLRHYrrsgahmgPHTFQ-----TLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd05122    52 KKCKHPNIVKYYGsyLKKDELWIVMEFCSGGSLKDLLKNT--------NKTLTeqqiaYVCKEVLKGLEYLHSHGIIHRD 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIY 1938
Cdd:cd05122   124 IKAANILL-------TSDG-----EVKLIDFGLSAQLSDGKTrNTFVGTPYWMAPEVIQ---GKPYGFKADIWSLGITAI 188
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1939 ENISLRQPFEGHESIKECILEGSRPALTQRETQFPTCCL-DLMVLCWHEQPRRRPTASQ 1996
Cdd:cd05122   189 EMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKEFkDFLKKCLQKDPEKRPTAEQ 247
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
1711-2003 5.29e-26

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: 109.35  E-value: 5.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSFkPVAMKMLQPvppGARAKESALMAFkvavgkwdrdplqhsckayctaRQELAVLLTLK 1790
Cdd:cd05040     3 LGDGSFGVVRRGEWTTPSGKVI-QVAVKCLKS---DVLSQPNAMDDF----------------------LKEVNAMHSLD 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICI-KPLALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwe 1869
Cdd:cd05040    57 HPNLIRLYGVVLsSPLMMVTELAPLG---SLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILL-- 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 lpqphtedSPRNLVhiKIADYGISRqTAPSGAKGFGGTE------GFMAPEIIRYngeEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd05040   132 --------ASKDKV--KIGDFGLMR-ALPQNEDHYVMQEhrkvpfAWCAPESLKT---RKFSHASDVWMFGVTLWEMFTY 197
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1944 -RQPFEGHESIKecIL-----EGSRpaLTQretqfPTCC----LDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05040   198 gEEPWLGLNGSQ--ILekidkEGER--LER-----PDDCpqdiYNVMLQCWAHKPADRPTFVALRDFLPE 258
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
1778-2002 6.16e-26

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: 109.79  E-value: 6.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRhyrRSGAHMGpHTFQ-TLVLQAARAIEYLHRRR 1854
Cdd:cd13992    42 TILQELNQLKELVHDNLNKFIGICINPpnIAVVTEYCTRGSLQDVLL---NREIKMD-WMFKsSFIKDIVKGMNYLHSSS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYR-DLKSENVLVwelpqphteDSprNLVhIKIADYGISR----------QTAPSGAKgfggtEGFMAPEIIRYN-GEE 1922
Cdd:cd13992   118 IGYHgRLKSSNCLV---------DS--RWV-VKLTDFGLRNlleeqtnhqlDEDAQHKK-----LLWTAPELLRGSlLEV 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1923 EYTEKVDCFSFGMFIYEnISLRQ---PFEGHESIKECILEGS----RPALTQRETQFPTCCLDLMVLCWHEQPRRRPTAS 1995
Cdd:cd13992   181 RGTQKGDVYSFAIILYE-ILFRSdpfALEREVAIVEKVISGGnkpfRPELAVLLDEFPPRLVLLVKQCWAENPEKRPSFK 259

                  ....*..
gi 442620116 1996 QIVSILS 2002
Cdd:cd13992   260 QIKKTLT 266
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
1772-2002 7.49e-26

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: 109.43  E-value: 7.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1772 SCKAYCTAR------QELAVLLTLKHPNIVPLVGICI-KPLALVLELAPLGGLDALLRHYRRSGAHMgphTFQTLVLQAA 1844
Cdd:cd05056    41 TCKNCTSPSvrekflQEAYIMRQFDHPHIVKLIGVITeNPVWIVMELAPLGELRSYLQVNKYSLDLA---SLILYAYQLS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1845 RAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISRQTAPSGAkgFGGTEG-----FMAPEIIRYn 1919
Cdd:cd05056   118 TALAYLESKRFVHRDIAARNVLV---------SSPDC---VKLGDFGLSRYMEDESY--YKASKGklpikWMAPESINF- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 geEEYTEKVDCFSFGMFIYENISL-RQPFEGHESiKECIL---EGSRPALTQretQFPTCCLDLMVLCWHEQPRRRPTAS 1995
Cdd:cd05056   183 --RRFTSASDVWMFGVCMWEILMLgVKPFQGVKN-NDVIGrieNGERLPMPP---NCPPTLYSLMTKCWAYDPSKRPRFT 256

                  ....*..
gi 442620116 1996 QIVSILS 2002
Cdd:cd05056   257 ELKAQLS 263
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
453-707 8.77e-26

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 112.72  E-value: 8.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  453 LTAITRIDFSHNvltsipQELFHLVSLRYLNVAQNKITDLPAPIGQtygCPVLDELFLQDNQLTTLPAAIFHLPALSILD 532
Cdd:COG4886    95 LTNLTELDLSGN------EELSNLTNLESLDLSGNQLTDLPEELAN---LTNLKELDLSNNQLTDLPEPLGNLTNLKSLD 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  533 VSNNKLQQLPFDLWRAPKLRELNVAFNLLRDLPVPpmqtsssllsldklnlqsfeeppsnkprnvtqqrlthrnlwsatl 612
Cdd:COG4886   166 LSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEP--------------------------------------------- 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  613 ditdndmkwqheqdLGdgktagvGSSQLSSLNIANNLFTSIPAALPCLAvNLTRLNMSYNSLRSMGHVTSYPAtLKQLDL 692
Cdd:COG4886   201 --------------LG-------NLTNLEELDLSGNQLTDLPEPLANLT-NLETLDLSNNQLTDLPELGNLTN-LEELDL 257
                         250
                  ....*....|....*
gi 442620116  693 SHNEISCWPSLPRIT 707
Cdd:COG4886   258 SNNQLTDLPPLANLT 272
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1779-2000 1.39e-25

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: 108.28  E-value: 1.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVG-------ICIkplalVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLH 1851
Cdd:cd08222    49 ANREAKLLSKLDHPAIVKFHDsfvekesFCI-----VTEYCEGGDLDDKISEYKKSGTTIDENQILDWFIQLLLAVQYMH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVwelpqphtedsPRNLvhIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRYNGeeeYTEKVD 1929
Cdd:cd08222   124 ERRILHRDLKAKNIFL-----------KNNV--IKVGDFGISRILMGTSdlATTFTGTPYYMSPEVLKHEG---YNSKSD 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1930 CFSFGMFIYENISLRQPFEGHE--SIKECILEGSRPALTQRetqFPTCCLDLMVLCWHEQPRRRPTASQIVSI 2000
Cdd:cd08222   188 IWSLGCILYEMCCLKHAFDGQNllSVMYKIVEGETPSLPDK---YSKELNAIYSRMLNKDPALRPSAAEILKI 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
1708-2000 1.52e-25

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: 108.13  E-value: 1.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGarsfKPVAMKmlqpvppgaRAKESALMAFKvavgkwdrdplqhsckayctARQ----EL 1783
Cdd:cd08224     5 EKKIGKGQFSVVYRARCLLDG----RLVALK---------KVQIFEMMDAK--------------------ARQdclkEI 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1784 AVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLK 1861
Cdd:cd08224    52 DLLQQLNHPNIIKYLASFIEnnELNIVLELADAGDLSRLIKHFKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIK 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphTEDSPrnlvhIKIADYGISRQTAP--SGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYE 1939
Cdd:cd08224   132 PANVFI-------TANGV-----VKLGDLGLGRFFSSktTAAHSLVGTPYYMSPERIREQG---YDFKSDIWSLGCLLYE 196
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1940 NISLRQPFEGHE----SIKECILEGSRPALtqRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSI 2000
Cdd:cd08224   197 MAALQSPFYGEKmnlySLCKKIEKCEYPPL--PADLYSQELRDLVAACIQPDPEKRPDISYVLDV 259
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
1711-1949 2.09e-25

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: 107.69  E-value: 2.09e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGArsfkPVAMKMLqpvppgARAKESAlmafkvavgkwdrdPLQHSCKayctarQELAVLLTLK 1790
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGE----VVAIKEI------SRKKLNK--------------KLQENLE------SEIAILKSIK 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGiCIKPLA---LVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd14009    51 HPNIVRLYD-VQKTEDfiyLVLEYCAGGDLSQYIRKRGR----LPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 welpqphteDSPRNLVHIKIADYGISRQTAPSG-AKGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd14009   126 ---------STSGDDPVLKIADFGFARSLQPASmAETLCGSPLYMAPEILQF---QKYDAKADLWSVGAILFEMLVGKPP 193

                  ...
gi 442620116 1947 FEG 1949
Cdd:cd14009   194 FRG 196
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
1700-2001 3.84e-25

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: 107.89  E-value: 3.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCKVRGARSFKP--VAMKMLqpvppgaraKESALmafkvavgkwDRDPLQhsckayc 1777
Cdd:cd05053     9 LPRDRLTLGKPLGEGAFGQVVKAEAVGLDNKPNEVvtVAVKML---------KDDAT----------EKDLSD------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 tARQELAVLLTL-KHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSG---------AHMGPHTFQTLV---LQ 1842
Cdd:cd05053    63 -LVSEMEMMKMIgKHKNIINLLGACTQdgPLYVVVEYASKGNLREFLRARRPPGeeaspddprVPEEQLTQKDLVsfaYQ 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1843 AARAIEYLHRRRIIYRDLKSENVLVWElpqphtedsprNLVhIKIADYGISR---------QTapsgakgfggTEG---- 1909
Cdd:cd05053   142 VARGMEYLASKKCIHRDLAARNVLVTE-----------DNV-MKIADFGLARdihhidyyrKT----------TNGrlpv 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1910 -FMAPEIIRYNgeeEYTEKVDCFSFGMFIYENISLR-QPFEG--HESIKECILEGSR---PALTQRETQFptccldLMVL 1982
Cdd:cd05053   200 kWMAPEALFDR---VYTHQSDVWSFGVLLWEIFTLGgSPYPGipVEELFKLLKEGHRmekPQNCTQELYM------LMRD 270
                         330
                  ....*....|....*....
gi 442620116 1983 CWHEQPRRRPTASQIVSIL 2001
Cdd:cd05053   271 CWHEVPSQRPTFKQLVEDL 289
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
1701-2020 1.17e-24

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: 107.36  E-value: 1.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECIIKGSLLGRGAFGFVFKANC-KVRGARSFKP--VAMKMLqpvppgaraKESALmafkvavgkwDRDplqhscKAYC 1777
Cdd:cd05099    10 PRDRLVLGKPLGEGCFGQVVRAEAyGIDKSRPDQTvtVAVKML---------KDNAT----------DKD------LADL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTlKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSG---------AHMGPHTFQTLV---LQA 1843
Cdd:cd05099    65 ISEMELMKLIG-KHKNIINLLGVCTQegPLYVIVEYAAKGNLREFLRARRPPGpdytfditkVPEEQLSFKDLVscaYQV 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1844 ARAIEYLHRRRIIYRDLKSENVLVwelpqphTEDSPrnlvhIKIADYGISR--QTAPSGAKGFGG--TEGFMAPEIIRyn 1919
Cdd:cd05099   144 ARGMEYLESRRCIHRDLAARNVLV-------TEDNV-----MKIADFGLARgvHDIDYYKKTSNGrlPVKWMAPEALF-- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 gEEEYTEKVDCFSFGMFIYENISL-RQPFEG--HESIKECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd05099   210 -DRVYTHQSDVWSFGILMWEIFTLgGSPYPGipVEELFKLLREGHR---MDKPSNCTHELYMLMRECWHAVPTQRPTFKQ 285
                         330       340
                  ....*....|....*....|....
gi 442620116 1997 IVsilsapeciHLLDVVAMPHSEK 2020
Cdd:cd05099   286 LV---------EALDKVLAAVSEE 300
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
1708-1997 1.88e-24

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: 104.91  E-value: 1.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvppgarakesalmafkvavgkwDRDPLQHSCKAYCtaRQELAVLL 1787
Cdd:cd14003     5 GKTLGEGSFGKVKLARHKLTG----EKVAIKII------------------------DKSKLKEEIEEKI--KREIEIMK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPlGG--LDALLRHYR------RsgahmgpHTFQTLVLqaarAIEYLHRRRIIY 1857
Cdd:cd14003    55 LLNHPNIIKLYEVIETEnkIYLVMEYAS-GGelFDYIVNNGRlsedeaR-------RFFQQLIS----AVDYCHSNGIVH 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphteDSPRNlvhIKIADYGISRQTAP-SGAKGFGGTEGFMAPEIIryNGEEEYTEKVDCFSFGMF 1936
Cdd:cd14003   123 RDLKLENILL---------DKNGN---LKIIDFGLSNEFRGgSLLKTFCGTPAYAAPEVL--LGRKYDGPKADVWSLGVI 188
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1937 IYENISLRQPFEGHE--SIKECILEGSRPaltqRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14003   189 LYAMLTGYLPFDDDNdsKLFRKILKGKYP----IPSHLSPDARDLIRRMLVVDPSKRITIEEI 247
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
1708-2001 2.15e-24

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: 104.63  E-value: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAncKVRGARSfkPVAMKML-QPVPPGARAKesalmafkvavgkwdrdplqhsckayctARQELAVL 1786
Cdd:cd05084     1 GERIGRGNFGEVFSG--RLRADNT--PVAVKSCrETLPPDLKAK----------------------------FLQEARIL 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd05084    49 KQYSHPNIVRLIGVCTQkqPIYIVMELVQGGDFLTFLRT---EGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARN 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphTEDSPrnlvhIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYNgeeEYTEKVDCFSFGMFIYEN 1940
Cdd:cd05084   126 CLV-------TEKNV-----LKISDFGMSREEEDGVYAATGGMKqipvKWTAPEALNYG---RYSSESDVWSFGILLWET 190
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1941 ISL-RQPFEG--HESIKECILEGSR-PAltqretqfPTCCLD----LMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05084   191 FSLgAVPYANlsNQQTREAVEQGVRlPC--------PENCPDevyrLMEQCWEYDPRKRPSFSTVHQDL 251
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
1709-2001 5.01e-24

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: 104.39  E-value: 5.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPvppgarAKESALMA-FKvavgkwdrdplqhsckayctarQELAVLL 1787
Cdd:cd05038    10 KQLGEGHFGSVELCRYDPLGDNTGEQVAVKSLQP------SGEEQHMSdFK----------------------REIEILR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP----LALVLELAPLGGLDALLRHYRRSGAHmgphtfQTLVL---QAARAIEYLHRRRIIYRDL 1860
Cdd:cd05038    62 TLDHEYIVKYKGVCESPgrrsLRLIMEYLPSGSLRDYLQRHRDQIDL------KRLLLfasQICKGMEYLGSQRYIHRDL 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1861 KSENVLVwelpqphteDSPRnlvHIKIADYGISRqTAPSGAKGFGGTEG------FMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd05038   136 AARNILV---------ESED---LVKISDFGLAK-VLPEDKEYYYVKEPgespifWYAPECLR---ESRFSSASDVWSFG 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1935 MFIYENISLRQPFEG--HESIKECILEGSRPALTQ---------RETQFPTC---CLDLMVLCWHEQPRRRPTASQIVSI 2000
Cdd:cd05038   200 VTLYELFTYGDPSQSppALFLRMIGIAQGQMIVTRllellksgeRLPRPPSCpdeVYDLMKECWEYEPQDRPSFSDLILI 279

                  .
gi 442620116 2001 L 2001
Cdd:cd05038   280 I 280
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
1708-2003 5.03e-24

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: 103.55  E-value: 5.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRgarsfKPVAMKMlqpvppgarAKESALMAFKVAVgkwdrdplqhsckayctaRQELAVLL 1787
Cdd:cd05085     1 GELLGKGNFGEVYKGTLKDK-----TPVAVKT---------CKEDLPQELKIKF------------------LSEARILK 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICI--KPLALVLELAPLGGldaLLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd05085    49 QYDHPNIVKLIGVCTqrQPIYIVMELVPGGD---FLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNC 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWElpqphtedspRNLvhIKIADYGISRQT-----APSGAKGFggTEGFMAPEIIRYNgeeEYTEKVDCFSFGMFIYEN 1940
Cdd:cd05085   126 LVGE----------NNA--LKISDFGMSRQEddgvySSSGLKQI--PIKWTAPEALNYG---RYSSESDVWSFGILLWET 188
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1941 ISLRQ-PFEG--HESIKECILEGSRPALTQRetqFPTCCLDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05085   189 FSLGVcPYPGmtNQQAREQVEKGYRMSAPQR---CPEDIYKIMQRCWDYNPENRPKFSELQKELAA 251
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1700-2003 7.53e-24

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: 103.96  E-value: 7.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCK-VRGARSFKPVAMKMLQPvppgaRAKESALMAFkvavgkwdrdplqhsckayct 1778
Cdd:cd05032     3 LPREKITLIRELGQGSFGMVYEGLAKgVVKGEPETRVAIKTVNE-----NASMRERIEF--------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 aRQELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYR---RSGAHMGPHTFQTL---VLQAARAIEYL 1850
Cdd:cd05032    57 -LNEASVMKEFNCHHVVRLLGVVSTgqPTLVVMELMAKGDLKSYLRSRRpeaENNPGLGPPTLQKFiqmAAEIADGMAYL 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGISRQTAPS-----GAKGFGGTEgFMAPEIIRyngEEEYT 1925
Cdd:cd05032   136 AAKKFVHRDLAARNCMV------AEDLT------VKIGDFGMTRDIYETdyyrkGGKGLLPVR-WMAPESLK---DGVFT 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1926 EKVDCFSFGMFIYENISL-RQPFEG--HESIKECILEGSrpALTQretqfPTCC----LDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd05032   200 TKSDVWSFGVVLWEMATLaEQPYQGlsNEEVLKFVIDGG--HLDL-----PENCpdklLELMRMCWQYNPKMRPTFLEIV 272

                  ....*
gi 442620116 1999 SILSA 2003
Cdd:cd05032   273 SSLKD 277
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
1697-2002 1.03e-23

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: 104.11  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1697 KHTIPSECIIKGSLLGRGAFGFVFKANC-KVRGARSFKPVAMKMLQPvppGARAKE-SALMAfkvavgkwdrdplqhsck 1774
Cdd:cd05054     1 KWEFPRDRLKLGKPLGRGAFGKVIQASAfGIDKSATCRTVAVKMLKE---GATASEhKALMT------------------ 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1775 ayctarqELAVLLTL-KHPNIVPLVGICIK---PLALVLELAPLGGLDALLRH-------YRRSGAHM------------ 1831
Cdd:cd05054    60 -------ELKILIHIgHHLNVVNLLGACTKpggPLMVIVEFCKFGNLSNYLRSkreefvpYRDKGARDveeeedddelyk 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1832 GPHTFQTLV---LQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedSPRNLVhiKIADYGISRQ--TAPSGAKGfGG 1906
Cdd:cd05054   133 EPLTLEDLIcysFQVARGMEFLASRKCIHRDLAARNILL----------SENNVV--KICDFGLARDiyKDPDYVRK-GD 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1907 TE---GFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISL-RQPFEG---HESIKECILEGSRpaltQRETQFPTCCL-D 1978
Cdd:cd05054   200 ARlplKWMAPESIF---DKVYTTQSDVWSFGVLLWEIFSLgASPYPGvqmDEEFCRRLKEGTR----MRAPEYTTPEIyQ 272
                         330       340
                  ....*....|....*....|....
gi 442620116 1979 LMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05054   273 IMLDCWHGEPKERPTFSELVEKLG 296
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
1711-2005 1.03e-23

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: 103.23  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAncKVRGarsfKPVAMKMLQPvppgaRAKESAlmafkvavgkwdrdplqhsckAYCTARQELAVLlTLK 1790
Cdd:cd13979    11 LGSGGFGSVYKA--TYKG----ETVAVKIVRR-----RRKNRA---------------------SRQSFWAELNAA-RLR 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGI--CIKPLAL---VLELAPLGGLDALLrhYRRSGAHMGPHTFQTLvLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd13979    58 HENIVRVLAAetGTDFASLgliIMEYCGNGTLQQLI--YEGSEPLPLAHRILIS-LDIARALRFCHSHGIVHLDVKPANI 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWELPQPhtedsprnlvhiKIADYGISRQ-----TAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYEN 1940
Cdd:cd13979   135 LISEQGVC------------KLCDFGCSVKlgegnEVGTPRSHIGGTYTYRAPELLK---GERVTPKADIYSFGITLWQM 199
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1941 ISLRQPFEGhesIKECIL-----EGSRPALT-QRETQFPTCCLDLMVLCWHEQPRRRPTASqiVSILSAPE 2005
Cdd:cd13979   200 LTRELPYAG---LRQHVLyavvaKDLRPDLSgLEDSEFGQRLRSLISRCWSAQPAERPNAD--ESLLKSLE 265
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
1711-1997 1.33e-23

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: 103.22  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSFK-PVAMKMLqpvppgaraKESALMafkvavgkwdrdPLQHSckayctARQELAVLLTL 1789
Cdd:cd05048    13 LGEGAFGKVYKGELLGPSSEESAiSVAIKTL---------KENASP------------KTQQD------FRREAELMSDL 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIK--PLALVLELAPLGGL-DALLRHYRRSGAH-----------MGPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd05048    66 QHPNIVCLLGVCTKeqPQCMLFEYMAHGDLhEFLVRHSPHSDVGvssdddgtassLDQSDFLHIAIQIAAGMEYLSSHHY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVWElpqphtedsprNLvHIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYNgeeEYTEKVDCF 1931
Cdd:cd05048   146 VHRDLAARNCLVGD-----------GL-TVKISDFGLSRDIYSSDYYRVQSKSllpvRWMPPEAILYG---KFTTESDVW 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1932 SFGMFIYENISL-RQPFEGH------ESIKECILEGSrpaltqrETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd05048   211 SFGVVLWEIFSYgLQPYYGYsnqeviEMIRSRQLLPC-------PEDCPARVYSLMVECWHEIPSRRPRFKEI 276
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
1710-2002 1.99e-23

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: 102.54  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAncKVRGARS---FKPVAMKMLQPVPpgaraKESALMAFkvavgkwdrdplqhsckayctaRQELAVL 1786
Cdd:cd05046    12 TLGRGEFGEVFLA--KAKGIEEeggETLVLVKALQKTK-----DENLQSEF----------------------RRELDMF 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGIC--IKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQT-----LVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd05046    63 RKLSHKNVVRLLGLCreAEPHYMILEYTDLGDLKQFLRATKSKDEKLKPPPLSTkqkvaLCTQIALGMDHLSNARFVHRD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphtedSPRNLVhiKIADYGISRQTAPSGAKGFGGTEG---FMAPEIIRyngEEEYTEKVDCFSFGMF 1936
Cdd:cd05046   143 LAARNCLV----------SSQREV--KVSLLSLSKDVYNSEYYKLRNALIplrWLAPEAVQ---EDDFSTKSDVWSFGVL 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1937 IYENISL-RQPFEGH------ESIKECILEGSRPALTqretqfPTCCLDLMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05046   208 MWEVFTQgELPFYGLsdeevlNRLQAGKLELPVPEGC------PSRLYKLMTRCWAVNPKDRPSFSELVSALG 274
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
1699-2003 1.99e-23

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: 102.54  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1699 TIPSECIIKGSLLGRGAFGFVFKANCkvrgaRSFKPvamkmlqpvppgarAKESALMAFKVavgkwdrdpLQHSCKAycT 1778
Cdd:cd05049     1 HIKRDTIVLKRELGEGAFGKVFLGEC-----YNLEP--------------EQDKMLVAVKT---------LKDASSP--D 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQ----ELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHY---RRSGAHMGPHTFQ-------TLVLQ 1842
Cdd:cd05049    51 ARKdferEAELLTNLQHENIVKFYGVCTEgdPLLMVFEYMEHGDLNKFLRSHgpdAAFLASEDSAPGEltlsqllHIAVQ 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1843 AARAIEYLHRRRIIYRDLKSENVLVWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRY 1918
Cdd:cd05049   131 IASGMVYLASQHFVHRDLATRNCLVGT-----------NLV-VKIGDFGMSRDIYSTDYYRVGGHTmlpiRWMPPESILY 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1919 NgeeEYTEKVDCFSFGMFIYENISL-RQPFEGH--ESIKECILEGSrpaLTQRETQFPTCCLDLMVLCWHEQPRRRPTAS 1995
Cdd:cd05049   199 R---KFTTESDVWSFGVVLWEIFTYgKQPWFQLsnTEVIECITQGR---LLQRPRTCPSEVYAVMLGCWKREPQQRLNIK 272

                  ....*...
gi 442620116 1996 QIVSILSA 2003
Cdd:cd05049   273 DIHKRLQE 280
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
1711-2001 2.04e-23

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: 102.99  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCK-VRGARSFKPVAMKMLqpvppgaraKESAlmafkvavgkwdrdplqhSCKAYCTARQELAVLLTL 1789
Cdd:cd05050    13 IGQGAFGRVFQARAPgLLPYEPFTMVAVKML---------KEEA------------------SADMQADFQREAALMAEF 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICI--KPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLV------------------LQAARAIEY 1849
Cdd:cd05050    66 DHPNIVKLLGVCAvgKPMCLLFEYMAYGDLNEFLRHRSPRAQCSLSHSTSSARkcglnplplscteqlciaKQVAAGMAY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1850 LHRRRIIYRDLKSENVLVWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFGGTEG----FMAPEIIRYNgeeEYT 1925
Cdd:cd05050   146 LSERKFVHRDLATRNCLVGE-----------NMV-VKIADFGLSRNIYSADYYKASENDAipirWMPPESIFYN---RYT 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1926 EKVDCFSFGMFIYENISL-RQPFEG--HESIKECILEGSRPALTQretQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05050   211 TESDVWAYGVVLWEIFSYgMQPYYGmaHEEVIYYVRDGNVLSCPD---NCPLELYNLMRLCWSKLPSDRPSFASINRIL 286
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1711-2001 2.27e-23

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: 101.76  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAncKVRGARSfkpVAMKMLQPvppGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd05059    12 LGSGQFGVVHLG--KWRGKID---VAIKMIKE---GSMSEDDFI--------------------------EEAKVMMKLS 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGahmGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVW 1868
Cdd:cd05059    58 HPKLVQLYGVCTKqrPIFIVTEYMANGCLLNYLRERRGKF---QTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 ElpqphtedspRNLVhiKIADYGISR------QTAPSGAKgfggtegF----MAPEIIRYNgeeEYTEKVDCFSFGMFIY 1938
Cdd:cd05059   135 E----------QNVV--KVSDFGLARyvlddeYTSSVGTK-------FpvkwSPPEVFMYS---KFSSKSDVWSFGVLMW 192
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1939 ENISL-RQPFEG--HESIKECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05059   193 EVFSEgKMPYERfsNSEVVEHISQGYR---LYRPHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
1711-1997 3.40e-23

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 101.48  E-value: 3.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGfvfkancKVRGARSFKP---VAMKMLqpvppgaraKESAL--MAFKVAVGKWDRDPLQHsckayctARQELAV 1785
Cdd:cd14008     1 LGRGSFG-------KVKLALDTETgqlYAIKIF---------NKSRLrkRREGKNDRGKIKNALDD-------VRREIAI 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTLKHPNIVPLVGICIKP----LALVLELAPLGGLDallrhYRRSGAHMGPHTFQTL---VLQAARAIEYLHRRRIIYR 1858
Cdd:cd14008    58 MKKLDHPNIVRLYEVIDDPesdkLYLVLEYCEGGPVM-----ELDSGDRVPPLPEETArkyFRDLVLGLEYLHENGIVHR 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFGMF 1936
Cdd:cd14008   133 DIKPENLLL-------TADG-----TVKISDFGVSEMFEDGNDtlQKTAGTPAFLAPELCDGDSKTYSGKAADIWALGVT 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1937 IYENISLRQPFEGHE--SIKECILEGSRPALTQRETqfPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14008   201 LYCLVFGRLPFNGDNilELYEAIQNQNDEFPIPPEL--SPELKDLLRRMLEKDPEKRITLKEI 261
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
1707-1997 7.21e-23

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: 100.55  E-value: 7.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKVRGarSFkpVAMKMLQPVPPGARAKESA--LMafkvavgkwdrdplqhsckayctarQELA 1784
Cdd:cd06632     4 KGQLLGSGSFGSVYEGFNGDTG--DF--FAVKEVSLVDDDKKSRESVkqLE-------------------------QEIA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYrrsGAHMGP----HTFQTLVlqaarAIEYLHRRRIIYR 1858
Cdd:cd06632    55 LLSKLRHPNIVQYYGTEREedNLYIFLEYVPGGSIHKLLQRY---GAFEEPvirlYTRQILS-----GLAYLHSRNTVHR 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphtEDSPRnlvhIKIADYGISRQ-TAPSGAKGFGGTEGFMAPEIIRYNGeEEYTEKVDCFSFGMFI 1937
Cdd:cd06632   127 DIKGANILV--------DTNGV----VKLADFGMAKHvEAFSFAKSFKGSPYWMAPEVIMQKN-SGYGLAVDIWSLGCTV 193
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1938 YENISLRQP---FEGHESIKECILEGSRPA----LTQRETQFPTCCLdlmvlcwHEQPRRRPTASQI 1997
Cdd:cd06632   194 LEMATGKPPwsqYEGVAAIFKIGNSGELPPipdhLSPDAKDFIRLCL-------QRDPEDRPTASQL 253
Pkinase pfam00069
Protein kinase domain;
1707-1999 7.26e-23

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 99.24  E-value: 7.26e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1707 KGSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvppgarakesalmaFKVAVGKWDRDplqhsckaycTARQELAVL 1786
Cdd:pfam00069    3 VLRKLGSGSFGTVYKAKHRDTG----KIVAIKKI----------------KKEKIKKKKDK----------NILREIKIL 52
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1787 LTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYlhrrriiyrdlksen 1864
Cdd:pfam00069   53 KKLNHPNIVRLYDAFEDKdnLYLVLEYVEGGSLFDLLSEKGA----FSEREAKFIMKQILEGLES--------------- 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1865 vlvwelpqphtedsprnlvhikiadygisrqtaPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLR 1944
Cdd:pfam00069  114 ---------------------------------GSSLTTFVGTPWYMAPEVLGGNP---YGPKVDVWSLGCILYELLTGK 157
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116  1945 QPFEGHES-------IKECILEGSRPALTQREtqfptcCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:pfam00069  158 PPFPGINGneiyeliIDQPYAFPELPSNLSEE------AKDLLKKLLKKDPSKRLTATQALQ 213
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
1711-2001 8.21e-23

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: 100.05  E-value: 8.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAncKVRGArsfKPVAMKMLQPvppGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd05034     3 LGAGQFGEVWMG--VWNGT---TKVAVKTLKP---GTMSPEAFL--------------------------QEAQIMKKLR 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRrsGAHMgphTFQTLV---LQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd05034    49 HDKLVQLYAVCSDeePIYIVTELMSKGSLLDYLRTGE--GRAL---RLPQLIdmaAQIASGMAYLESRNYIHRDLAARNI 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWElpqphtedsprNLVhIKIADYGISR------QTAPSGAKgfggtegF----MAPEIIRYNgeeEYTEKVDCFSFGM 1935
Cdd:cd05034   124 LVGE-----------NNV-CKVADFGLARlieddeYTAREGAK-------FpikwTAPEAALYG---RFTIKSDVWSFGI 181
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1936 FIYENISL-RQPFEG---HESIkECILEGSRPAltqRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05034   182 LLYEIVTYgRVPYPGmtnREVL-EQVERGYRMP---KPPGCPDELYDIMLQCWKKEPEERPTFEYLQSFL 247
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
453-667 1.05e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.47  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  453 LTAITRIDFSHNVLTSIPQELFHLVSLRYLNVAQNKITDLPAPIGQtygCPVLDELFLQDNQLTTLPAAIFHLPALSILD 532
Cdd:COG4886   158 LTNLKSLDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGN---LTNLEELDLSGNQLTDLPEPLANLTNLETLD 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  533 VSNNKLQQLPF---------------------DLWRAPKLRELNVAFNLLRDLPVPPMQTSSSLLSLDKLNLQSFEEPPS 591
Cdd:COG4886   235 LSNNQLTDLPElgnltnleeldlsnnqltdlpPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELL 314
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116  592 NKPRNVTQQRLTHRNLWSATLDITDNDMKWQHEQDLGDGKTAGVGSSQLSSLNIANNLFTSIPAALPCLAVNLTRL 667
Cdd:COG4886   315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLL 390
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
1780-1999 1.38e-22

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: 99.61  E-value: 1.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVG----ICIKPLALVLELAPLGGLdallRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRR- 1854
Cdd:cd13983    48 KQEIEILKSLKHPNIIKFYDswesKSKKEVIFITELMTSGTL----KQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDp 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 -IIYRDLKSENVLVwelpqphteDSPRNLVhiKIADYGISRQTAPSGAKGFGGTEGFMAPEIirYngEEEYTEKVDCFSF 1933
Cdd:cd13983   124 pIIHRDLKCDNIFI---------NGNTGEV--KIGDLGLATLLRQSFAKSVIGTPEFMAPEM--Y--EEHYDEKVDIYAF 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1934 GMFIYENISLRQPFeghesiKEC---------ILEGSRPALTQReTQFPtCCLDLMVLCWhEQPRRRPTASQIVS 1999
Cdd:cd13983   189 GMCLLEMATGEYPY------SECtnaaqiykkVTSGIKPESLSK-VKDP-ELKDFIEKCL-KPPDERPSARELLE 254
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1711-2000 1.64e-22

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: 99.72  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgarakesalmAFKVAVGKWDRDplqhsckayCTarQELAVLLTLK 1790
Cdd:cd08228    10 IGRGQFSEVYRATCLLDR----KPVALKKVQ--------------IFEMMDAKARQD---------CV--KEIDLLKQLN 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVW 1868
Cdd:cd08228    61 HPNVIKYLDSFIEdnELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFIT 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 ELPQphtedsprnlvhIKIADYGISR--QTAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd08228   141 ATGV------------VKLGDLGLGRffSSKTTAAHSLVGTPYYMSPERIHENG---YNFKSDIWSLGCLLYEMAALQSP 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1947 FEGHE----SIKECILEGSRPALTQRetQFPTCCLDLMVLCWHEQPRRRPTASQIVSI 2000
Cdd:cd08228   206 FYGDKmnlfSLCQKIEQCDYPPLPTE--HYSEKLRELVSMCIYPDPDQRPDIGYVHQI 261
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
1781-2003 2.88e-22

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: 98.11  E-value: 2.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGphTFQTLVLQAARAIEYLHRR---RI 1855
Cdd:cd14060    31 KEAEILSVLSHRNIIQFYGAILEApnYGIVTEYASYGSLFDYLNSNESEEMDMD--QIMTWATDIAKGMHYLHMEapvKV 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphTEDSPrnlvhIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGM 1935
Cdd:cd14060   109 IHRDLKSRNVVI-------AADGV-----LKICDFGASRFHSHTTHMSLVGTFPWMAPEVIQ---SLPVSETCDTYSYGV 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1936 FIYENISLRQPFEGHESIKECIL---EGSRPALtqretqfPTCC----LDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd14060   174 VLWEMLTREVPFKGLEGLQVAWLvveKNERPTI-------PSSCprsfAELMRRCWEADVKERPSFKQIIGILES 241
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
1781-1997 3.21e-22

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: 98.73  E-value: 3.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGphtfqTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14027    40 EEGKMMNRLRHSRVVKLLGVILEEgkYSLVMEYMEKGNLMHVLKKVSVPLSVKG-----RIILEIIEGMAYLHGKGVIHK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphtedspRNLVHIKIADYGIS--------------RQTAPSGA-KGFGGTEGFMAPEIIRyNGEEE 1923
Cdd:cd14027   115 DLKPENILV------------DNDFHIKIADLGLAsfkmwskltkeehnEQREVDGTaKKNAGTLYYMAPEHLN-DVNAK 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFE---GHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14027   182 PTEKSDVYSFAIVLWAIFANKEPYEnaiNEDQIIMCIKSGNRPDVDDITEYCPREIIDLMKLCWEANPEARPTFPGI 258
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
1698-2003 4.20e-22

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: 98.61  E-value: 4.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1698 HTIPSECIIKGSLLGRGAFGFVFKA--NCKVRGARSFkPVAMKMLqPVPPGARAKESALMafkvavgkwdrdplqhscka 1775
Cdd:cd05036     1 KEVPRKNLTLIRALGQGAFGEVYEGtvSGMPGDPSPL-QVAVKTL-PELCSEQDEMDFLM-------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1776 yctarqELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQA---ARAIEYL 1850
Cdd:cd05036    59 ------EALIMSKFNHPNIVRCIGVCFQrlPRFILLELMAGGDLKSFLRENRPRPEQPSSLTMLDLLQLAqdvAKGCRYL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVwelpqphTEDSPRNLVhiKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRyngEEEYTE 1926
Cdd:cd05036   133 EENHFIHRDIAARNCLL-------TCKGPGRVA--KIGDFGMARDIYRADYYRKGGKAmlpvKWMPPEAFL---DGIFTS 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1927 KVDCFSFGMFIYENISL-RQPFEG--HESIKECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05036   201 KTDVWSFGVLLWEIFSLgYMPYPGksNQEVMEFVTSGGR---MDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLNY 277
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
1707-1996 8.34e-22

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: 97.28  E-value: 8.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVfkanCKVRGARSFKPVAMKMLQPvpPGARAKESALMafkvavgkwdrdplqhsckayctarQELAVL 1786
Cdd:cd06623     5 RVKVLGQGSSGVV----YKVRHKPTGKIYALKKIHV--DGDEEFRKQLL-------------------------RELKTL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRrsgaHMGPHTFQTLVLQAARAIEYLHR-RRIIYRDLKSE 1863
Cdd:cd06623    54 RSCESPYVVKCYGAFYKEgeISIVLEYMDGGSLADLLKKVG----KIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPS 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphtedsprNLV-HIKIADYGISRQTAPSGAKG--FGGTEGFMAPEiiRYNGeEEYTEKVDCFSFGMFIYEN 1940
Cdd:cd06623   130 NLLI-------------NSKgEVKIADFGISKVLENTLDQCntFVGTVTYMSPE--RIQG-ESYSYAADIWSLGLTLLEC 193
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1941 ISLRQPFEGHES-----IKECILEGSRPALTQRE-----TQFPTCCLdlmvlcwHEQPRRRPTASQ 1996
Cdd:cd06623   194 ALGKFPFLPPGQpsffeLMQAICDGPPPSLPAEEfspefRDFISACL-------QKDPKKRPSAAE 252
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
1781-1999 9.47e-22

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: 97.88  E-value: 9.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP----LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd06621    48 RELEINKSCASPYIVKYYGAFLDEqdssIGIAMEYCEGGSLDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKII 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMF 1936
Cdd:cd06621   128 HRDIKPSNILLTRKGQ------------VKLCDFGVSGELVNSLAGTFTGTSYYMAPERIQ---GGPYSITSDVWSLGLT 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1937 IYENISLRQPF--EGHESIK-----ECILEGSRPALTQRET----------QFPTCCLDlmvlcwhEQPRRRPTASQIVS 1999
Cdd:cd06621   193 LLEVAQNRFPFppEGEPPLGpiellSYIVNMPNPELKDEPEngikwsesfkDFIEKCLE-------KDGTRRPGPWQMLA 265
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
1709-1999 9.78e-22

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: 97.46  E-value: 9.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKvrgaRSFKPVAMKMLqpvppgaraKESALMAFKVAVGKWDRDplqhsckayctARQELAVLLT 1788
Cdd:cd14084    12 RTLGSGACGEVKLAYDK----STCKKVAIKII---------NKRKFTIGSRREINKPRN-----------IETEIEILKK 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKPLA--LVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLqaarAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14084    68 LSHPCIIKIEDFFDAEDDyyIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLL----AVKYLHSNGIIHRDLKPENVL 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqPHTEDSPRnlvhIKIADYGISRQTAP-SGAKGFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd14084   144 L-----SSQEEECL----IKITDFGLSKILGEtSLMKTLCGTPTYLAPEVLRSFGTEGYTRAVDCWSLGVILFICLSGYP 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1946 PFEGH---ESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14084   215 PFSEEytqMSLKEQILSGKYTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALE 271
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
1711-2000 1.65e-21

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 96.61  E-value: 1.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSFkpVAMKMLQpvppgarakesalmafkvavgKWDRDPLQHSCKAYCTARQELAVllTLK 1790
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSGVL--YAVKEYR---------------------RRDDESKRKDYVKRLTSEYIISS--KLH 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLA---LVLELAPLGGLDALLRHYRrsgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd13994    56 HPNIVKVLDLCQDLHGkwcLVMEYCPGGDLFTLIEKAD----SLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 welpqphTEDSprnlvHIKIADYGIS-------RQTAPSGaKGFGGTEGFMAPEI---IRYNGeeeytEKVDCFSFGMFI 1937
Cdd:cd13994   132 -------DEDG-----VLKLTDFGTAevfgmpaEKESPMS-AGLCGSEPYMAPEVftsGSYDG-----RAVDVWSCGIVL 193
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1938 YENISLRQPFE----GHESIKECILEGSRP--ALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSI 2000
Cdd:cd13994   194 FALFTGRFPWRsakkSDSAYKAYEKSGDFTngPYEPIENLLPSECRRLIYRMLHPDPEKRITIDEALND 262
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1711-1997 2.41e-21

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: 95.76  E-value: 2.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARsfkpVAMKMLQPVPPGARAKESALMAfkvavgkwdrdpLQHSCKAyctarqelavlltLK 1790
Cdd:cd05118     7 IGEGAFGTVWLARDKVTGEK----VAIKKIKNDFRHPKAALREIKL------------LKHLNDV-------------EG 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGI----CIKPLALVLELaplGGLDaLLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd05118    58 HPNIVKLLDVfehrGGNHLCLVFEL---MGMN-LYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENIL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphtedsprNLVH--IKIADYGISRQTAPSGAKGFGGTEGFMAPEIIryNGEEEYTEKVDCFSFGMFIYENISLR 1944
Cdd:cd05118   134 I-------------NLELgqLKLADFGLARSFTSPPYTPYVATRWYRAPEVL--LGAKPYGSSIDIWSLGCILAELLTGR 198
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1945 QPFEGHESIKE--CILE--GSRPAltqretqfptccLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd05118   199 PLFPGDSEVDQlaKIVRllGTPEA------------LDLLSKMLKYDPAKRITASQA 243
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
1707-1999 2.79e-21

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: 95.70  E-value: 2.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKanckVRGARSFKPVAMKMlqpVPPGARAKESALMAFKvavgkwdrdplqhsckayctarQELAVL 1786
Cdd:cd14099     5 RGKFLGKGGFAKCYE----VTDMSTGKVYAGKV---VPKSSLTKPKQREKLK----------------------SEIKIH 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGI-----CIkplALVLELAPLGGLDALLRhyrRSGAHMGPHTfQTLVLQAARAIEYLHRRRIIYRDLK 1861
Cdd:cd14099    56 RSLKHPNIVKFHDCfedeeNV---YILLELCSNGSLMELLK---RRKALTEPEV-RYFMRQILSGVKYLHSNRIIHRDLK 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphTEDsprnlVHIKIADYGISRQTAPSGAKGFG--GTEGFMAPEIIryNGEEEYTEKVDCFSFGMFIYE 1939
Cdd:cd14099   129 LGNLFL-------DEN-----MNVKIGDFGLAARLEYDGERKKTlcGTPNYIAPEVL--EKKKGHSFEVDIWSLGVILYT 194
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1940 NISLRQPFEGH--ESIKECILegsrpaltQRETQFPTCCL------DLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14099   195 LLVGKPPFETSdvKETYKRIK--------KNEYSFPSHLSisdeakDLIRSMLQPDPTKRPSLDEILS 254
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
1711-2003 3.35e-21

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: 96.19  E-value: 3.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKvrgarSFKPVAMKMLQPVPPGARAKESALMAFKvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd05092    13 LGEGAFGKVFLAECH-----NLLPEQDKMLVAVKALKEATESARQDFQ----------------------REAELLTVLQ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICI--KPLALVLELAPLGGLDALLRHY--------RRSGAHMGPHTFQTLV---LQAARAIEYLHRRRIIY 1857
Cdd:cd05092    66 HQHIVRFYGVCTegEPLIMVFEYMRHGDLNRFLRSHgpdakildGGEGQAPGQLTLGQMLqiaSQIASGMVYLASLHFVH 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYngeEEYTEKVDCFSF 1933
Cdd:cd05092   146 RDLATRNCLVGQ-----------GLV-VKIGDFGMSRDIYSTDYYRVGGRTmlpiRWMPPESILY---RKFTTESDIWSF 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1934 GMFIYENISL-RQPF---EGHESIkECILEGsrpaltqRETQFPTCC----LDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05092   211 GVVLWEIFTYgKQPWyqlSNTEAI-ECITQG-------RELERPRTCppevYAIMQGCWQREPQQRHSIKDIHSRLQA 280
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
1711-1959 3.50e-21

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: 96.90  E-value: 3.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKvrgaRSFKPVAMKMLQpvppgaraKESALMafkvavgkwDRDplqhsckAYCTARQELAVLLTLK 1790
Cdd:cd05570     3 LGKGSFGKVMLAERK----KTDELYAIKVLK--------KEVIIE---------DDD-------VECTMTEKRVLALANR 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGiCI---KPLALVLELAPlGGlDaLLRHYRRSGAHMGPHTfqtlVLQAAR---AIEYLHRRRIIYRDLKSEN 1864
Cdd:cd05570    55 HPFLTGLHA-CFqteDRLYFVMEYVN-GG-D-LMFHIQRARRFTEERA----RFYAAEiclALQFLHERGIIYRDLKLDN 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAKG--FGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENIS 1942
Cdd:cd05570   127 VLL-------DAEG-----HIKIADFGMCKEGIWGGNTTstFCGTPDYIAPEILR---EQDYGFSVDWWALGVLLYEMLA 191
                         250
                  ....*....|....*....
gi 442620116 1943 LRQPFEG--HESIKECILE 1959
Cdd:cd05570   192 GQSPFEGddEDELFEAILN 210
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
1711-2003 4.10e-21

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: 95.29  E-value: 4.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCkvRGarsfKPVAMKmlqpvppgaRAKESALMAfkvavgKWDRDplqhsckAYCtarQELAVLLTLK 1790
Cdd:cd14064     1 IGSGSFGKVYKGRC--RN----KIVAIK---------RYRANTYCS------KSDVD-------MFC---REVSILCRLN 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICI---KPLALVLELAPLGGLDALLRHYRRSgahMGPHTFQTLVLQAARAIEYLHR--RRIIYRDLKSENV 1865
Cdd:cd14064    50 HPCVIQFVGACLddpSQFAIVTQYVSGGSLFSLLHEQKRV---IDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWElpqphteDSprnlvHIKIADYGISR---QTAPSGAKGFGGTEGFMAPEIIRYNGEeeYTEKVDCFSFGMFIYENIS 1942
Cdd:cd14064   127 LLYE-------DG-----HAVVADFGESRflqSLDEDNMTKQPGNLRWMAPEVFTQCTR--YSIKADVFSYALCLWELLT 192
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1943 LRQPFeGH----ESIKECILEGSRPALTqreTQFPTCCLDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd14064   193 GEIPF-AHlkpaAAAADMAYHHIRPPIG---YSIPKPISSLLMRGWNAEPESRPSFVEIVALLEP 253
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
1700-2003 5.21e-21

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: 95.13  E-value: 5.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCKVRGaRSFKPVAMKMLQPvppgarakesalmafkvavgkwdrdplQHSCKAYCTA 1779
Cdd:cd05033     1 IDASYVTIEKVIGGGEFGEVCSGSLKLPG-KKEIDVAIKTLKS---------------------------GYSDKQRLDF 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHyrrsgaHMGPHTFQTLV--LQA-ARAIEYLHRRR 1854
Cdd:cd05033    53 LTEASIMGQFDHPNVIRLEGVVTKsrPVMIVTEYMENGSLDKFLRE------NDGKFTVTQLVgmLRGiASGMKYLSEMN 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphtedsPRNLVhIKIADYGISRQTAPSgaKGFGGTEG------FMAPEIIRYngeEEYTEKV 1928
Cdd:cd05033   127 YVHRDLAARNILV-----------NSDLV-CKVSDFGLSRRLEDS--EATYTTKGgkipirWTAPEAIAY---RKFTSAS 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1929 DCFSFGMFIYENISL-RQPFE---GHESIKEcILEGSR-PAltqrETQFPTCCLDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05033   190 DVWSFGIVMWEVMSYgERPYWdmsNQDVIKA-VEDGYRlPP----PMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLDK 264
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1700-2004 5.53e-21

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: 94.72  E-value: 5.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANckVRGarsfKPVAMKMLQPVppgARAKESALmafkvavgkwdrdplqhsckaycta 1779
Cdd:cd05039     3 INKKDLKLGELIGKGEFGDVMLGD--YRG----QKVAVKCLKDD---STAAQAFL------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 rQELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd05039    49 -AEASVMTTLRHPNLVQLLGVVLegNGLYIVTEYMAKGSLVDYLR--SRGRAVITRKDQLGFALDVCEGMEYLESKKFVH 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVWElpqphtedsprNLVhIKIADYGISRqtapsgaKGFGGTEG------FMAPEIIRYNgeeEYTEKVDCF 1931
Cdd:cd05039   126 RDLAARNVLVSE-----------DNV-AKVSDFGLAK-------EASSNQDGgklpikWTAPEALREK---KFSTKSDVW 183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1932 SFGMFIYENISL-RQPF--EGHESIKECILEGSRpaltqreTQFPTCC----LDLMVLCWHEQPRRRPTASQIVSILSAP 2004
Cdd:cd05039   184 SFGILLWEIYSFgRVPYprIPLKDVVPHVEKGYR-------MEAPEGCppevYKVMKNCWELDPAKRPTFKQLREKLEHI 256
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
1710-1998 6.81e-21

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: 94.85  E-value: 6.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAnCKVRGARSFkpvAMKMLqpvppgarakesalMAFKVAVGKWDRDPLQhsckayctarQELAVLLTL 1789
Cdd:cd14098     7 RLGSGTFAEVKKA-VEVETGKMR---AIKQI--------------VKRKVAGNDKNLQLFQ----------REINILKSL 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP--LALVLELAPLGGL-DALLRHyrrsGAhMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14098    59 EHPGIVRLIDWYEDDqhIYLVMEYVEGGDLmDFIMAW----GA-IPEQHARELTKQILEAMAYTHSMGITHRDLKPENIL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphTEDSPrnlVHIKIADYGISR-QTAPSGAKGFGGTEGFMAPEIIR---YNGEEEYTEKVDCFSFGMFIYENIS 1942
Cdd:cd14098   134 I-------TQDDP---VIVKISDFGLAKvIHTGTFLVTFCGTMAYLAPEILMskeQNLQGGYSNLVDMWSVGCLVYVMLT 203
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1943 LRQPFEG--HESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14098   204 GALPFDGssQLPVEKRIRKGRYTQPPLVDFNISEEAIDFILRLLDVDPEKRMTAAQAL 261
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1711-1960 7.34e-21

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: 95.58  E-value: 7.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckVRGARSFKPVAMKMLQpvppgaRAKESAlmafkvavgkwdrDPLQHSCKAycTARQELAVLLTLK 1790
Cdd:cd14096     9 IGEGAFSNVYKA---VPLRNTGKPVAIKVVR------KADLSS-------------DNLKGSSRA--NILKEVQIMKRLS 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPLGGL-----------DALLRHyrrsgahmgphtfqtLVLQAARAIEYLHRRRIIY 1857
Cdd:cd14096    65 HPNIVKLLDFQESDeyYYIVLELADGGEIfhqivrltyfsEDLSRH---------------VITQVASAVKYLHEIGVVH 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVWELP-------QPHTEDSPRNLVH--------------IKIADYGISRQTAPSGAKGFGGTEGFMAPEII 1916
Cdd:cd14096   130 RDIKPENLLFEPIPfipsivkLRKADDDETKVDEgefipgvggggigiVKLADFGLSKQVWDSNTKTPCGTVGYTAPEVV 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 442620116 1917 RyngEEEYTEKVDCFSFGMFIYENISLRQPF--EGHESIKECILEG 1960
Cdd:cd14096   210 K---DERYSKKVDMWALGCVLYTLLCGFPPFydESIETLTEKISRG 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
1781-1997 7.89e-21

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: 94.72  E-value: 7.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALlrhYRRSGAhMGPHTFQTLVLQAARAIEYLH-RRRIIY 1857
Cdd:cd06605    48 RELDVLHKCNSPYIVGFYGAFYSegDISICMEYMDGGSLDKI---LKEVGR-IPERILGKIAVAVVKGLIYLHeKHKIIH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFI 1937
Cdd:cd06605   124 RDVKPSNILVNSRGQ------------VKLCDFGVSGQLVDSLAKTFVGTRSYMAPERISGGK---YTVKSDIWSLGLSL 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1938 YENISLRQPF-----EGHESIKE---CILEGSRPALTQREtqFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd06605   189 VELATGRFPYpppnaKPSMMIFEllsYIVDEPPPLLPSGK--FSPDFQDFVSQCLQKDPTERPSYKEL 254
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
1782-1996 8.13e-21

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: 94.68  E-value: 8.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRHYRRSGAHMgphtFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd06626    49 EMKVLEGLDHPNLVRYYGVEVhrEEVYIFMEYCQEGTLEELLRHGRILDEAV----IRVYTLQLLEGLAYLHENGIVHRD 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphteDSpRNLvhIKIADYG----ISRQTAPSG---AKGFGGTEGFMAPEIIRYNGEEEYTEKVDCFS 1932
Cdd:cd06626   125 IKPANIFL---------DS-NGL--IKLGDFGsavkLKNNTTTMApgeVNSLVGTPAYMAPEVITGNKGEGHGRAADIWS 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1933 FGMFIYENISLRQP---FEGHESIKECILEGSRPALTQREtQFPTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd06626   193 LGCVVLEMATGKRPwseLDNEWAIMYHVGMGHKPPIPDSL-QLSPEGKDFLSRCLESDPKKRPTASE 258
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
1711-1947 1.60e-20

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 94.09  E-value: 1.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvppgarakesalmafkvavgKWDRD----PlqhsckayCTARQELAVL 1786
Cdd:cd07829     7 LGEGTYGVVYKAKDKKTG----EIVALKKI----------------------RLDNEeegiP--------STALREISLL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPL--VGICIKPLALVLELaplggLDALLRHY-RRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd07829    53 KELKHPNIVKLldVIHTENKLYLVFEY-----CDQDLKKYlDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphtedSPRNLvhIKIADYGISRQ-TAPSGAKgfggTEGFM-----APEIIRynGEEEYTEKVDCFSFGMFI 1937
Cdd:cd07829   128 NLLI----------NRDGV--LKLADFGLARAfGIPLRTY----THEVVtlwyrAPEILL--GSKHYSTAVDIWSVGCIF 189
                         250
                  ....*....|
gi 442620116 1938 YENIsLRQPF 1947
Cdd:cd07829   190 AELI-TGKPL 198
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
1706-1947 1.64e-20

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 93.75  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1706 IKGSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPVPPGARA---KESALMAFKvavgkwdrdplqhsckayctarQE 1782
Cdd:cd06628     3 IKGALIGSGSFGSVYLG----MNASSGELMAVKQVELPSVSAENkdrKKSMLDALQ----------------------RE 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1783 LAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYrrsGAHMGPhTFQTLVLQAARAIEYLHRRRIIYRDL 1860
Cdd:cd06628    57 IALLRELQHENIVQYLGSSSDAnhLNIFLEYVPGGSVATLLNNY---GAFEES-LVRNFVRQILKGLNYLHNRGIIHRDI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1861 KSENVLVwelpqphtedspRNLVHIKIADYGISRQ-------TAPSGAK-GFGGTEGFMAPEIIRyngEEEYTEKVDCFS 1932
Cdd:cd06628   133 KGANILV------------DNKGGIKISDFGISKKleanslsTKNNGARpSLQGSVFWMAPEVVK---QTSYTRKADIWS 197
                         250
                  ....*....|....*
gi 442620116 1933 FGMFIYENISLRQPF 1947
Cdd:cd06628   198 LGCLVVEMLTGTHPF 212
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
1711-1996 1.87e-20

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: 93.10  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLqPVPPGARAkesalmafkvavgkwdrdplqhsckaycTARQELAVLLTLK 1790
Cdd:cd14006     1 LGRGRFGVVKRCIEKATG----REFAAKFI-PKRDKKKE----------------------------AVLREISILNQLQ 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLALVLELAPLGG---LDALLRHYRRSGAHMgphtfQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd14006    48 HPRIIQLHEAYESPTELVLILELCSGgelLDRLAERGSLSEEEV-----RTYMRQLLEGLQYLHNHHILHLDLKPENILL 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 WELPQPhtedsprnlvHIKIADYGISRQTAPSGAKG-FGGTEGFMAPEIIRYNGEEEYTekvDCFSFGMFIYENISLRQP 1946
Cdd:cd14006   123 ADRPSP----------QIKIIDFGLARKLNPGEELKeIFGTPEFVAPEIVNGEPVSLAT---DMWSIGVLTYVLLSGLSP 189
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1947 FEGH------ESIKECILEGSRPA---LTQRETQFptccldLM-VLCwhEQPRRRPTASQ 1996
Cdd:cd14006   190 FLGEddqetlANISACRVDFSEEYfssVSQEAKDF------IRkLLV--KEPRKRPTAQE 241
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
1710-2001 1.89e-20

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: 93.64  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFK-ANCKVRGARSFK-PVAMKMLQPvppGARAKESALMAfkvavgkwdrdplqhsckayctarQELAVLL 1787
Cdd:cd05044     2 FLGSGAFGEVFEgTAKDILGDGSGEtKVAVKTLRK---GATDQEKAEFL------------------------KEAHLMS 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLV---LQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd05044    55 NFKHPNILKLLGVCLdnDPQYIILELMEGGDLLSYLRAARPTAFTPPLLTLKDLLsicVDVAKGCVYLEDMHFVHRDLAA 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphTEDSPRNLVhIKIADYGISRQTAPSGAKGFGGtEG-----FMAPEIIRyngEEEYTEKVDCFSFGMFI 1937
Cdd:cd05044   135 RNCLV-------SSKDYRERV-VKIGDFGLARDIYKNDYYRKEG-EGllpvrWMAPESLV---DGVFTTQSDVWAFGVLM 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1938 YENISL-RQPFEGHESIK--ECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05044   203 WEILTLgQQPYPARNNLEvlHFVRAGGR---LDQPDNCPDDLYELMLRCWSTDPEERPSFARILEQL 266
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1710-1938 2.01e-20

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 93.21  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVPpgARAKESALmafkvavgkwdrdplqhsckayctaRQELAVLLTL 1789
Cdd:cd14083    10 VLGTGAFSEVVLAEDKATG----KLVAIKCIDKKA--LKGKEDSL-------------------------ENEIAVLRKI 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP--LALVLELAPLGGL-DALLRHyrrsgahmGPHTFQ---TLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14083    59 KHPNIVQLLDIYESKshLYLVMELVTGGELfDRIVEK--------GSYTEKdasHLIRQVLEAVDYLHSLGIVHRDLKPE 130
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1864 NVLVWElpqpHTEDSPrnlvhIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIY 1938
Cdd:cd14083   131 NLLYYS----PDEDSK-----IMISDFGLSKMEDSGVMSTACGTPGYVAPEVLA---QKPYGKAVDCWSIGVISY 193
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
1705-1999 2.92e-20

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: 93.22  E-value: 2.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1705 IIKGSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLQpVPPGARAKESALMAFKVAVGKWDRDPLQHsckayctarqela 1784
Cdd:cd06629     3 WVKGELIGKGTYGRVYLA----MNATTGEMLAVKQVE-LPKTSSDRADSRQKTVVDALKSEIDTLKD------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 vlltLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPH-TFQTLvlqaaRAIEYLHRRRIIYRDLK 1861
Cdd:cd06629    65 ----LDHPNIVQYLGFEETEdyFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFfTRQIL-----DGLAYLHSKGILHRDLK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphteDSPRNlvhIKIADYGISRQTA----PSGAKGFGGTEGFMAPEIIRYNGeEEYTEKVDCFSFGMFI 1937
Cdd:cd06629   136 ADNILV---------DLEGI---CKISDFGISKKSDdiygNNGATSMQGSVFWMAPEVIHSQG-QGYSAKVDIWSLGCVV 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1938 YENISLRQPFEGHESIKECILEG---SRPALTQrETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd06629   203 LEMLAGRRPWSDDEAIAAMFKLGnkrSAPPVPE-DVNLSPEALDFLNACFAIDPRDRPTAAELLS 266
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
1781-1998 3.03e-20

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: 93.66  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP---LALVLELAPLGGLDALLRHYrrsgahmGPhtFQTLVL-QAARAI----EYLHR 1852
Cdd:cd06620    52 RELQILHECHSPYIVSFYGAFLNEnnnIIICMEYMDCGSLDKILKKK-------GP--FPEEVLgKIAVAVleglTYLYN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 R-RIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCF 1931
Cdd:cd06620   123 VhRIIHRDIKPSNILV------------NSKGQIKLCDFGVSGELINSIADTFVGTSTYMSPERIQGGK---YSVKSDVW 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1932 SFGMFIYENISLRQPFEGHE----------SIKE---CILEGSRPALTQrETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06620   188 SLGLSIIELALGEFPFAGSNddddgyngpmGILDllqRIVNEPPPRLPK-DRIFPKDLRDFVDRCLLKDPRERPSPQLLL 266
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
1781-2005 4.61e-20

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: 92.56  E-value: 4.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALLrhyrRSGAHMGPHTFQtLVLQAARAIEYLHRRR--IIYR 1858
Cdd:cd14025    44 EEAKKMEMAKFRHILPVYGICSEPVGLVMEYMETGSLEKLL----ASEPLPWELRFR-IIHETAVGMNFLHCMKppLLHL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphteDSPrnlVHIKIADYGISRQTAPSGAK-----GFGGTEGFMAPEIIRYNGEEEYTeKVDCFSF 1933
Cdd:cd14025   119 DLKPANILL---------DAH---YHVKISDFGLAKWNGLSHSHdlsrdGLRGTIAYLPPERFKEKNRCPDT-KHDVYSF 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1934 GMFIYENISLRQPFEGHESIKECILE---GSRPALTQRETQFPTCC---LDLMVLCWHEQPRRRPTASQIVS----ILSA 2003
Cdd:cd14025   186 AIVIWGILTQKKPFAGENNILHIMVKvvkGHRPSLSPIPRQRPSECqqmICLMKRCWDQDPRKRPTFQDITSetenLLSL 265

                  ..
gi 442620116 2004 PE 2005
Cdd:cd14025   266 LE 267
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
1781-1997 6.97e-20

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: 91.71  E-value: 6.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd05052    51 KEAAVMKEIKHPNLVQLLGVCTRepPFYIITEFMPYGNLLDYLR--ECNREELNAVVLLYMATQIASAMEYLEKKNFIHR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphtedSPRNLVhiKIADYGISR------QTAPSGAKgfggtegF----MAPEIIRYNgeeEYTEKV 1928
Cdd:cd05052   129 DLAARNCLV----------GENHLV--KVADFGLSRlmtgdtYTAHAGAK-------FpikwTAPESLAYN---KFSIKS 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1929 DCFSFGMFIYENISL-RQPFEGHE--SIKECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd05052   187 DVWAFGVLLWEIATYgMSPYPGIDlsQVYELLEKGYR---MERPEGCPPKVYELMRACWQWNPSDRPSFAEI 255
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
1781-2001 7.36e-20

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: 91.85  E-value: 7.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd05114    48 EEAKVMMKLTHPKLVQLYGVCTqqKPIYIVTEFMENG---CLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELpqpHTedsprnlvhIKIADYGISR------QTAPSGAKgfgGTEGFMAPEIIRYNgeeEYTEKVDCFS 1932
Cdd:cd05114   125 DLAARNCLVNDT---GV---------VKVSDFGMTRyvlddqYTSSSGAK---FPVKWSPPEVFNYS---KFSSKSDVWS 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1933 FGMFIYENISL-RQPFEGHESIK--ECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05114   187 FGVLMWEVFTEgKMPFESKSNYEvvEMVSRGHR---LYRPKLASKSVYEVMYSCWHEKPEGRPTFADLLRTI 255
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
1781-2002 9.46e-20

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: 91.74  E-value: 9.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICI----KPLALvLELAPLGGLDALLRHYRRSGAHmGPHTFQT-----LVLQAARAIEYLH 1851
Cdd:cd05043    56 QESSLLYGLSHQNLLPILHVCIedgeKPMVL-YPYMNWGNLKLFLQQCRLSEAN-NPQALSTqqlvhMALQIACGMSYLH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAKGFGGTEG----FMAPEIIRyngEEEYTEK 1927
Cdd:cd05043   134 RRGVIHKDIAARNCVIDDELQ------------VKITDNALSRDLFPMDYHCLGDNENrpikWMSLESLV---NKEYSSA 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1928 VDCFSFGMFIYENISLRQ-------PFEghesIKECILEGSRpaLTQretqfPTCCLD----LMVLCWHEQPRRRPTASQ 1996
Cdd:cd05043   199 SDVWSFGVLLWELMTLGQtpyveidPFE----MAAYLKDGYR--LAQ-----PINCPDelfaVMACCWALDPEERPSFQQ 267

                  ....*.
gi 442620116 1997 IVSILS 2002
Cdd:cd05043   268 LVQCLT 273
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
1708-1996 1.13e-19

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: 91.13  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLqpvppgarakesalmafkvavgKWDRDPLQhsckAYCTARQELAVLL 1787
Cdd:cd06627     5 GDLIGRGAFGSVYKG----LNLNTGEFVAIKQI----------------------SLEKIPKS----DLKSVMGEIDLLK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGiCIKP---LALVLELAPLGGLDALLRHYRRSGAHM-GPHTFQTLvlqaaRAIEYLHRRRIIYRDLKSE 1863
Cdd:cd06627    55 KLNHPNIVKYIG-SVKTkdsLYIILEYVENGSLASIIKKFGKFPESLvAVYIYQVL-----EGLAYLHEQGVIHRDIKGA 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAKGFG--GTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENI 1941
Cdd:cd06627   129 NILT-------TKDG-----LVKLADFGVATKLNEVEKDENSvvGTPYWMAPEVIEMSG---VTTASDIWSVGCTVIELL 193
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1942 SLRQPFegHE----SIKECILEGSRPALTQRETQfptCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd06627   194 TGNPPY--YDlqpmAALFRIVQDDHPPLPENISP---ELRDFLLQCFQKDPTLRPSAKE 247
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
1781-1999 1.46e-19

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 90.69  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPL---VGICIKPLALVLELAPLGGLDALLRHYRRSGAHMgphtfQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd14164    49 RELSILRRVNHPNIVQMfecIEVANGRLYIVMEAAATDLLQKIQEVHHIPKDLA-----RDMFAQMVGAVNYLHDMNIVH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphTEDSPRnlvhIKIADYGISRQTA--PSGAKGFGGTEGFMAPEIIryNGEEEYTEKVDCFSFGM 1935
Cdd:cd14164   124 RDLKCENILL-------SADDRK----IKIADFGFARFVEdyPELSTTFCGSRAYTPPEVI--LGTPYDPKKYDVWSLGV 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1936 FIYENISLRQPFegHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14164   191 VLYVMVTGTMPF--DETNVRRLRLQQRGVLYPSGVALEEPCRALIRTLLQFNPSTRPSIQQVAG 252
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
1710-2002 1.53e-19

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: 91.67  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPVPpgarakesalmafkvavgkwdrdplqhSCKAYCTARQELAVLLTL 1789
Cdd:cd05110    14 VLGSGAFGTVYKGIWVPEGETVKIPVAIKILNETT---------------------------GPKANVEFMDEALIMASM 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP-LALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd05110    67 DHPHLVRLLGVCLSPtIQLVTQLMPHG---CLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLV- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphteDSPRnlvHIKIADYGISR----QTAPSGAKGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYENISL- 1943
Cdd:cd05110   143 --------KSPN---HVKITDFGLARllegDEKEYNADGGKMPIKWMALECIHY---RKFTHQSDVWSYGVTIWELMTFg 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1944 RQPFEG--HESIKECILEGsrpaltQRETQFPTCCLD---LMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05110   209 GKPYDGipTREIPDLLEKG------ERLPQPPICTIDvymVMVKCWMIDADSRPKFKELAAEFS 266
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
1781-2002 1.58e-19

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: 90.78  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd05112    48 EEAEVMMKLSHPKLVQLYGVCLEqaPICLVFEFMEHGCLSDYLRTQRGL---FSAETLLGMCLDVCEGMAYLEEASVIHR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFGGTE---GFMAPEIIRYNgeeEYTEKVDCFSFGM 1935
Cdd:cd05112   125 DLAARNCLVGE-----------NQV-VKVSDFGMTRFVLDDQYTSSTGTKfpvKWSSPEVFSFS---RYSSKSDVWSFGV 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1936 FIYENISL-RQPFEGHES--IKECILEGSR---PALTqretqfPTCCLDLMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05112   190 LMWEVFSEgKIPYENRSNseVVEDINAGFRlykPRLA------STHVYEIMNHCWKERPEDRPSFSLLLRQLA 256
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
1708-1960 1.62e-19

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: 90.69  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGARSfkpvAMKMLQpvppgaraKESAlmafkvavGKWDRDPLQHsckayctarqELAVLL 1787
Cdd:cd14097     6 GRKLGQGSFGVVIEATHKETQTKW----AIKKIN--------REKA--------GSSAVKLLER----------EVDILK 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPL--VGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLvlqaARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14097    56 HVNHAHIIHLeeVFETPKRMYLVMELCEDGELKELLLRKGFFSENETRHIIQSL----ASAVAYLHKNDIVHRDLKLENI 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWELPqphteDSPRNLVHIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENIS 1942
Cdd:cd14097   132 LVKSSI-----IDNNDKLNIKVTDFGLSVQKYGLGEDMLQetcGTPIYMAPEVISAHG---YSQQCDIWSIGVIMYMLLC 203
                         250       260
                  ....*....|....*....|
gi 442620116 1943 LRQPFEG--HESIKECILEG 1960
Cdd:cd14097   204 GEPPFVAksEEKLFEEIRKG 223
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
1711-1997 1.80e-19

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: 90.88  E-value: 1.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKvrgaRSFKPVAMKML-------------QPVPPGARAKESALmafkvavgkwdRDPLQhscKAYc 1777
Cdd:cd14118     2 IGKGSYGIVKLAYNE----EDNTLYAMKILskkkllkqagffrRPPPRRKPGALGKP-----------LDPLD---RVY- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 tarQELAVLLTLKHPNIVPLVGICIKP----LALVLELAPLGGL----------DALLRHYrrsgahmgphtFQTLVLqa 1843
Cdd:cd14118    63 ---REIAILKKLDHPNVVKLVEVLDDPnednLYMVFELVDKGAVmevptdnplsEETARSY-----------FRDIVL-- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1844 arAIEYLHRRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRYNGE 1921
Cdd:cd14118   127 --GIEYLHYQKIIHRDIKPSNLLL-------GDDG-----HVKIADFGVSNEFEGDDALlsSTAGTPAFMAPEALSESRK 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1922 EEYTEKVDCFSFGMFIYENISLRQPFEG------HESIKecilegsrpaltQRETQFPTCCL------DLMVLCWHEQPR 1989
Cdd:cd14118   193 KFSGKALDIWAMGVTLYCFVFGRCPFEDdhilglHEKIK------------TDPVVFPDDPVvseqlkDLILRMLDKNPS 260

                  ....*...
gi 442620116 1990 RRPTASQI 1997
Cdd:cd14118   261 ERITLPEI 268
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
1711-1997 1.81e-19

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: 91.24  E-value: 1.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFV--FKANC---KVRGARSFKP-------VAMKMLQPvppgaRAKESALMAFkvavgkwdrdplqhsckayct 1778
Cdd:cd05051    13 LGEGQFGEVhlCEANGlsdLTSDDFIGNDnkdepvlVAVKMLRP-----DASKNAREDF--------------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 aRQELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRHY-------RRSGAHMGPhtFQTLV---LQAARA 1846
Cdd:cd05051    67 -LKEVKIMSQLKDPNIVRLLGVCTrdEPLCMIVEYMENGDLNQFLQKHeaetqgaSATNSKTLS--YGTLLymaTQIASG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHRRRIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRqTAPSGakGFGGTEG-------FMAPEIIRYn 1919
Cdd:cd05051   144 MKYLESLNFVHRDLATRNCLV------------GPNYTIKIADFGMSR-NLYSG--DYYRIEGravlpirWMAWESILL- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 geEEYTEKVDCFSFGMFIYENISL--RQPFEgH-------ESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRR 1990
Cdd:cd05051   208 --GKFTTKSDVWAFGVTLWEILTLckEQPYE-HltdeqviENAGEFFRDDGMEVYLSRPPNCPKEIYELMLECWRRDEED 284

                  ....*..
gi 442620116 1991 RPTASQI 1997
Cdd:cd05051   285 RPTFREI 291
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
1707-2002 1.82e-19

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: 90.85  E-value: 1.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPvppgarakesalmafkvavgkwdrdplQHSCKAYCTARQELAVL 1786
Cdd:cd05109    11 KVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRE---------------------------NTSPKANKEILDEAYVM 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICI-KPLALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd05109    64 AGVGSPYVCRLLGICLtSTVQLVTQLMPYG---CLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphtedspRNLVHIKIADYGISR----QTAPSGAKGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYENI 1941
Cdd:cd05109   141 LV------------KSPNHVKITDFGLARlldiDETEYHADGGKVPIKWMALESILH---RRFTHQSDVWSYGVTVWELM 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1942 SL-RQPFEGHES--IKECILEGsrpaltQRETQFPTCCLD---LMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05109   206 TFgAKPYDGIPAreIPDLLEKG------ERLPQPPICTIDvymIMVKCWMIDSECRPRFRELVDEFS 266
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
1707-2002 2.11e-19

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: 91.62  E-value: 2.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLqpvppgaraKESAlmafkvavgkwdrdplqhSCKAYCTARQELAVL 1786
Cdd:cd05108    11 KIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKEL---------REAT------------------SPKANKEILDEAYVM 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICI-KPLALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd05108    64 ASVDNPHVCRLLGICLtSTVQLITQLMPFG---CLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwELPQphtedsprnlvHIKIADYGISRQTApSGAKGFGGTEG-----FMAPEIIRYngeEEYTEKVDCFSFGMFIYEN 1940
Cdd:cd05108   141 LV-KTPQ-----------HVKITDFGLAKLLG-AEEKEYHAEGGkvpikWMALESILH---RIYTHQSDVWSYGVTVWEL 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1941 ISL-RQPFEGHESIK-ECILEGSrpaltQRETQFPTCCLD---LMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05108   205 MTFgSKPYDGIPASEiSSILEKG-----ERLPQPPICTIDvymIMVKCWMIDADSRPKFRELIIEFS 266
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
1696-1999 2.20e-19

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: 90.51  E-value: 2.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1696 DKHTIPSECIIKGSLLGRGAFGFVFKAncKVRGarsfkPVAMKMLQPVPPGARAkesaLMAFKvavgkwdrdplqhscka 1775
Cdd:cd14151     1 DDWEIPDGQITVGQRIGSGSFGTVYKG--KWHG-----DVAVKMLNVTAPTPQQ----LQAFK----------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1776 yctarQELAVLLTLKHPNIVPLVGICIKP-LALVLELAPLgglDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRR 1854
Cdd:cd14151    53 -----NEVGVLRKTRHVNILLFMGYSTKPqLAIVTQWCEG---SSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKS 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGI----SRQTAPSGAKGFGGTEGFMAPEIIRYNGEEEYTEKVDC 1930
Cdd:cd14151   125 IIHRDLKSNNIFL------HEDLT------VKIGDFGLatvkSRWSGSHQFEQLSGSILWMAPEVIRMQDKNPYSFQSDV 192
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1931 FSFGMFIYENISLRQPFE---GHESIKECILEGS-RPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14151   193 YAFGIVLYELMTGQLPYSninNRDQIIFMVGRGYlSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILA 265
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
1700-2001 2.37e-19

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: 91.96  E-value: 2.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANC-KVRGARSFKPVAMKMLQPvppGARAKE-SALMAfkvavgkwdrdplqhsckayc 1777
Cdd:cd05102     4 FPRDRLRLGKVLGHGAFGKVVEASAfGIDKSSSCETVAVKMLKE---GATASEhKALMS--------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 tarqELAVLLTL-KHPNIVPLVGICIK---PLALVLELAPLGGLDALLRHYR---------------------------- 1825
Cdd:cd05102    60 ----ELKILIHIgNHLNVVNLLGACTKpngPLMVIVEFCKYGNLSNFLRAKRegfspyrersprtrsqvrsmveavradr 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1826 --RSGAHMG-----------------------PHTFQTLV---LQAARAIEYLHRRRIIYRDLKSENVLVwelpqphted 1877
Cdd:cd05102   136 rsRQGSDRVasftestsstnqprqevddlwqsPLTMEDLIcysFQVARGMEFLASRKCIHRDLAARNILL---------- 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1878 SPRNLVhiKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISL-RQPFEG--- 1949
Cdd:cd05102   206 SENNVV--KICDFGLARDIYKDPDYVRKGSArlplKWMAPESIF---DKVYTTQSDVWSFGVLLWEIFSLgASPYPGvqi 280
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1950 HESIKECILEGSR---PALTQRETQfptcclDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05102   281 NEEFCQRLKDGTRmraPEYATPEIY------RIMLSCWHGDPKERPTFSDLVEIL 329
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
1707-2001 2.75e-19

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: 90.10  E-value: 2.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKAnckvrgaRSFKPVAMKMLQPvppgARAKESALMAFKVAVgkwdrdplqhscKAYCTARqelavl 1786
Cdd:cd14063     4 IKEVIGKGRFGRVHRG-------RWHGDVAIKLLNI----DYLNEEQLEAFKEEV------------AAYKNTR------ 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 ltlkHPNIVPLVGICIKP--LALVLELAPLGGLDALLrHYRRSGAHMGpHTFQtLVLQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd14063    55 ----HDNLVLFMGACMDPphLAIVTSLCKGRTLYSLI-HERKEKFDFN-KTVQ-IAQQICQGMGYLHAKGIIHKDLKSKN 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphteDSPRnlvhIKIADYGISRQTAPSGAKGFGGTEG-------FMAPEIIR-------YNGEEEYTEKVDC 1930
Cdd:cd14063   128 IFL---------ENGR----VVITDFGLFSLSGLLQPGRREDTLVipngwlcYLAPEIIRalspdldFEESLPFTKASDV 194
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1931 FSFGMFIYENISLRQPFEGH--ESIKECILEGSRPALTQreTQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14063   195 YAFGTVWYELLAGRWPFKEQpaESIIWQVGCGKKQSLSQ--LDIGREVKDILMQCWAYDPEKRPTFSDLLRML 265
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
1711-1992 3.79e-19

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: 89.64  E-value: 3.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRgaRSFKPVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd05116     3 LGSGNFGTVKKGYYQMK--KVVKTVAVKILKNEANDPALKDELL--------------------------REANVMQQLD 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGIC-IKPLALVLELAPLGGLDALLRHYRrsgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLvwe 1869
Cdd:cd05116    55 NPYIVRMIGICeAESWMLVMEMAELGPLNKFLQKNR----HVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVL--- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 LPQPHtedsprnlvHIKIADYGISRQTAPS----GAKGFGG-TEGFMAPEIIRYNgeeEYTEKVDCFSFGMFIYENISLR 1944
Cdd:cd05116   128 LVTQH---------YAKISDFGLSKALRADenyyKAQTHGKwPVKWYAPECMNYY---KFSSKSDVWSFGVLMWEAFSYG 195
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1945 Q-PFEGHE--SIKECILEGSRPALTQRetqFPTCCLDLMVLCWHEQPRRRP 1992
Cdd:cd05116   196 QkPYKGMKgnEVTQMIEKGERMECPAG---CPPEMYDLMKLCWTYDVDERP 243
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
1701-2001 4.94e-19

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: 90.24  E-value: 4.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECIIKGSLLGRGAFGFVFKANCK--VRGARSFKpVAMKMLQPVppgARAKES-ALMAfkvavgkwdrdplqhsckayc 1777
Cdd:cd05055    33 PRNNLSFGKTLGAGAFGKVVEATAYglSKSDAVMK-VAVKMLKPT---AHSSEReALMS--------------------- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 tarqELAVLLTL-KHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAhmgphTFQTLV---LQAARAIEYLH 1851
Cdd:cd05055    88 ----ELKIMSHLgNHENIVNLLGACTIggPILVITEYCCYGDLLNFLRRKRESFL-----TLEDLLsfsYQVAKGMAFLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLvweLPQPHTedsprnlvhIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYNgeeEYTEK 1927
Cdd:cd05055   159 SKNCIHRDLAARNVL---LTHGKI---------VKICDFGLARDIMNDSNYVVKGNArlpvKWMAPESIFNC---VYTFE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1928 VDCFSFGMFIYENISL-RQPFEG---HESIKECILEGSR---PALTQRETqfptccLDLMVLCWHEQPRRRPTASQIVSI 2000
Cdd:cd05055   224 SDVWSYGILLWEIFSLgSNPYPGmpvDSKFYKLIKEGYRmaqPEHAPAEI------YDIMKTCWDADPLKRPTFKQIVQL 297

                  .
gi 442620116 2001 L 2001
Cdd:cd05055   298 I 298
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
1711-1939 5.70e-19

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: 88.81  E-value: 5.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKmlqpvppgarakesalmafKVAVGKWDRDPLqhsckayctaRQELAVLLTLK 1790
Cdd:cd06614     8 IGEGASGEVYKATDRATG----KEVAIK-------------------KMRLRKQNKELI----------INEILIMKECK 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVG--ICIKPLALVLELAPLGGLDALLRHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd06614    55 HPNIVDYYDsyLVGDELWVVMEYMDGGSLTDIITQNPVR---MNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILL- 130
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1869 elpqphTEDSprnlvHIKIADYGISRQ--TAPSGAKGFGGTEGFMAPEIIRYNgeeEYTEKVDCFSFGMFIYE 1939
Cdd:cd06614   131 ------SKDG-----SVKLADFGFAAQltKEKSKRNSVVGTPYWMAPEVIKRK---DYGPKVDIWSLGIMCIE 189
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
1706-1999 8.67e-19

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: 88.64  E-value: 8.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1706 IKGSLLGRGAFGFVFKANckvrgarsfkpvamkmlqpvppgaRAKESALMAFKVAvgKWDRDPLQHSCKAYCTARQELAV 1785
Cdd:cd06630     3 LKGPLLGTGAFSSCYQAR------------------------DVKTGTLMAVKQV--SFCRNSSSEQEEVVEAIREEIRM 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYrrsgahmGPHTFQTLV---LQAARAIEYLHRRRIIYRDL 1860
Cdd:cd06630    57 MARLNHPNIVRMLGATQHKshFNIFVEWMAGGSVASLLSKY-------GAFSENVIInytLQILRGLAYLHDNQIIHRDL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1861 KSENVLVwelpqphteDSPRNlvHIKIADYGISRQTAP--SGAKGFG----GTEGFMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd06630   130 KGANLLV---------DSTGQ--RLRIADFGAAARLASkgTGAGEFQgqllGTIAFMAPEVLR---GEQYGRSCDVWSVG 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1935 MFIYENISLRQPFEGHE------------------SIKECILEGSRpaltqretqfptcclDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd06630   196 CVIIEMATAKPPWNAEKisnhlalifkiasattppPIPEHLSPGLR---------------DVTLRCLELQPEDRPPARE 260

                  ...
gi 442620116 1997 IVS 1999
Cdd:cd06630   261 LLK 263
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1782-1997 8.91e-19

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: 88.75  E-value: 8.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP----LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRR---- 1853
Cdd:cd08217    49 EVNILRELKHPNIVRYYDRIVDRanttLYIVMEYCEGGDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRsvgg 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 -RIIYRDLKSENVLVwelpqphTEDsprnlVHIKIADYGISR--QTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDC 1930
Cdd:cd08217   129 gKILHRDLKPANIFL-------DSD-----NNVKLGDFGLARvlSHDSSFAKTYVGTPYYMSPELLN---EQSYDEKSDI 193
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1931 FSFGMFIYENISLRQPFEG--HESIKECILEGSRPALTQRETQfptcclDLMVL---CWHEQPRRRPTASQI 1997
Cdd:cd08217   194 WSLGCLIYELCALHPPFQAanQLELAKKIKEGKFPRIPSRYSS------ELNEViksMLNVDPDKRPSVEEL 259
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
1711-1955 9.26e-19

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: 88.74  E-value: 9.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVfkanCKVRGARSFKPVAMKMLQPvppgARAKESalmafkvavgkwdrdplqhscKAYCTARQELAVLLTLK 1790
Cdd:cd05577     1 LGRGGFGEV----CACQVKATGKMYACKKLDK----KRIKKK---------------------KGETMALNEKIILEKVS 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLvlQAARAIEYLHRRRIIYRDLKSENVLVW 1868
Cdd:cd05577    52 SPFIVSLAYAFETKdkLCLVLTLMNGGDLKYHIYNVGTRGFSEARAIFYAA--EIICGLEHLHNRFIVYRDLKPENILLD 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 ELPqphtedsprnlvHIKIADYGI----SRQTAPsgaKGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLR 1944
Cdd:cd05577   130 DHG------------HVRISDLGLavefKGGKKI---KGRVGTHGYMAPEVLQ--KEVAYDFSVDWFALGCMLYEMIAGR 192
                         250
                  ....*....|.
gi 442620116 1945 QPFEGHESIKE 1955
Cdd:cd05577   193 SPFRQRKEKVD 203
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
1781-1999 1.02e-18

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: 88.40  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd05113    48 EEAKVMMNLSHEKLVQLYGVCTKqrPIFIITEYMANG---CLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHR 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphtedsPRNLVhIKIADYGISRQ------TAPSGAKgFggTEGFMAPEIIRYNgeeEYTEKVDCFS 1932
Cdd:cd05113   125 DLAARNCLV-----------NDQGV-VKVSDFGLSRYvlddeyTSSVGSK-F--PVRWSPPEVLMYS---KFSSKSDVWA 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1933 FGMFIYENISL-RQPFE--GHESIKECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd05113   187 FGVLMWEVYSLgKMPYErfTNSETVEHVSQGLR---LYRPHLASEKVYTIMYSCWHEKADERPTFKILLS 253
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
1703-1955 1.09e-18

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: 88.91  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1703 ECIIKGSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgarakesalmafkvavgkwdrdpLQHSCKAYCTARQE 1782
Cdd:cd07871     5 ETYVKLDKLGEGTYATVFKGRSKLTE----NLVALKEIR---------------------------LEHEEGAPCTAIRE 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1783 LAVLLTLKHPNIVPLVGI--CIKPLALVLELaplggLDALLRHY-RRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd07871    54 VSLLKNLKHANIVTLHDIihTERCLTLVFEY-----LDSDLKQYlDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRD 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVWELPQphtedsprnlvhIKIADYGISR-QTAPSgaKGFGG---TEGFMAPEIIRynGEEEYTEKVDCFSFGM 1935
Cdd:cd07871   129 LKPQNLLINEKGE------------LKLADFGLARaKSVPT--KTYSNevvTLWYRPPDVLL--GSTEYSTPIDMWGVGC 192
                         250       260
                  ....*....|....*....|
gi 442620116 1936 FIYENISLRQPFEGhESIKE 1955
Cdd:cd07871   193 ILYEMATGRPMFPG-STVKE 211
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
1710-1960 1.12e-18

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: 88.79  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGarsfKPVAMKMLqPVPPGARAKEsalmafkvavgkwdrdpLQHSCKayctarqELAVLLTL 1789
Cdd:cd05580     8 TLGTGSFGRVRLVKHKDSG----KYYALKIL-KKAKIIKLKQ-----------------VEHVLN-------EKRILSEV 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGIC--IKPLALVLELAPLGGLDALLRHYRRsgahmgphtFQTLVLQ--AAR---AIEYLHRRRIIYRDLKS 1862
Cdd:cd05580    59 RHPFIVNLLGSFqdDRNLYMVMEYVPGGELFSLLRRSGR---------FPNDVAKfyAAEvvlALEYLHSLDIVYRDLKP 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSgAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENIS 1942
Cdd:cd05580   130 ENLLL------------DSDGHIKITDFGFAKRVKDR-TYTLCGTPEYLAPEIILSKG---HGKAVDWWALGILIYEMLA 193
                         250       260
                  ....*....|....*....|
gi 442620116 1943 LRQPF--EGHESIKECILEG 1960
Cdd:cd05580   194 GYPPFfdENPMKIYEKILEG 213
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1711-2000 1.14e-18

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 88.93  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGArsfkPVAMKMLQPVppgarakesalmafkvavgkwdrDPLQHSCKAYCTarQELAVLLTLK 1790
Cdd:cd08229    32 IGRGQFSEVYRATCLLDGV----PVALKKVQIF-----------------------DLMDAKARADCI--KEIDLLKQLN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVW 1868
Cdd:cd08229    83 HPNVIKYYASFIEdnELNIVLELADAGDLSRMIKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFIT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 ELPQphtedsprnlvhIKIADYGISR--QTAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd08229   163 ATGV------------VKLGDLGLGRffSSKTTAAHSLVGTPYYMSPERIHENG---YNFKSDIWSLGCLLYEMAALQSP 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1947 FEGHE----SIKECILEGSRPALTQreTQFPTCCLDLMVLCWHEQPRRRPTASQIVSI 2000
Cdd:cd08229   228 FYGDKmnlySLCKKIEQCDYPPLPS--DHYSEELRQLVNMCINPDPEKRPDITYVYDV 283
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
1782-2004 1.18e-18

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: 88.32  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKPLA--LVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRR---RII 1856
Cdd:cd14664    40 EIQTLGMIRHRNIVRLRGYCSNPTTnlLVYEYMPNGSLGELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDcspLII 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVWELPQPHtedsprnlvhikIADYGISRQTAPSGAK---GFGGTEGFMAPEiirYNGEEEYTEKVDCFSF 1933
Cdd:cd14664   120 HRDVKSNNILLDEEFEAH------------VADFGLAKLMDDKDSHvmsSVAGSYGYIAPE---YAYTGKVSEKSDVYSY 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1934 GMFIYENISLRQPFEG-------------HESIKECILE-------GSRPALTQRETQFptcclDLMVLCWHEQPRRRPT 1993
Cdd:cd14664   185 GVVLLELITGKRPFDEaflddgvdivdwvRGLLEEKKVEalvdpdlQGVYKLEEVEQVF-----QVALLCTQSSPMERPT 259
                         250
                  ....*....|.
gi 442620116 1994 ASQIVSILSAP 2004
Cdd:cd14664   260 MREVVRMLEGD 270
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
1711-2003 1.43e-18

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: 88.53  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCkvrgaRSFKPVAMKMLqpvppgarakesalmafkVAVgKWDRDPLQHSCKAYctaRQELAVLLTLK 1790
Cdd:cd05094    13 LGEGAFGKVFLAEC-----YNLSPTKDKML------------------VAV-KTLKDPTLAARKDF---QREAELLTNLQ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLRHY------------RRSGAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd05094    66 HDHIVKFYGVCGDgdPLIMVFEYMKHGDLNKFLRAHgpdamilvdgqpRQAKGELGLSQMLHIATQIASGMVYLASQHFV 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYngeEEYTEKVDCFS 1932
Cdd:cd05094   146 HRDLATRNCLV------------GANLLVKIGDFGMSRDVYSTDYYRVGGHTmlpiRWMPPESIMY---RKFTTESDVWS 210
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1933 FGMFIYENISL-RQPF--EGHESIKECILEG---SRPALTQRETqfptccLDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05094   211 FGVILWEIFTYgKQPWfqLSNTEVIECITQGrvlERPRVCPKEV------YDIMLGCWQREPQQRLNIKEIYKILHA 281
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
1710-2002 1.52e-18

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: 88.17  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGARsfKPVAMKMLQPVPPGARAKESAlmafkvavgkwdrdplqhsckayctarQELAVLLTL 1789
Cdd:cd05047     2 VIGEGNFGQVLKARIKKDGLR--MDAAIKRMKEYASKDDHRDFA---------------------------GELEVLCKL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 -KHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYR------------RSGAHMGPHTFQTLVLQAARAIEYLHRRR 1854
Cdd:cd05047    53 gHHPNIINLLGACEHRgyLYLAIEYAPHGNLLDFLRKSRvletdpafaianSTASTLSSQQLLHFAADVARGMDYLSQKQ 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFGGTE-GFMAPEIIRYNgeeEYTEKVDCFSF 1933
Cdd:cd05047   133 FIHRDLAARNILVGE-----------NYV-AKIADFGLSRGQEVYVKKTMGRLPvRWMAIESLNYS---VYTTNSDVWSY 197
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1934 GMFIYENISLR-QPFEGHE--SIKECILEGSRpaltqreTQFPTCC----LDLMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05047   198 GVLLWEIVSLGgTPYCGMTcaELYEKLPQGYR-------LEKPLNCddevYDLMRQCWREKPYERPSFAQILVSLN 266
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
1781-1960 1.62e-18

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: 87.58  E-value: 1.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGI--CIKPLALVLELAPlGG--LDALLRHYRrsgahMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd14072    48 REVRIMKILNHPNIVKLFEVieTEKTLYLVMEYAS-GGevFDYLVAHGR-----MKEKEARAKFRQIVSAVQYCHQKRIV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISRQTAPsGAK--GFGGTEGFMAPEII---RYNGEEeytekVDCF 1931
Cdd:cd14072   122 HRDLKAENLLL---------DADMN---IKIADFGFSNEFTP-GNKldTFCGSPPYAAPELFqgkKYDGPE-----VDVW 183
                         170       180       190
                  ....*....|....*....|....*....|.
gi 442620116 1932 SFGMFIYENISLRQPFEGH--ESIKECILEG 1960
Cdd:cd14072   184 SLGVILYTLVSGSLPFDGQnlKELRERVLRG 214
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
1700-2001 1.74e-18

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: 88.53  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKAncKVRGARSFKP-----VAMKMLQpvppgARAKESALMAFkvavgkwdrdplqhsck 1774
Cdd:cd05098    10 LPRDRLVLGKPLGEGCFGQVVLA--EAIGLDKDKPnrvtkVAVKMLK-----SDATEKDLSDL----------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1775 aycTARQELAVLLTlKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMGPH---------TFQTLV--- 1840
Cdd:cd05098    66 ---ISEMEMMKMIG-KHKNIINLLGACTQdgPLYVIVEYASKGNLREYLQARRPPGMEYCYNpshnpeeqlSSKDLVsca 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1841 LQAARAIEYLHRRRIIYRDLKSENVLVwelpqphTEDSPrnlvhIKIADYGISRQTAPSG--AKGFGG--TEGFMAPEII 1916
Cdd:cd05098   142 YQVARGMEYLASKKCIHRDLAARNVLV-------TEDNV-----MKIADFGLARDIHHIDyyKKTTNGrlPVKWMAPEAL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1917 RyngEEEYTEKVDCFSFGMFIYENISL-RQPFEG--HESIKECILEGSRpaltqreTQFPTCCLD----LMVLCWHEQPR 1989
Cdd:cd05098   210 F---DRIYTHQSDVWSFGVLLWEIFTLgGSPYPGvpVEELFKLLKEGHR-------MDKPSNCTNelymMMRDCWHAVPS 279
                         330
                  ....*....|..
gi 442620116 1990 RRPTASQIVSIL 2001
Cdd:cd05098   280 QRPTFKQLVEDL 291
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
1707-1999 2.18e-18

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: 87.41  E-value: 2.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQ--PVPPGARAKESALmafkvavgkwdrdplqhsckayctaRQELA 1784
Cdd:cd06625     4 QGKLLGQGAFGQVYLCYDADTG----RELAVKQVEidPINTEASKEVKAL-------------------------ECEIQ 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVGiCI---KPLALVLELAPLGGLDALLRHYrrsGA----HMGPHTFQTLvlqaaRAIEYLHRRRIIY 1857
Cdd:cd06625    55 LLKNLQHERIVQYYG-CLqdeKSLSIFMEYMPGGSVKDEIKAY---GAltenVTRKYTRQIL-----EGLAYLHSNMIVH 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLvwelpqphtEDSPRNlvhIKIADYGISR--QTAPS--GAKGFGGTEGFMAPEIIryNGeEEYTEKVDCFSF 1933
Cdd:cd06625   126 RDIKGANIL---------RDSNGN---VKLGDFGASKrlQTICSstGMKSVTGTPYWMSPEVI--NG-EGYGRKADIWSV 190
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1934 GMFIYENISLRQP---FEGHESIKECILEGSRPALTQRETQfptCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd06625   191 GCTVVEMLTTKPPwaeFEPMAAIFKIATQPTNPQLPPHVSE---DARDFLSLIFVRNKKQRPSAEELLS 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
1711-1997 2.26e-18

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: 87.08  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd08529     8 LGKGSFGVVYKVVRKVDG----RVYALKQIDISRMSRKMREEAI--------------------------DEARVLSKLN 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRrsGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd08529    58 SPYVIKYYDSFVDKgkLNIVMEYAENGDLHSLIKSQR--GRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFL- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphTEDSprnlvHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd08529   135 ------DKGD-----NVKIGDLGVAKILSDTTnfAQTIVGTPYYLSPELCE---DKPYNEKSDVWALGCVLYELCTGKHP 200
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1947 FEG--HESIKECILEGSRPALTQRETQFPTcclDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd08529   201 FEAqnQGALILKIVRGKYPPISASYSQDLS---QLIDSCLTKDYRQRPDTTEL 250
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
1711-1993 2.87e-18

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: 87.67  E-value: 2.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckvRGARSFKPVAMKMLQ-PVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLTL 1789
Cdd:cd14026     5 LSRGAFGTVSRA----RHADWRVTVAIKCLKlDSPVGDSERNCLL--------------------------KEAEILHKA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLvLQAARAIEYLHRRR--IIYRDLKSENV 1865
Cdd:cd14026    55 RFSYILPILGICNEPefLGIVTEYMTNGSLNELLHEKDIYPDVAWPLRLRIL-YEIALGVNYLHNMSppLLHHDLKTQNI 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphtedspRNLVHIKIADYGISR-------QTAPSGAKGFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFGMFIY 1938
Cdd:cd14026   134 LL------------DGEFHVKIADFGLSKwrqlsisQSRSSKSAPEGGTIIYMPPEEYEPSQKRRASVKHDIYSYAIIMW 201
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1939 ENISLRQPFEGHES---IKECILEGSRPALTqrETQFP------TCCLDLMVLCWHEQPRRRPT 1993
Cdd:cd14026   202 EVLSRKIPFEEVTNplqIMYSVSQGHRPDTG--EDSLPvdiphrATLINLIESGWAQNPDERPS 263
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
1709-1997 2.90e-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: 87.06  E-value: 2.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANckvrgarsfkpvamkmlqpvppgaRAKESALMAFKVAvgkwDRDPLQHSCKAycTARQELAVLLT 1788
Cdd:cd08530     6 KKLGKGSYGSVYKVK------------------------RLSDNQVYALKEV----NLGSLSQKERE--DSVNEIRLLAS 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVP-----LVG--ICIkplalVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLK 1861
Cdd:cd08530    56 VNHPNIIRykeafLDGnrLCI-----VMEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLK 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENI 1941
Cdd:cd08530   131 SANILLSAGDL------------VKIGDLGISKVLKKNLAKTQIGTPLYAAPEVWK---GRPYDYKSDIWSLGCLLYEMA 195
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1942 SLRQPFEGH--ESIKECILEGSRPAL----TQRETQFPTCCLDLmvlcwheQPRRRPTASQI 1997
Cdd:cd08530   196 TFRPPFEARtmQELRYKVCRGKFPPIppvySQDLQQIIRSLLQV-------NPKKRPSCDKL 250
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
1709-1996 3.10e-18

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: 87.76  E-value: 3.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLT 1788
Cdd:cd07833     7 GVVGEGAYGVVLKCRNKATG----EIVAIKKFKESEDDEDVKKTAL--------------------------REVKVLRQ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRhyRRSGahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd07833    57 LRHENIVNLKEAFRRKgrLYLVFEYVERTLLELLEA--SPGG--LPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENIL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd07833   133 VSE-----------SGV-LKLCDFGFARALTARPASPLTdyvATRWYRAPELLV--GDTNYGKPVDVWAIGCIMAELLDG 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1944 RQPFEGHES------IKECI----------------LEGSR-PALTQRET---QFPTCC----LDLMVLCWHEQPRRRPT 1993
Cdd:cd07833   199 EPLFPGDSDidqlylIQKCLgplppshqelfssnprFAGVAfPEPSQPESlerRYPGKVsspaLDFLKACLRMDPKERLT 278

                  ...
gi 442620116 1994 ASQ 1996
Cdd:cd07833   279 CDE 281
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
1707-1999 3.59e-18

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: 87.32  E-value: 3.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPvpPGARAKESALMAFKVAVGkwdrdplqhsckayctarqelavl 1786
Cdd:cd05111    11 KLKVLGSGVFGTVHKGIWIPEGDSIKIPVAIKVIQD--RSGRQSFQAVTDHMLAIG------------------------ 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 lTLKHPNIVPLVGICIKP-LALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd05111    65 -SLDHAYIVRLLGICPGAsLQLVTQLLPLG---SLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNV 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphteDSPrnlVHIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYNgeeEYTEKVDCFSFGMFIYENI 1941
Cdd:cd05111   141 LL---------KSP---SQVQVADFGVADLLYPDDKKYFYSEAktpiKWMALESIHFG---KYTHQSDVWSYGVTVWEMM 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1942 SL-RQPFEG---HEsIKECILEGSRPALTQretqfpTCCLD---LMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd05111   206 TFgAEPYAGmrlAE-VPDLLEKGERLAQPQ------ICTIDvymVMVKCWMIDENIRPTFKELAN 263
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
1777-2001 3.68e-18

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: 86.39  E-value: 3.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1777 CTARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRhyrrsgAHMGPHTFQT---LVLQAARAIEYLH 1851
Cdd:cd14065    33 RSFLKEVKLMRRLSHPNILRFIGVCVKDnkLNFITEYVNGGTLEELLK------SMDEQLPWSQrvsLAKDIASGMAYLH 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVWElpqphtEDSPRNLVhikIADYGISRQ----TAPSGAKGFG----GTEGFMAPEIIRyngEEE 1923
Cdd:cd14065   107 SKNIIHRDLNSKNCLVRE------ANRGRNAV---VADFGLAREmpdeKTKKPDRKKRltvvGSPYWMAPEMLR---GES 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1924 YTEKVDCFSFGMFIYENISlRQPFEGHESIKECILEGSRPALTQRETQ-FPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14065   175 YDEKVDVFSFGIVLCEIIG-RVPADPDYLPRTMDFGLDVRAFRTLYVPdCPPSFLPLAIRCCQLDPEKRPSFVELEHHL 252
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
1700-2001 5.33e-18

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: 86.57  E-value: 5.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCKVRGaRSFKPVAMKMLQPvppGARAKESalmafkvavgkwdRDPLQhsckaycta 1779
Cdd:cd05063     2 IHPSHITKQKVIGAGEFGEVFRGILKMPG-RKEVAVAIKTLKP---GYTEKQR-------------QDFLS--------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 rqELAVLLTLKHPNIVPLVGIC--IKPLALVLELAPLGGLDALLRHYrrsGAHMGPHTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd05063    56 --EASIMGQFSHHNIIRLEGVVtkFKPAMIITEYMENGALDKYLRDH---DGEFSSYQLVGMLRGIAAGMKYLSDMNYVH 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphtedspRNLVHIKIADYGISR--QTAPSGAKGFGGTE---GFMAPEIIRYngeEEYTEKVDCFS 1932
Cdd:cd05063   131 RDLAARNILV------------NSNLECKVSDFGLSRvlEDDPEGTYTTSGGKipiRWTAPEAIAY---RKFTSASDVWS 195
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1933 FGMFIYENISL-RQPF---EGHESIKeCILEGSR-PAltqrETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05063   196 FGIVMWEVMSFgERPYwdmSNHEVMK-AINDGFRlPA----PMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLL 264
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
1790-2001 5.94e-18

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: 87.38  E-value: 5.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMG---------PHTFQTLV---LQAARAIEYLHRRRI 1855
Cdd:cd05101    88 KHKNIINLLGACTQdgPLYVIVEYASKGNLREYLRARRPPGMEYSydinrvpeeQMTFKDLVsctYQLARGMEYLASQKC 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphTEDSPrnlvhIKIADYGISRQTapSGAKGFGGTEG------FMAPEIIRyngEEEYTEKVD 1929
Cdd:cd05101   168 IHRDLAARNVLV-------TENNV-----MKIADFGLARDI--NNIDYYKKTTNgrlpvkWMAPEALF---DRVYTHQSD 230
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1930 CFSFGMFIYENISL-RQPFEG--HESIKECILEGSR---PALTQRETQFptccldLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05101   231 VWSFGVLMWEIFTLgGSPYPGipVEELFKLLKEGHRmdkPANCTNELYM------MMRDCWHAVPSQRPTFKQLVEDL 302
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
1708-2001 6.66e-18

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: 86.78  E-value: 6.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKanckvrGARSFKPVAMKMLQPVPPGARAKESalmafkvavgkwdrdplqhsckayCTARQELAVLL 1787
Cdd:cd14158    20 GNKLGEGGFGVVFK------GYINDKNVAVKKLAAMVDISTEDLT------------------------KQFEQEIQVMA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhyrrSGAHMGPHTFQT---LVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd14158    70 KCQHENLVELLGYSCDgpQLCLVYTYMPNGSLLDRLA----CLNDTPPLSWHMrckIAQGTANGINYLHENNHIHRDIKS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVWELPQPhtedsprnlvhiKIADYGISRQTaPSGAKGFG-----GTEGFMAPEIIRYngeeEYTEKVDCFSFGMFI 1937
Cdd:cd14158   146 ANILLDETFVP------------KISDFGLARAS-EKFSQTIMterivGTTAYMAPEALRG----EITPKSDIFSFGVVL 208
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1938 YENISLRQPFEGHE------SIKE--CILEGSRPALTQRETQ-FPTCCLDLM----VLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14158   209 LEIITGLPPVDENRdpqlllDIKEeiEDEEKTIEDYVDKKMGdWDSTSIEAMysvaSQCLNDKKNRRPDIAKVQQLL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
35-369 7.42e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.55  E-value: 7.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   35 LLAALGTERQIIVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDHFPELI 114
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  115 QQPTVERWLPLHAACINGHIKLLELLISYsypdylyqtyrdeegqwewrlPFDANAHDVTGQTSLYIASILGNKQLVGVL 194
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA---------------------GADVNARDKDGETPLHLAAYNGNLEIVKLL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  195 LKwqlhcrrtlgdsassvstpitptrkrisfgiqaimsklhiSGesegpddlasqestecqrcpINVNLlCGAARETALL 274
Cdd:COG0666   140 LE----------------------------------------AG--------------------ADVNA-QDNDGNTPLH 158
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  275 AAVRGGHLDVVQSLLQHGANPNIVAKpvedhndpkcceeiYGLSnvPIAEACKQRSLAMLDLLLKHGA----RDDNG-TA 349
Cdd:COG0666   159 LAAANGNLEIVKLLLEAGADVNARDN--------------DGET--PLHLAAENGHLEIVKLLLEAGAdvnaKDNDGkTA 222
                         330       340
                  ....*....|....*....|
gi 442620116  350 IGMAITCGDEAILSRLLARR 369
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAG 242
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
1842-1947 8.54e-18

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: 86.47  E-value: 8.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1842 QAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTA--PSGAKGFGGTEGFMAPEIIRyn 1919
Cdd:cd05608   113 QIISGLEHLHQRRIIYRDLKPENVLL------------DDDGNVRISDLGLAVELKdgQTKTKGYAGTPGFMAPELLL-- 178
                          90       100
                  ....*....|....*....|....*...
gi 442620116 1920 gEEEYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd05608   179 -GEEYDYSVDYFTLGVTLYEMIAARGPF 205
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
1697-2001 9.96e-18

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: 87.34  E-value: 9.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1697 KHTIPSECIIKGSLLGRGAFGFVFKANC-KVRGARSFKPVAMKMLQPvppGARAKE-SALMAfkvavgkwdrdplqhsck 1774
Cdd:cd05103     1 KWEFPRDRLKLGKPLGRGAFGQVIEADAfGIDKTATCRTVAVKMLKE---GATHSEhRALMS------------------ 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1775 ayctarqELAVLLTL-KHPNIVPLVGICIK---PLALVLELAPLGGLDALLR--------------HYRRSGAHMG---- 1832
Cdd:cd05103    60 -------ELKILIHIgHHLNVVNLLGACTKpggPLMVIVEFCKFGNLSAYLRskrsefvpyktkgaRFRQGKDYVGdisv 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1833 ------------------------------------------PHTFQTLV---LQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd05103   133 dlkrrldsitssqssassgfveekslsdveeeeagqedlykdFLTLEDLIcysFQVAKGMEFLASRKCIHRDLAARNILL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 welpqphtedSPRNLVhiKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd05103   213 ----------SENNVV--KICDFGLARDIYKDPDYVRKGDArlplKWMAPETIF---DRVYTIQSDVWSFGVLLWEIFSL 277
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1944 -RQPFEGHESIKE-C--ILEGSR---PALTQRETqfptccLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05103   278 gASPYPGVKIDEEfCrrLKEGTRmraPDYTTPEM------YQTMLDCWHGEPSQRPTFSELVEHL 336
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
1711-1998 1.12e-17

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 86.24  E-value: 1.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSfkpvAMKMLQPvppgarAKESALMAFKVavgkwdrdplqhsckayctarqELAVLLTLK 1790
Cdd:cd06644    20 LGDGAFGKVYKAKNKETGALA----AAKVIET------KSEEELEDYMV----------------------EIEILATCN 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICI--KPLALVLELAPLGGLDALLRHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd06644    68 HPYIVKLLGAFYwdGKLWIMIEFCPGGAVDAIMLELDRG---LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLL- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRYNGEEE--YTEKVDCFSFGMFIYENISLR 1944
Cdd:cd06644   144 ------TLDG-----DIKLADFGVSAKNVKTLQRrdSFIGTPYWMAPEVVMCETMKDtpYDYKADIWSLGITLIEMAQIE 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1945 QPFEGHESIKECI-LEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06644   213 PPHHELNPMRVLLkIAKSEPPTLSQPSKWSMEFRDFLKTALDKHPETRPSAAQLL 267
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
1790-2035 1.53e-17

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: 86.61  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMG------PH---TFQTLV---LQAARAIEYLHRRRI 1855
Cdd:cd05100    76 KHKNIINLLGACTQdgPLYVLVEYASKGNLREYLRARRPPGMDYSfdtcklPEeqlTFKDLVscaYQVARGMEYLASQKC 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphTEDSPrnlvhIKIADYGISR--QTAPSGAKGFGG--TEGFMAPEIIRyngEEEYTEKVDCF 1931
Cdd:cd05100   156 IHRDLAARNVLV-------TEDNV-----MKIADFGLARdvHNIDYYKKTTNGrlPVKWMAPEALF---DRVYTHQSDVW 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1932 SFGMFIYENISL-RQPFEG--HESIKECILEGSR---PAltqretqfpTCCLDLMVL---CWHEQPRRRPTASQIVS--- 1999
Cdd:cd05100   221 SFGVLLWEIFTLgGSPYPGipVEELFKLLKEGHRmdkPA---------NCTHELYMImreCWHAVPSQRPTFKQLVEdld 291
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 442620116 2000 -ILSAPECIHLLDVVAMPHSEKIVCGVFQSLVGMGDD 2035
Cdd:cd05100   292 rVLTVTSTDEYLDLSVPFEQYSPGCPDSPSSCSSGDD 328
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
1708-1999 1.55e-17

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: 85.40  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANC-KVRGARSFKPVAMKMLQpvppgARAKESALMAFkvavgkwdrdplqhsckayctaRQELAVL 1786
Cdd:cd05045     5 GKTLGEGEFGKVVKATAfRLKGRAGYTTVAVKMLK-----ENASSSELRDL----------------------LSEFNLL 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSG-AHMGPHTFQ-------------------TLVLQAA 1844
Cdd:cd05045    58 KQVNHPHVIKLYGACSQdgPLLLIVEYAKYGSLRSFLRESRKVGpSYLGSDGNRnssyldnpderaltmgdliSFAWQIS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1845 RAIEYLHRRRIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAKgFGGTEG-----FMAPEIIryn 1919
Cdd:cd05045   138 RGMQYLAEMKLVHRDLAARNVLVAEGRK------------MKISDFGLSRDVYEEDSY-VKRSKGripvkWMAIESL--- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 GEEEYTEKVDCFSFGMFIYENISL-RQPFEG--HESIKECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd05045   202 FDHIYTTQSDVWSFGVLLWEIVTLgGNPYPGiaPERLFNLLKTGYR---MERPENCSEEMYNLMLTCWKQEPDKRPTFAD 278

                  ...
gi 442620116 1997 IVS 1999
Cdd:cd05045   279 ISK 281
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
1708-1994 2.22e-17

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: 84.96  E-value: 2.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgarakesalmafKVAVGKWDRdplQHSCKayctarQELAVLL 1787
Cdd:cd05581     6 GKPLGEGSYSTVVLAKEKETG----KEYAIKVLD----------------KRHIIKEKK---VKYVT------IEKEVLS 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYrrsgahmGPHTFQTLVLQAAR---AIEYLHRRRIIYRDLKS 1862
Cdd:cd05581    57 RLAHPGIVKLYYTFQDEskLYFVLEYAPNGDLLEYIRKY-------GSLDEKCTRFYTAEivlALEYLHSKGIIHRDLKP 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphTEDsprnlVHIKIADYGISRQTAPSG-------------------AKGFGGTEGFMAPEIIrynGEEE 1923
Cdd:cd05581   130 ENILL-------DED-----MHIKITDFGTAKVLGPDSspestkgdadsqiaynqarAASFVGTAEYVSPELL---NEKP 194
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFEGH------ESIKECilEGSRPALtqretqFPTCCLDLMVLCWHEQPRRRPTA 1994
Cdd:cd05581   195 AGKSSDLWALGCIIYQMLTGKPPFRGSneyltfQKIVKL--EYEFPEN------FPPDAKDLIQKLLVLDPSKRLGV 263
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
1710-1997 2.24e-17

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: 84.83  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVPPgarakesalmAFKVAvgkwdrdPLQHsckayctarqELAVLLTL 1789
Cdd:cd06917     8 LVGRGSYGAVYRGYHVKTG----RVVALKVLNLDTD----------DDDVS-------DIQK----------EVALLSQL 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KH---PNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVlqaarAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd06917    57 KLgqpKNIIKYYGSYLKgpSLWIIMDYCEGGSIRTLMRAGPIAERYIAVIMREVLV-----ALKFIHKDGIIHRDIKAAN 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphteDSPRNlvhIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRYNgeEEYTEKVDCFSFGMFIYENIS 1942
Cdd:cd06917   132 ILV---------TNTGN---VKLCDFGVAASLNQNSSKrsTFVGTPYWMAPEVITEG--KYYDTKADIWSLGITTYEMAT 197
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1943 LRQPFEGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd06917   198 GNPPYSDVDALRAVMLIPKSKPPRLEGNGYSPLLKEFVAACLDEEPKDRLSADEL 252
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
1708-2001 2.62e-17

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: 85.82  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANC-KVRGARSFKPVAMKMLQPvppGARAKE-SALMAfkvavgkwdrdplqhsckayctarqELAV 1785
Cdd:cd14207    12 GKSLGRGAFGKVVQASAfGIKKSPTCRVVAVKMLKE---GATASEyKALMT-------------------------ELKI 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTL-KHPNIVPLVGICIK---PLALVLELAPLGGLDALLRHYR------------------------------------ 1825
Cdd:cd14207    64 LIHIgHHLNVVNLLGACTKsggPLMVIVEYCKYGNLSNYLKSKRdffvtnkdtslqeelikekkeaeptggkkkrlesvt 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1826 --RSGAHMG-----------------------PHTFQTLV---LQAARAIEYLHRRRIIYRDLKSENVLVwelpqphted 1877
Cdd:cd14207   144 ssESFASSGfqedkslsdveeeeedsgdfykrPLTMEDLIsysFQVARGMEFLSSRKCIHRDLAARNILL---------- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1878 SPRNLVhiKIADYGISRQ--TAPSGAKGfGGTE---GFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISL-RQPFEGHE 1951
Cdd:cd14207   214 SENNVV--KICDFGLARDiyKNPDYVRK-GDARlplKWMAPESIF---DKIYSTKSDVWSYGVLLWEIFSLgASPYPGVQ 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1952 sIKECILEGSRPALTQRETQFPTCCL-DLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14207   288 -IDEDFCSKLKEGIRMRAPEFATSEIyQIMLDCWQGDPNERPRFSELVERL 337
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
1710-1948 3.05e-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: 84.29  E-value: 3.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAnckvrgarsfkpvamkmlqpvppgaRAKESalMAFKVAVGKWDRDPLqhsCKAYCTARQELAVLLTL 1789
Cdd:cd14202     9 LIGHGAFAVVFKG-------------------------RHKEK--HDLEVAVKCINKKNL---AKSQTLLGKEIKILKEL 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGI--CIKPLALVLELAPLGGLDALLrHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLv 1867
Cdd:cd14202    59 KHENIVALYDFqeIANSVYLVMEYCNGGDLADYL-HTMRT---LSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNIL- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 weLPQPHTEDSPRNLVHIKIADYGISRQTAPSG-AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd14202   134 --LSYSGGRKSNPNNIRIKIADFGFARYLQNNMmAATLCGSPMYMAPEVIM---SQHYDAKADLWSIGTIIYQCLTGKAP 208

                  ..
gi 442620116 1947 FE 1948
Cdd:cd14202   209 FQ 210
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
1712-1950 3.38e-17

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: 83.84  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1712 GRGAFGFVfkanCKVRGARSFKPVAMKMLQpvppgarakesalmafKVAVGKwdRDPLQHsckayctARQELAVLLTLKH 1791
Cdd:cd05578     9 GKGSFGKV----CIVQKKDTKKMFAMKYMN----------------KQKCIE--KDSVRN-------VLNELEILQELEH 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1792 PNIVPLvgiC-----IKPLALVLELapLGGLDalLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd05578    60 PFLVNL---WysfqdEEDMYMVVDL--LLGGD--LRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNIL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VWELPqphtedsprnlvHIKIADYGISRQTAPSG-AKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd05578   133 LDEQG------------HVHITDFNIATKLTDGTlATSTSGTKPYMAPEVFMRAG---YSFAVDWWSLGVTAYEMLRGKR 197

                  ....*
gi 442620116 1946 PFEGH 1950
Cdd:cd05578   198 PYEIH 202
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
1700-2001 3.52e-17

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: 84.32  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCKvrgaRSFKpVAMKMLQPvppGARAKESALmafkvavgkwdrdplqhsckaycta 1779
Cdd:cd05072     4 IPRESIKLVKKLGAGQFGEVWMGYYN----NSTK-VAVKTLKP---GTMSVQAFL------------------------- 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 rQELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHyRRSGAHMGPHTFQtLVLQAARAIEYLHRRRIIY 1857
Cdd:cd05072    51 -EEANLMKTLQHDKLVRLYAVVTKeePIYIITEYMAKGSLLDFLKS-DEGGKVLLPKLID-FSAQIAEGMAYIERKNYIH 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVWElpqphtedsprnLVHIKIADYGISR------QTAPSGAKgfgGTEGFMAPEIIRYNgeeEYTEKVDCF 1931
Cdd:cd05072   128 RDLRAANVLVSE------------SLMCKIADFGLARviedneYTAREGAK---FPIKWTAPEAINFG---SFTIKSDVW 189
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1932 SFGMFIYENISL-RQPFEGHeSIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05072   190 SFGILLYEIVTYgKIPYPGM-SNSDVMSALQRGYRMPRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVL 259
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
1782-2003 3.61e-17

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: 84.37  E-value: 3.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP---LALVLEL--APLGGLDAllrhyRRSGAHMGP---HTFQTLVLQAARAIEYLHR- 1852
Cdd:cd14001    55 EAKILKSLNHPNIVGFRAFTKSEdgsLCLAMEYggKSLNDLIE-----ERYEAGLGPfpaATILKVALSIARALEYLHNe 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 RRIIYRDLKSENVLV---WELpqphtedsprnlvhIKIADYGISRQ-----TAPSGAKG-FGGTEGFMAPEIIRYNGEee 1923
Cdd:cd14001   130 KKILHGDIKSGNVLIkgdFES--------------VKLCDFGVSLPltenlEVDSDPKAqYVGTEPWKAKEALEEGGV-- 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQP-----FEGHESIKECILE------------GSRPAL----TQRETQFptcCLDLMVL 1982
Cdd:cd14001   194 ITDKADIFAYGLVLWEMMTLSVPhlnllDIEDDDEDESFDEdeedeeayygtlGTRPALnlgeLDDSYQK---VIELFYA 270
                         250       260
                  ....*....|....*....|.
gi 442620116 1983 CWHEQPRRRPTASQIVSILSA 2003
Cdd:cd14001   271 CTQEDPKDRPSAAHIVEALEA 291
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
968-1060 3.69e-17

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 79.47  E-value: 3.69e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   968 ISTVGVDIGTWICEKRkraPGSHGPVVFRTWDFGGQKEYYATHQYFLSKRSLYLVLWRISDGHKglaeLLQWLGNIQARA 1047
Cdd:pfam08477   29 KSTIGVDFKTKTVLEN---DDNGKKIKLNIWDTAGQERFRSLHPFYYRGAAAALLVYDSRTFSN----LKYWLRELKKYA 101
                           90
                   ....*....|...
gi 442620116  1048 PNSPVIIVGTHFD 1060
Cdd:pfam08477  102 GNSPVILVGNKID 114
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
1710-1999 3.72e-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: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGarsfKPVAMKMLqPVPPgarakesalmafkvavgkwDRDPLQhsckayctarQELAVLLTL 1789
Cdd:cd06612    10 KLGEGSYGSVYKAIHKETG----QVVAIKVV-PVEE-------------------DLQEII----------KEISILKQC 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd06612    56 DSPYIVKYYGSYFKNtdLWIVMEYCGAGSVSDIMKITNKT---LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILL 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 welpqphTEDSprnlvHIKIADYGISRQTAPSGAKG--FGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd06612   133 -------NEEG-----QAKLADFGVSGQLTDTMAKRntVIGTPFWMAPEVIQEIG---YNNKADIWSLGITAIEMAEGKP 197
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1946 PFEGHESIKECILEGSRPALTQRE-TQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd06612   198 PYSDIHPMRAIFMIPNKPPPTLSDpEKWSPEFNDFVKKCLVKDPEERPSAIQLLQ 252
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
1700-2003 3.88e-17

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: 83.76  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCKVRGARSFkPVAMKMLQPvppGARAKESalmafkvavgkwdRDPLQhsckaycta 1779
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGKREI-PVAIKTLKA---GYTEKQR-------------RDFLS--------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 rqELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRhyrrsgAHMGPHTFQTLV--LQA-ARAIEYLHRRR 1854
Cdd:cd05066    55 --EASIMGQFDHPNIIHLEGVVTrsKPVMIVTEYMENGSLDAFLR------KHDGQFTVIQLVgmLRGiASGMKYLSDMG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphteDSprNLVhIKIADYGISR--QTAPSGAKGFGGTE---GFMAPEIIRYngeEEYTEKVD 1929
Cdd:cd05066   127 YVHRDLAARNILV---------NS--NLV-CKVSDFGLSRvlEDDPEAAYTTRGGKipiRWTAPEAIAY---RKFTSASD 191
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1930 CFSFGMFIYENISL-RQPF--EGHESIKECILEGSR-PAltqrETQFPTCCLDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05066   192 VWSYGIVMWEVMSYgERPYweMSNQDVIKAIEEGYRlPA----PMDCPAALHQLMLDCWQKDRNERPKFEQIVSILDK 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-383 3.88e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 3.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   33 RVLLAALGTERQIIVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDHFPE 112
Cdd:COG0666    33 LLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  113 LIQQpTVERWLPLHAACINGHIKLLELLIsysypdylyqtyrdEEGqwewrlpFDANAHDVTGQTSLYIASILGNKQLVG 192
Cdd:COG0666   113 VNAR-DKDGETPLHLAAYNGNLEIVKLLL--------------EAG-------ADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  193 VLLKwqlhcrrtlgdsassvstpitptrkrisfgiqaimsklhisgesEGPDdlasqestecqrcpINVNLLCGaarETA 272
Cdd:COG0666   171 LLLE--------------------------------------------AGAD--------------VNARDNDG---ETP 189
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  273 LLAAVRGGHLDVVQSLLQHGANPNIVAKpvedhndpkcceeiYGLSnvPIAEACKQRSLAMLDLLLKHGAR-----DDNG 347
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGADVNAKDN--------------DGKT--ALDLAAENGNLEIVKLLLEAGADlnakdKDGL 253
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 442620116  348 TAIGMAITCGDEAILSRLLARRVHPDSDYKINKKGL 383
Cdd:COG0666   254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-196 4.63e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 4.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   20 LRTAVISGDERTVRVLLAALgterqIIVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGH 99
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAG-----ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  100 LGIARLMLDHFPElIQQPTVERWLPLHAACINGHIKLLELLISYsypdylyqtyrdeegqwewrlPFDANAHDVTGQTSL 179
Cdd:COG0666   133 LEIVKLLLEAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEA---------------------GADVNARDNDGETPL 190
                         170
                  ....*....|....*..
gi 442620116  180 YIASILGNKQLVGVLLK 196
Cdd:COG0666   191 HLAAENGHLEIVKLLLE 207
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
1711-1998 5.04e-17

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: 83.20  E-value: 5.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKvrgaRSFKPVAMKMLqpvppgarAKEsalmafKVAVGKWDRDPlqhSCKaycTARQELAVLLTLK 1790
Cdd:cd14004     8 MGEGAYGQVNLAIYK----SKGKEVVIKFI--------FKE------RILVDTWVRDR---KLG---TVPLEIHILDTLN 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 ---HPNIVPLVGICIKPLALVLELAPLG-GLDALLRHYRRSGahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14004    64 krsHPNIVKLLDFFEDDEFYYLVMEKHGsGMDLFDFIERKPN--MDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphteDSPrnlVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIR---YNGEEEytekvDCFSFGMFIYENISL 1943
Cdd:cd14004   142 L---------DGN---GTIKLIDFGSAAYIKSGPFDTFVGTIDYAAPEVLRgnpYGGKEQ-----DIWALGVLLYTLVFK 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1944 RQPFeghESIKEcILEGSR--PALTQREtqfptcCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14004   205 ENPF---YNIEE-ILEADLriPYAVSED------LIDLISRMLNRDVGDRPTIEELL 251
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
1781-2001 5.08e-17

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: 83.40  E-value: 5.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK-PLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd05067    51 AEANLMKQLQHQRLVRLYAVVTQePIYIITEYMENGSLVDFLK--TPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVWELpqphtedsprnlVHIKIADYGISR------QTAPSGAKgFggTEGFMAPEIIRYNgeeEYTEKVDCFSF 1933
Cdd:cd05067   129 LRAANILVSDT------------LSCKIADFGLARliedneYTAREGAK-F--PIKWTAPEAINYG---TFTIKSDVWSF 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1934 GMFIYENISL-RQPFEGHESiKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05067   191 GILLTEIVTHgRIPYPGMTN-PEVIQNLERGYRMPRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVL 258
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1779-1999 5.44e-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: 83.24  E-value: 5.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd08220    46 ALNEVKVLSMLHHPNIIEYYESFLedKALMIVMEYAPGGTLFEYIQ--QRKGSLLSEEEILHFFVQILLALHHVHSKQIL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphteDSPRNLVhiKIADYGISRQ-TAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGM 1935
Cdd:cd08220   124 HRDLKTQNILL---------NKKRTVV--KIGDFGISKIlSSKSKAYTVVGTPCYISPELCE---GKPYNQKSDIWALGC 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1936 FIYENISLRQPFEGhESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd08220   190 VLYELASLKRAFEA-ANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEIMA 252
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
1710-1950 5.57e-17

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 84.60  E-value: 5.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgaraKESALmafkvavgkwDRDPLQHsckayctARQELAVLLTL 1789
Cdd:cd05574     8 LLGKGDVGRVYLVRLKGTG----KLFAMKVLD--------KEEMI----------KRNKVKR-------VLTEREILATL 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGiCI---KPLALVLELAPLGGLDALLRhyRRSGahmgpHTFQTlvlQAAR--------AIEYLHRRRIIYR 1858
Cdd:cd05574    59 DHPFLPTLYA-SFqtsTHLCFVMDYCPGGELFRLLQ--KQPG-----KRLPE---EVARfyaaevllALEYLHLLGFVYR 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSG-------------------------------AKGFGGT 1907
Cdd:cd05574   128 DLKPENILL-------HESG-----HIMLTDFDLSKQSSVTPppvrkslrkgsrrssvksieketfvaepsarSNSFVGT 195
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 442620116 1908 EGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQPFEGH 1950
Cdd:cd05574   196 EEYIAPEVIKGDG---HGSAVDWWTLGILLYEMLYGTTPFKGS 235
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
1805-2006 5.67e-17

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 86.85  E-value: 5.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedSPRNLVh 1884
Cdd:PTZ00283  114 IALVLDYANAGDLRQEIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILL----------CSNGLV- 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1885 iKIADYGISRQTAPSGA----KGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEGhESIKECI--- 1957
Cdd:PTZ00283  183 -KLGDFGFSKMYAATVSddvgRTFCGTPYYVAPEIWR---RKPYSKKADMFSLGVLLYELLTLKRPFDG-ENMEEVMhkt 257
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1958 LEGS---RPALTQRETQfptcclDLMVLCWHEQPRRRPTASQivsILSAPEC 2006
Cdd:PTZ00283  258 LAGRydpLPPSISPEMQ------EIVTALLSSDPKRRPSSSK---LLNMPIC 300
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
1700-2001 5.89e-17

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: 83.86  E-value: 5.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCK--VRGARSFKpVAMKMLQpvppgarakESAlmafkvavgkwdrdplqhSCKAYC 1777
Cdd:cd05061     3 VSREKITLLRELGQGSFGMVYEGNARdiIKGEAETR-VAVKTVN---------ESA------------------SLRERI 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAH---MGPHTFQTLVLQAAR---AIEY 1849
Cdd:cd05061    55 EFLNEASVMKGFTCHHVVRLLGVVSKgqPTLVVMELMAHGDLKSYLRSLRPEAENnpgRPPPTLQEMIQMAAEiadGMAY 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1850 LHRRRIIYRDLKSENVLVwelpqphTEDSPrnlvhIKIADYGISRQTAPS-----GAKGFGGTEGfMAPEIIRyngEEEY 1924
Cdd:cd05061   135 LNAKKFVHRDLAARNCMV-------AHDFT-----VKIGDFGMTRDIYETdyyrkGGKGLLPVRW-MAPESLK---DGVF 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1925 TEKVDCFSFGMFIYENISL-RQPFEG--HESIKECILEGsrpALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05061   199 TTSSDMWSFGVVLWEITSLaEQPYQGlsNEQVLKFVMDG---GYLDQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLL 275
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
1711-2023 5.94e-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: 83.92  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKmlqpvppgarakesalmafKVAVGKwdrdplQHSCKAYCTARqELAVLLTLK 1790
Cdd:cd07832     8 IGEGAHGIVFKAKDRETG----ETVALK-------------------KVALRK------LEGGIPNQALR-EIKALQACQ 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 -HPNIVPLVGICIKP--LALVLELAPlGGLDALLRHYRRsgahmgPHT---FQTLVLQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd07832    58 gHPYVVKLRDVFPHGtgFVLVFEYML-SSLSEVLRDEER------PLTeaqVKRYMRMLLKGVAYMHANRIMHRDLKPAN 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphtedSPRNlvHIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENI 1941
Cdd:cd07832   131 LLI----------SSTG--VLKIADFGLARLFSEEDPRLYShqvATRWYRAPELLY--GSRKYDEGVDLWAVGCIFAELL 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1942 SLRQPFEGHESIKE--CILegsRPALTQRETQFP--TCCLDLMVLCWHEQPRRRPtaSQIVSILSaPECIHLLD-VVAMP 2016
Cdd:cd07832   197 NGSPLFPGENDIEQlaIVL---RTLGTPNEKTWPelTSLPDYNKITFPESKGIRL--EEIFPDCS-PEAIDLLKgLLVYN 270

                  ....*..
gi 442620116 2017 HSEKIVC 2023
Cdd:cd07832   271 PKKRLSA 277
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
1708-1994 6.35e-17

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 83.15  E-value: 6.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLqPVPPGArakesalmafkvavgkwdrdplQHSCKAYCTARQELAVLL 1787
Cdd:cd06653     7 GKLLGRGAFGEVYLC----YDADTGRELAVKQV-PFDPDS----------------------QETSKEVNALECEIQLLK 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGiCI-----KPLALVLELAPLGGLDALLRHYrrsGAhMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd06653    60 NLRHDRIVQYYG-CLrdpeeKKLSIFVEYMPGGSVKDQLKAY---GA-LTENVTRRYTRQILQGVSYLHSNMIVHRDIKG 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLvwelpqphtEDSPRNlvhIKIADYGISR--QT---APSGAKGFGGTEGFMAPEIIryNGeEEYTEKVDCFSFGMFI 1937
Cdd:cd06653   135 ANIL---------RDSAGN---VKLGDFGASKriQTicmSGTGIKSVTGTPYWMSPEVI--SG-EGYGRKADVWSVACTV 199
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1938 YENISLRQPFEGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQpRRRPTA 1994
Cdd:cd06653   200 VEMLTEKPPWAEYEAMAAIFKIATQPTKPQLPDGVSDACRDFLRQIFVEE-KRRPTA 255
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
1711-1997 6.56e-17

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: 83.18  E-value: 6.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGArsfkpvamkmlqpvppgarakesalmafKVAVGKWDRDPLQHSCKaycTARQELAVLLTLK 1790
Cdd:cd06610     9 IGSGATAVVYAAYCLPKKE----------------------------KVAIKRIDLEKCQTSMD---ELRKEIQAMSQCN 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVP-----LVGICikpLALVLELAPLGGLDALLRH-YRRSGAhmgPHTFQTLVLQAA-RAIEYLHRRRIIYRDLKSE 1863
Cdd:cd06610    58 HPNVVSyytsfVVGDE---LWLVMPLLSGGSLLDIMKSsYPRGGL---DEAIIATVLKEVlKGLEYLHSNGQIHRDVKAG 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphTEDSPrnlvhIKIADYGISRQTAPSGA------KGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFI 1937
Cdd:cd06610   132 NILL-------GEDGS-----VKIADFGVSASLATGGDrtrkvrKTFVGTPCWMAPEVME--QVRGYDFKADIWSFGITA 197
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1938 YENISLRQPFEGHESIKEC--ILEGSRPAL-TQRETQ-FPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd06610   198 IELATGAAPYSKYPPMKVLmlTLQNDPPSLeTGADYKkYSKSFRKMISLCLQKDPSKRPTAEEL 261
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1709-2001 9.04e-17

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 82.73  E-value: 9.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGARsfkpVAMKMLqpvppgaRAKESALMAFKVAvgkwdrdplqhsckayctarQELAVLLT 1788
Cdd:cd13996    12 ELLGSGGFGSVYKVRNKVDGVT----YAIKKI-------RLTEKSSASEKVL--------------------REVKALAK 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQT-LVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd13996    61 LNHPNIVRYYTAWVEepPLYIQMELCEGGTLRDWID--RRNSSSKNDRKLALeLFKQILKGVSYIHSKGIVHRDLKPSNI 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphtedSPRNLVhIKIADYGISR------------QTAPSGA----KGFGGTEGFMAPEIIRyngEEEYTEKVD 1929
Cdd:cd13996   139 FL----------DNDDLQ-VKIGDFGLATsignqkrelnnlNNNNNGNtsnnSVGIGTPLYASPEQLD---GENYNEKAD 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1930 CFSFGMFIYEnisLRQPFE-GHESIKecilegsrpALTQ-RETQFPTCCLDLMVlCWHE--------QPRRRPTASQIVS 1999
Cdd:cd13996   205 IYSLGIILFE---MLHPFKtAMERST---------ILTDlRNGILPESFKAKHP-KEADliqsllskNPEERPSAEQLLR 271

                  ..
gi 442620116 2000 IL 2001
Cdd:cd13996   272 SL 273
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
1710-2002 9.97e-17

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: 83.51  E-value: 9.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGARsfKPVAMKMLQPVppgarAKESALMAFKvavgkwdrdplqhsckayctarQELAVLLTL 1789
Cdd:cd05089     9 VIGEGNFGQVIKAMIKKDGLK--MNAAIKMLKEF-----ASENDHRDFA----------------------GELEVLCKL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 -KHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYR---RSGAHMGPH-TFQTLVLQ--------AARAIEYLHRRR 1854
Cdd:cd05089    60 gHHPNIINLLGACENRgyLYIAIEYAPYGNLLDFLRKSRvleTDPAFAKEHgTASTLTSQqllqfasdVAKGMQYLSEKQ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFGGTE-GFMAPEIIRYNgeeEYTEKVDCFSF 1933
Cdd:cd05089   140 FIHRDLAARNVLVGE-----------NLV-SKIADFGLSRGEEVYVKKTMGRLPvRWMAIESLNYS---VYTTKSDVWSF 204
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1934 GMFIYENISL-RQPFEGH--ESIKECILEGSRpaltqreTQFPTCCLD----LMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05089   205 GVLLWEIVSLgGTPYCGMtcAELYEKLPQGYR-------MEKPRNCDDevyeLMRQCWRDRPYERPPFSQISVQLS 273
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
1708-2002 1.02e-16

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: 82.58  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKvRGARSFKPVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLL 1787
Cdd:cd05035     4 GKILGEGEFGSVMEAQLK-QDDGSQLKVAVKTMKVDIHTYSEIEEFL--------------------------SEAACMK 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICI---------KPLaLVLELAPLGGLDALLrHYRRSGAHMGPHTFQTLVLQA---ARAIEYLHRRRI 1855
Cdd:cd05035    57 DFDHPNVMRLIGVCFtasdlnkppSPM-VILPFMKHGDLHSYL-LYSRLGGLPEKLPLQTLLKFMvdiAKGMEYLSNRNF 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphTEDsprnlVHIKIADYGISRqtapsgaKGFGGT---EGFMAPEIIRYNGEEE-----YTEK 1927
Cdd:cd05035   135 IHRDLAARNCML-------DEN-----MTVCVADFGLSR-------KIYSGDyyrQGRISKMPVKWIALESladnvYTSK 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1928 VDCFSFGMFIYENISLRQ-PFEG---HEsIKECILEGSRpaLTQretqfPTCCLD----LMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd05035   196 SDVWSFGVTMWEIATRGQtPYPGvenHE-IYDYLRNGNR--LKQ-----PEDCLDevyfLMYFCWTVDPKDRPTFTKLRE 267

                  ...
gi 442620116 2000 ILS 2002
Cdd:cd05035   268 VLE 270
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1696-1993 1.06e-16

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: 82.45  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1696 DKHTIPSECIIKGSLLGRGAFGFVFKA--NCKVrgarsfkPVAMKMLQPvppGARAKESALmafkvavgkwdrdplqhsc 1773
Cdd:cd05068     1 DQWEIDRKSLKLLRKLGSGQFGEVWEGlwNNTT-------PVAVKTLKP---GTMDPEDFL------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1774 kayctarQELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGgldALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLH 1851
Cdd:cd05068    52 -------REAQIMKKLRHPKLIQLYAVCTLeePIYIITELMKHG---SLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLE 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVWElpqphtedspRNLVhiKIADYGISR-------QTAPSGAKgfggtegF----MAPEIIRYNg 1920
Cdd:cd05068   122 SQNYIHRDLAARNVLVGE----------NNIC--KVADFGLARvikvedeYEAREGAK-------FpikwTAPEAANYN- 181
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1921 eeEYTEKVDCFSFGMFIYENISL-RQPFEG---HESIkECILEGSR-PALTQRETQFptccLDLMVLCWHEQPRRRPT 1993
Cdd:cd05068   182 --RFSIKSDVWSFGILLTEIVTYgRIPYPGmtnAEVL-QQVERGYRmPCPPNCPPQL----YDIMLECWKADPMERPT 252
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
1709-1957 1.07e-16

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 83.61  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANcKVRGARSFKPVAMKMLQPVPPGARAKESAlmafkvavgkwdrdplqHSckayctaRQELAVLLT 1788
Cdd:cd05584     2 KVLGKGGYGKVFQVR-KTTGSDKGKIFAMKVLKKASIVRNQKDTA-----------------HT-------KAERNILEA 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLV------GicikPLALVLELAPlGGldALLRHYRRSGAHMgPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd05584    57 VKHPFIVDLHyafqtgG----KLYLILEYLS-GG--ELFMHLEREGIFM-EDTACFYLAEITLALGHLHSLGIIYRDLKP 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYEN 1940
Cdd:cd05584   129 ENILL---------DAQG---HVKLTDFGLCKESIHDGTVthTFCGTIEYMAPEILTRSG---HGKAVDWWSLGALMYDM 193
                         250
                  ....*....|....*..
gi 442620116 1941 ISLRQPFEGhESIKECI 1957
Cdd:cd05584   194 LTGAPPFTA-ENRKKTI 209
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
1782-1993 1.09e-16

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: 82.23  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP-LALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDL 1860
Cdd:cd05083    49 ETAVMTKLQHKNLVRLLGVILHNgLYIVMELMSKGNLVNFLR--SRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1861 KSENVLVwelpqphTEDSPrnlvhIKIADYGISRqTAPSGAKGFGGTEGFMAPEIIRYNgeeEYTEKVDCFSFGMFIYEN 1940
Cdd:cd05083   127 AARNILV-------SEDGV-----AKISDFGLAK-VGSMGVDNSRLPVKWTAPEALKNK---KFSSKSDVWSYGVLLWEV 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1941 ISL-RQPFEGH--ESIKECILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPT 1993
Cdd:cd05083   191 FSYgRAPYPKMsvKEVKEAVEKGYR---MEPPEGCPPDVYSIMTSCWEAEPGKRPS 243
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
1781-1998 1.26e-16

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: 82.18  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKPLAL--VLELAPLGGLDALLRH------YRRSGAhmgphtfqtLVLQAARAIEYLHR 1852
Cdd:cd14156    37 REISLLQKLSHPNIVRYLGICVKDEKLhpILEYVSGGCLEELLAReelplsWREKVE---------LACDISRGMVYLHS 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 RRIIYRDLKSENVLVwelpqphtEDSPRNLVHIkIADYGISRQTA------PSGAKGFGGTEGFMAPEIIRyngEEEYTE 1926
Cdd:cd14156   108 KNIYHRDLNSKNCLI--------RVTPRGREAV-VTDFGLAREVGempandPERKLSLVGSAFWMAPEMLR---GEPYDR 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1927 KVDCFSFGMFIYEnISLRQPFEGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14156   176 KVDVFSFGIVLCE-ILARIPADPEVLPRTGDFGLDVQAFKEMVPGCPEPFLDLAASCCRMDAFKRPSFAELL 246
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1782-1996 1.30e-16

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: 82.38  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGI--CIKPLALVLELAPLGGL-DALLRH--YRRSGAhmgphtfQTLVLQAARAIEYLHRRRII 1856
Cdd:cd14167    51 EIAVLHKIKHPNIVALDDIyeSGGHLYLIMQLVSGGELfDRIVEKgfYTERDA-------SKLIFQILDAVKYLHDMGIV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVWELpqphTEDSprnlvHIKIADYGISRQTAPSGAKGFG-GTEGFMAPEIIrynGEEEYTEKVDCFSFGM 1935
Cdd:cd14167   124 HRDLKPENLLYYSL----DEDS-----KIMISDFGLSKIEGSGSVMSTAcGTPGYVAPEVL---AQKPYSKAVDCWSIGV 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1936 FIYENISLRQPF--EGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd14167   192 IAYILLCGYPPFydENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIQHLMEKDPEKRFTCEQ 254
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
1782-1999 1.45e-16

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: 81.85  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGI-------CIkplalVLELAPLGglDaLLRHYRRSGAhMGPHTFQTLVLQAARAIEYLHRRR 1854
Cdd:cd14080    52 ELEILRKLRHPNIIQVYSIfergskvFI-----FMEYAEHG--D-LLEYIQKRGA-LSESQARIWFRQLALAVQYLHSLD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGA----KGFGGTEGFMAPEIIR---YNGeeeytEK 1927
Cdd:cd14080   123 IAHRDLKCENILL---------DSNN---NVKLSDFGFARLCPDDDGdvlsKTFCGSAAYAAPEILQgipYDP-----KK 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1928 VDCFSFG--MFIYENISLrqPFEGhESIKEcILEgsrpALTQRETQFPTC-------CLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14080   186 YDIWSLGviLYIMLCGSM--PFDD-SNIKK-MLK----DQQNRKVRFPSSvkklspeCKDLIDQLLEPDPTKRATIEEIL 257

                  .
gi 442620116 1999 S 1999
Cdd:cd14080   258 N 258
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
1711-1999 1.50e-16

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: 81.99  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckvrgaRSFKPVAMKMLQPVPPGARAkesaLMAFKvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd14150     8 IGTGSFGTVFRG-------KWHGDVAVKILKVTEPTPEQ----LQAFK----------------------NEMQVLRKTR 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLALVLELAPLGglDALLRHYrrsgaHMGPHTFQTLVL-----QAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14150    55 HVNILLFMGFMTRPNFAIITQWCEG--SSLYRHL-----HVTETRFDTMQLidvarQTAQGMDYLHAKNIIHRDLKSNNI 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWElpqphtedsprnLVHIKIADYGISR-QTAPSGAKGFGGTEG---FMAPEIIRYNGEEEYTEKVDCFSFGMFIYENI 1941
Cdd:cd14150   128 FLHE------------GLTVKIGDFGLATvKTRWSGSQQVEQPSGsilWMAPEVIRMQDTNPYSFQSDVYAYGVVLYELM 195
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1942 SLRQPFEGHESIKECILEGSR----PALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14150   196 SGTLPYSNINNRDQIIFMVGRgylsPDLSKLSSNCPKAMKRLLIDCLKFKREERPLFPQILV 257
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
1713-1960 1.71e-16

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


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 81.88  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1713 RGAFGFVFKANCKVRGarsfKPVAMKMLqpvppgaRAKEsalMAFKVAVgkwdrdplqHSCKAyctarqELAVLLTLKHP 1792
Cdd:cd05579     3 RGAYGRVYLAKKKSTG----DLYAIKVI-------KKRD---MIRKNQV---------DSVLA------ERNILSQAQNP 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1793 NIVPLVG--ICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLqaarAIEYLHRRRIIYRDLKSENVLVwel 1870
Cdd:cd05579    54 FVVKLYYsfQGKKNLYLVMEYLPGGDLYSLLENVGALDEDVARIYIAEIVL----ALEYLHSHGIIHRDLKPDNILI--- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1871 pqphTEDSprnlvHIKIADYGISR-----------------QTAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSF 1933
Cdd:cd05579   127 ----DANG-----HLKLTDFGLSKvglvrrqiklsiqkksnGAPEKEDRRIVGTPDYLAPEILLGQG---HGKTVDWWSL 194
                         250       260
                  ....*....|....*....|....*....
gi 442620116 1934 GMFIYENISLRQPFEGH--ESIKECILEG 1960
Cdd:cd05579   195 GVILYEFLVGIPPFHAEtpEEIFQNILNG 223
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1779-2004 1.74e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 81.78  E-value: 1.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVGIC--IKPLALVLELAPLGGLdallrhYRRSGAHMGPHTFQTLVL----QAARAIEYLHR 1852
Cdd:cd08218    46 SRKEVAVLSKMKHPNIVQYQESFeeNGNLYIVMDYCDGGDL------YKRINAQRGVLFPEDQILdwfvQLCLALKHVHD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 RRIIYRDLKSENVLVwelpqphTEDSPrnlvhIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEEYTEKVDC 1930
Cdd:cd08218   120 RKILHRDIKSQNIFL-------TKDGI-----IKLGDFGIARVLNSTVelARTCIGTPYYLSPEICE---NKPYNNKSDI 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1931 FSFGMFIYENISLRQPFEGHeSIKECILE---GSRPALTQRetqFPTCCLDLMVLCWHEQPRRRPTasqIVSILSAP 2004
Cdd:cd08218   185 WALGCVLYEMCTLKHAFEAG-NMKNLVLKiirGSYPPVPSR---YSYDLRSLVSQLFKRNPRDRPS---INSILEKP 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
1710-1996 1.89e-16

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: 81.91  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgarakesalmafkvavgkwdrdpLQHSCKAYCTARQELAVLLTL 1789
Cdd:cd06609     8 RIGKGSFGEVYKGIDKRTN----QVVAIKVID---------------------------LEEAEDEIEDIQQEIQFLSQC 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRrsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd06609    57 DSPYITKYYGSFLKgsKLWIIMEYCGGGSVLDLLKPGP-----LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 welpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd06609   132 -------SEEG-----DVKLADFGVSGQLTSTMSKrnTFVGTPFWMAPEVIK---QSGYDEKADIWSLGITAIELAKGEP 196
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1946 PFEGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd06609   197 PLSDLHPMRVLFLIPKNNPPSLEGNKFSKPFKDFVELCLNKDPKERPSAKE 247
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
1781-1947 1.90e-16

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: 81.59  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVG---------ICIkplALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLH 1851
Cdd:cd14033    49 EEVEMLKGLQHPNIVRFYDswkstvrghKCI---ILVTELMTSGTLKTYLKRFRE----MKLKLLQRWSRQILKGLHFLH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRR--IIYRDLKSENVLVwelpqphteDSPRNLVhiKIADYGISRQTAPSGAKGFGGTEGFMAPEIIryngEEEYTEKVD 1929
Cdd:cd14033   122 SRCppILHRDLKCDNIFI---------TGPTGSV--KIGDLGLATLKRASFAKSVIGTPEFMAPEMY----EEKYDEAVD 186
                         170
                  ....*....|....*...
gi 442620116 1930 CFSFGMFIYENISLRQPF 1947
Cdd:cd14033   187 VYAFGMCILEMATSEYPY 204
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
1709-1947 2.05e-16

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: 81.53  E-value: 2.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGarsfKPVAMKmlqpvppgarakesalmaFKVAVGKWDRDPLqhsckaycTARQELAVLLT 1788
Cdd:cd14002     7 ELIGEGSFGKVYKGRRKYTG----QVVALK------------------FIPKRGKSEKELR--------NLRQEIEILRK 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGiCI---KPLALVLELApLGGLDALLRhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14002    57 LNHPNIIEMLD-SFetkKEFVVVTEYA-QGELFQILE----DDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNI 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphTEDSprnlvHIKIADYGISRqtapsgAKGFG--------GTEGFMAPEIIRyngEEEYTEKVDCFSFGMFI 1937
Cdd:cd14002   131 LI-------GKGG-----VVKLCDFGFAR------AMSCNtlvltsikGTPLYMAPELVQ---EQPYDHTADLWSLGCIL 189
                         250
                  ....*....|
gi 442620116 1938 YENISLRQPF 1947
Cdd:cd14002   190 YELFVGQPPF 199
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
1789-2003 2.46e-16

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: 81.37  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKPLALVLELAPLGgLDALLRHYRRSGAHmGPhTFQTLV---LQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd05058    53 FSHPNVLSLLGICLPSEGSPLVVLPYM-KHGDLRNFIRSETH-NP-TVKDLIgfgLQVAKGMEYLASKKFVHRDLAARNC 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWELpqphtedsprnlVHIKIADYGISRQT------APSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYE 1939
Cdd:cd05058   130 MLDES------------FTVKVADFGLARDIydkeyySVHNHTGAKLPVKWMALESLQ---TQKFTTKSDVWSFGVLLWE 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1940 NISLRQPFEGHES---IKECILEGSRpaLTQRETqFPTCCLDLMVLCWHEQPRRRPTASQIVSILSA 2003
Cdd:cd05058   195 LMTRGAPPYPDVDsfdITVYLLQGRR--LLQPEY-CPDPLYEVMLSCWHPKPEMRPTFSELVSRISQ 258
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
1711-1997 2.51e-16

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: 81.98  E-value: 2.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSFKPVAMKMLQPVppgarakesalmafkvavgkwdrdplqHSCKAYCTARQELAVLLTLK 1790
Cdd:cd05090    13 LGECAFGKIYKGHLYLPGMDHAQLVAIKTLKDY---------------------------NNPQQWNEFQQEASLMTELH 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLrhYRRSgahmgPHT--------------------FQTLVLQAARAIE 1848
Cdd:cd05090    66 HPNIVCLLGVVTQeqPVCMLFEFMNQGDLHEFL--IMRS-----PHSdvgcssdedgtvkssldhgdFLHIAIQIAAGME 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHRRRIIYRDLKSENVLVWElpqphtedsprnLVHIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYNgeeEY 1924
Cdd:cd05090   139 YLSSHFFVHKDLAARNILVGE------------QLHVKISDLGLSREIYSSDYYRVQNKSllpiRWMPPEAIMYG---KF 203
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1925 TEKVDCFSFGMFIYENISL-RQPFEGHeSIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd05090   204 SSDSDIWSFGVVLWEIFSFgLQPYYGF-SNQEVIEMVRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDI 276
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
1711-2001 2.93e-16

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: 81.63  E-value: 2.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCkvrgaRSFKPVAMKMLQPVPPGARAKESALMAFkvavgkwdrdplqhsckayctaRQELAVLLTLK 1790
Cdd:cd05093    13 LGEGAFGKVFLAEC-----YNLCPEQDKILVAVKTLKDASDNARKDF----------------------HREAELLTNLQ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAHMG---PHTFQT------LVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd05093    66 HEHIVKFYGVCVEgdPLIMVFEYMKHGDLNKFLRAHGPDAVLMAegnRPAELTqsqmlhIAQQIAAGMVYLASQHFVHRD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYngeEEYTEKVDCFSFGM 1935
Cdd:cd05093   146 LATRNCLVGE-----------NLL-VKIGDFGMSRDVYSTDYYRVGGHTmlpiRWMPPESIMY---RKFTTESDVWSLGV 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1936 FIYENISL-RQPFE--GHESIKECILEGSrpaLTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05093   211 VLWEIFTYgKQPWYqlSNNEVIECITQGR---VLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLL 276
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
1780-1949 3.10e-16

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: 81.12  E-value: 3.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGI--CIKPLALVLELApLGGLdalLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd05572    41 FSEKEILEECNSPFIVKLYRTfkDKKYLYMLMEYC-LGGE---LWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIY 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQtAPSGAKG--FGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGM 1935
Cdd:cd05572   117 RDLKPENLLL---------DSNG---YVKLVDFGFAKK-LGSGRKTwtFCGTPEYVAPEIILNKG---YDFSVDYWSLGI 180
                         170
                  ....*....|....
gi 442620116 1936 FIYENISLRQPFEG 1949
Cdd:cd05572   181 LLYELLTGRPPFGG 194
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
1708-1948 3.15e-16

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: 81.16  E-value: 3.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAnckvrgarsfkpvamkmlqpvppgaRAKESA-LMAFKVAV-GKWDRDPLQHSCkayctaRQELAV 1785
Cdd:cd14116    10 GRPLGKGKFGNVYLA-------------------------REKQSKfILALKVLFkAQLEKAGVEHQL------RREVEI 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTLKHPNIVPLVGIC--IKPLALVLELAPLGgldALLRHYRRSGAHMGPHTfQTLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14116    59 QSHLRHPNILRLYGYFhdATRVYLILEYAPLG---TVYRELQKLSKFDEQRT-ATYITELANALSYCHSKRVIHRDIKPE 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd14116   135 NLLLGSAGE------------LKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIE---GRMHDEKVDLWSLGVLCYEFLVG 199

                  ....*
gi 442620116 1944 RQPFE 1948
Cdd:cd14116   200 KPPFE 204
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
1709-1994 3.35e-16

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: 81.24  E-value: 3.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKAnckvRGARSFKPVAMKMLqpvppgaraKESALmafkvaVGKWDRDPLQHsckaycTARQELAVLLT 1788
Cdd:cd13993     6 SPIGEGAYGVVYLA----VDLRTGRKYAIKCL---------YKSGP------NSKDGNDFQKL------PQLREIDLHRR 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 L-KHPNIVPLV-----GICIkplALVLELAPLGGL-DALL--RHYRRSGAHMgphtfQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd13993    61 VsRHPNIITLHdvfetEVAI---YIVLEYCPNGDLfEAITenRIYVGKTELI-----KNVFLQLIDAVKHCHSLGIYHRD 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphTEDSPRnlvhIKIADYGISRQTAPSgaKGFG-GTEGFMAPEIIRYNGEEE---YTEKVDCFSFGM 1935
Cdd:cd13993   133 IKPENILL-------SQDEGT----VKLCDFGLATTEKIS--MDFGvGSEFYMAPECFDEVGRSLkgyPCAAGDIWSLGI 199
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1936 FIYENISLRQPFE--GHESIKECILEGSRPALTQretQFPTC---CLDLMVLCWHEQPRRRPTA 1994
Cdd:cd13993   200 ILLNLTFGRNPWKiaSESDPIFYDYYLNSPNLFD---VILPMsddFYNLLRQIFTVNPNNRILL 260
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
1780-2003 3.51e-16

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: 81.60  E-value: 3.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRhYRRSGAHMG-------------PHTFQTLVLQAA 1844
Cdd:cd05091    57 RHEAMLRSRLQHPNIVCLLGVVTKeqPMSMIFSYCSHGDLHEFLV-MRSPHSDVGstdddktvkstlePADFLHIVTQIA 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1845 RAIEYLHRRRIIYRDLKSENVLVWElpqphtedsprnLVHIKIADYGISRQTAPSGAKGFGGTEGF----MAPEIIRYNg 1920
Cdd:cd05091   136 AGMEYLSSHHVVHKDLATRNVLVFD------------KLNVKISDLGLFREVYAADYYKLMGNSLLpirwMSPEAIMYG- 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1921 eeEYTEKVDCFSFGMFIYENISL-RQPFEGHESIKECILEGSRPALTQREtQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd05091   203 --KFSIDSDIWSYGVVLWEVFSYgLQPYCGYSNQDVIEMIRNRQVLPCPD-DCPAWVYTLMLECWNEFPSRRPRFKDIHS 279

                  ....
gi 442620116 2000 ILSA 2003
Cdd:cd05091   280 RLRT 283
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
1777-1951 4.40e-16

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 81.97  E-value: 4.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1777 CTARQELAVLLTLKHPNIVPLVGiCIKP---LALVLELapLGGLDaLLRHYRRSGAHMGPHTfqtlVLQAAR---AIEYL 1850
Cdd:cd05616    46 CTMVEKRVLALSGKPPFLTQLHS-CFQTmdrLYFVMEY--VNGGD-LMYHIQQVGRFKEPHA----VFYAAEiaiGLFFL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRYngeEEYTEKV 1928
Cdd:cd05616   118 QSKGIIYRDLKLDNVML---------DSEG---HIKIADFGMCKENIWDGvtTKTFCGTPDYIAPEIIAY---QPYGKSV 182
                         170       180
                  ....*....|....*....|...
gi 442620116 1929 DCFSFGMFIYENISLRQPFEGHE 1951
Cdd:cd05616   183 DWWAFGVLLYEMLAGQAPFEGED 205
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
1705-1957 4.83e-16

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: 80.53  E-value: 4.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1705 IIKGSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvppgarakesalmafkvavgkwdrDPLQHSCKAYCTARQELA 1784
Cdd:cd14082     5 IFPDEVLGSGQFGIVYGGKHRKTG----RDVAIKVI--------------------------DKLRFPTKQESQLRNEVA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVGICIKPLALVLELAPLGG--LDALLRHYRrsgAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd14082    55 ILQQLSHPGVVNLECMFETPERVFVVMEKLHGdmLEMILSSEK---GRLPERITKFLVTQILVALRYLHSKNIVHCDLKP 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphteDSPRNLVHIKIADYGISRQTapsGAKGFG----GTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIY 1938
Cdd:cd14082   132 ENVLL---------ASAEPFPQVKLCDFGFARII---GEKSFRrsvvGTPAYLAPEVLRNKG---YNRSLDMWSVGVIIY 196
                         250
                  ....*....|....*....
gi 442620116 1939 ENISLRQPFEGHESIKECI 1957
Cdd:cd14082   197 VSLSGTFPFNEDEDINDQI 215
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
1700-2002 5.09e-16

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: 81.52  E-value: 5.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKanCKVRgarsfKPVAMKMLQpVPPGARAKESALMAFKVAVGKWDRDPLQHSCKaycta 1779
Cdd:cd05096     2 FPRGHLLFKEKLGEGQFGEVHL--CEVV-----NPQDLPTLQ-FPFNVRKGRPLLVAVKILRPDANKNARNDFLK----- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 rqELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYR-----------RSGAHMGPH-TFQTLV---LQ 1842
Cdd:cd05096    69 --EVKILSRLKDPNIIRLLGVCVDedPLCMITEYMENGDLNQFLSSHHlddkeengndaVPPAHCLPAiSYSSLLhvaLQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1843 AARAIEYLHRRRIIYRDLKSENVLVWElpqphtedsprNLvHIKIADYGISRQTApsgAKGFGGTEG-------FMAPEI 1915
Cdd:cd05096   147 IASGMKYLSSLNFVHRDLATRNCLVGE-----------NL-TIKIADFGMSRNLY---AGDYYRIQGravlpirWMAWEC 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1916 IRYNgeeEYTEKVDCFSFGMFIYENISL--RQPF------EGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQ 1987
Cdd:cd05096   212 ILMG---KFTTASDVWAFGVTLWEILMLckEQPYgeltdeQVIENAGEFFRDQGRQVYLFRPPPCPQGLYELMLQCWSRD 288
                         330
                  ....*....|....*
gi 442620116 1988 PRRRPTASQIVSILS 2002
Cdd:cd05096   289 CRERPSFSDIHAFLT 303
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
1774-1999 5.46e-16

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: 80.46  E-value: 5.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1774 KAYCTARQ-----ELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGL-DALL---RHYRRSGAHMgphtfqtlVLQ 1842
Cdd:cd14184    36 KAKCCGKEhlienEVSILRRVKHPNIIMLIEEMDTPaeLYLVMELVKGGDLfDAITsstKYTERDASAM--------VYN 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1843 AARAIEYLHRRRIIYRDLKSENVLVWELPqphteDSPRNLvhiKIADYGISrqTAPSGA-KGFGGTEGFMAPEIIrynGE 1921
Cdd:cd14184   108 LASALKYLHGLCIVHRDIKPENLLVCEYP-----DGTKSL---KLGDFGLA--TVVEGPlYTVCGTPTYVAPEII---AE 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1922 EEYTEKVDCFSFGMFIYENISLRQPFEGHESIKECILEgsrpALTQRETQFPTCCLD--------LMVLCWHEQPRRRPT 1993
Cdd:cd14184   175 TGYGLKVDIWAAGVITYILLCGFPPFRSENNLQEDLFD----QILLGKLEFPSPYWDnitdsakeLISHMLQVNVEARYT 250

                  ....*.
gi 442620116 1994 ASQIVS 1999
Cdd:cd14184   251 AEQILS 256
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
1830-1954 5.61e-16

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: 80.86  E-value: 5.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1830 HMGPHTF--QTLVLQAAR---AIEYLHRRRIIYRDLKSENVLVwelpqphtEDSPrnlvHIKIADYGISRQTaPSG--AK 1902
Cdd:cd05605    93 NMGNPGFeeERAVFYAAEitcGLEHLHSERIVYRDLKPENILL--------DDHG----HVRISDLGLAVEI-PEGetIR 159
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1903 GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEGH-ESIK 1954
Cdd:cd05605   160 GRVGTVGYMAPEVVK---NERYTFSPDWWGLGCLIYEMIEGQAPFRARkEKVK 209
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
1779-1997 6.07e-16

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: 80.39  E-value: 6.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLL-TLKHPNIVPLvgICIKP----LALVLELAPlggldALLRHYRRSGAHMGP---HTFQ--TLVLQAARAIE 1848
Cdd:cd13982    41 ADREVQLLReSDEHPNVIRY--FCTEKdrqfLYIALELCA-----ASLQDLVESPRESKLflrPGLEpvRLLRQIASGLA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHRRRIIYRDLKSENVLVwelpqphTEDSPRNLVHIKIADYGISR-----QTAPSGAKGFGGTEGFMAPEIIRYNGEEE 1923
Cdd:cd13982   114 HLHSLNIVHRDLKPQNILI-------STPNAHGNVRAMISDFGLCKkldvgRSSFSRRSGVAGTSGWIAPEMLSGSTKRR 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1924 YTEKVDCFSFGMFIYENISL-RQPFEGHESIKECILEG-SRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd13982   187 QTRAVDIFSLGCVFYYVLSGgSHPFGDKLEREANILKGkYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRPSAEEV 262
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
1139-1302 6.23e-16

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


Pssm-ID: 406489  Cd Length: 196  Bit Score: 78.44  E-value: 6.23e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1139 PASYIALEDIvnviacnLRAAGRD-PVLDGEQYKRLVTEQmrlhnykSFRDAAELQQATTWCHENGVLLHY-DDATLRDY 1216
Cdd:pfam16095    1 PKSWLAVREA-------LEKERQKkPYISYEEYRKICAEN-------GIDDEEDQDTLLEFLHDLGVLLYFqDDPGLRDI 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  1217 YFLDPQWLCDMLAHVVTVREINpfAPTGVMKLDDLQMLFRSVQVQGNgNRSYIVSLLNKFEVALT---WDSRTLLIPSLL 1293
Cdd:pfam16095   67 VILNPQWLTNAVYRVLDSKHVL--NNNGILTHEDLEQIWKDPGYPRE-LHPYLLRLMEKFELCYElpgDEEGTYLVPQLL 143

                   ....*....
gi 442620116  1294 PSQEAATPN 1302
Cdd:pfam16095  144 PENPPELYD 152
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
1769-1949 8.77e-16

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


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 80.43  E-value: 8.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1769 LQHSCKAYCTARQELAVLLTLKHPNIVPLVGI--CIKPLALVLELaplggLDALLRHYRRS-GAHMGPHTFQTLVLQAAR 1845
Cdd:cd07873    37 LEHEEGAPCTAIREVSLLKDLKHANIVTLHDIihTEKSLTLVFEY-----LDKDLKQYLDDcGNSINMHNVKLFLFQLLR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISR-QTAPSgaKGFGG---TEGFMAPEIIRynGE 1921
Cdd:cd07873   112 GLAYCHRRKVLHRDLKPQNLLINERGE------------LKLADFGLARaKSIPT--KTYSNevvTLWYRPPDILL--GS 175
                         170       180
                  ....*....|....*....|....*...
gi 442620116 1922 EEYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd07873   176 TDYSTQIDMWGVGCIFYEMSTGRPLFPG 203
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
1769-1949 9.97e-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: 80.42  E-value: 9.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1769 LQHSCKAYCTARQELAVLLTLKHPNIVPLVGIC--IKPLALVLELaplggLDALLRHYRRS-GAHMGPHTFQTLVLQAAR 1845
Cdd:cd07872    41 LEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVhtDKSLTLVFEY-----LDKDLKQYMDDcGNIMSMHNVKIFLYQILR 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISR-QTAPSgaKGFGG---TEGFMAPEIIRynGE 1921
Cdd:cd07872   116 GLAYCHRRKVLHRDLKPQNLLINERGE------------LKLADFGLARaKSVPT--KTYSNevvTLWYRPPDVLL--GS 179
                         170       180
                  ....*....|....*....|....*...
gi 442620116 1922 EEYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd07872   180 SEYSTQIDMWGVGCIFFEMASGRPLFPG 207
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1779-2004 1.04e-15

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: 79.62  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd08225    46 SKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphtedsPRNLVHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMF 1936
Cdd:cd08225   126 DIKSQNIFL-----------SKNGMVAKLGDFGIARQLNDSMelAYTCVGTPYYLSPEICQ---NRPYNNKTDIWSLGCV 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1937 IYENISLRQPFEGHeSIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTasqIVSILSAP 2004
Cdd:cd08225   192 LYELCTLKHPFEGN-NLHQLVLKICQGYFAPISPNFSRDLRSLISQLFKVSPRDRPS---ITSILKRP 255
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
1849-1949 1.08e-15

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 80.51  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQ--TAPSGAKGFGGTEGFMAPEIIRYngeEEYTE 1926
Cdd:cd05587   112 FLHSKGIIYRDLKLDNVML---------DAEG---HIKIADFGMCKEgiFGGKTTRTFCGTPDYIAPEIIAY---QPYGK 176
                          90       100
                  ....*....|....*....|...
gi 442620116 1927 KVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd05587   177 SVDWWAYGVLLYEMLAGQPPFDG 199
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
1711-1947 1.09e-15

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: 79.33  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKvrgARSFKPVAMKMLQPvppgarakesalmafkvavgkwdrdplQHSCKAYCTARQELAVLLTLK 1790
Cdd:cd14120     1 IGHGAFAVVFKGRHR---KKPDLPVAIKCITK---------------------------KNLSKSQNLLGKEIKILKELS 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLALVLELAPLGGLDalLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLvweL 1870
Cdd:cd14120    51 HENVVALLDCQETSSSVYLVMEYCNGGD--LADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNIL---L 125
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1871 PQPHTEDSPRNLVHIKIADYGISRQTaPSG--AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd14120   126 SHNSGRKPSPNDIRLKIADFGFARFL-QDGmmAATLCGSPMYMAPEVIM---SLQYDAKADLWSIGTIVYQCLTGKAPF 200
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
1711-1949 1.10e-15

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: 79.92  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgaraKESALMAFKVavgkwdrdplqhsckaycTARQELAVLLTLK 1790
Cdd:cd07840     7 IGEGTYGQVYKARNKKTG----ELVALKKIR--------MENEKEGFPI------------------TAIREIKLLQKLD 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLA--------LVLELAP--LGGLdalLRHYrrsGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDL 1860
Cdd:cd07840    57 HPNVVRLKEIVTSKGSakykgsiyMVFEYMDhdLTGL---LDNP---EVKFTESQIKCYMKQLLEGLQYLHSNGILHRDI 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1861 KSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFGG---TEGFMAPEIIRynGEEEYTEKVDCFSFGMFI 1937
Cdd:cd07840   131 KGSNILI------------NNDGVLKLADFGLARPYTKENNADYTNrviTLWYRPPELLL--GATRYGPEVDMWSVGCIL 196
                         250
                  ....*....|..
gi 442620116 1938 YENISLRQPFEG 1949
Cdd:cd07840   197 AELFTGKPIFQG 208
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
1711-1960 1.17e-15

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: 80.14  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKanckVRGARSFKPVAMKMLQpvppgaraKEsalmafKVAVGKwdrdPLQHSCkayctarQELAVLLTLK 1790
Cdd:cd14209     9 LGTGSFGRVML----VRHKETGNYYAMKILD--------KQ------KVVKLK----QVEHTL-------NEKRILQAIN 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVgICIKP---LALVLELAPlGGldALLRHYRRSGAHMGPH-TFqtLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14209    60 FPFLVKLE-YSFKDnsnLYMVMEYVP-GG--EMFSHLRRIGRFSEPHaRF--YAAQIVLAFEYLHSLDLIYRDLKPENLL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphteDSprnLVHIKIADYGISRQTapsgaKG----FGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENIS 1942
Cdd:cd14209   134 I---------DQ---QGYIKVTDFGFAKRV-----KGrtwtLCGTPEYLAPEIILSKG---YNKAVDWWALGVLIYEMAA 193
                         250       260
                  ....*....|....*....|
gi 442620116 1943 LRQPFEGHESIK--ECILEG 1960
Cdd:cd14209   194 GYPPFFADQPIQiyEKIVSG 213
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
1711-1997 1.27e-15

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: 79.79  E-value: 1.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSfkpvAMKMLQpvppgaRAKESALMAFKVavgkwdrdplqhsckayctarqELAVLLTLK 1790
Cdd:cd06611    13 LGDGAFGKVYKAQHKETGLFA----AAKIIQ------IESEEELEDFMV----------------------EIDILSECK 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLV-GICIKP-LALVLELAPLGGLDALLRHYRR--SGAHMGPHTFQTLvlqaaRAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd06611    61 HPNIVGLYeAYFYENkLWILIEFCDGGALDSIMLELERglTEPQIRYVCRQML-----EALNFLHSHKVIHRDLKAGNIL 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEII--RYNGEEEYTEKVDCFSFGMFIYENIS 1942
Cdd:cd06611   136 L-------TLDG-----DVKLADFGVSAKNKSTLQKrdTFIGTPYWMAPEVVacETFKDNPYDYKADIWSLGITLIELAQ 203
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1943 LRQPFEGHESIKEC--ILEGSRPALTQrETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd06611   204 MEPPHHELNPMRVLlkILKSEPPTLDQ-PSKWSSSFNDFLKSCLVKDPDDRPTAAEL 259
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
1712-1951 1.32e-15

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: 80.41  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1712 GRGAFGFVFKANCKvrgarsfkpvamkmlqpvpPGARAKESALMAFKVAVGKWDRDPLqhsckaycTARQELAVLLTLKH 1791
Cdd:cd07842     9 GRGTYGRVYKAKRK-------------------NGKDGKEYAIKKFKGDKEQYTGISQ--------SACREIALLRELKH 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1792 PNIVPLVGICI----KPLALVLELAPLGgLDALLRHYRRSGAHMGP-HTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd07842    62 ENVVSLVEVFLehadKSVYLLFDYAEHD-LWQIIKFHRQAKRVSIPpSMVKSLLWQILNGIHYLHSNWVLHRDLKPANIL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphTEDSPRNLVhIKIADYGISRQTAPSGAKGFGG-----TEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENI 1941
Cdd:cd07842   141 V-------MGEGPERGV-VKIGDLGLARLFNAPLKPLADLdpvvvTIWYRAPELLL--GARHYTKAIDIWAIGCIFAELL 210
                         250
                  ....*....|
gi 442620116 1942 SLRQPFEGHE 1951
Cdd:cd07842   211 TLEPIFKGRE 220
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1710-2002 1.49e-15

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: 79.08  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAnCKVRGARSFkpVAMKMLQPVPPGARAKESalmafkvavgkwDRDplqhscKAYCTARQELAVLL-T 1788
Cdd:cd08528     7 LLGSGAFGCVYKV-RKKSNGQTL--LALKEINMTNPAFGRTEQ------------ERD------KSVGDIISEVNIIKeQ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKP--LALVLEL---APLGGLDALLRHyrrSGAHMGPHTFQTLVLQAARAIEYLHR-RRIIYRDLKS 1862
Cdd:cd08528    66 LRHPNIVRYYKTFLENdrLYIVMELiegAPLGEHFSSLKE---KNEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKP 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYEN 1940
Cdd:cd08528   143 NNIML-------GEDD-----KVTITDFGLAKQKGPESSKmtSVVGTILYSCPEIVQ---NEPYGEKADIWALGCILYQM 207
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1941 ISLRQPFEGHE--SIKECILEGSRPALTqrETQFPTCCLDLMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd08528   208 CTLQPPFYSTNmlTLATKIVEAEYEPLP--EGMYSDDITFVIRSCLTPDPEARPDIVEVSSMIS 269
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1711-2011 1.70e-15

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: 79.41  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVfkanCKVRGARSFKPVAMKMLqpvppgarakesalmafkvavgKWDRDPLQHSCKAYCtarQELAVLLTLK 1790
Cdd:cd13989     1 LGSGGFGYV----TLWKHQDTGEYVAIKKC----------------------RQELSPSDKNRERWC---LEVQIMKKLN 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIV-------PLVGICIKPLALV-LELAPLGGLDALLRHYRrSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd13989    52 HPNVVsardvppELEKLSPNDLPLLaMEYCSGGDLRKVLNQPE-NCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKP 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphtEDSPRNLVHiKIADYGISRQ-TAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENI 1941
Cdd:cd13989   131 ENIVL--------QQGGGRVIY-KLIDLGYAKElDQGSLCTSFVGTLQYLAPELFE---SKKYTCTVDYWSFGTLAFECI 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1942 S-------LRQPFEGHESIKE------CILEGSRPALT-----QRETQFPTCC-------LDLMvLCWHEQPRRRPTASQ 1996
Cdd:cd13989   199 TgyrpflpNWQPVQWHGKVKQkkpehiCAYEDLTGEVKfsselPSPNHLSSILkeyleswLQLM-LRWDPRQRGGGPQNN 277
                         330
                  ....*....|....*
gi 442620116 1997 ivsilsaPECIHLLD 2011
Cdd:cd13989   278 -------PGCFQLLD 285
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
1696-2001 1.93e-15

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: 78.96  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1696 DKHTIPSECIIKGSLLGRGAFGFVFKANCKvrgarSFKPVAMKMLQPvppGARAKESALmafkvavgkwdrdplqhscka 1775
Cdd:cd05069     5 DAWEIPRESLRLDVKLGQGCFGEVWMGTWN-----GTTKVAIKTLKP---GTMMPEAFL--------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1776 yctarQELAVLLTLKHPNIVPLVGICIK-PLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRR 1854
Cdd:cd05069    56 -----QEAQIMKKLRHDKLVPLYAVVSEePIYIVTEFMGKGSLLDFLK--EGDGKYLKLPQLVDMAAQIADGMAYIERMN 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVWElpqphtedsprNLVhIKIADYGISR------QTAPSGAKGfggTEGFMAPEIIRYNgeeEYTEKV 1928
Cdd:cd05069   129 YIHRDLRAANILVGD-----------NLV-CKIADFGLARliedneYTARQGAKF---PIKWTAPEAALYG---RFTIKS 190
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1929 DCFSFGMFIYENISL-RQPFEG--HESIKECILEGSRPALTQretQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05069   191 DVWSFGILLTELVTKgRVPYPGmvNREVLEQVERGYRMPCPQ---GCPESLHELMKLCWKKDPDERPTFEYIQSFL 263
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
1711-1999 2.41e-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: 78.50  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLqPVPPGArakesalmafkvavgkwDRDPLQhsckayctarQELAVLLTLK 1790
Cdd:cd06613     8 IGSGTYGDVYKARNIATG----ELAAVKVI-KLEPGD-----------------DFEIIQ----------QEISMLKECR 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALlrhYRRSG-------AHMgphTFQTLvlqaaRAIEYLHRRRIIYRDLK 1861
Cdd:cd06613    56 HPNIVAYFGSYLRrdKLWIVMEYCGGGSLQDI---YQVTGplselqiAYV---CRETL-----KGLAYLHSTGKIHRDIK 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFGMFIYE 1939
Cdd:cd06613   125 GANILL-------TEDG-----DVKLADFGVSAQLTATIAKrkSFIGTPYWMAPEVAAVERKGGYDGKCDIWALGITAIE 192
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1940 NISLRQP-FEGHeSIKECILEGSR----PALTQRE------TQFPTCCLDlmvlcwhEQPRRRPTASQIVS 1999
Cdd:cd06613   193 LAELQPPmFDLH-PMRALFLIPKSnfdpPKLKDKEkwspdfHDFIKKCLT-------KNPKKRPTATKLLQ 255
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1711-2010 2.76e-15

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: 78.96  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgarakesalmafkvavgkwdrdpLQHSCKAYCTARQELAVLLTLK 1790
Cdd:cd07844     8 LGEGSYATVYKGRSKLTG----QLVALKEIR---------------------------LEHEEGAPFTAIREASLLKDLK 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGI--CIKPLALVLELaplggLDALLRHY-RRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd07844    57 HANIVTLHDIihTKKTLTLVFEY-----LDTDLKQYmDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLI 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 WELPQphtedsprnlvhIKIADYGISR-QTAPSgaKGFGG---TEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd07844   132 SERGE------------LKLADFGLARaKSVPS--KTYSNevvTLWYRPPDVLL--GSTEYSTSLDMWGVGCIFYEMATG 195
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1944 RQPFEGHESIKECILEGSRPALTQRETQFPTCC-LDLMVLCWHEQPRRRPTASQIVSILSAPECIHLL 2010
Cdd:cd07844   196 RPLFPGSTDVEDQLHKIFRVLGTPTEETWPGVSsNPEFKPYSFPFYPPRPLINHAPRLDRIPHGEELA 263
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
1711-1959 2.90e-15

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: 78.85  E-value: 2.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKA-NCKVRGARSFKPVAMKML--------QPVPPGAR-AKESALMAfkvavgkwdRDPLQhscKAYctar 1780
Cdd:cd14199    10 IGKGSYGVVKLAyNEDDNTYYAMKVLSKKKLmrqagfprRPPPRGARaAPEGCTQP---------RGPIE---RVY---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP----LALVLELAPLGGLDAL--LRHYRRSGAHMgphTFQTLVlqaaRAIEYLHRRR 1854
Cdd:cd14199    74 QEIAILKKLDHPNVVKLVEVLDDPsedhLYMVFELVKQGPVMEVptLKPLSEDQARF---YFQDLI----KGIEYLHYQK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYNGEEEYTEKVDCFS 1932
Cdd:cd14199   147 IIHRDVKPSNLLV-------GEDG-----HIKIADFGVSNEFEGSDAllTNTVGTPAFMAPETLSETRKIFSGKALDVWA 214
                         250       260       270
                  ....*....|....*....|....*....|...
gi 442620116 1933 FGMFIYENISLRQPFEG------HESIKECILE 1959
Cdd:cd14199   215 MGVTLYCFVFGQCPFMDerilslHSKIKTQPLE 247
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
1707-1999 3.52e-15

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: 78.25  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFkanCKVrgarsfkpvamkmlqpvppgarAKESALMAFK-VAVGKWDRDPLQhscKAYCTARQELAV 1785
Cdd:cd06631     5 KGNVLGKGAYGTVY---CGL----------------------TSTGQLIAVKqVELDTSDKEKAE---KEYEKLQEEVDL 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRhyrRSGAHMGPhTFQTLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd06631    57 LKTLKHVNIVGYLGTCLEDnvVSIFMEFVPGGSIASILA---RFGALEEP-VFCRYTKQILEGVAYLHNNNVIHRDIKGN 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVweLPqphtedsprNLVhIKIADYGISRQTAPSGA--------KGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGM 1935
Cdd:cd06631   133 NIML--MP---------NGV-IKLIDFGCAKRLCINLSsgsqsqllKSMRGTPYWMAPEVIN---ETGHGRKSDIWSIGC 197
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1936 FIYENISLRQPFEGHESIKECILEGSR----PALTQRetqFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd06631   198 TVFEMATGKPPWADMNPMAAIFAIGSGrkpvPRLPDK---FSPEARDFVHACLTRDQDERPSAEQLLK 262
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
1696-2001 3.56e-15

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: 78.14  E-value: 3.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1696 DKHTIPSECIIKGSLLGRGAFGFVFKANckvrgARSFKPVAMKMLQPvppGARAKESALmafkvavgkwdrdplqhscka 1775
Cdd:cd05073     4 DAWEIPRESLKLEKKLGAGQFGEVWMAT-----YNKHTKVAVKTMKP---GSMSVEAFL--------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1776 yctarQELAVLLTLKHPNIVPLVGICIK-PLALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRR 1854
Cdd:cd05073    55 -----AEANVMKTLQHDKLVKLHAVVTKePIYIITEFMAKGSLLDFLK--SDEGSKQPLPKLIDFSAQIAEGMAFIEQRN 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISR------QTAPSGAKGfggTEGFMAPEIIRYNgeeEYTEKV 1928
Cdd:cd05073   128 YIHRDLRAANILV------------SASLVCKIADFGLARviedneYTAREGAKF---PIKWTAPEAINFG---SFTIKS 189
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1929 DCFSFGMFIYENISL-RQPFEGHESiKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05073   190 DVWSFGILLMEIVTYgRIPYPGMSN-PEVIRALERGYRMPRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVL 262
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
1806-1948 3.63e-15

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: 78.53  E-value: 3.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1806 ALVLELAPLGGLDALLRHYrrsgaHMGPHTFQT--LVLQAAR---AIEYLHRRRIIYRDLKSENVLVwelpqphtEDSPr 1880
Cdd:cd05630    74 ALCLVLTLMNGGDLKFHIY-----HMGQAGFPEarAVFYAAEiccGLEDLHRERIVYRDLKPENILL--------DDHG- 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1881 nlvHIKIADYGISRQTaPSGA--KGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd05630   140 ---HIRISDLGLAVHV-PEGQtiKGRVGTVGYMAPEVVK---NERYTFSPDWWALGCLLYEMIAGQSPFQ 202
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
1846-1958 3.97e-15

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 78.97  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGAKG--FGGTEGFMAPEIIRyngEEE 1923
Cdd:cd05592   108 GLQFLHSRGIIYRDLKLDNVLL---------DREG---HIKIADFGMCKENIYGENKAstFCGTPDYIAPEILK---GQK 172
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFEG--HESIKECIL 1958
Cdd:cd05592   173 YNQSVDWWSFGVLLYEMLIGQSPFHGedEDELFWSIC 209
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
1758-1999 3.97e-15

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: 77.84  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWDRDPLQHSCKAYCTarQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGL-DALLRHYRRSGAHMGPH 1834
Cdd:cd14074    30 KVAVKVIDKTKLDDVSKAHLF--QEVRCMKLVQHPNVVRLYEVIDTQtkLYLILELGDGGDMyDYIMKHENGLNEDLARK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1835 TFQTLVlqaaRAIEYLHRRRIIYRDLKSENVLVWElpqphtedsprNLVHIKIADYGISRQTAPsGAK--GFGGTEGFMA 1912
Cdd:cd14074   108 YFRQIV----SAISYCHKLHVVHRDLKPENVVFFE-----------KQGLVKLTDFGFSNKFQP-GEKleTSCGSLAYSA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1913 PEIIRynGEEEYTEKVDCFSFGMFIYENISLRQPF-EGHES-----IKECilEGSRPALTQREtqfptcCLDLMVLCWHE 1986
Cdd:cd14074   172 PEILL--GDEYDAPAVDIWSLGVILYMLVCGQPPFqEANDSetltmIMDC--KYTVPAHVSPE------CKDLIRRMLIR 241
                         250
                  ....*....|...
gi 442620116 1987 QPRRRPTASQIVS 1999
Cdd:cd14074   242 DPKKRASLEEIEN 254
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
1778-2011 4.46e-15

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 78.10  E-value: 4.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPL--VGICIKPLALVLELaplggLDALLRHYRRSGAHM--GPHTFQTLVLQAARAIEYLHRR 1853
Cdd:cd07835    44 TAIREISLLKELNHPNIVRLldVVHSENKLYLVFEF-----LDLDLKKYMDSSPLTglDPPLIKSYLYQLLQGIAFCHSH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVwelpqphteDSPRNLvhiKIADYGISRqtapsgakGFG----------GTEGFMAPEIIRynGEEE 1923
Cdd:cd07835   119 RVLHRDLKPQNLLI---------DTEGAL---KLADFGLAR--------AFGvpvrtythevVTLWYRAPEILL--GSKH 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1924 YTEKVDCFSFGMfIYENISLRQP-FEGHESIKEcILEGSRPALTQRETQFP--TCCLDLmvlcWHEQPR-RRPTASQIVS 1999
Cdd:cd07835   177 YSTPVDIWSVGC-IFAEMVTRRPlFPGDSEIDQ-LFRIFRTLGTPDEDVWPgvTSLPDY----KPTFPKwARQDLSKVVP 250
                         250
                  ....*....|..
gi 442620116 2000 ILSaPECIHLLD 2011
Cdd:cd07835   251 SLD-EDGLDLLS 261
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
1706-1996 5.04e-15

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: 78.38  E-value: 5.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1706 IKGSLLGRGAFGFVFKANCKVRGarsfKPVAMKmlqpvppgarakesalmafKVAVGKWDRDPlqhsCKAYCTARQELAV 1785
Cdd:cd07841     3 EKGKKLGEGTYAVVYKARDKETG----RIVAIK-------------------KIKLGERKEAK----DGINFTALREIKL 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTLKHPNIVPLVGI-CIKP-LALVLELAPlGGLDALLRH--YRRSGAHMGPHTFQTLvlqaaRAIEYLHRRRIIYRDLK 1861
Cdd:cd07841    56 LQELKHPNIIGLLDVfGHKSnINLVFEFME-TDLEKVIKDksIVLTPADIKSYMLMTL-----RGLEYLHSNWILHRDLK 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphtedSPRNLVhiKIADYGISRQtapsgakgFGGTEGFM----------APEIIRynGEEEYTEKVDCF 1931
Cdd:cd07841   130 PNNLLI----------ASDGVL--KLADFGLARS--------FGSPNRKMthqvvtrwyrAPELLF--GARHYGVGVDMW 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1932 SFGMFIYENIsLRQPF-------------------------EGHESIKECILEGSRPAlTQRETQFPTC---CLDLMVLC 1983
Cdd:cd07841   188 SVGCIFAELL-LRVPFlpgdsdidqlgkifealgtpteenwPGVTSLPDYVEFKPFPP-TPLKQIFPAAsddALDLLQRL 265
                         330
                  ....*....|...
gi 442620116 1984 WHEQPRRRPTASQ 1996
Cdd:cd07841   266 LTLNPNKRITARQ 278
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1782-1960 5.53e-15

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: 77.73  E-value: 5.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGI--CIKPLALVLELAPLGGL-DALLRH--YRRSGAhmgphtfQTLVLQAARAIEYLHRRRII 1856
Cdd:cd14166    50 EIAVLKRIKHENIVTLEDIyeSTTHYYLVMQLVSGGELfDRILERgvYTEKDA-------SRVINQVLSAVKYLHENGIV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVWelpqphtedSPRNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIrynGEEEYTEKVDCFSFGMF 1936
Cdd:cd14166   123 HRDLKPENLLYL---------TPDENSKIMITDFGLSKMEQNGIMSTACGTPGYVAPEVL---AQKPYSKAVDCWSIGVI 190
                         170       180
                  ....*....|....*....|....*.
gi 442620116 1937 IYENISLRQPF--EGHESIKECILEG 1960
Cdd:cd14166   191 TYILLCGYPPFyeETESRLFEKIKEG 216
Ank_2 pfam12796
Ankyrin repeats (3 copies);
58-143 6.97e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 6.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116    58 LFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDHFpelIQQPTVERWLPLHAACINGHIKLL 137
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA---DVNLKDNGRTALHYAARSGHLEIV 77

                   ....*.
gi 442620116   138 ELLISY 143
Cdd:pfam12796   78 KLLLEK 83
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
1711-1999 6.98e-15

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: 76.92  E-value: 6.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANckvrgARSFKPVAMKMLQPvppgARAKesalmafkvavgkwDRDPLQHsckayctARQELAVLLTLK 1790
Cdd:cd14161    11 LGKGTYGRVKKAR-----DSSGRLVAIKSIRK----DRIK--------------DEQDLLH-------IRREIEIMSSLN 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGIC--IKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVlqaaRAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd14161    61 HPHIISVYEVFenSSKIVIVMEYASRGDLYDYISERQRLSELEARHFFRQIV----SAVHYCHANGIVHRDLKLENILL- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphteDSPRNlvhIKIADYGISR-QTAPSGAKGFGGTEGFMAPEIIryNGEEEYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd14161   136 --------DANGN---IKIADFGLSNlYNQDKFLQTYCGSPLYASPEIV--NGRPYIGPEVDSWSLGVLLYILVHGTMPF 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1948 EGHE--SIKECILEGSrpaltQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14161   203 DGHDykILVKQISSGA-----YREPTKPSDACGLIRWLLMVNPERRATLEDVAS 251
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
1708-1894 9.12e-15

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: 77.32  E-value: 9.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAnckvRGARSFKPVAMKmlqpvppgarakesalmafKVAVgKWDRDPLQHSckaycTARqELAVLL 1787
Cdd:cd07838     4 VAEIGEGAYGTVYKA----RDLQDGRFVALK-------------------KVRV-PLSEEGIPLS-----TIR-EIALLK 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLK---HPNIVPLVGICIKP-------LALVLELAPlGGLDALLRHYRRSGahMGPHTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd07838    54 QLEsfeHPNVVRLLDVCHGPrtdrelkLTLVFEHVD-QDLATYLDKCPKPG--LPPETIKDLMRQLLRGLDFLHSHRIVH 130
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 442620116 1858 RDLKSENVLVwelpqphTEDSprnlvHIKIADYGISR 1894
Cdd:cd07838   131 RDLKPQNILV-------TSDG-----QVKLADFGLAR 155
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
1846-1973 1.11e-14

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: 77.78  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYNgeeE 1923
Cdd:cd05571   107 ALGYLHSQGIVYRDLKLENLLL---------DKDG---HIKITDFGLCKEEISYGAttKTFCGTPEYLAPEVLEDN---D 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPF--EGHESIKECILegsrpaltQRETQFP 1973
Cdd:cd05571   172 YGRAVDWWGLGVVMYEMMCGRLPFynRDHEVLFELIL--------MEEVRFP 215
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1708-1947 1.14e-14

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: 77.17  E-value: 1.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKanCKVRGARsfKPVAMKMLQpvppgarakesalmafKVAVGKwdrdplqhsckaycTARQELAVLL 1787
Cdd:cd14085     8 ESELGRGATSVVYR--CRQKGTQ--KPYAVKKLK----------------KTVDKK--------------IVRTEIGVLL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPLGGL-DALLR--HYRRSGAhmgphtfQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd14085    54 RLSHPNIIKLKEIFETPteISLVLELVTGGELfDRIVEkgYYSERDA-------ADAVKQILEAVAYLHENGIVHRDLKP 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENvLVWELPQPhteDSPrnlvhIKIADYGISRQTAPS-GAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENI 1941
Cdd:cd14085   127 EN-LLYATPAP---DAP-----LKIADFGLSKIVDQQvTMKTVCGTPGYCAPEILR---GCAYGPEVDMWSVGVITYILL 194

                  ....*.
gi 442620116 1942 SLRQPF 1947
Cdd:cd14085   195 CGFEPF 200
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
1711-1995 1.22e-14

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 76.55  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKanCKVRGARsfKPVAMKMLQpvppgarakeSALMafkvavgkwDRDPLQHsckayctarqELAVLLTLK 1790
Cdd:cd14113    15 LGRGRFSVVKK--CDQRGTK--RAVATKFVN----------KKLM---------KRDQVTH----------ELGVLQSLQ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPLGGL-DALLRHYRRSGAHMGPHTFQTLvlqaaRAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd14113    62 HPQLVGLLDTFETPtsYILVLEMADQGRLlDYVVRWGNLTEEKIRFYLREIL-----EALQYLHNCRIAHLDLKPENILV 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 WELPQPHTedsprnlvhIKIADYGISRQ--TAPSGAKGFGGTEgFMAPEIIRYNgeeEYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd14113   137 DQSLSKPT---------IKLADFGDAVQlnTTYYIHQLLGSPE-FAAPEIILGN---PVSLTSDLWSIGVLTYVLLSGVS 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1946 PFEgHESIKE-----CILEGSRP-----ALTQRETQFptccldlMVLCWHEQPRRRPTAS 1995
Cdd:cd14113   204 PFL-DESVEEtclniCRLDFSFPddyfkGVSQKAKDF-------VCFLLQMDPAKRPSAA 255
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
1707-1950 1.43e-14

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


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 76.20  E-value: 1.43e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKvrgARSFKPVAMKMLQpvppgarakESALMAFKVAVGKwdrdplqhsckayctarqELAVL 1786
Cdd:cd14201    10 RKDLVGHGAFAVVFKGRHR---KKTDWEVAIKSIN---------KKNLSKSQILLGK------------------EIKIL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIKPLALVLELAPLGGLDalLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14201    60 KELQHENIVALYDVQEMPNSVFLVMEYCNGGD--LADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNIL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 vweLPQPHTEDSPRNLVHIKIADYGISRQTAPS-GAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd14201   138 ---LSYASRKKSSVSGIRIKIADFGFARYLQSNmMAATLCGSPMYMAPEVIM---SQHYDAKADLWSIGTVIYQCLVGKP 211

                  ....*
gi 442620116 1946 PFEGH 1950
Cdd:cd14201   212 PFQAN 216
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
1700-2003 1.47e-14

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: 76.49  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCKVRGArSFKPVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckaycta 1779
Cdd:cd05074     6 IQEQQFTLGRMLGKGEFGSVREAQLKSEDG-SFQKVAVKMLKADIFSSSDIEEFL------------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 rQELAVLLTLKHPNIVPLVGICIK-------PLALV-LELAPLGGLDALLRHYRrsgahMGPHTF----QTLV---LQAA 1844
Cdd:cd05074    60 -REAACMKEFDHPNVIKLIGVSLRsrakgrlPIPMViLPFMKHGDLHTFLLMSR-----IGEEPFtlplQTLVrfmIDIA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1845 RAIEYLHRRRIIYRDLKSENVLVwelpqphTEDsprnlVHIKIADYGISRQTApSGAKGFGGTEG-----FMAPEIIRYN 1919
Cdd:cd05074   134 SGMEYLSSKNFIHRDLAARNCML-------NEN-----MTVCVADFGLSKKIY-SGDYYRQGCASklpvkWLALESLADN 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 geeEYTEKVDCFSFGMFIYENISLRQ-PFEGHES--IKECILEGSRpaLTQretqfPTCCL----DLMVLCWHEQPRRRP 1992
Cdd:cd05074   201 ---VYTTHSDVWAFGVTMWEIMTRGQtPYAGVENseIYNYLIKGNR--LKQ-----PPDCLedvyELMCQCWSPEPKCRP 270
                         330
                  ....*....|.
gi 442620116 1993 TASQIVSILSA 2003
Cdd:cd05074   271 SFQHLRDQLEL 281
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
1711-1999 1.50e-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: 76.33  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckvRGARSFKPVAMKMLQPVPPGARaKESALMAFKVAVGKWDRdplqhsckaycTARqELAVLLTLK 1790
Cdd:cd14077     9 IGAGSMGKVKLA----KHIRTGEKCAIKIIPRASNAGL-KKEREKRLEKEISRDIR-----------TIR-EAALSSLLN 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--LALVLELAPlGG--LDALLRHYRrsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14077    72 HPHICRLRDFLRTPnhYYMLFEYVD-GGqlLDYIISHGK-----LKEKQARKFARQIASALDYLHRNSIVHRDLKIENIL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphteDSPRNlvhIKIADYGISRQTAPSGA-KGFGGTEGFMAPEII---RYNGEEeytekVDCFSFGMFIYENIS 1942
Cdd:cd14077   146 I---------SKSGN---IKIIDFGLSNLYDPRRLlRTFCGSLYFAAPELLqaqPYTGPE-----VDVWSFGVVLYVLVC 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1943 LRQPFEG------HESIKECILEgsRPALTQREtqfptcCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14077   209 GKVPFDDenmpalHAKIKKGKVE--YPSYLSSE------CKSLISRMLVVDPKKRATLEQVLN 263
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
1710-1973 1.69e-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: 76.97  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgaraKEsalmafkVAVGKwdrDPLQHSCKayctarqELAVLLTL 1789
Cdd:cd05595     2 LLGKGTFGKVILVREKATG----RYYAMKILR--------KE-------VIIAK---DEVAHTVT-------ESRVLQNT 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPL--VGICIKPLALVLELAPLGgldALLRHYRRSgahmgphtfQTLVLQAAR--------AIEYLHRRRIIYRD 1859
Cdd:cd05595    53 RHPFLTALkyAFQTHDRLCFVMEYANGG---ELFFHLSRE---------RVFTEDRARfygaeivsALEYLHSRDVVYRD 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYNgeeEYTEKVDCFSFGMFI 1937
Cdd:cd05595   121 IKLENLML-------DKDG-----HIKITDFGLCKEGITDGAtmKTFCGTPEYLAPEVLEDN---DYGRAVDWWGLGVVM 185
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 442620116 1938 YENISLRQPF--EGHESIKECILegsrpaltQRETQFP 1973
Cdd:cd05595   186 YEMMCGRLPFynQDHERLFELIL--------MEEIRFP 215
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
1711-1949 1.92e-14

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 76.67  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANcKVRGARSFKPVAMKMLqpvppgaraKESALmafKVavgkwdRDPLQhsckayctARQELAVLLTLK 1790
Cdd:cd05582     3 LGQGSFGKVFLVR-KITGPDAGTLYAMKVL---------KKATL---KV------RDRVR--------TKMERDILADVN 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLALVLELAPLGGLDALlrhYRRSGAHM-GPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwe 1869
Cdd:cd05582    56 HPFIVKLHYAFQTEGKLYLILDFLRGGDLF---TRLSKEVMfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL-- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 lpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd05582   131 -----DEDG-----HIKLTDFGLSKESIDHEKKaySFCGTVEYMAPEVVNRRG---HTQSADWWSFGVLMFEMLTGSLPF 197

                  ..
gi 442620116 1948 EG 1949
Cdd:cd05582   198 QG 199
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
1708-1997 2.10e-14

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: 76.13  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGARSFKpVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLL 1787
Cdd:cd14204    12 GKVLGEGEFGSVMEGELQQPDGTNHK-VAVKTMKLDNFSQREIEEFL--------------------------SEAACMK 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICI--------KPLaLVLELAPLGGLDALLrhyRRSGAHMGPH--TFQTLV---LQAARAIEYLHRRR 1854
Cdd:cd14204    65 DFNHPNVIRLLGVCLevgsqripKPM-VILPFMKYGDLHSFL---LRSRLGSGPQhvPLQTLLkfmIDIALGMEYLSSRN 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRqtapsgaKGFGGT---EGFMAPEIIRYNGEEE-----YTE 1926
Cdd:cd14204   141 FLHRDLAARNCML------------RDDMTVCVADFGLSK-------KIYSGDyyrQGRIAKMPVKWIAVESladrvYTV 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1927 KVDCFSFGMFIYEnISLR--QPFEG---HEsIKECILEGSRpaLTQretqfPTCCLD----LMVLCWHEQPRRRPTASQI 1997
Cdd:cd14204   202 KSDVWAFGVTMWE-IATRgmTPYPGvqnHE-IYDYLLHGHR--LKQ-----PEDCLDelydIMYSCWRSDPTDRPTFTQL 272
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
1806-1954 2.29e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 76.18  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1806 ALVLELAPLGGLDALLRHYrrsgaHMGPHTF--QTLVLQAAR---AIEYLHRRRIIYRDLKSENVLVwelpqphtEDSPr 1880
Cdd:cd05631    74 ALCLVLTIMNGGDLKFHIY-----NMGNPGFdeQRAIFYAAElccGLEDLQRERIVYRDLKPENILL--------DDRG- 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1881 nlvHIKIADYGISRQTaPSG--AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEGH-ESIK 1954
Cdd:cd05631   140 ---HIRISDLGLAVQI-PEGetVRGRVGTVGYMAPEVIN---NEKYTFSPDWWGLGCLIYEMIQGQSPFRKRkERVK 209
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1846-1947 2.30e-14

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: 75.51  E-value: 2.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSG---AKGFGGTEGFMAPEIIRyNGEE 1922
Cdd:cd05583   111 ALEHLHKLGIIYRDIKLENILL---------DSEG---HVVLTDFGLSKEFLPGEndrAYSFCGTIEYMAPEVVR-GGSD 177
                          90       100
                  ....*....|....*....|....*
gi 442620116 1923 EYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd05583   178 GHDKAVDWWSLGVLTYELLTGASPF 202
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
1782-1998 2.34e-14

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: 76.19  E-value: 2.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTL-KHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYR------------RSGAHMGPHTFQTLVLQAARA 1846
Cdd:cd05088    57 ELEVLCKLgHHPNIINLLGACEHRgyLYLAIEYAPHGNLLDFLRKSRvletdpafaianSTASTLSSQQLLHFAADVARG 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHRRRIIYRDLKSENVLVWElpqphtedsprNLVhIKIADYGISRQTAPSGAKGFGGTE-GFMAPEIIRYNgeeEYT 1925
Cdd:cd05088   137 MDYLSQKQFIHRDLAARNILVGE-----------NYV-AKIADFGLSRGQEVYVKKTMGRLPvRWMAIESLNYS---VYT 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1926 EKVDCFSFGMFIYENISL-RQPFEGH--ESIKECILEGSRpaltqreTQFPTCC----LDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd05088   202 TNSDVWSYGVLLWEIVSLgGTPYCGMtcAELYEKLPQGYR-------LEKPLNCddevYDLMRQCWREKPYERPSFAQIL 274
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1779-1999 2.44e-14

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 75.55  E-value: 2.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPL-------VGIcikpLALVLELAPLGGLDALLRHyrRSGAHMGPHTFQTLVLQAARAIEYLH 1851
Cdd:cd08223    46 AEQEAKLLSKLKHPNIVSYkesfegeDGF----LYIVMGFCEGGDLYTRLKE--QKGVLLEERQVVEWFVQIAMALQYMH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVwelpqphtedSPRNLvhIKIADYGISR--QTAPSGAKGFGGTEGFMAPEIIrynGEEEYTEKVD 1929
Cdd:cd08223   120 ERNILHRDLKTQNIFL----------TKSNI--IKVGDLGIARvlESSSDMATTLIGTPYYMSPELF---SNKPYNHKSD 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1930 CFSFGMFIYENISLRQPFEGHE--SIKECILEGSRPALTqreTQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd08223   185 VWALGCCVYEMATLKHAFNAKDmnSLVYKILEGKLPPMP---KQYSPELGELIKAMLHQDPEKRPSVKRILR 253
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
1752-1998 2.93e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 76.79  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1752 SALMAFKVAVGKWDRDPLQHSCKayctarqELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDallrhyrrsGA 1829
Cdd:PLN00034   99 GRLYALKVIYGNHEDTVRRQICR-------EIEILRDVNHPNVVKCHDMFDHngEIQVLLEFMDGGSLE---------GT 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1830 HMGPHTFQT-LVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISR---QTA-PSGAKgf 1904
Cdd:PLN00034  163 HIADEQFLAdVARQILSGIAYLHRRHIVHRDIKPSNLLI---------NSAKN---VKIADFGVSRilaQTMdPCNSS-- 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1905 GGTEGFMAPEII-------RYNGeeeYTEkvDCFSFGMFIYENISLRQPF----EGHESIKECILEGSR----PALTQRE 1969
Cdd:PLN00034  229 VGTIAYMSPERIntdlnhgAYDG---YAG--DIWSLGVSILEFYLGRFPFgvgrQGDWASLMCAICMSQppeaPATASRE 303
                         250       260       270
                  ....*....|....*....|....*....|
gi 442620116 1970 -TQFPTCCLdlmvlcwHEQPRRRPTASQIV 1998
Cdd:PLN00034  304 fRHFISCCL-------QREPAKRWSAMQLL 326
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
1693-1959 2.97e-14

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: 76.56  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1693 DIPDKHTIPSeciikgsLLGRGAFGFVFKANCKVRGARsfkpVAMKMLqpvppgARAKESALmafkvavgkwdrdplqHS 1772
Cdd:cd07851    12 EVPDRYQNLS-------PVGSGAYGQVCSAFDTKTGRK----VAIKKL------SRPFQSAI----------------HA 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1773 CKAYctarQELAVLLTLKHPNIVPLVGICIKPLAL-----VLELAPLGG--LDALLRHYRRSGAHMgphtfQTLVLQAAR 1845
Cdd:cd07851    59 KRTY----RELRLLKHMKHENVIGLLDVFTPASSLedfqdVYLVTHLMGadLNNIVKCQKLSDDHI-----QFLVYQILR 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTApSGAKGFGGTEGFMAPEIIrYNgEEEYT 1925
Cdd:cd07851   130 GLKYIHSAGIIHRDLKPSNLAV-------NEDC-----ELKILDFGLARHTD-DEMTGYVATRWYRAPEIM-LN-WMHYN 194
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 442620116 1926 EKVDCFSFGMFIYENISLRQPFEGHESIKE--CILE 1959
Cdd:cd07851   195 QTVDIWSVGCIMAELLTGKTLFPGSDHIDQlkRIMN 230
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
1779-2001 3.02e-14

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: 75.71  E-value: 3.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRH--------YRRSgahmgphtfqtLVLQAARAIE 1848
Cdd:cd14042    49 VLKELKHMRDLQHDNLTRFIGACVDPpnICILTEYCPKGSLQDILENedikldwmFRYS-----------LIHDIVKGMH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHRRRIIYR-DLKSENVLV---WELpqphtedsprnlvhiKIADYGIS--RQTAPSGAKGFGGTEGF--MAPEIIRYNG 1920
Cdd:cd14042   118 YLHDSEIKSHgNLKSSNCVVdsrFVL---------------KITDFGLHsfRSGQEPPDDSHAYYAKLlwTAPELLRDPN 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1921 EEEY-TEKVDCFSFGMFIYEnISLRQ-PF--EGHE-SIKECILE----GS----RPALTqrETQFPTCCLDLMVLCWHEQ 1987
Cdd:cd14042   183 PPPPgTQKGDVYSFGIILQE-IATRQgPFyeEGPDlSPKEIIKKkvrnGEkppfRPSLD--ELECPDEVLSLMQRCWAED 259
                         250
                  ....*....|....
gi 442620116 1988 PRRRPTASQIVSIL 2001
Cdd:cd14042   260 PEERPDFSTLRNKL 273
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
1780-1964 3.04e-14

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 75.53  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPL------VGICIKPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRR 1853
Cdd:cd14031    57 KEEAEMLKGLQHPNIVRFydswesVLKGKKCIVLVTELMTSGTLKTYLKRFKV----MKPKVLRSWCRQILKGLQFLHTR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 R--IIYRDLKSENVLVwelpqphteDSPRNlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIryngEEEYTEKVDCF 1931
Cdd:cd14031   133 TppIIHRDLKCDNIFI---------TGPTG--SVKIGDLGLATLMRTSFAKSVIGTPEFMAPEMY----EEHYDESVDVY 197
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 442620116 1932 SFGMFIYENISLRQPF---EGHESIKECILEGSRPA 1964
Cdd:cd14031   198 AFGMCMLEMATSEYPYsecQNAAQIYRKVTSGIKPA 233
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1769-1999 3.66e-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: 75.01  E-value: 3.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1769 LQHSCKAYCTARQELAVLLTLKHPNIVPLvgiciKP-------LALVLELAPLGGLDALLRHYRrsGAHMGPHTFQTLVL 1841
Cdd:cd08219    35 LPKSSSAVEDSRKEAVLLAKMKHPNIVAF-----KEsfeadghLYIVMEYCDGGDLMQKIKLQR--GKLFPEDTILQWFV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1842 QAARAIEYLHRRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAKG--FGGTEGFMAPEIIRyn 1919
Cdd:cd08219   108 QMCLGVQHIHEKRVLHRDIKSKNIFL-------TQNG-----KVKLGDFGSARLLTSPGAYActYVGTPYYVPPEIWE-- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 gEEEYTEKVDCFSFGMFIYENISLRQPFEGHeSIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd08219   174 -NMPYNNKSDIWSLGCILYELCTLKHPFQAN-SWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKRNPRSRPSATTILS 251
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
1758-1960 3.86e-14

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: 74.74  E-value: 3.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWDRDPLQHS--CKAYctarQELAVLLTLKHPNIVPL--VGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGP 1833
Cdd:cd14071    27 EVAIKIIDKSQLDEEnlKKIY----REVQIMKMLNHPHIIKLyqVMETKDMLYLVTEYASNGEIFDYLAQHGRMSEKEAR 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1834 HTFQTLVLqaarAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISRQTAPSGA-KGFGGTEGFMA 1912
Cdd:cd14071   103 KKFWQILS----AVEYCHKRHIVHRDLKAENLLL---------DANMN---IKIADFGFSNFFKPGELlKTWCGSPPYAA 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 442620116 1913 PEIirYNGEEEYTEKVDCFSFGMFIYENISLRQPFEGH--ESIKECILEG 1960
Cdd:cd14071   167 PEV--FEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGStlQTLRDRVLSG 214
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
1711-1947 3.87e-14

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: 75.14  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKA---NCKVRGArsFKPVAMKMLQPVppgarakesalmafkvavgkwdrDPLQhsckayctarQELAVLL 1787
Cdd:cd06624    16 LGKGTFGVVYAArdlSTQVRIA--IKEIPERDSREV-----------------------QPLH----------EEIALHS 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRH----YRRSGAHMGPHTFQTLvlqaaRAIEYLHRRRIIYRDLK 1861
Cdd:cd06624    61 RLSHKNIVQYLGSVSEDgfFKIFMEQVPGGSLSALLRSkwgpLKDNENTIGYYTKQIL-----EGLKYLHDNKIVHRDIK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphtedsprNLVH--IKIADYGISRQTA---PSgAKGFGGTEGFMAPEIIRyNGEEEYTEKVDCFSFGMF 1936
Cdd:cd06624   136 GDNVLV-------------NTYSgvVKISDFGTSKRLAginPC-TETFTGTLQYMAPEVID-KGQRGYGPPADIWSLGCT 200
                         250
                  ....*....|.
gi 442620116 1937 IYENISLRQPF 1947
Cdd:cd06624   201 IIEMATGKPPF 211
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
1709-1974 4.42e-14

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: 75.05  E-value: 4.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKA-NCKvrgarSFKPVAMKMLQPVPpgarakesalmafkvavgKWDRDPLQHSCKaycTARQELAVLL 1787
Cdd:cd13990     6 NLLGKGGFSEVYKAfDLV-----EQRYVACKIHQLNK------------------DWSEEKKQNYIK---HALREYEIHK 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPL---VGICIKPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYL--HRRRIIYRDLKS 1862
Cdd:cd13990    60 SLDHPRIVKLydvFEIDTDSFCTVLEYCDGNDLDFYLKQHKS----IPEREARSIIMQVVSALKYLneIKPPIIHYDLKP 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphteDSPRNLVHIKIADYGISRQ-TAPSGAKG-------FGGTEGFMAPEIIRYNGEE-EYTEKVDCFSF 1933
Cdd:cd13990   136 GNILL---------HSGNVSGEIKITDFGLSKImDDESYNSDgmeltsqGAGTYWYLPPECFVVGKTPpKISSKVDVWSV 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 442620116 1934 GMFIYENISLRQPFeGHESIKECILEgSRPALTQRETQFPT 1974
Cdd:cd13990   207 GVIFYQMLYGRKPF-GHNQSQEAILE-ENTILKATEVEFPS 245
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
1781-1997 4.58e-14

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: 74.99  E-value: 4.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP----LALVLELAPLGGLDALLRHYRRSgAHMGPHTFQTLVLqaarAIEYLHRRRII 1856
Cdd:cd14200    72 QEIAILKKLDHVNIVKLIEVLDDPaednLYMVFDLLRKGPVMEVPSDKPFS-EDQARLYFRDIVL----GIEYLHYQKIV 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFG 1934
Cdd:cd14200   147 HRDIKPSNLLL-------GDDG-----HVKIADFGVSNQFEGNDALlsSTAGTPAFMAPETLSDSGQSFSGKALDVWAMG 214
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1935 MFIYENISLRQPFeghesIKECILE-----GSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14200   215 VTLYCFVYGKCPF-----IDEFILAlhnkiKNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEI 277
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
1780-2001 4.90e-14

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: 74.94  E-value: 4.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICI----KPLALVLELAPLGGL-DALLRHyrrsgaHMGPHTFQTLVLQAARAIEYLHRRR 1854
Cdd:cd05080    54 KQEIDILKTLYHENIVKYKGCCSeqggKSLQLIMEYVPLGSLrDYLPKH------SIGLAQLLLFAQQICEGMAYLHSQH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTaPSGAKGFGGTEG------FMAPEIIRyngEEEYTEKV 1928
Cdd:cd05080   128 YIHRDLAARNVLL---------DNDR---LVKIGDFGLAKAV-PEGHEYYRVREDgdspvfWYAPECLK---EYKFYYAS 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1929 DCFSFGMFIYE-------NISLRQPFEGHESIKECILEGSR-PALTQRETQFP---TCCLD---LMVLCWHEQPRRRPTA 1994
Cdd:cd05080   192 DVWSFGVTLYEllthcdsSQSPPTKFLEMIGIAQGQMTVVRlIELLERGERLPcpdKCPQEvyhLMKNCWETEASFRPTF 271

                  ....*..
gi 442620116 1995 SQIVSIL 2001
Cdd:cd05080   272 ENLIPIL 278
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
1782-1997 5.19e-14

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: 74.25  E-value: 5.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP---LALVLELAPLGGLDALLRHYRRSgaHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd05082    49 EASVMTQLRHSNLVQLLGVIVEEkggLYIVTEYMAKGSLVDYLRSRGRS--VLGGDCLLKFSLDVCEAMEYLEGNNFVHR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphTEDsprNLVhiKIADYGISRQTAPSGAKGFGGTEgFMAPEIIRyngEEEYTEKVDCFSFGMFIY 1938
Cdd:cd05082   127 DLAARNVLV-------SED---NVA--KVSDFGLTKEASSTQDTGKLPVK-WTAPEALR---EKKFSTKSDVWSFGILLW 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1939 ENISL-RQPFEgHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd05082   191 EIYSFgRVPYP-RIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAAMRPSFLQL 249
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
1710-1934 5.61e-14

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


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 74.65  E-value: 5.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPVppgarakesalmafkvavgkWDRDPlqhsckaycTARQELAVLLTL 1789
Cdd:cd06608    13 VIGEGTYGKVYKA----RHKKTGQLAAIKIMDII--------------------EDEEE---------EIKLEINILRKF 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 -KHPNIVPLVGICIKP--------LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDL 1860
Cdd:cd06608    60 sNHPNIATFYGAFIKKdppggddqLWLVMEYCGGGSVTDLVKGLRKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDI 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1861 KSENVLVwelpqphTEDSprnlvHIKIADYGISRQ-TAPSGAKG-FGGTEGFMAPEII--RYNGEEEYTEKVDCFSFG 1934
Cdd:cd06608   140 KGQNILL-------TEEA-----EVKLVDFGVSAQlDSTLGRRNtFIGTPYWMAPEVIacDQQPDASYDARCDVWSLG 205
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
1709-1960 6.39e-14

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: 74.78  E-value: 6.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVfkanCKVRGARSFKPVAMKMLQpVPPGARAKESalmafkvavgkwdrdplQHsckayctARQELAVLLT 1788
Cdd:cd05612     7 KTIGTGTFGRV----HLVRDRISEHYYALKVMA-IPEVIRLKQE-----------------QH-------VHNEKRVLKE 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLqaarAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd05612    58 VSHPFIIRLFWTEHDQrfLYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVC----ALEYLHSKEIVYRDLKPENIL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphTEDSprnlvHIKIADYGISRQTAPSgAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd05612   134 L-------DKEG-----HIKLTDFGFAKKLRDR-TWTLCGTPEYLAPEVIQSKG---HNKAVDWWALGILIYEMLVGYPP 197
                         250
                  ....*....|....*.
gi 442620116 1947 FEGHE--SIKECILEG 1960
Cdd:cd05612   198 FFDDNpfGIYEKILAG 213
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1708-1948 6.93e-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: 73.98  E-value: 6.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPvppgARAKESALMAfkvavgkwdrdplqhsckaycTARQELAVLL 1787
Cdd:cd14663     5 GRTLGEGTFAKVKFA----RNTKTGESVAIKIIDK----EQVAREGMVE---------------------QIKREIAIMK 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPL--VGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVlqaaRAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14663    56 LLRHPNIVELheVMATKTKIFFVMELVTGGELFSKIAKNGRLKEDKARKYFQQLI----DAVDYCHSRGVFHRDLKPENL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphteDSPRNLvhiKIADYGISRQTAPSGAKG----FGGTEGFMAPEIIRYNGEEEYteKVDCFSFGMFIYENI 1941
Cdd:cd14663   132 LL---------DEDGNL---KISDFGLSALSEQFRQDGllhtTCGTPNYVAPEVLARRGYDGA--KADIWSCGVILFVLL 197

                  ....*..
gi 442620116 1942 SLRQPFE 1948
Cdd:cd14663   198 AGYLPFD 204
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1782-1947 7.17e-14

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: 74.61  E-value: 7.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPL--VGICIKPLA------LVLELAPLGGLDALLRHYRRS-GAHMGPhtFQTLVLQAARAIEYLHR 1852
Cdd:cd14038    42 EIQIMKRLNHPNVVAArdVPEGLQKLApndlplLAMEYCQGGDLRKYLNQFENCcGLREGA--ILTLLSDISSALRYLHE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 RRIIYRDLKSENVLVwelpqphtEDSPRNLVHiKIADYGISRQTAPSG-AKGFGGTEGFMAPEIIRyngEEEYTEKVDCF 1931
Cdd:cd14038   120 NRIIHRDLKPENIVL--------QQGEQRLIH-KIIDLGYAKELDQGSlCTSFVGTLQYLAPELLE---QQKYTVTVDYW 187
                         170
                  ....*....|....*.
gi 442620116 1932 SFGMFIYENISLRQPF 1947
Cdd:cd14038   188 SFGTLAFECITGFRPF 203
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
1780-1999 7.24e-14

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: 73.96  E-value: 7.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPL--VGICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQtlvlQAARAIEYLHRRRIIY 1857
Cdd:cd14073    49 RREIEIMSSLNHPHIIRIyeVFENKDKIVIVMEYASGGELYDYISERRRLPEREARRIFR----QIVSAVHYCHKNGVVH 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLvweLPQPHTedsprnlvhIKIADYGISR--------QTapsgakgFGGTEGFMAPEIIryNGEEEYTEKVD 1929
Cdd:cd14073   125 RDLKLENIL---LDQNGN---------AKIADFGLSNlyskdkllQT-------FCGSPLYASPEIV--NGTPYQGPEVD 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1930 CFSFGMFIYENISLRQPFEG--HESIKECILEGSrpaltQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14073   184 CWSLGVLLYTLVYGTMPFDGsdFKRLVKQISSGD-----YREPTQPSDASGLIRWMLTVNPKRRATIEDIAN 250
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
1782-1938 8.55e-14

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: 73.90  E-value: 8.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGL-DAL---LRHYRRSGAHMgphtfqtlVLQAARAIEYLHRRRI 1855
Cdd:cd14095    48 EVAILRRVKHPNIVQLIEEYDTDteLYLVMELVKGGDLfDAItssTKFTERDASRM--------VTDLAQALKYLHSLSI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVWElpqphTEDSPRNLvhiKIADYGISrQTAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGM 1935
Cdd:cd14095   120 VHRDIKPENLLVVE-----HEDGSKSL---KLADFGLA-TEVKEPLFTVCGTPTYVAPEILAETG---YGLKVDIWAAGV 187

                  ...
gi 442620116 1936 FIY 1938
Cdd:cd14095   188 ITY 190
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
1734-1955 9.00e-14

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: 75.08  E-value: 9.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1734 PVAMKMLQPVPPGAR----AKESALMAFKVAVGKWDRdPLQHSCKAYCTARqELAVLLTLKHPNIVPLVGICIKPLAL-- 1807
Cdd:cd07877    16 PERYQNLSPVGSGAYgsvcAAFDTKTGLRVAVKKLSR-PFQSIIHAKRTYR-ELRLLKHMKHENVIGLLDVFTPARSLee 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1808 ---VLELAPLGG--LDALLRHYRRSGAHMgphtfQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphTEDsprnl 1882
Cdd:cd07877    94 fndVYLVTHLMGadLNNIVKCQKLTDDHV-----QFLIYQILRGLKYIHSADIIHRDLKPSNLAV-------NED----- 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1883 VHIKIADYGISRQTAPSgAKGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07877   157 CELKILDFGLARHTDDE-MTGYVATRWYRAPEIML--NWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQ 226
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
1768-1999 1.00e-13

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: 73.39  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1768 PLQHSCKAycTARQELAVLLTLKHPNIVPLVGI--CIKPLALVLELAplgGLDALLRHYRRSGAhMGPHTFQTLVLQAAR 1845
Cdd:cd14107    36 PLRSSTRA--RAFQERDILARLSHRRLTCLLDQfeTRKTLILILELC---SSEELLDRLFLKGV-VTEAEVKLYIQQVLE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLvweLPQPHTEDsprnlvhIKIADYGISRQTAPSGAK--GFGGTEgFMAPEIIRyngEEE 1923
Cdd:cd14107   110 GIGYLHGMNILHLDIKPDNIL---MVSPTRED-------IKICDFGFAQEITPSEHQfsKYGSPE-FVAPEIVH---QEP 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFEGHE------SIKECILEGSRPALTQRETQfptcCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14107   176 VSAATDIWALGVIAYLSLTCHSPFAGENdratllNVAEGVVSWDTPEITHLSED----AKDFIKRVLQPDPEKRPSASEC 251

                  ..
gi 442620116 1998 VS 1999
Cdd:cd14107   252 LS 253
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
1710-1991 1.02e-13

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: 74.96  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKvrGARSFkpVAMKMLQpvppgaraKESALMafkvavgkwDRDplqhsckAYCTARQELAVLLTL 1789
Cdd:cd05619    12 MLGKGSFGKVFLAELK--GTNQF--FAIKALK--------KDVVLM---------DDD-------VECTMVEKRVLSLAW 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLALVLELAPLGGLDaLLRHYRRSgahmgpHTFQ--TLVLQAARAI---EYLHRRRIIYRDLKSEN 1864
Cdd:cd05619    64 EHPFLTHLFCTFQTKENLFFVMEYLNGGD-LMFHIQSC------HKFDlpRATFYAAEIIcglQFLHSKGIVYRDLKLDN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENIS 1942
Cdd:cd05619   137 ILL------------DKDGHIKIADFGMCKENMLGDAKtsTFCGTPDYIAPEILL---GQKYNTSVDWWSFGVLLYEMLI 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1943 LRQPFEGHEsiKECILEGSR------PALTQRETQfptcclDLMVLCWHEQPRRR 1991
Cdd:cd05619   202 GQSPFHGQD--EEELFQSIRmdnpfyPRWLEKEAK------DILVKLFVREPERR 248
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
1778-2001 1.02e-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: 73.74  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGL-DALLRH-------YRRSGAhmgphtfqtlvLQAARAI 1847
Cdd:cd14045    48 RIRKEVKQVRELDHPNLCKFIGGCIEvpNVAIITEYCPKGSLnDVLLNEdiplnwgFRFSFA-----------TDIARGM 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1848 EYLHRRRIIYRDLKSENVLV---WElpqphtedsprnlvhIKIADYGIS---RQTAPSGAKGFGG--TEGFMAPEIiRYN 1919
Cdd:cd14045   117 AYLHQHKIYHGRLKSSNCVIddrWV---------------CKIADYGLTtyrKEDGSENASGYQQrlMQVYLPPEN-HSN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 GEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIKECILEGSRPALTQRETQ----FPTCCLDLMVLCWHEQPRRRPTAS 1995
Cdd:cd14045   181 TDTEPTQATDVYSYAIILLEIATRNDPVPEDDYSLDEAWCPPLPELISGKTEnscpCPADYVELIRRCRKNNPAQRPTFE 260

                  ....*.
gi 442620116 1996 QIVSIL 2001
Cdd:cd14045   261 QIKKTL 266
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
1709-1998 1.09e-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: 74.00  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGARSFkpvAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLT 1788
Cdd:cd14052     6 ELIGSGEFSQVYKVSERVPTGKVY---AVKKLKPNYAGAKDRLRRL--------------------------EEVSILRE 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LK---HPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVlQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14052    57 LTldgHDNIVQLIDSWEYHghLYIQTELCENGSLDVFLSELGLLGRLDEFRVWKILV-ELSLGLRFIHDHHFVHLDLKPA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphTEDSprNLvhiKIADYGI-SRQTAPSGAKGFGGTEgFMAPEIIrynGEEEYTEKVDCFSFGMFIYE--- 1939
Cdd:cd14052   136 NVLI-------TFEG--TL---KIGDFGMaTVWPLIRGIEREGDRE-YIAPEIL---SEHMYDKPADIFSLGLILLEaaa 199
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1940 NISLrqPFEGHE-------------SIKECILEG-SRPALTQRETQ--FPTCCLDLM-VLCW--HEQPRRRPTASQIV 1998
Cdd:cd14052   200 NVVL--PDNGDAwqklrsgdlsdapRLSSTDLHSaSSPSSNPPPDPpnMPILSGSLDrVVRWmlSPEPDRRPTADDVL 275
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
1780-1947 1.09e-13

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: 73.93  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTL-KHPNIVPLVGICIKP--LALVLELAPLGGL-DALLRHYRRSGAHMgphtfQTLVLQAARAIEYLHRRRI 1855
Cdd:cd14093    56 RREIEILRQVsGHPNIIELHDVFESPtfIFLVFELCRKGELfDYLTEVVTLSEKKT-----RRIMRQLFEAVEFLHSLNI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIR---YNGEEEYTEKVDCF 1931
Cdd:cd14093   131 VHRDLKPENILL---------DDNLN---VKISDFGFATRLDEGEKlRELCGTPGYLAPEVLKcsmYDNAPGYGKEVDMW 198
                         170
                  ....*....|....*.
gi 442620116 1932 SFGMFIYENISLRQPF 1947
Cdd:cd14093   199 ACGVIMYTLLAGCPPF 214
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
1708-1998 1.21e-13

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: 73.54  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLQ--PVPPGARAKESALmafkvavgkwdrdplqhSCkayctarqELAV 1785
Cdd:cd06652     7 GKLLGQGAFGRVYLC----YDADTGRELAVKQVQfdPESPETSKEVNAL-----------------EC--------EIQL 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTLKHPNIVPLVGiCI-----KPLALVLELAPLGGLDALLRHYrrsGAhMGPHTFQTLVLQAARAIEYLHRRRIIYRDL 1860
Cdd:cd06652    58 LKNLLHERIVQYYG-CLrdpqeRTLSIFMEYMPGGSIKDQLKSY---GA-LTENVTRKYTRQILEGVHYLHSNMIVHRDI 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1861 KSENVLvwelpqphtEDSPRNlvhIKIADYGISR--QT---APSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGM 1935
Cdd:cd06652   133 KGANIL---------RDSVGN---VKLGDFGASKrlQTiclSGTGMKSVTGTPYWMSPEVISGEG---YGRKADIWSVGC 197
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1936 FIYENISLRQPFEGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQpRRRPTASQIV 1998
Cdd:cd06652   198 TVVEMLTEKPPWAEFEAMAAIFKIATQPTNPQLPAHVSDHCRDFLKRIFVEA-KLRPSADELL 259
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1782-1960 1.32e-13

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: 73.93  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGL-DALLRH--YRRSGAhmgphtfQTLVLQAARAIEYLHRRRII 1856
Cdd:cd14168    58 EIAVLRKIKHENIVALEDIYESPnhLYLVMQLVSGGELfDRIVEKgfYTEKDA-------STLIRQVLDAVYYLHRMGIV 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVWelpqphtedSPRNLVHIKIADYGISRQTAPSGAKGFG-GTEGFMAPEIIrynGEEEYTEKVDCFSFGM 1935
Cdd:cd14168   131 HRDLKPENLLYF---------SQDEESKIMISDFGLSKMEGKGDVMSTAcGTPGYVAPEVL---AQKPYSKAVDCWSIGV 198
                         170       180
                  ....*....|....*....|....*..
gi 442620116 1936 FIYENISLRQPF--EGHESIKECILEG 1960
Cdd:cd14168   199 IAYILLCGYPPFydENDSKLFEQILKA 225
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
1783-1997 1.33e-13

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: 73.21  E-value: 1.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1783 LAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRH--------YRRSgahmgphtfqtLVLQAARAIEYLHR 1852
Cdd:cd14043    47 FSKLRELRHENVNLFLGLFVDCgiLAIVSEHCSRGSLEDLLRNddmkldwmFKSS-----------LLLDLIKGMRYLHH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 RRIIYRDLKSENVLVwelpqphteDSPRNLvhiKIADYGISR-------QTAPSGAKGFGGTegfmAPEIIR-YNGEEEY 1924
Cdd:cd14043   116 RGIVHGRLKSRNCVV---------DGRFVL---KITDYGYNEileaqnlPLPEPAPEELLWT----APELLRdPRLERRG 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1925 TEKVDCFSFGMFIYENISLRQPFEGHESIKECILEG-SRPALTQRET----QFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14043   180 TFPGDVFSFAIIMQEVIVRGAPYCMLGLSPEEIIEKvRSPPPLCRPSvsmdQAPLECIQLMKQCWSEAPERRPTFDQI 257
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
1734-1955 1.34e-13

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: 74.60  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1734 PVAMKMLQPVPPGARAKE-SAL---MAFKVAVGKWDRdPLQHSCKAYcTARQELAVLLTLKHPNIVPLVGICIKPLAL-- 1807
Cdd:cd07880    14 PDRYRDLKQVGSGAYGTVcSALdrrTGAKVAIKKLYR-PFQSELFAK-RAYRELRLLKHMKHENVIGLLDVFTPDLSLdr 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1808 ---VLELAPLGGLD--ALLRHYRrsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphTEDsprnl 1882
Cdd:cd07880    92 fhdFYLVMPFMGTDlgKLMKHEK-----LSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAV-------NED----- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1883 VHIKIADYGISRQTaPSGAKGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07880   155 CELKILDFGLARQT-DSEMTGYVVTRWYRAPEVIL--NWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQ 224
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
1710-1953 1.34e-13

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: 73.69  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGarsfKPVAMKMlqpVPPGARAKEsalmafkvavgkwdrdplqhsckayctarQELAVLLTL 1789
Cdd:cd14137    11 VIGSGSFGVVYQAKLLETG----EVVAIKK---VLQDKRYKN-----------------------------RELQIMRRL 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP--------LALVLELAPLGgLDALLRHYRRSGAHMGP-----HTFQTLvlqaaRAIEYLHRRRII 1856
Cdd:cd14137    55 KHPNIVKLKYFFYSSgekkdevyLNLVMEYMPET-LYRVIRHYSKNKQTIPIiyvklYSYQLF-----RGLAYLHSLGIC 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphtedSPRNLVhIKIADYGiSrqtapsgAKgfggtegFM----------------APEIIRynG 1920
Cdd:cd14137   129 HRDIKPQNLLV----------DPETGV-LKLCDFG-S-------AK-------RLvpgepnvsyicsryyrAPELIF--G 180
                         250       260       270
                  ....*....|....*....|....*....|....
gi 442620116 1921 EEEYTEKVDCFSFGMFIYENIsLRQP-FEGHESI 1953
Cdd:cd14137   181 ATDYTTAIDIWSAGCVLAELL-LGQPlFPGESSV 213
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
1781-2001 1.52e-13

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: 73.03  E-value: 1.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK-PLALVLELAPLGGLDALLRHyrRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd14203    39 EEAQIMKKLRHDKLVQLYAVVSEePIYIVTEFMSKGSLLDFLKD--GEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVWElpqphtedsprNLVhIKIADYGISR------QTAPSGAKgFggTEGFMAPEIIRYNgeeEYTEKVDCFSF 1933
Cdd:cd14203   117 LRAANILVGD-----------NLV-CKIADFGLARliedneYTARQGAK-F--PIKWTAPEAALYG---RFTIKSDVWSF 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1934 GMFIYENISL-RQPFEG--HESIKECILEGSRPALTQretQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14203   179 GILLTELVTKgRVPYPGmnNREVLEQVERGYRMPCPP---GCPESLHELMCQCWRKDPEERPTFEYLQSFL 246
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
1700-1999 1.63e-13

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: 73.53  E-value: 1.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCKvrGARSFKPVAMKMLQPVPPGARAKESALMAFKVAVGKwdrdplQHSCKaycta 1779
Cdd:cd05062     3 VAREKITMSRELGQGSFGMVYEGIAK--GVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMK------EFNCH----- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 rqelavlltlkhpNIVPLVGICIK--PLALVLELAPLGGLDALLRHYR---RSGAHMGPHTFQTLVLQA---ARAIEYLH 1851
Cdd:cd05062    70 -------------HVVRLLGVVSQgqPTLVIMELMTRGDLKSYLRSLRpemENNPVQAPPSLKKMIQMAgeiADGMAYLN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVwelpqphTEDsprnlVHIKIADYGISRQTAPS-----GAKGFGGTEgFMAPEIIRyngEEEYTE 1926
Cdd:cd05062   137 ANKFVHRDLAARNCMV-------AED-----FTVKIGDFGMTRDIYETdyyrkGGKGLLPVR-WMSPESLK---DGVFTT 200
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1927 KVDCFSFGMFIYENISL-RQPFEG--HESIKECILEGsrpALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd05062   201 YSDVWSFGVVLWEIATLaEQPYQGmsNEQVLRFVMEG---GLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIIS 273
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
1711-2009 1.88e-13

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: 72.93  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvppgARAKESALMAFkvavgkwdrdplqhsckayctaRQELAVLLTLK 1790
Cdd:cd14154     1 LGKGFFGQAIKVTHRETG----EVMVMKEL------IRFDEEAQRNF----------------------LKEVKVMRSLD 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRsgahmgPHTFQTLVLQA---ARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14154    49 HPNVLKFIGVLYKdkKLNLITEYIPGGTLKDVLKDMAR------PLPWAQRVRFAkdiASGMAYLHSMNIIHRDLNSHNC 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphtedspRNLVHIKIADYGISR-----QTAPSGAKGFG-----------------GTEGFMAPEIIryNGeEE 1923
Cdd:cd14154   123 LV------------REDKTVVVADFGLARliveeRLPSGNMSPSEtlrhlkspdrkkrytvvGNPYWMAPEML--NG-RS 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1924 YTEKVDCFSFGMFIYENIslrqpfeGH-ESIKECILEGSRPALTQRE------TQFPTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd14154   188 YDEKVDIFSFGIVLCEII-------GRvEADPDYLPRTKDFGLNVDSfrekfcAGCPPPFFKLAFLCCDLDPEKRPPFET 260
                         330
                  ....*....|...
gi 442620116 1997 IVSILSAPeCIHL 2009
Cdd:cd14154   261 LEEWLEAL-YLHL 272
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
1709-1997 2.13e-13

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: 73.00  E-value: 2.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGARSFKPVAMKMLQpvppgarakesalmafkvavgkwdrdplQHSCKAYCTARQELAVLLT 1788
Cdd:cd05081    10 SQLGKGNFGSVELCRYDPLGDNTGALVAVKQLQ----------------------------HSGPDQQRDFQREIQILKA 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKP----LALVLELAPLGGL-DALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd05081    62 LHSDFIVKYRGVSYGPgrrsLRLVMEYLPSGCLrDFLQRHRAR----LDASRLLLYSSQICKGMEYLGSRRCVHRDLAAR 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphtedspRNLVHIKIADYGISRqTAPSGAKGF-----GGTEGF-MAPEIIRYNgeeEYTEKVDCFSFGMFI 1937
Cdd:cd05081   138 NILV------------ESEAHVKIADFGLAK-LLPLDKDYYvvrepGQSPIFwYAPESLSDN---IFSRQSDVWSFGVVL 201
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1938 YENISL----RQPFEGHESIKECilEGSRPAL---------TQRETQFPTCCLD---LMVLCWHEQPRRRPTASQI 1997
Cdd:cd05081   202 YELFTYcdksCSPSAEFLRMMGC--ERDVPALcrllelleeGQRLPAPPACPAEvheLMKLCWAPSPQDRPSFSAL 275
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
1709-1934 3.60e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 73.33  E-value: 3.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPVppgarakesalmafkvavgkwDRDPLqhSCKAycTARqELAVLLT 1788
Cdd:cd07834     6 KPIGSGAYGVVCSA----YDKRTGRKVAIKKISNV---------------------FDDLI--DAKR--ILR-EIKILRH 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGIcIKP--------LALVLELaplggLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDL 1860
Cdd:cd07834    56 LKHENIIGLLDI-LRPpspeefndVYIVTEL-----METDLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDL 129
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1861 KSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAKGFgGTEG-----FMAPEIIRynGEEEYTEKVDCFSFG 1934
Cdd:cd07834   130 KPSNILV-------NSNC-----DLKICDFGLARGVDPDEDKGF-LTEYvvtrwYRAPELLL--SSKKYTKAIDIWSVG 193
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
1758-1999 4.00e-13

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: 71.60  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWDRDPLQHscKAYCTARQELAVLLTLKHPNIVPL--VGICIKPLALVLELAPlGGLdalLRHYRRSGAHMGPHT 1835
Cdd:cd14075    29 KVAIKILDKTKLDQ--KTQRLLSREISSMEKLHHPNIIRLyeVVETLSKLHLVMEYAS-GGE---LYTKISTEGKLSESE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1836 FQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGA-KGFGGTEGFMAPE 1914
Cdd:cd14075   103 AKPLFAQIVSAVKHMHENNIIHRDLKAENVFY---------ASNN---CVKVGDFGFSTHAKRGETlNTFCGSPPYAAPE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1915 IIRyngEEEYT-EKVDCFSFGMFIYENISLRQPFEGHE--SIKECILEGSrpaltqreTQFPTC----CLDLMVLCWHEQ 1987
Cdd:cd14075   171 LFK---DEHYIgIYVDIWALGVLLYFMVTGVMPFRAETvaKLKKCILEGT--------YTIPSYvsepCQELIRGILQPV 239
                         250
                  ....*....|..
gi 442620116 1988 PRRRPTASQIVS 1999
Cdd:cd14075   240 PSDRYSIDEIKN 251
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1711-1938 4.11e-13

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 72.23  E-value: 4.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAncKVRGarSFKPVAMKMlqpVPPGA-RAKESALmafkvavgkwdrdplqhsckayctaRQELAVLLTL 1789
Cdd:cd14169    11 LGEGAFSEVVLA--QERG--SQRLVALKC---IPKKAlRGKEAMV-------------------------ENEIAVLRRI 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRsGAHMGPHTFQtLVLQAARAIEYLHRRRIIYRDLKSENvLVWE 1869
Cdd:cd14169    59 NHENIVSLEDIYESPTHLYLAMELVTGGELFDRIIER-GSYTEKDASQ-LIGQVLQAVKYLHQLGIVHRDLKPEN-LLYA 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1870 LPqphTEDSprnlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIY 1938
Cdd:cd14169   136 TP---FEDS-----KIMISDFGLSKIEAQGMLSTACGTPGYVAPELLE---QKPYGKAVDVWAIGVISY 193
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
1711-1997 4.21e-13

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: 72.18  E-value: 4.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARsfkpVAMK-MLQPVPpgarakesalmafkvavgKWDRdplqhsckayCTARQELAVLLTL 1789
Cdd:cd07830     7 LGDGTFGSVYLARNKETGEL----VAIKkMKKKFY------------------SWEE----------CMNLREVKSLRKL 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 K-HPNIVPLVGICI--KPLALVLELAPlGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd07830    55 NeHPNIVKLKEVFRenDELYFVFEYME-GNLYQLMK--DRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLL 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphtedSPRNLVhiKIADYGISRQTAPSgaKGFG---GTEGFMAPEIIRYNGeeEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd07830   132 V----------SGPEVV--KIADFGLAREIRSR--PPYTdyvSTRWYRAPEILLRST--SYSSPVDIWALGCIMAELYTL 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1944 RQPFEGHESIKE-----CIL---------EGSRPAlTQRETQFPTC---------------CLDLMVLCWHEQPRRRPTA 1994
Cdd:cd07830   196 RPLFPGSSEIDQlykicSVLgtptkqdwpEGYKLA-SKLGFRFPQFaptslhqlipnaspeAIDLIKDMLRWDPKKRPTA 274

                  ...
gi 442620116 1995 SQI 1997
Cdd:cd07830   275 SQA 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-143 4.28e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.29  E-value: 4.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   20 LRTAVISGDERTVRVLLAAlGTErqiiVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGH 99
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEA-GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 442620116  100 LGIARLMLDHFPElIQQPTVERWLPLHAACINGHIKLLELLISY 143
Cdd:COG0666   199 LEIVKLLLEAGAD-VNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
1781-1991 4.29e-13

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: 71.55  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14121    44 TEIELLKKLKHPHIVELKDFQWdeEHIYLIMEYCSGGDLSRFIRSRRT----LPESTVRRFLQQLASALQFLREHNISHM 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELPQPhtedsprnlvHIKIADYGISRQTAPSG-AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFI 1937
Cdd:cd14121   120 DLKPQNLLLSSRYNP----------VLKLADFGFAQHLKPNDeAHSLRGSPLYMAPEMIL---KKKYDARVDLWSVGVIL 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1938 YENISLRQPF------EGHESIKEcilegSRPALTQRETQFPTCCLDLMVLCWHEQPRRR 1991
Cdd:cd14121   187 YECLFGRAPFasrsfeELEEKIRS-----SKPIEIPTRPELSADCRDLLLRLLQRDPDRR 241
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1778-1956 4.80e-13

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: 72.38  E-value: 4.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSgaHMGPHTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd14179    48 TQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLKGGELLERIKKKQ--HFSETEASHIMRKLVSAVSHMHDVGVVH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphtEDSPRNLvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGM 1935
Cdd:cd14179   126 RDLKPENLLF--------TDESDNS-EIKIIDFGFARLKPPDNQplKTPCFTLHYAAPELLNYNG---YDESCDLWSLGV 193
                         170       180
                  ....*....|....*....|.
gi 442620116 1936 FIYENISLRQPFEGHESIKEC 1956
Cdd:cd14179   194 ILYTMLSGQVPFQCHDKSLTC 214
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
1714-1953 4.94e-13

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDC2L1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 72.26  E-value: 4.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1714 GAFGFVFKANCKVRGarsfKPVAMKMLQpvppgaraKESALMAFKVavgkwdrdplqhsckaycTARQELAVLLTLKHPN 1793
Cdd:cd07843    16 GTYGVVYRARDKKTG----EIVALKKLK--------MEKEKEGFPI------------------TSLREINILLKLQHPN 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1794 IVPL----VGICIKPLALVLELaplggldalLRHYRRSGAHMGPHTFQ-----TLVLQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd07843    66 IVTVkevvVGSNLDKIYMVMEY---------VEHDLKSLMETMKQPFLqsevkCLMLQLLSGVAHLHDNWILHRDLKTSN 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphtedspRNLVHIKIADYGISRQtapsgakgFGG----------TEGFMAPEIIRynGEEEYTEKVDCFSFG 1934
Cdd:cd07843   137 LLL------------NNRGILKICDFGLARE--------YGSplkpytqlvvTLWYRAPELLL--GAKEYSTAIDMWSVG 194
                         250
                  ....*....|....*....
gi 442620116 1935 MFIYENISLRQPFEGHESI 1953
Cdd:cd07843   195 CIFAELLTKKPLFPGKSEI 213
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
1711-1998 5.13e-13

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: 71.98  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckvrgarsfkpvamkmlqpvppgaRAKESALMAFKVAVGKWDRDPLQHsckaYCTarqELAVLLTLK 1790
Cdd:cd06643    13 LGDGAFGKVYKA-------------------------QNKETGILAAAKVIDTKSEEELED----YMV---EIDILASCD 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICI--KPLALVLELAPLGGLDALLRHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd06643    61 HPNIVKLLDAFYyeNNLWILIEFCAGGAVDAVMLELERP---LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILF- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEII--RYNGEEEYTEKVDCFSFGMFIYENISLR 1944
Cdd:cd06643   137 ------TLDG-----DIKLADFGVSAKNTRTLQRrdSFIGTPYWMAPEVVmcETSKDRPYDYKADVWSLGVTLIEMAQIE 205
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1945 QPFEGHESIKECI-LEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06643   206 PPHHELNPMRVLLkIAKSEPPTLAQPSRWSPEFKDFLRKCLEKNVDARWTTSQLL 260
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
1689-1935 5.40e-13

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 71.97  E-value: 5.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1689 VIFADIPDkhtiPSECIIKGSLLGRGAFGFVFKANCKVRGARSfkpvAMKMLQPVppgarakesalmafkvavgkwdrdp 1768
Cdd:cd06638     8 IIFDSFPD----PSDTWEIIETIGKGTYGKVFKVLNKKNGSKA----AVKILDPI------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1769 lqHSCKAYCTArqELAVLLTLK-HPNIVPLVGICIKP-------LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLV 1840
Cdd:cd06638    55 --HDIDEEIEA--EYNILKALSdHPNVVKFYGMYYKKdvkngdqLWLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYIL 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1841 LQAARAIEYLHRRRIIYRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGISRQTAPSGAKGFG--GTEGFMAPEII-- 1916
Cdd:cd06638   131 HEALMGLQHLHVNKTIHRDVKGNNILL------TTEGG------VKLVDFGVSAQLTSTRLRRNTsvGTPFWMAPEVIac 198
                         250
                  ....*....|....*....
gi 442620116 1917 RYNGEEEYTEKVDCFSFGM 1935
Cdd:cd06638   199 EQQLDSTYDARCDVWSLGI 217
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
1705-1999 5.41e-13

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: 71.99  E-value: 5.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1705 IIKGSLLGRGAFGFVFKAncKVRGarsfkPVAMKMLQPVppgarakesalmafkvavgkwdrDPLQHSCKAYctaRQELA 1784
Cdd:cd14149    14 VMLSTRIGSGSFGTVYKG--KWHG-----DVAVKILKVV-----------------------DPTPEQFQAF---RNEVA 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVGICIKP-LALVLELAPLgglDALLRHYrrsgaHMGPHTFQTLVL-----QAARAIEYLHRRRIIYR 1858
Cdd:cd14149    61 VLRKTRHVNILLFMGYMTKDnLAIVTQWCEG---SSLYKHL-----HVQETKFQMFQLidiarQTAQGMDYLHAKNIIHR 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWElpqphtedsprnLVHIKIADYGI----SRQTAPSGAKGFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFG 1934
Cdd:cd14149   133 DMKSNNIFLHE------------GLTVKIGDFGLatvkSRWSGSQQVEQPTGSILWMAPEVIRMQDNNPFSFQSDVYSYG 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1935 MFIYENISLRQPFEGHESIKECILEGSR----PALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14149   201 IVLYELMTGELPYSHINNRDQIIFMVGRgyasPDLSKLYKNCPKAMKRLVADCIKKVKEERPLFPQILS 269
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
1711-2001 5.41e-13

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: 72.33  E-value: 5.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKanCKVRGARSFKpvAMKMLQPVPPGarakESALMAFKVAVGKWDRDPLQHSCKayctarqELAVLLTLK 1790
Cdd:cd05095    13 LGEGQFGEVHL--CEAEGMEKFM--DKDFALEVSEN----QPVLVAVKMLRADANKNARNDFLK-------EIKIMSRLK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICI--KPLALVLELAPLGGLDALL-RHYRRSGAHMGPHT-------FQTLVLQAARAIEYLHRRRIIYRDL 1860
Cdd:cd05095    78 DPNIIRLLAVCItdDPLCMITEYMENGDLNQFLsRQQPEGQLALPSNAltvsysdLRFMAAQIASGMKYLSSLNFVHRDL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1861 KSENVLVwelpqphtedsPRNLVhIKIADYGISRQTAPSGAKGFGGTegfmAPEIIRYNGEE-----EYTEKVDCFSFGM 1935
Cdd:cd05095   158 ATRNCLV-----------GKNYT-IKIADFGMSRNLYSGDYYRIQGR----AVLPIRWMSWEsillgKFTTASDVWAFGV 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1936 FIYENISL--RQPFE--GHESIKECILEGSRPALTQRETQFPTCCLD----LMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05095   222 TLWETLTFcrEQPYSqlSDEQVIENTGEFFRDQGRQTYLPQPALCPDsvykLMLSCWRRDTKDRPSFQEIHTLL 295
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
1701-1998 5.98e-13

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: 72.38  E-value: 5.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECIIKGSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPvpPGARAKEsalmafkvavgKWdRDPLQhsckayctar 1780
Cdd:cd06633    19 PEEIFVDLHEIGHGSFGAVYFA----TNSHTNEVVAIKKMSY--SGKQTNE-----------KW-QDIIK---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 qELAVLLTLKHPNIVPLVGICIKPLA--LVLELApLGGLDALLRHYRRSGAHMgphTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd06633    71 -EVKFLQQLKHPNTIEYKGCYLKDHTawLVMEYC-LGSASDLLEVHKKPLQEV---EIAAITHGALQGLAYLHSHNMIHR 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPsgAKGFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFGMFIY 1938
Cdd:cd06633   146 DIKAGNILLTEPGQ------------VKLADFGSASIASP--ANSFVGTPYWMAPEVILAMDEGQYDGKVDIWSLGITCI 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1939 ENISLRQPFEGHESIKEC--ILEGSRPALTQRETQFPTccLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06633   212 ELAERKPPLFNMNAMSALyhIAQNDSPTLQSNEWTDSF--RGFVDYCLQKIPQERPSSAELL 271
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
1708-1948 6.24e-13

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: 71.43  E-value: 6.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLqpvppgarakesalmaFKVAVGKwdrDPLQHSCkayctaRQELAVLL 1787
Cdd:cd14117    11 GRPLGKGKFGNVYLA----REKQSKFIVALKVL----------------FKSQIEK---EGVEHQL------RREIEIQS 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGIC--IKPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14117    62 HLRHPNILRLYNYFhdRKRIYLILEYAPRGELYKELQKHGR----FDEQRTATFMEELADALHYCHEKKVIHRDIKPENL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWELPQphtedsprnlvhIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd14117   138 LMGYKGE------------LKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIE---GRTHDEKVDLWCIGVLCYELLVGMP 202

                  ...
gi 442620116 1946 PFE 1948
Cdd:cd14117   203 PFE 205
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
1782-1993 6.38e-13

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: 71.31  E-value: 6.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRHyrRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd05148    52 EVQALKRLRHKHLISLFAVCSvgEPVYIITELMEKGSLLAFLRS--PEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVWElpqphtedsprNLVhIKIADYGISR------QTAPSGAKGFGGTegfmAPEIIRYNgeeEYTEKVDCFSF 1933
Cdd:cd05148   130 LAARNILVGE-----------DLV-CKVADFGLARlikedvYLSSDKKIPYKWT----APEAASHG---TFSTKSDVWSF 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1934 GMFIYENISLRQ-PFEG---HESIKEcILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPT 1993
Cdd:cd05148   191 GILLYEMFTYGQvPYPGmnnHEVYDQ-ITAGYR---MPCPAKCPQEIYKIMLECWAAEPEDRPS 250
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
1780-1947 6.46e-13

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 71.26  E-value: 6.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGI---------CIkplALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYL 1850
Cdd:cd14032    48 KEEAEMLKGLQHPNIVRFYDFwescakgkrCI---VLVTELMTSGTLKTYLKRFKV----MKPKVLRSWCRQILKGLLFL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRR--IIYRDLKSENVLVwelpqphteDSPRNlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIryngEEEYTEKV 1928
Cdd:cd14032   121 HTRTppIIHRDLKCDNIFI---------TGPTG--SVKIGDLGLATLKRASFAKSVIGTPEFMAPEMY----EEHYDESV 185
                         170
                  ....*....|....*....
gi 442620116 1929 DCFSFGMFIYENISLRQPF 1947
Cdd:cd14032   186 DVYAFGMCMLEMATSEYPY 204
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
1779-2030 6.74e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 73.51  E-value: 6.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVG--ICIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:PTZ00267  112 ARSELHCLAACDHFGIVKHFDdfKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMM 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVWelpqphtedsPRNLvhIKIADYGISRQTAPS----GAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFS 1932
Cdd:PTZ00267  192 HRDLKSANIFLM----------PTGI--IKLGDFGFSKQYSDSvsldVASSFCGTPYYLAPELWE---RKRYSKKADMWS 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1933 FGMFIYENISLRQPFEG--HESIKECILEGsrpaltqRETQFPTCCLD----LMVLCWHEQPRRRPTASQIVsilsapec 2006
Cdd:PTZ00267  257 LGVILYELLTLHRPFKGpsQREIMQQVLYG-------KYDPFPCPVSSgmkaLLDPLLSKNPALRPTTQQLL-------- 321
                         250       260
                  ....*....|....*....|....*.
gi 442620116 2007 ihlldvvampHSE--KIVCGVFQSLV 2030
Cdd:PTZ00267  322 ----------HTEflKYVANLFQDIV 337
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
1778-1955 7.96e-13

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: 71.30  E-value: 7.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIKP--LALVLELaplggLDALLRHYR---RSGAHMGPHTFQTLVLQAARAIEYLHR 1852
Cdd:cd07861    45 TAIREISLLKELQHPNIVCLEDVLMQEnrLYLVFEF-----LSMDLKKYLdslPKGKYMDAELVKSYLYQILQGILFCHS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 RRIIYRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISRqtapsgakGFG----------GTEGFMAPEIIRynGEE 1922
Cdd:cd07861   120 RRVLHRDLKPQNLLI---------DNKGV---IKLADFGLAR--------AFGipvrvythevVTLWYRAPEVLL--GSP 177
                         170       180       190
                  ....*....|....*....|....*....|...
gi 442620116 1923 EYTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07861   178 RYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQ 210
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
1780-1959 8.72e-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: 71.18  E-value: 8.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGL-DALL---RHYRRSGAHMgphtfqtlVLQAARAIEYLHRR 1853
Cdd:cd14183    52 QNEVSILRRVKHPNIVLLIEEMDMPteLYLVMELVKGGDLfDAITstnKYTERDASGM--------LYNLASAIKYLHSL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVWElpqphTEDSPRNLvhiKIADYGISrqTAPSGA-KGFGGTEGFMAPEIIrynGEEEYTEKVDCFS 1932
Cdd:cd14183   124 NIVHRDIKPENLLVYE-----HQDGSKSL---KLGDFGLA--TVVDGPlYTVCGTPTYVAPEII---AETGYGLKVDIWA 190
                         170       180
                  ....*....|....*....|....*..
gi 442620116 1933 FGMFIYENISLRQPFEGHESIKECILE 1959
Cdd:cd14183   191 AGVITYILLCGFPPFRGSGDDQEVLFD 217
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
1820-1951 9.15e-13

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: 71.95  E-value: 9.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1820 LLRHYRRSGAHMGPHTfqtlVLQAAR---AIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQT 1896
Cdd:cd05615    98 LMYHIQQVGKFKEPQA----VFYAAEisvGLFFLHKKGIIYRDLKLDNVML---------DSEG---HIKIADFGMCKEH 161
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1897 APSG--AKGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYENISLRQPFEGHE 1951
Cdd:cd05615   162 MVEGvtTRTFCGTPDYIAPEIIAY---QPYGRSVDWWAYGVLLYEMLAGQPPFDGED 215
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1710-1962 9.85e-13

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: 71.87  E-value: 9.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANcKVRGARSFKPVAMKMLQPVPPGARAKesalmafKVAVGKWDRDPLQHsckayctARQElAVLLTL 1789
Cdd:cd05614     7 VLGTGAYGKVFLVR-KVSGHDANKLYAMKVLRKAALVQKAK-------TVEHTRTERNVLEH-------VRQS-PFLVTL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPlvgiciKPLALVLELAPLGGLDALLrhYRRSgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwe 1869
Cdd:cd05614    71 HYAFQTD------AKLHLILDYVSGGELFTHL--YQRD--HFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILL-- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 lpqphteDSPRnlvHIKIADYGISRQTAPSGAK---GFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd05614   139 -------DSEG---HVVLTDFGLSKEFLTEEKErtySFCGTIEYMAPEIIR--GKSGHGKAVDWWSLGILMFELLTGASP 206
                         250
                  ....*....|....*.
gi 442620116 1947 FeghesikecILEGSR 1962
Cdd:cd05614   207 F---------TLEGEK 213
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1710-1963 1.03e-12

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: 71.18  E-value: 1.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANcKVRGARSFKPVAMKMLQPVPPGARAKESALMafkvavgKWDRDPLQHsckayctARQElAVLLTL 1789
Cdd:cd05613     7 VLGTGAYGKVFLVR-KVSGHDAGKLYAMKVLKKATIVQKAKTAEHT-------RTERQVLEH-------IRQS-PFLVTL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPlvgiciKPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwe 1869
Cdd:cd05613    71 HYAFQTD------TKLHLILDYINGGELFTHLSQRER----FTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILL-- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 lpqphteDSPRnlvHIKIADYGISRQ---TAPSGAKGFGGTEGFMAPEIIRyNGEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd05613   139 -------DSSG---HVVLTDFGLSKEfllDENERAYSFCGTIEYMAPEIVR-GGDSGHDKAVDWWSLGVLMYELLTGASP 207
                         250       260
                  ....*....|....*....|...
gi 442620116 1947 F------EGHESIKECILEGSRP 1963
Cdd:cd05613   208 FtvdgekNSQAEISRRILKSEPP 230
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
1711-2013 1.11e-12

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: 71.62  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckvRGARSFKPVAMKMLQPvpPGARAKEsalmafkvavgKWdRDPLQhsckayctarqELAVLLTLK 1790
Cdd:cd06635    33 IGHGSFGAVYFA----RDVRTSEVVAIKKMSY--SGKQSNE-----------KW-QDIIK-----------EVKFLQRIK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLA--LVLELApLGGLDALLRHYRRSGAHMgphTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVW 1868
Cdd:cd06635    84 HPNSIEYKGCYLREHTawLVMEYC-LGSASDLLEVHKKPLQEI---EIAAITHGALQGLAYLHSHNMIHRDIKAGNILLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 ELPQphtedsprnlvhIKIADYGISRQTAPsgAKGFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd06635   160 EPGQ------------VKLADFGSASIASP--ANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIELAERKPPLF 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1949 GHESIKEC--ILEGSRPALtqRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS----ILSAPECIhLLDVV 2013
Cdd:cd06635   226 NMNAMSALyhIAQNESPTL--QSNEWSDYFRNFVDSCLQKIPQDRPTSEELLKhmfvLRERPETV-LIDLI 293
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
1780-1997 1.12e-12

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: 70.36  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIKP----LALVLELApLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd14119    42 KREIQILRRLNHRNVIKLVDVLYNEekqkLYMVMEYC-VGGLQEMLD--SAPDKRLPIWQAHGYFVQLIDGLEYLHSQGI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGISRQT---APSGA-KGFGGTEGFMAPEIIryNGEEEYTE-KVDC 1930
Cdd:cd14119   119 IHKDIKPGNLLL------TTDGT------LKISDFGVAEALdlfAEDDTcTTSQGSPAFQPPEIA--NGQDSFSGfKVDI 184
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1931 FSFGMFIYENISLRQPFEG------HESIKECilegsrpaltqrETQFPTCC----LDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14119   185 WSAGVTLYNMTTGKYPFEGdniyklFENIGKG------------EYTIPDDVdpdlQDLLRGMLEKDPEKRFTIEQI 249
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
1701-1998 1.12e-12

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: 70.86  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECIIKGSLLGRGAFGFVFKanckvrgarsfkpvamkmlqpvppGARAKESALMAFKVAVGKWDRDPLQhsckaycTAR 1780
Cdd:cd06642     2 PEELFTKLERIGKGSFGEVYK------------------------GIDNRTKEVVAIKIIDLEEAEDEIE-------DIQ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDAL--LRHYRRSGAHMGphtfqTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd06642    51 QEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSALdlLKPGPLEETYIA-----TILREILKGLDYLHSERKIHR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMF 1936
Cdd:cd06642   126 DIKAANVLLSEQGD------------VKLADFGVAGQLTDTQIKrnTFVGTPFWMAPEVIK---QSAYDFKADIWSLGIT 190
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1937 IYENISLRQPFEGHESIKECIL--EGSRPALtqrETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06642   191 AIELAKGEPPNSDLHPMRVLFLipKNSPPTL---EGQHSKPFKEFVEACLNKDPRFRPTAKELL 251
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
1696-2001 1.14e-12

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: 70.87  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1696 DKHTIPSECIIKGSLLGRGAFGFVFKANCKvrgarSFKPVAMKMLQPvppGARAKESALmafkvavgkwdrdplqhscka 1775
Cdd:cd05070     2 DVWEIPRESLQLIKRLGNGQFGEVWMGTWN-----GNTKVAIKTLKP---GTMSPESFL--------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1776 yctarQELAVLLTLKHPNIVPLVGICIK-PLALVLELAPLGGLDALLRHyrRSGAHMGPHTFQTLVLQAARAIEYLHRRR 1854
Cdd:cd05070    53 -----EEAQIMKKLKHDKLVQLYAVVSEePIYIVTEYMSKGSLLDFLKD--GEGRALKLPNLVDMAAQVAAGMAYIERMN 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISR------QTAPSGAKgfgGTEGFMAPEIIRYNgeeEYTEKV 1928
Cdd:cd05070   126 YIHRDLRSANILV------------GNGLICKIADFGLARliedneYTARQGAK---FPIKWTAPEAALYG---RFTIKS 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1929 DCFSFGMFIYENISL-RQPFEG--HESIKECILEGSRPALTQretQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05070   188 DVWSFGILLTELVTKgRVPYPGmnNREVLEQVERGYRMPCPQ---DCPISLHELMIHCWKKDPEERPTFEYLQGFL 260
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
1734-1955 1.15e-12

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: 72.00  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1734 PVAMKMLQPVPPGARAkeSALMAF------KVAVGKWDRdPLQHSCKAYCTARqELAVLLTLKHPNIVPLVGI-----CI 1802
Cdd:cd07878    14 PERYQNLTPVGSGAYG--SVCSAYdtrlrqKVAVKKLSR-PFQSLIHARRTYR-ELRLLKHMKHENVIGLLDVftpatSI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1803 KPLALVLELAPLGG--LDALLRHYRRSGAHMgphtfQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphTEDspr 1880
Cdd:cd07878    90 ENFNEVYLVTNLMGadLNNIVKCQKLSDEHV-----QFLIYQLLRGLKYIHSAGIIHRDLKPSNVAV-------NED--- 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1881 nlVHIKIADYGISRQTAPSgAKGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07878   155 --CELRILDFGLARQADDE-MTGYVATRWYRAPEIML--NWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQ 224
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
1782-1955 1.33e-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: 70.36  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGI--CIKPLALVLELAPLGGL-DALLRHYRrsgahMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14185    48 EILIIKSLSHPNIVKLFEVyeTEKEIYLILEYVRGGDLfDAIIESVK-----FTEHDAALMIIDLCEALVYIHSKHIVHR 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqPHTEDSPRNLvhiKIADYGISRQ-TAPSGAkgFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFI 1937
Cdd:cd14185   123 DLKPENLLV-----QHNPDKSTTL---KLADFGLAKYvTGPIFT--VCGTPTYVAPEILSEKG---YGLEVDMWAAGVIL 189
                         170
                  ....*....|....*...
gi 442620116 1938 YENISLRQPFEGHESIKE 1955
Cdd:cd14185   190 YILLCGFPPFRSPERDQE 207
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1781-1960 1.53e-12

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 71.39  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLvgICI----KPLALVLELApLGGldALLRHYRRSGA---HMGPHTFQTLVLqaarAIEYLHRR 1853
Cdd:PTZ00263   67 QEKSILMELSHPFIVNM--MCSfqdeNRVYFLLEFV-VGG--ELFTHLRKAGRfpnDVAKFYHAELVL----AFEYLHSK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTaPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSF 1933
Cdd:PTZ00263  138 DIIYRDLKPENLLL------------DNKGHVKVTDFGFAKKV-PDRTFTLCGTPEYLAPEVIQSKG---HGKAVDWWTM 201
                         170       180
                  ....*....|....*....|....*....
gi 442620116 1934 GMFIYENISLRQPF--EGHESIKECILEG 1960
Cdd:PTZ00263  202 GVLLYEFIAGYPPFfdDTPFRIYEKILAG 230
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
1709-1948 1.58e-12

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: 69.87  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVrgarSFKPVAMKMLQPVPPGARAKESalmafkvavgkwdrdplqhsckayctarqELAVLLT 1788
Cdd:cd14087     7 ALIGRGSFSRVVRVEHRV----TRQPYAIKMIETKCRGREVCES-----------------------------ELNVLRR 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGI--CIKPLALVLELAPLGGLdallrhYRRSGAHmGPHTFQ--TLVLQAA-RAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14087    54 VRHTNIIQLIEVfeTKERVYMVMELATGGEL------FDRIIAK-GSFTERdaTRVLQMVlDGVKYLHGLGITHRDLKPE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVWElpqphtedsPRNLVHIKIADYGIS--RQTAPSG-AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYEN 1940
Cdd:cd14087   127 NLLYYH---------PGPDSKIMITDFGLAstRKKGPNClMKTTCGTPEYIAPEILL---RKPYTQSVDMWAVGVIAYIL 194

                  ....*...
gi 442620116 1941 ISLRQPFE 1948
Cdd:cd14087   195 LSGTMPFD 202
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
554-870 1.73e-12

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.89  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  554 LNVAFNLLRDLPVPPMQTSSSLLSLDKLNLQSFEEPPSNKPRNVTQQRLTHRNLWSATLDITDNDMKWQHEQDLGDGKTA 633
Cdd:COG4886     6 LSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  634 GVGSSQLSSLNIANNLFTSIPAALPCLAvNLTRLNMSYNSLRSMGHVTSYPATLKQLDLSHNEIScwpSLPritesdphl 713
Cdd:COG4886    86 LLGLTDLGDLTNLTELDLSGNEELSNLT-NLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLT---DLP--------- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  714 lcyscvqlpegrdddyktasskgssssatsfraSVLKSvcrhrrhlrLEALRTLILADNLLTRIQLStddattLFNesed 793
Cdd:COG4886   153 ---------------------------------EPLGN---------LTNLKSLDLSNNQLTDLPEE------LGN---- 180
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116  794 adwsvvgvnrskviFPNLSMLDMTNNCLKEIPASLHELSSLSVLNISGNvNITELPPHLGLLSRLWNLNTRGCLLQE 870
Cdd:COG4886   181 --------------LTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGN-QLTDLPEPLANLTNLETLDLSNNQLTD 242
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
1700-2001 1.85e-12

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: 69.90  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCKVRGARSFkPVAMKMLQPvppGARAKESalmafkvavgkwdRDPLQhsckaycta 1779
Cdd:cd05065     1 IDVSCVKIEEVIGAGEFGEVCRGRLKLPGKREI-FVAIKTLKS---GYTEKQR-------------RDFLS--------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 rqELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHyrrsgaHMGPHTFQTLV--LQA-ARAIEYLHRRR 1854
Cdd:cd05065    55 --EASIMGQFDHPNIIHLEGVVTKsrPVMIITEFMENGALDSFLRQ------NDGQFTVIQLVgmLRGiAAGMKYLSEMN 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphtedsPRNLVhIKIADYGISR-----QTAPSGAKGFGGTEG--FMAPEIIRYngeEEYTEK 1927
Cdd:cd05065   127 YVHRDLAARNILV-----------NSNLV-CKVSDFGLSRfleddTSDPTYTSSLGGKIPirWTAPEAIAY---RKFTSA 191
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1928 VDCFSFGMFIYENISL-RQPF--EGHESIKECILEGSR-PAltqrETQFPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05065   192 SDVWSYGIVMWEVMSYgERPYwdMSNQDVINAIEQDYRlPP----PMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTL 265
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
1703-1958 2.70e-12

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


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 70.41  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1703 ECIikgSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgarakesalmafkvavgkwdrdplqhscKAYCTARQE 1782
Cdd:cd05589     2 RCI---AVLGRGHFGKVLLAEYKPTG----ELFAIKALK--------------------------------KGDIIARDE 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1783 LAVLLTLK----------HPNIVPLVGiCIKP---LALVLELAPlGGldALLRHyrrsgAHMGPHTFQTLVLQAA---RA 1846
Cdd:cd05589    43 VESLMCEKrifetvnsarHPFLVNLFA-CFQTpehVCFVMEYAA-GG--DLMMH-----IHEDVFSEPRAVFYAAcvvLG 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEY 1924
Cdd:cd05589   114 LQFLHEHKIVYRDLKLDNLLL---------DTEG---YVKIADFGLCKEGMGFGDRtsTFCGTPEFLAPEVLT---DTSY 178
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 442620116 1925 TEKVDCFSFGMFIYENISLRQPFEG--HESIKECIL 1958
Cdd:cd05589   179 TRAVDWWGLGVLIYEMLVGESPFPGddEEEVFDSIV 214
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
454-565 2.82e-12

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 72.42  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  454 TAITRIDFSHNVLTSIPQELFHlvSLRYLNVAQNKITDLPA--PIGQTygcpvldELFLQDNQLTTLPA----------- 520
Cdd:PRK15370  262 SALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAhlPSGIT-------HLNVQSNSLTALPEtlppglktlea 332
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 442620116  521 ---AIFHL-----PALSILDVSNNKLQQLPFDLwrAPKLRELNVAFNLLRDLP 565
Cdd:PRK15370  333 genALTSLpaslpPELQVLDVSKNQITVLPETL--PPTITTLDVSRNALTNLP 383
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
1708-1948 3.17e-12

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: 69.22  E-value: 3.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGARsfkpVAMKMLqpvppgARAK-ESALMAFKVavgkwdrdplqhsckayctaRQELAVL 1786
Cdd:cd14079     7 GKTLGVGSFGKVKLAEHELTGHK----VAVKIL------NRQKiKSLDMEEKI--------------------RREIQIL 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIKP--LALVLELAPLGGL-DALLRHYRRSgAHMGPHTFQtlvlQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14079    57 KLFRHPHIIRLYEVIETPtdIFMVMEYVSGGELfDYIVQKGRLS-EDEARRFFQ----QIISGVEYCHRHMVVHRDLKPE 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphteDSPRNlvhIKIADYGISrQTAPSGA--KGFGGTEGFMAPEIIR---YNGEEeytekVDCFSFGMFIY 1938
Cdd:cd14079   132 NLLL---------DSNMN---VKIADFGLS-NIMRDGEflKTSCGSPNYAAPEVISgklYAGPE-----VDVWSCGVILY 193
                         250
                  ....*....|
gi 442620116 1939 ENISLRQPFE 1948
Cdd:cd14079   194 ALLCGSLPFD 203
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
1711-1997 3.27e-12

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: 69.62  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKanCKVRGARSFkpvamkmlQPVPPGARAKESALMAFKvavgkwdrdplQHSCKAYCTAR----QELAVL 1786
Cdd:cd05097    13 LGEGQFGEVHL--CEAEGLAEF--------LGEGAPEFDGQPVLVAVK-----------MLRADVTKTARndflKEIKIM 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALL--RHYRRSGAHMG--PH-TFQTLV---LQAARAIEYLHRRRII 1856
Cdd:cd05097    72 SRLKNPNIIRLLGVCVSddPLCMITEYMENGDLNQFLsqREIESTFTHANniPSvSIANLLymaVQIASGMKYLASLNFV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYNgeeEYTEKVDCFS 1932
Cdd:cd05097   152 HRDLATRNCLV------------GNHYTIKIADFGMSRNLYSGDYYRIQGRAvlpiRWMAWESILLG---KFTTASDVWA 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1933 FGMFIYENISL--RQPFE--GHESIKECILEGSRPALTQ-RETQFPTC---CLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd05097   217 FGVTLWEMFTLckEQPYSllSDEQVIENTGEFFRNQGRQiYLSQTPLCpspVFKLMMRCWSRDIKDRPTFNKI 289
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1709-2001 3.42e-12

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 69.06  E-value: 3.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGarsfKPVAMKmlqpvppgaRAKesalmafkvavgkwdrdplQHSCKAyctaRQELAVLLT 1788
Cdd:cd14047    12 ELIGSGGFGQVFKAKHRIDG----KTYAIK---------RVK-------------------LNNEKA----EREVKALAK 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGI------CIKP------------LALVLELAPLGGLDALLRhyRRSGAHMGPHTFQTLVLQAARAIEYL 1850
Cdd:cd14047    56 LDHPNIVRYNGCwdgfdyDPETsssnssrsktkcLFIQMEFCEKGTLESWIE--KRNGEKLDKVLALEIFEQITKGVEYI 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYG-ISRQTAPSGAKGFGGTEGFMAPEIIrynGEEEYTEKVD 1929
Cdd:cd14047   134 HSKKLIHRDLKPSNIFLVDTGK------------VKIGDFGlVTSLKNDGKRTKSKGTLSYMSPEQI---SSQDYGKEVD 198
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1930 CFSFGMFIYENISLRQpfEGHESIKEC--ILEGSRPALTQRETQFPTCCLDLMVlcwHEQPRRRPTASQIVSIL 2001
Cdd:cd14047   199 IYALGLILFELLHVCD--SAFEKSKFWtdLRNGILPDIFDKRYKIEKTIIKKML---SKKPEDRPNASEILRTL 267
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
1780-1964 3.43e-12

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: 69.69  E-value: 3.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIV--------PLVGIciKPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLH 1851
Cdd:cd14030    72 KEEAGMLKGLQHPNIVrfydswesTVKGK--KCIVLVTELMTSGTLKTYLKRFKV----MKIKVLRSWCRQILKGLQFLH 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRR--IIYRDLKSENVLVwelpqphteDSPRNlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIryngEEEYTEKVD 1929
Cdd:cd14030   146 TRTppIIHRDLKCDNIFI---------TGPTG--SVKIGDLGLATLKRASFAKSVIGTPEFMAPEMY----EEKYDESVD 210
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 442620116 1930 CFSFGMFIYENISLRQPF---EGHESIKECILEGSRPA 1964
Cdd:cd14030   211 VYAFGMCMLEMATSEYPYsecQNAAQIYRRVTSGVKPA 248
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
1846-1948 3.71e-12

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 70.14  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEE 1923
Cdd:cd05588   108 ALNFLHEKGIIYRDLKLDNVLL---------DSEG---HIKLTDYGMCKEGLRPGdtTSTFCGTPNYIAPEILR---GED 172
                          90       100
                  ....*....|....*....|....*
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd05588   173 YGFSVDWWALGVLMFEMLAGRSPFD 197
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
1759-1993 3.72e-12

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 69.27  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1759 VAVGKwdrdpLQHSCKAYCTA-RQELAVLLTLKHPNIVPLVGICI----KPLALVLELAPLGGLDALLRHYRRSGAHMGP 1833
Cdd:cd14205    36 VAVKK-----LQHSTEEHLRDfEREIEILKSLQHDNIVKYKGVCYsagrRNLRLIMEYLPYGSLRDYLQKHKERIDHIKL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1834 HTFQTlvlQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRqTAPSGAKGFGGTEG---- 1909
Cdd:cd14205   111 LQYTS---QICKGMEYLGTKRYIHRDLATRNILV------------ENENRVKIGDFGLTK-VLPQDKEYYKVKEPgesp 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1910 --FMAPEIIRyngEEEYTEKVDCFSFG-----MFIYENISLRQPFE-----GHESIKECIL---------EGSRPAltqr 1968
Cdd:cd14205   175 ifWYAPESLT---ESKFSVASDVWSFGvvlyeLFTYIEKSKSPPAEfmrmiGNDKQGQMIVfhliellknNGRLPR---- 247
                         250       260
                  ....*....|....*....|....*....
gi 442620116 1969 etqfPTCCLD----LMVLCWHEQPRRRPT 1993
Cdd:cd14205   248 ----PDGCPDeiymIMTECWNNNVNQRPS 272
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
1839-1998 3.82e-12

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: 68.95  E-value: 3.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1839 LVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTaPSGAKGFGGTEGFMAPEIIry 1918
Cdd:cd13997   108 LLLQVALGLAFIHSKGIVHLDIKPDNIFI------------SNKGTCKIGDFGLATRL-ETSGDVEEGDSRYLAPELL-- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1919 NGEEEYTEKVDCFSFGMFIYE---NISLRQPFEGHESIKECILegSRPALTQRETQFPtcclDLMVLCWHEQPRRRPTAS 1995
Cdd:cd13997   173 NENYTHLPKADIFSLGVTVYEaatGEPLPRNGQQWQQLRQGKL--PLPPGLVLSQELT----RLLKVMLDPDPTRRPTAD 246

                  ...
gi 442620116 1996 QIV 1998
Cdd:cd13997   247 QLL 249
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
1710-1958 3.97e-12

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


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 70.11  E-value: 3.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKanckVRGARSFKPVAMKMLqpvppgaraKESALMAfkvavgkwdRDPLQHSCKayctarqELAVLLTL 1789
Cdd:cd05593    22 LLGKGTFGKVIL----VREKASGKYYAMKIL---------KKEVIIA---------KDEVAHTLT-------ESRVLKNT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPL-VGICIKP-LALVLELAPLGgldALLRHYRRSGAHMGPHTfQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd05593    73 RHPFLTSLkYSFQTKDrLCFVMEYVNGG---ELFFHLSRERVFSEDRT-RFYGAEIVSALDYLHSGKIVYRDLKLENLML 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 welpqphTEDSprnlvHIKIADYGISRQ--TAPSGAKGFGGTEGFMAPEIIRYNgeeEYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd05593   149 -------DKDG-----HIKITDFGLCKEgiTDAATMKTFCGTPEYLAPEVLEDN---DYGRAVDWWGLGVVMYEMMCGRL 213
                         250
                  ....*....|....*
gi 442620116 1946 PF--EGHESIKECIL 1958
Cdd:cd05593   214 PFynQDHEKLFELIL 228
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
1725-1958 4.91e-12

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: 69.55  E-value: 4.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1725 KVRGARSFKPVamkMLqpvppgARAKESA-LMAFKVAvgkwDRDPLQHSCKAYCTARQELAVLLTLKHPNIVPLVGICIK 1803
Cdd:cd05590     1 RVLGKGSFGKV---ML------ARLKESGrLYAVKVL----KKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCCFQT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1804 PLALVLELAPLGGLDaLLRHYRRSGAHMGPHTfQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqPHTEdsprnlv 1883
Cdd:cd05590    68 PDRLFFVMEFVNGGD-LMFHIQKSRRFDEARA-RFYAAEITSALMFLHDKGIIYRDLKLDNVLL-----DHEG------- 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1884 HIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEG--HESIKECIL 1958
Cdd:cd05590   134 HCKLADFGMCKEGIFNGktTSTFCGTPDYIAPEILQ---EMLYGPSVDWWAMGVLLYEMLCGHAPFEAenEDDLFEAIL 209
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
1817-1997 4.99e-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: 68.99  E-value: 4.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1817 LDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRR-RIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQ 1895
Cdd:cd06617    86 LDKFYKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ------------VKLCDFGISGY 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1896 TAPSGAKGF-GGTEGFMAPEiiRYNGEEE---YTEKVDCFSFGMFIYENISLRQPFEG----HESIKEcILEGSRPALTq 1967
Cdd:cd06617   154 LVDSVAKTIdAGCKPYMAPE--RINPELNqkgYDVKSDVWSLGITMIELATGRFPYDSwktpFQQLKQ-VVEEPSPQLP- 229
                         170       180       190
                  ....*....|....*....|....*....|
gi 442620116 1968 rETQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd06617   230 -AEKFSPEFQDFVNKCLKKNYKERPNYPEL 258
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
1782-1949 5.42e-12

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: 68.43  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPL--VGICIKPLALVLELAPLGGL-DALLRHYR---RSGAHMgphtFQTLVLqaarAIEYLHRRRI 1855
Cdd:cd14081    51 EIAIMKLIEHPNVLKLydVYENKKYLYLVLEYVSGGELfDYLVKKGRlteKEARKF----FRQIIS----ALDYCHSHSI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISR-QTAPSGAKGFGGTEGFMAPEIIR---YNGeeeytEKVDCF 1931
Cdd:cd14081   123 CHRDLKPENLLL---------DEKNN---IKIADFGMASlQPEGSLLETSCGSPHYACPEVIKgekYDG-----RKADIW 185
                         170
                  ....*....|....*...
gi 442620116 1932 SFGMFIYENISLRQPFEG 1949
Cdd:cd14081   186 SCGVILYALLVGALPFDD 203
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
1701-1998 5.56e-12

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: 68.95  E-value: 5.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECIIKGSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLQpvppgarakesalmafkvavgkwdrdpLQHSCKAYCTAR 1780
Cdd:cd06641     2 PEELFTKLEKIGKGSFGEVFKG----IDNRTQKVVAIKIID---------------------------LEEAEDEIEDIQ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALlrhyrrSGAHMGP---HTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd06641    51 QEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSAL------DLLEPGPldeTQIATILREILKGLDYLHSEKKIH 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVWElpqpHTEdsprnlvhIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGM 1935
Cdd:cd06641   125 RDIKAANVLLSE----HGE--------VKLADFGVAGQLTDTQIKrn*FVGTPFWMAPEVIK---QSAYDSKADIWSLGI 189
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1936 FIYENISLRQPFEGHESIKECIL--EGSRPALtqrETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06641   190 TAIELARGEPPHSELHPMKVLFLipKNNPPTL---EGNYSKPLKEFVEACLNKEPSFRPTAKELL 251
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
1696-1993 5.77e-12

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: 68.56  E-value: 5.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1696 DKHTIPSECIIKGSLLGRGAFGFVFKA--NCKVRgarsfkpVAMKMLQPvppGARAKESALmafkvavgkwdrdplqhsc 1773
Cdd:cd05071     2 DAWEIPRESLRLEVKLGQGCFGEVWMGtwNGTTR-------VAIKTLKP---GTMSPEAFL------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1774 kayctarQELAVLLTLKHPNIVPLVGICIK-PLALVLELAPLGGLDALLRHyrRSGAHMGPHTFQTLVLQAARAIEYLHR 1852
Cdd:cd05071    53 -------QEAQVMKKLRHEKLVQLYAVVSEePIYIVTEYMSKGSLLDFLKG--EMGKYLRLPQLVDMAAQIASGMAYVER 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 RRIIYRDLKSENVLVWElpqphtedsprNLVhIKIADYGISR------QTAPSGAKGfggTEGFMAPEIIRYNgeeEYTE 1926
Cdd:cd05071   124 MNYVHRDLRAANILVGE-----------NLV-CKVADFGLARliedneYTARQGAKF---PIKWTAPEAALYG---RFTI 185
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1927 KVDCFSFGMFIYE-NISLRQPFEGHESiKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPT 1993
Cdd:cd05071   186 KSDVWSFGILLTElTTKGRVPYPGMVN-REVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPT 252
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
1758-1948 5.86e-12

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: 68.66  E-value: 5.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWDRDPLQHSCKAYCTARqELAVLLTLKHPNIVPLVGI--CIKPLALVLELAPLGGL-DALLRHYRrsgahMGPH 1834
Cdd:cd14076    33 QVAIKLIRRDTQQENCQTSKIMR-EINILKGLTHPNIVRLLDVlkTKKYIGIVLEFVSGGELfDYILARRR-----LKDS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1835 TFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNLVhikIADYGISRQTAPSGAKGFG---GTEGFM 1911
Cdd:cd14076   107 VACRLFAQLISGVAYLHKKGVVHRDLKLENLLL---------DKNRNLV---ITDFGFANTFDHFNGDLMStscGSPCYA 174
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 442620116 1912 APEIIryNGEEEYT-EKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd14076   175 APELV--VSDSMYAgRKADIWSCGVILYAMLAGYLPFD 210
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
1781-1942 7.12e-12

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: 67.89  E-value: 7.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14155    37 REVQLMNRLSHPNILRFMGVCVHQgqLHALTEYINGGNLEQLLD----SNEPLSWTVRVKLALDIARGLSYLHSKGIFHR 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqPHTEDSPRNLVhikiADYGISRQTAPSGAKGFG----GTEGFMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd14155   113 DLTSKNCLI-----KRDENGYTAVV----GDFGLAEKIPDYSDGKEKlavvGSPYWMAPEVLR---GEPYNEKADVFSYG 180

                  ....*...
gi 442620116 1935 MFIYENIS 1942
Cdd:cd14155   181 IILCEIIA 188
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
1782-1947 7.21e-12

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: 68.24  E-value: 7.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVP-----LVGiciKPLALVLELAPLGGLDALLRHYRrsgahMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd06648    54 EVVIMRDYQHPNIVEmyssyLVG---DELWVVMEFLEGGALTDIVTHTR-----MNEEQIATVCRAVLKALSFLHSQGVI 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTA---PSgAKGFGGTEGFMAPEIIrynGEEEYTEKVDCFSF 1933
Cdd:cd06648   126 HRDIKSDSILL-------TSDG-----RVKLSDFGFCAQVSkevPR-RKSLVGTPYWMAPEVI---SRLPYGTEVDIWSL 189
                         170
                  ....*....|....
gi 442620116 1934 GMFIYENISLRQPF 1947
Cdd:cd06648   190 GIMVIEMVDGEPPY 203
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
1780-1950 7.31e-12

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: 68.70  E-value: 7.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLvLQAARAIEYLHRRR--I 1855
Cdd:cd14159    40 LTEVEKLSRFRHPNIVDLAGYSAQQgnYCLIYVYLPNGSLEDRLHCQVSCPCLSWSQRLHVL-LGTARAIQYLHSDSpsL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVWELPQPhtedsprnlvhiKIADYGISR----QTAPSGAKGFG------GTEGFMAPEIIRYNgeeEYT 1925
Cdd:cd14159   119 IHGDVKSSNILLDAALNP------------KLGDFGLARfsrrPKQPGMSSTLArtqtvrGTLAYLPEEYVKTG---TLS 183
                         170       180
                  ....*....|....*....|....*
gi 442620116 1926 EKVDCFSFGMFIYENISLRQPFEGH 1950
Cdd:cd14159   184 VEIDVYSFGVVLLELLTGRRAMEVD 208
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
1847-1949 7.41e-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: 68.82  E-value: 7.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHRRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQT--APSGAKGFGGTEGFMAPEIIRyngEEEY 1924
Cdd:cd05620   109 LQFLHSKGIIYRDLKLDNVML-------DRDG-----HIKIADFGMCKENvfGDNRASTFCGTPDYIAPEILQ---GLKY 173
                          90       100
                  ....*....|....*....|....*
gi 442620116 1925 TEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd05620   174 TFSVDWWSFGVLLYEMLIGQSPFHG 198
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
1782-1998 7.82e-12

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: 68.03  E-value: 7.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVP-----LVGiciKPLALVLELAPLGGLDALLrhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd06647    54 EILVMRENKNPNIVNyldsyLVG---DELWVVMEYLAGGSLTDVV-----TETCMDEGQIAAVCRECLQALEFLHSNQVI 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd06647   126 HRDIKSDNILL------GMDGS------VKLTDFGFCAQITPEQSKrsTMVGTPYWMAPEVVT---RKAYGPKVDIWSLG 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1935 MFIYENISLRQPFEGHESIKE--CILEGSRPALTQRETQFPTcCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06647   191 IMAIEMVEGEPPYLNENPLRAlyLIATNGTPELQNPEKLSAI-FRDFLNRCLEMDVEKRGSAKELL 255
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
1782-2003 7.85e-12

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 68.05  E-value: 7.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHyrrsgahMGPHTFQTLVLQA---ARAIEYLHRRRII 1856
Cdd:cd14222    40 EVKVMRSLDHPNVLKFIGVLYKDkrLNLLTEFIEGGTLKDFLRA-------DDPFPWQQKVSFAkgiASGMAYLHSMSII 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwELPQPhtedsprnlvhIKIADYGISR-----------QTAPSGAKGFG-----------GTEGFMAPE 1914
Cdd:cd14222   113 HRDLNSHNCLI-KLDKT-----------VVVADFGLSRliveekkkpppDKPTTKKRTLRkndrkkrytvvGNPYWMAPE 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1915 IIryNGeEEYTEKVDCFSFGMFIYENISlrQPFegheSIKECILEGSRPALTQR---ETQFPTCC----LDLMVLCWHEQ 1987
Cdd:cd14222   181 ML--NG-KSYDEKVDIFSFGIVLCEIIG--QVY----ADPDCLPRTLDFGLNVRlfwEKFVPKDCppafFPLAAICCRLE 251
                         250
                  ....*....|....*.
gi 442620116 1988 PRRRPTASQIVSILSA 2003
Cdd:cd14222   252 PDSRPAFSKLEDSFEA 267
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1779-1998 8.37e-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: 67.84  E-value: 8.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGG---LDALLRHYRrsgahmgpHTFQTLVL-----QAARAIEYL 1850
Cdd:cd08221    46 ALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGgnlHDKIAQQKN--------QLFPEEVVlwylyQIVSAVSHI 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVwelpqphtedSPRNLVhiKIADYGISRQ--TAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKV 1928
Cdd:cd08221   118 HKAGILHRDIKTLNIFL----------TKADLV--KLGDFGISKVldSESSMAESIVGTPYYMSPELVQ---GVKYNFKS 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1929 DCFSFGMFIYENISLRQPFEGHESIKEC--ILEGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd08221   183 DIWAVGCVLYELLTLKRTFDATNPLRLAvkIVQGEY---EDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELL 251
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
1696-1996 8.66e-12

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: 69.12  E-value: 8.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1696 DKHTIPSECIIKGslLGRGAFGFVFKANCKvrgaRSFKPVAMKmlqpvppgarakesalmafKVAvgkwdrDPLQHSCKA 1775
Cdd:cd07852     2 DKHILRRYEILKK--LGKGAYGIVWKAIDK----KTGEVVALK-------------------KIF------DAFRNATDA 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1776 YCTARqELAVLLTLK-HPNIVPLVGI----CIKPLALVLELaplggLDALLRHYRRSGAHMGPHTfQTLVLQAARAIEYL 1850
Cdd:cd07852    51 QRTFR-EIMFLQELNdHPNIIKLLNViraeNDKDIYLVFEY-----METDLHAVIRANILEDIHK-QYIMYQLLKALKYL 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVwelpqphteDSPrnlVHIKIADYGISRqTAPSGAKGFGG--------TEGFMAPEIIRynGEE 1922
Cdd:cd07852   124 HSGGVIHRDLKPSNILL---------NSD---CRVKLADFGLAR-SLSQLEEDDENpvltdyvaTRWYRAPEILL--GST 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1923 EYTEKVDCFSFGMFIYENISLRQPFEGH---------------------ESIK----ECILEgSRPALTQR--ETQFPTC 1975
Cdd:cd07852   189 RYTKGVDMWSVGCILGEMLLGKPLFPGTstlnqlekiievigrpsaediESIQspfaATMLE-SLPPSRPKslDELFPKA 267
                         330       340
                  ....*....|....*....|....
gi 442620116 1976 C---LDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd07852   268 SpdaLDLLKKLLVFNPNKRLTAEE 291
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
1789-2002 9.12e-12

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: 68.00  E-value: 9.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYR--RSGAHmGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd05042    52 LQHPNILQCLGQCVEaiPYLLVMEFCDLGDLKAYLRSERehERGDS-DTRTLQRMACEVAAGLAHLHKLNFVHSDLALRN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphTEDsprnlVHIKIADYGIS-------------------RQTAPSGAKGFGGTegFMAPEIIRYNgeeeyt 1925
Cdd:cd05042   131 CLL-------TSD-----LTVKIGDYGLAhsrykedyietddklwfplRWTAPELVTEFHDR--LLVVDQTKYS------ 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1926 ekvDCFSFGMFIYENISL-RQPFEGHES-------IKECILEGSRPALTQRETQFptcCLDLMVLCWhEQPRRRPTASQI 1997
Cdd:cd05042   191 ---NIWSLGVTLWELFENgAQPYSNLSDldvlaqvVREQDTKLPKPQLELPYSDR---WYEVLQFCW-LSPEQRPAAEDV 263

                  ....*
gi 442620116 1998 VSILS 2002
Cdd:cd05042   264 HLLLT 268
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1782-1997 9.52e-12

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: 68.30  E-value: 9.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKPLALVL-------ELAPLGGLDALLRHYRRSGAHMGPHTFQ-----TLVLQA-ARAIE 1848
Cdd:cd14049    55 EVKVLAGLQHPNIVGYHTAWMEHVQLMLyiqmqlcELSLWDWIVERNKRPCEEEFKSAPYTPVdvdvtTKILQQlLEGVT 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHRRRIIYRDLKSENVLVwelpqpHTEDsprnlVHIKIADYGIS---------RQTAPSGAKGFGGTEGF-----MAPE 1914
Cdd:cd14049   135 YIHSMGIVHRDLKPRNIFL------HGSD-----IHVRIGDFGLAcpdilqdgnDSTTMSRLNGLTHTSGVgtclyAAPE 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1915 iiRYNGeEEYTEKVDCFSFGMFIYEnisLRQPFEGHesikeciLEGSRPALTQRETQFPtCCLD--------LMVLCWHE 1986
Cdd:cd14049   204 --QLEG-SHYDFKSDMYSIGVILLE---LFQPFGTE-------MERAEVLTQLRNGQIP-KSLCkrwpvqakYIKLLTST 269
                         250
                  ....*....|.
gi 442620116 1987 QPRRRPTASQI 1997
Cdd:cd14049   270 EPSERPSASQL 280
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
1711-1939 1.01e-11

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: 68.55  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKmlqpvppgarakesalmafKVAVGKwDRD--PLqhsckaycTARQELAVLLT 1788
Cdd:cd07845    15 IGEGTYGIVYRARDTTSG----EIVALK-------------------KVRMDN-ERDgiPI--------SSLREITLLLN 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPL----VGICIKPLALVLE-----LAPLggLDALLRHYRRSgahmgphTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd07845    63 LRHPNIVELkevvVGKHLDSIFLVMEyceqdLASL--LDNMPTPFSES-------QVKCLMLQLLRGLQYLHENFIIHRD 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSgAKGFGG---TEGFMAPEIIRynGEEEYTEKVDCFSFGMF 1936
Cdd:cd07845   134 LKVSNLLL-------TDKG-----CLKIADFGLARTYGLP-AKPMTPkvvTLWYRAPELLL--GCTTYTTAIDMWAVGCI 198

                  ...
gi 442620116 1937 IYE 1939
Cdd:cd07845   199 LAE 201
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
1788-2002 1.04e-11

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: 67.71  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGIC--IKPLALVLELAPLGGLDALLRHYRRSGAHM-GPHTFQTLVLQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd05087    53 ALQHTNLLQCLAQCaeVTPYLLVMEFCPLGDLKGYLRSCRAAESMApDPLTLQRMACEVACGLLHLHRNNFVHSDLALRN 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphTEDsprnlVHIKIADYGIS----RQTAPSGAKGFGGTEGFMAPEII-RYNGE---EEYTEKVDCFSFGMF 1936
Cdd:cd05087   133 CLL-------TAD-----LTVKIGDYGLShckyKEDYFVTADQLWVPLRWIAPELVdEVHGNllvVDQTKQSNVWSLGVT 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1937 IYENISL-RQPFEGHE-------SIKECILEGSRPALtqrETQFPTCCLDLMVLCWHeQPRRRPTASQIVSILS 2002
Cdd:cd05087   201 IWELFELgNQPYRHYSdrqvltyTVREQQLKLPKPQL---KLSLAERWYEVMQFCWL-QPEQRPTAEEVHLLLS 270
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
1703-1955 1.07e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 68.14  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1703 ECIIKgslLGRGAFGFVFKANCKVRGARSfkpVAMKMLQpvppgARAKESALmafkvavgkwdrdPLQhsckaycTARqE 1782
Cdd:cd07862     4 ECVAE---IGEGAYGKVFKARDLKNGGRF---VALKRVR-----VQTGEEGM-------------PLS-------TIR-E 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1783 LAVLL---TLKHPNIVPLVGICI-------KPLALVLElaplgGLDALLRHYRRSGAHMG--PHTFQTLVLQAARAIEYL 1850
Cdd:cd07862    52 VAVLRhleTFEHPNVVRLFDVCTvsrtdreTKLTLVFE-----HVDQDLTTYLDKVPEPGvpTETIKDMMFQLLRGLDFL 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISR----QTAPSGAKgfgGTEGFMAPEIIRyngEEEYTE 1926
Cdd:cd07862   127 HSHRVVHRDLKPQNILVTSSGQ------------IKLADFGLARiysfQMALTSVV---VTLWYRAPEVLL---QSSYAT 188
                         250       260
                  ....*....|....*....|....*....
gi 442620116 1927 KVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07862   189 PVDLWSVGCIFAEMFRRKPLFRGSSDVDQ 217
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
1781-1955 1.28e-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: 68.02  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIV------PLVGICIKPLALV-LELAPLGGLDALLRHYRRSgahMGPHTFQTLVL--QAARAIEYLH 1851
Cdd:cd14039    40 HEIQIMKKLNHPNVVkacdvpEEMNFLVNDVPLLaMEYCSGGDLRKLLNKPENC---CGLKESQVLSLlsDIGSGIQYLH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVwelpqphtEDSPRNLVHiKIADYGISRQT-APSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDC 1930
Cdd:cd14039   117 ENKIIHRDLKPENIVL--------QEINGKIVH-KIIDLGYAKDLdQGSLCTSFVGTLQYLAPELFE---NKSYTVTVDY 184
                         170       180       190
                  ....*....|....*....|....*....|..
gi 442620116 1931 FSFGMFIYENIS-LR------QPFEGHESIKE 1955
Cdd:cd14039   185 WSFGTMVFECIAgFRpflhnlQPFTWHEKIKK 216
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
1805-1951 1.45e-11

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: 67.62  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLvlQAARAIEYLHRRRIIYRDLKSENVLVWELPQphtedsprnlvh 1884
Cdd:cd05607    77 LCLVMSLMNGGDLKYHIYNVGERGIEMERVIFYSA--QITCGILHLHSLKIVYRDMKPENVLLDDNGN------------ 142
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1885 IKIADYGISRQTaPSGA--KGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEGHE 1951
Cdd:cd05607   143 CRLSDLGLAVEV-KEGKpiTQRAGTNGYMAPEILK---EESYSYPVDWFAMGCSIYEMVAGRTPFRDHK 207
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
1710-1991 1.57e-11

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 68.07  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGARsfkpVAMKMLQPVPPGARAKESALMAfkvavgkwdrdplqhsckayctarqELAVLL-T 1788
Cdd:cd05603     2 VIGKGSFGKVLLAKRKCDGKF----YAVKVLQKKTILKKKEQNHIMA-------------------------ERNVLLkN 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKPLALVLELAPLGGLDaLLRHYRRSGAHMGPHTfQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd05603    53 LKHPFLVGLHYSFQTSEKLYFVLDYVNGGE-LFFHLQRERCFLEPRA-RFYAAEVASAIGYLHSLNIIYRDLKPENILL- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphteDSPRnlvHIKIADYGISRQ-TAPSGAKG-FGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd05603   130 --------DCQG---HVVLTDFGLCKEgMEPEETTStFCGTPEYLAPEVLR---KEPYDRTVDWWCLGAVLYEMLYGLPP 195
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 442620116 1947 FEGHE--SIKECILegSRPALTQRETQFPTCclDLMVLCWHEQPRRR 1991
Cdd:cd05603   196 FYSRDvsQMYDNIL--HKPLHLPGGKTVAAC--DLLQGLLHKDQRRR 238
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
1846-1958 1.60e-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: 68.52  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLH-RRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYNgee 1922
Cdd:cd05594   137 ALDYLHsEKNVVYRDLKLENLML-------DKDG-----HIKITDFGLCKEGIKDGAtmKTFCGTPEYLAPEVLEDN--- 201
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 442620116 1923 EYTEKVDCFSFGMFIYENISLRQPF--EGHESIKECIL 1958
Cdd:cd05594   202 DYGRAVDWWGLGVVMYEMMCGRLPFynQDHEKLFELIL 239
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
1711-1955 1.80e-11

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: 67.97  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARsfkpVAMKMLQ-PVPPGArakESALMAFkvavgkWDRDPLQHSCKAY-----CTArQELA 1784
Cdd:cd13977     8 VGRGSYGVVYEAVVRRTGAR----VAVKKIRcNAPENV---ELALREF------WALSSIQRQHPNViqleeCVL-QRDG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPN-----IVPLVGICIKP-----------LALVLELAPLGGLDALLRHYRRSgahmgPHTFQTLVLQAARAIE 1848
Cdd:cd13977    74 LAQRMSHGSsksdlYLLLVETSLKGercfdprsacyLWFVMEFCDGGDMNEYLLSRRPD-----RQTNTSFMLQLSSALA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHRRRIIYRDLKSENVLVwelpqPHTEDSPRnlvhIKIADYGISRQTAPSGAKGFG-------------GTEGFMAPEI 1915
Cdd:cd13977   149 FLHRNQIVHRDLKPDNILI-----SHKRGEPI----LKVADFGLSKVCSGSGLNPEEpanvnkhflssacGSDFYMAPEV 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 442620116 1916 irynGEEEYTEKVDCFSFGMFIYENISlRQPFEGHESIKE 1955
Cdd:cd13977   220 ----WEGHYTAKADIFALGIIIWAMVE-RITFRDGETKKE 254
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1782-1996 1.87e-11

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: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVL-LTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14106    57 EIAVLeLCKDCPRVVNLHEVYETRseLILILELAAGGELQTLLD----EEECLTEADVRRLMRQILEGVQYLHERNIVHL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphteDSPRNLVHIKIADYGISRQTAPsGAK--GFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMF 1936
Cdd:cd14106   133 DLKPQNILL---------TSEFPLGDIKLCDFGISRVIGE-GEEirEILGTPDYVAPEILSY---EPISLATDMWSIGVL 199
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1937 IYENISLRQPFEGhESIKECILEGSRPALTQRETQF---PTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd14106   200 TYVLLTGHSPFGG-DDKQETFLNISQCNLDFPEELFkdvSPLAIDFIKRLLVKDPEKRLTAKE 261
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
1711-1992 1.93e-11

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: 66.89  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSfkPVAMKMLqpvppgarakesalmafKVAVGKWDRDPLQhsckayctarQELAVLLTLK 1790
Cdd:cd05115    12 LGSGNFGCVKKGVYKMRKKQI--DVAIKVL-----------------KQGNEKAVRDEMM----------REAQIMHQLD 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGIC-IKPLALVLELAPLGGLDALLRHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwe 1869
Cdd:cd05115    63 NPYIVRMIGVCeAEALMLVMEMASGGPLNKFLSGKKDE---ITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLL-- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 lpqphtedspRNLVHIKIADYGISRQTAPSG----AKGFGGTE-GFMAPEIIRYNgeeEYTEKVDCFSFGMFIYENISLR 1944
Cdd:cd05115   138 ----------VNQHYAKISDFGLSKALGADDsyykARSAGKWPlKWYAPECINFR---KFSSRSDVWSYGVTMWEAFSYG 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1945 Q-PF---EGHESIKeCILEGSRPALTqreTQFPTCCLDLMVLCWHEQPRRRP 1992
Cdd:cd05115   205 QkPYkkmKGPEVMS-FIEQGKRMDCP---AECPPEMYALMSDCWIYKWEDRP 252
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1701-1998 1.94e-11

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: 67.21  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECiikgslLGRGAFGFVFKANCKVRGARsfkpVAMKMLQpVPPGARAKESALmafkvavgkwdrdplqhsckayctar 1780
Cdd:cd14048    10 PIQC------LGRGGFGVVFEAKNKVDDCN----YAVKRIR-LPNNELAREKVL-------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIV---------PLVGICIKP----LALVLELAPLGGLDALLRHyRRSGAHMGPHTFQTLVLQAARAI 1847
Cdd:cd14048    53 REVRALAKLDHPGIVryfnawlerPPEGWQEKMdevyLYIQMQLCRKENLKDWMNR-RCTMESRELFVCLNIFKQIASAV 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1848 EYLHRRRIIYRDLKSENVLVwelpqphTEDSPrnlvhIKIADYGIS------------RQTAPSGAKGFG--GTEGFMAP 1913
Cdd:cd14048   132 EYLHSKGLIHRDLKPSNVFF-------SLDDV-----VKVGDFGLVtamdqgepeqtvLTPMPAYAKHTGqvGTRLYMSP 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1914 EIIRYNgeeEYTEKVDCFSFGMFIYEnisLRQPFeGHESIKECILEGSR-----PALTQRETQFPTCCLDLMVLcwheQP 1988
Cdd:cd14048   200 EQIHGN---QYSEKVDIFALGLILFE---LIYSF-STQMERIRTLTDVRklkfpALFTNKYPEERDMVQQMLSP----SP 268
                         330
                  ....*....|
gi 442620116 1989 RRRPTASQIV 1998
Cdd:cd14048   269 SERPEAHEVI 278
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1788-1955 1.95e-11

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: 66.93  E-value: 1.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVlqaaRAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14665    52 SLRHPNIVRFKEVILTPthLAIVMEYAAGGELFERICNAGRFSEDEARFFFQQLI----SGVSYCHSMQICHRDLKLENT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWELPQPhtedsprnlvHIKIADYGISRQTA-PSGAKGFGGTEGFMAPEIIRyngEEEYTEKV-DCFSFGMFIYENISL 1943
Cdd:cd14665   128 LLDGSPAP----------RLKICDFGYSKSSVlHSQPKSTVGTPAYIAPEVLL---KKEYDGKIaDVWSCGVTLYVMLVG 194
                         170
                  ....*....|..
gi 442620116 1944 RQPFEGHESIKE 1955
Cdd:cd14665   195 AYPFEDPEEPRN 206
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
1775-1993 2.18e-11

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: 66.95  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1775 AYCTaRQELAVLLT-------LKHPNIVPLVGICIKPL--------ALVLELAPLGGLDALLRhYRRSG---AHMGPHTF 1836
Cdd:cd05075    38 AICT-RSEMEDFLSeavcmkeFDHPNVMRLIGVCLQNTesegypspVVILPFMKHGDLHSFLL-YSRLGdcpVYLPTQML 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1837 QTLVLQAARAIEYLHRRRIIYRDLKSENVLVWElpqphtedsprNLvHIKIADYGISRqtapsgaKGFGGT---EGFMAP 1913
Cdd:cd05075   116 VKFMTDIASGMEYLSSKNFIHRDLAARNCMLNE-----------NM-NVCVADFGLSK-------KIYNGDyyrQGRISK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1914 EIIRYNGEEE-----YTEKVDCFSFGMFIYEnISLR--QPFEGHES--IKECILEGSRpaLTQretqfPTCCLD----LM 1980
Cdd:cd05075   177 MPVKWIAIESladrvYTTKSDVWSFGVTMWE-IATRgqTPYPGVENseIYDYLRQGNR--LKQ-----PPDCLDglyeLM 248
                         250
                  ....*....|...
gi 442620116 1981 VLCWHEQPRRRPT 1993
Cdd:cd05075   249 SSCWLLNPKDRPS 261
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
1708-2001 2.46e-11

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: 66.57  E-value: 2.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKAnckvrgaRSFKPVAMKMLQPvppgARAKESALMAFKvavgkwdrdplqhsckayctarQELAVLL 1787
Cdd:cd14153     5 GELIGKGRFGQVYHG-------RWHGEVAIRLIDI----ERDNEEQLKAFK----------------------REVMAYR 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRrsgAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14153    52 QTRHENVVLFMGACMSPphLAIITSLCKGRTLYSVVRDAK---VVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNV 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphteDSPRnlvhIKIADYGIsrqTAPSGAKGFGGTEG----------FMAPEIIRY---NGEEE---YTEKVD 1929
Cdd:cd14153   129 FY---------DNGK----VVITDFGL---FTISGVLQAGRREDklriqsgwlcHLAPEIIRQlspETEEDklpFSKHSD 192
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1930 CFSFGMFIYENISLRQPFEGH--ESIKECILEGSRPALTQ----RETQfptcclDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14153   193 VFAFGTIWYELHAREWPFKTQpaEAIIWQVGSGMKPNLSQigmgKEIS------DILLFCWAYEQEERPTFSKLMEML 264
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
1846-1948 2.73e-11

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: 67.52  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRyngEEE 1923
Cdd:cd05591   108 ALMFLHRHGVIYRDLKLDNILL---------DAEG---HCKLADFGMCKEGILNGKttTTFCGTPDYIAPEILQ---ELE 172
                          90       100
                  ....*....|....*....|....*
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd05591   173 YGPSVDWWALGVLMYEMMAGQPPFE 197
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
1781-1999 2.76e-11

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: 66.34  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP---LALVLELAPLGgldALLRHYRRSGAhMGPHTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd14165    50 RELEILARLNHKSIIKTYEIFETSdgkVYIVMELGVQG---DLLEFIKLRGA-LPEDVARKMFHQLSSAIKYCHELDIVH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSG------AKGFGGTEGFMAPEIIRYngeEEYTEKV-DC 1930
Cdd:cd14165   126 RDLKCENLLL------------DKDFNIKLTDFGFSKRCLRDEngrivlSKTFCGSAAYAAPEVLQG---IPYDPRIyDI 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1931 FSFGMFIYENISLRQPFEgHESIKECIlegsRPALTQReTQFP-----TC-CLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14165   191 WSLGVILYIMVCGSMPYD-DSNVKKML----KIQKEHR-VRFPrsknlTSeCKDLIYRLLQPDVSQRLCIDEVLS 259
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
1701-1949 2.99e-11

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 67.39  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECIikgsllGRGAFGFVfkanCKVRGARSFKPVAMKmlqpvppgarakesalmafKVAvgkwdrdplqHSCKAYCTAR 1780
Cdd:cd07855     9 PIETI------GSGAYGVV----CSAIDTKSGQKVAIK-------------------KIP----------NAFDVVTTAK 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 Q---ELAVLLTLKHPNIVPLVGIcIKP---------LALVLELaplggLDALLRHYRRSGAHMGPHTFQTLVLQAARAIE 1848
Cdd:cd07855    50 RtlrELKILRHFKHDNIIAIRDI-LRPkvpyadfkdVYVVLDL-----MESDLHHIIHSDQPLTLEHIRYFLYQLLRGLK 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHRRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISR--QTAPSGAKGFG----GTEGFMAPEIIRYNGee 1922
Cdd:cd07855   124 YIHSANVIHRDLKPSNLLV-------NENC-----ELKIGDFGMARglCTSPEEHKYFMteyvATRWYRAPELMLSLP-- 189
                         250       260
                  ....*....|....*....|....*..
gi 442620116 1923 EYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd07855   190 EYTQAIDMWSVGCIFAEMLGRRQLFPG 216
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
1711-1963 3.13e-11

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: 67.21  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVfkanCKVRGARSFKPVAMK-MLQPVPPGARAKESAlmafkvavgkwdrdplqhsckayctarQELAVLLTL 1789
Cdd:cd07856    18 VGMGAFGLV----CSARDQLTGQNVAVKkIMKPFSTPVLAKRTY---------------------------RELKLLKHL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLALVLELAPLGGLDAllrHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVWE 1869
Cdd:cd07856    67 RHENIISLSDIFISPLEDIYFVTELLGTDL---HRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNE 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1870 lpqphtedsprnLVHIKIADYGISRQTAPSgAKGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd07856   144 ------------NCDLKICDFGLARIQDPQ-MTGYVSTRYYRAPEIML--TWQKYDVEVDIWSAGCIFAEMLEGKPLFPG 208
                         250
                  ....*....|....*...
gi 442620116 1950 HESIKE-CI---LEGSRP 1963
Cdd:cd07856   209 KDHVNQfSIiteLLGTPP 226
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
1701-1998 3.26e-11

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 66.61  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECIIKGSLLGRGAFGFVFKanckvrgarsfkpvamkmlqpvppGARAKESALMAFKVAVGKWDRDPLQhsckaycTAR 1780
Cdd:cd06640     2 PEELFTKLERIGKGSFGEVFK------------------------GIDNRTQQVVAIKIIDLEEAEDEIE-------DIQ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDAL--LRhyrrsgahMGP-HTFQ--TLVLQAARAIEYLHRRRI 1855
Cdd:cd06640    51 QEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSALdlLR--------AGPfDEFQiaTMLKEILKGLDYLHSEKK 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSF 1933
Cdd:cd06640   123 IHRDIKAANVLLSEQGD------------VKLADFGVAGQLTDTQIKrnTFVGTPFWMAPEVIQ---QSAYDSKADIWSL 187
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1934 GMFIYENISLRQPFEGHESIKECILEGSRPALTQrETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06640   188 GITAIELAKGEPPNSDMHPMRVLFLIPKNNPPTL-VGDFSKPFKEFIDACLNKDPSFRPTAKELL 251
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
1707-1999 3.39e-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: 66.26  E-value: 3.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQ--PVPPGARAKESALmafkvavgkwdrdplqhSCkayctarqELA 1784
Cdd:cd06651    11 RGKLLGQGAFGRVYLCYDVDTG----RELAAKQVQfdPESPETSKEVSAL-----------------EC--------EIQ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVGiCI-----KPLALVLELAPLGGLDALLRHYrrsGAhMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd06651    62 LLKNLQHERIVQYYG-CLrdraeKTLTIFMEYMPGGSVKDQLKAY---GA-LTESVTRKYTRQILEGMSYLHSNMIVHRD 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLvwelpqphtEDSPRNlvhIKIADYGISRQ-----TAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFG 1934
Cdd:cd06651   137 IKGANIL---------RDSAGN---VKLGDFGASKRlqticMSGTGIRSVTGTPYWMSPEVISGEG---YGRKADVWSLG 201
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1935 MFIYENISLRQPFEGHESIKECILEGSRPALTQRETQFPTCCLDLmVLCWHEQPRRRPTASQIVS 1999
Cdd:cd06651   202 CTVVEMLTEKPPWAEYEAMAAIFKIATQPTNPQLPSHISEHARDF-LGCIFVEARHRPSAEELLR 265
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
1846-1948 3.57e-11

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: 67.35  E-value: 3.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEE 1923
Cdd:cd05617   128 ALNFLHERGIIYRDLKLDNVLL-------DADG-----HIKLTDYGMCKEGLGPGdtTSTFCGTPNYIAPEILR---GEE 192
                          90       100
                  ....*....|....*....|....*
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd05617   193 YGFSVDWWALGVLMFEMMAGRSPFD 217
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
1711-1949 3.59e-11

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: 65.71  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLQpvppgarakesalmafkvAVGKWDRDPLQHsckayctarqELAVLLTLK 1790
Cdd:cd14103     1 LGRGKFGTVYRCVEKATG----KELAAKFIK------------------CRKAKDREDVRN----------EIEIMNQLR 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGI--CIKPLALVLELAPLGGL-----DALLRHYRRSGAHmgphtfqtLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14103    49 HPRLLQLYDAfeTPREMVLVMEYVAGGELfervvDDDFELTERDCIL--------FMRQICEGVQYMHKQGILHLDLKPE 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqpHTEDSPrnlvHIKIADYGISRQTAPSG-AKGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYENIS 1942
Cdd:cd14103   121 NILC------VSRTGN----QIKIIDFGLARKYDPDKkLKVLFGTPEFVAPEVVNY---EPISYATDMWSVGVICYVLLS 187

                  ....*..
gi 442620116 1943 LRQPFEG 1949
Cdd:cd14103   188 GLSPFMG 194
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
1711-1946 4.01e-11

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: 65.93  E-value: 4.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKvrgaRSFKPVAMKMlqpvppgarakesalMAF--KVAVGKWdRDPLQhsckayctarqELAVLLT 1788
Cdd:cd06607     9 IGHGSFGAVYYARNK----RTSEVVAIKK---------------MSYsgKQSTEKW-QDIIK-----------EVKFLRQ 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKPLA--LVLELApLGGLDALLRHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd06607    58 LRHPNTIEYKGCYLREHTawLVMEYC-LGSASDIVEVHKKP---LQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNIL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphTEDSPrnlvhIKIADYGISRQTAPsgAKGFGGTEGFMAPEIIRYNGEEEYTEKVDCFSFGMFIYEnISLRQP 1946
Cdd:cd06607   134 L-------TEPGT-----VKLADFGSASLVCP--ANSFVGTPYWMAPEVILAMDEGQYDGKVDVWSLGITCIE-LAERKP 198
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
1701-1957 4.13e-11

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 67.75  E-value: 4.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1701 PSECIIKGSLLGRGAFGFVFKANCkvrgarsfkpvamkmlqpvppgARAKEsalmafKVAVGKWDRDPlQHSckayctaR 1780
Cdd:PTZ00036   64 PNKSYKLGNIIGNGSFGVVYEAIC----------------------IDTSE------KVAIKKVLQDP-QYK-------N 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGI----CIKP------LALVLELAPlGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYL 1850
Cdd:PTZ00036  108 RELLIMKNLNHINIIFLKDYyyteCFKKneknifLNVVMEFIP-QTVHKYMKHYARNNHALPLFLVKLYSYQLCRALAYI 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVweLPQPHTedsprnlvhIKIADYGISRQ-TAPSGAKGFGGTEGFMAPEIIRynGEEEYTEKVD 1929
Cdd:PTZ00036  187 HSKFICHRDLKPQNLLI--DPNTHT---------LKLCDFGSAKNlLAGQRSVSYICSRFYRAPELML--GATNYTTHID 253
                         250       260
                  ....*....|....*....|....*...
gi 442620116 1930 CFSFGMFIYENISLRQPFEGHESIKECI 1957
Cdd:PTZ00036  254 LWSLGCIIAEMILGYPIFSGQSSVDQLV 281
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
1846-1948 4.29e-11

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: 67.37  E-value: 4.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEE 1923
Cdd:cd05618   133 ALNYLHERGIIYRDLKLDNVLL---------DSEG---HIKLTDYGMCKEGLRPGdtTSTFCGTPNYIAPEILR---GED 197
                          90       100
                  ....*....|....*....|....*
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd05618   198 YGFSVDWWALGVLMFEMMAGRSPFD 222
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
1687-1999 4.40e-11

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: 66.58  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1687 PDVIFADIPDkhtipseciikgslLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPvpPGARAKEsalmafkvavgKWdR 1766
Cdd:cd06634    13 PEKLFSDLRE--------------IGHGSFGAVYFA----RDVRNNEVVAIKKMSY--SGKQSNE-----------KW-Q 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1767 DPLQhsckayctarqELAVLLTLKHPNIVPLVGICIKPLA--LVLELApLGGLDALLRHYRRSGAHMgphTFQTLVLQAA 1844
Cdd:cd06634    61 DIIK-----------EVKFLQKLRHPNTIEYRGCYLREHTawLVMEYC-LGSASDLLEVHKKPLQEV---EIAAITHGAL 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1845 RAIEYLHRRRIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPsgAKGFGGTEGFMAPEIIRYNGEEEY 1924
Cdd:cd06634   126 QGLAYLHSHNMIHRDVKAGNILLTEPGL------------VKLGDFGSASIMAP--ANSFVGTPYWMAPEVILAMDEGQY 191
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1925 TEKVDCFSFGMFIYENISLRQPFEGHESIKEC--ILEGSRPALtqRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd06634   192 DGKVDVWSLGITCIELAERKPPLFNMNAMSALyhIAQNESPAL--QSGHWSEYFRNFVDSCLQKIPQDRPTSDVLLK 266
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
1806-1954 4.54e-11

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: 66.53  E-value: 4.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1806 ALVLELAPLGGLDALLRHYrrsgaHMGPHTFQT--LVLQAAR---AIEYLHRRRIIYRDLKSENVLVwelpqphtEDSPr 1880
Cdd:cd05632    76 ALCLVLTIMNGGDLKFHIY-----NMGNPGFEEerALFYAAEilcGLEDLHRENTVYRDLKPENILL--------DDYG- 141
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1881 nlvHIKIADYGISRQTaPSGA--KGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPFEGH-ESIK 1954
Cdd:cd05632   142 ---HIRISDLGLAVKI-PEGEsiRGRVGTVGYMAPEVLN---NQRYTLSPDYWGLGCLIYEMIEGQSPFRGRkEKVK 211
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
1788-1954 4.72e-11

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: 65.56  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVlqaaRAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14662    52 SLRHPNIIRFKEVVLTPthLAIVMEYAAGGELFERICNAGRFSEDEARYFFQQLI----SGVSYCHSMQICHRDLKLENT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVWELPQPhtedsprnlvHIKIADYGISRQTA-PSGAKGFGGTEGFMAPEIIrynGEEEYTEKV-DCFSFGMFIYENISL 1943
Cdd:cd14662   128 LLDGSPAP----------RLKICDFGYSKSSVlHSQPKSTVGTPAYIAPEVL---SRKEYDGKVaDVWSCGVTLYVMLVG 194
                         170
                  ....*....|.
gi 442620116 1944 RQPFEGHESIK 1954
Cdd:cd14662   195 AYPFEDPDDPK 205
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
1756-1998 5.12e-11

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: 66.20  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1756 AFKVaVGKWDRDPlqhsckayctaRQELAVLLTL-KHPNIVPLVGICI--KPLALVLELAPlGG--LDALLRH--YRRSG 1828
Cdd:cd14175    30 AVKV-IDKSKRDP-----------SEEIEILLRYgQHPNIITLKDVYDdgKHVYLVTELMR-GGelLDKILRQkfFSERE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1829 AHMGPHTFqtlvlqaARAIEYLHRRRIIYRDLKSENVLVwelpqphtEDSPRNLVHIKIADYGISRQTAPSGAKGFGG-- 1906
Cdd:cd14175    97 ASSVLHTI-------CKTVEYLHSQGVVHRDLKPSNILY--------VDESGNPESLRICDFGFAKQLRAENGLLMTPcy 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1907 TEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQPF-EGHESIKECILE---GSRPALTQRE-TQFPTCCLDLMV 1981
Cdd:cd14175   162 TANFVAPEVLKRQG---YDEGCDIWSLGILLYTMLAGYTPFaNGPSDTPEEILTrigSGKFTLSGGNwNTVSDAAKDLVS 238
                         250
                  ....*....|....*..
gi 442620116 1982 LCWHEQPRRRPTASQIV 1998
Cdd:cd14175   239 KMLHVDPHQRLTAKQVL 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
1781-1949 5.13e-11

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: 65.79  E-value: 5.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHyRRSGAHMGPHTFQTLVLQAaraIEYLHRRRIIYR 1858
Cdd:cd14195    57 REVNILREIQHPNIITLHDIFENKtdVVLILELVSGGELFDFLAE-KESLTEEEATQFLKQILDG---VHYLHSKRIAHF 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELPQPhtedSPRnlvhIKIADYGISRQT-APSGAKGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFI 1937
Cdd:cd14195   133 DLKPENIMLLDKNVP----NPR----IKLIDFGIAHKIeAGNEFKNIFGTPEFVAPEIVNY---EPLGLEADMWSIGVIT 201
                         170
                  ....*....|..
gi 442620116 1938 YENISLRQPFEG 1949
Cdd:cd14195   202 YILLSGASPFLG 213
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
1781-1949 5.73e-11

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


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 65.59  E-value: 5.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPL--VGICIKPLALVLELAPLGGLDALLRHyRRSGAHMGPHTFQTLVLQAaraIEYLHRRRIIYR 1858
Cdd:cd14105    57 REVSILRQVLHPNIITLhdVFENKTDVVLILELVAGGELFDFLAE-KESLSEEEATEFLKQILDG---VNYLHTKNIAHF 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELPQPHTedsprnlvHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFI 1937
Cdd:cd14105   133 DLKPENIMLLDKNVPIP--------RIKLIDFGLAHKIEDGNEfKNIFGTPEFVAPEIVNY---EPLGLEADMWSIGVIT 201
                         170
                  ....*....|..
gi 442620116 1938 YENISLRQPFEG 1949
Cdd:cd14105   202 YILLSGASPFLG 213
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1791-1961 5.95e-11

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 66.17  E-value: 5.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLA--LVLELAPlGGldALLRHYRR------SGAhmgPHTFQTLVlqaaRAIEYLHRRRIIYRDLKS 1862
Cdd:cd14092    58 HPNIVKLHEVFQDELHtyLVMELLR-GG--ELLERIRKkkrfteSEA---SRIMRQLV----SAVSFMHSKGVVHRDLKP 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphtEDSPRNLvHIKIADYGISR---QTAPSGAKGFggTEGFMAPEIIR-YNGEEEYTEKVDCFSFGMFIY 1938
Cdd:cd14092   128 ENLLF--------TDEDDDA-EIKIVDFGFARlkpENQPLKTPCF--TLPYAAPEVLKqALSTQGYDESCDLWSLGVILY 196
                         170       180
                  ....*....|....*....|....*....
gi 442620116 1939 ENISLRQPFEGH------ESIKECILEGS 1961
Cdd:cd14092   197 TMLSGQVPFQSPsrnesaAEIMKRIKSGD 225
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
1779-1998 6.10e-11

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: 65.91  E-value: 6.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVGIC--IKPLALVLELAPLGGLDALlRHYRRSgahMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd07846    47 AMREIKMLKQLRHENLVNLIEVFrrKKRWYLVFEFVDHTVLDDL-EKYPNG---LDESRVRKYLFQILRGIDFCHSHNII 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphtedSPRNLVhiKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFG 1934
Cdd:cd07846   123 HRDIKPENILV----------SQSGVV--KLCDFGFARTLAAPGEvyTDYVATRWYRAPELLV--GDTKYGKAVDVWAVG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1935 MFIYENISLRQPFEG--------------------HESI--KECILEGSR-PALTQRET---QFPT---CCLDLMVLCWH 1985
Cdd:cd07846   189 CLVTEMLTGEPLFPGdsdidqlyhiikclgnliprHQELfqKNPLFAGVRlPEVKEVEPlerRYPKlsgVVIDLAKKCLH 268
                         250
                  ....*....|...
gi 442620116 1986 EQPRRRPTASQIV 1998
Cdd:cd07846   269 IDPDKRPSCSELL 281
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
1778-1955 7.22e-11

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 65.61  E-value: 7.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPL--VGICIKPLALVLELaplggLDALLRHYRRSGAHMG--PHTFQTLVLQAARAIEYLHRR 1853
Cdd:PLN00009   47 TAIREISLLKEMQHGNIVRLqdVVHSEKRLYLVFEY-----LDLDLKKHMDSSPDFAknPRLIKTYLYQILRGIAYCHSH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVwelpqphteDSPRNLvhIKIADYGISRqtapsgakGFG----------GTEGFMAPEIIRynGEEE 1923
Cdd:PLN00009  122 RVLHRDLKPQNLLI---------DRRTNA--LKLADFGLAR--------AFGipvrtfthevVTLWYRAPEILL--GSRH 180
                         170       180       190
                  ....*....|....*....|....*....|..
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:PLN00009  181 YSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDE 212
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
1778-1943 7.63e-11

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


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 65.36  E-value: 7.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYrrsGAHMGPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd14221    36 TFLKEVKVMRCLEHPNVLKFIGVLYKDkrLNFITEYIKGGTLRGIIKSM---DSHYPWSQRVSFAKDIASGMAYLHSMNI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVWElpqphtedsPRNLVhikIADYGISR-----QTAPSGAKGFG-----------GTEGFMAPEIIryN 1919
Cdd:cd14221   113 IHRDLNSHNCLVRE---------NKSVV---VADFGLARlmvdeKTQPEGLRSLKkpdrkkrytvvGNPYWMAPEMI--N 178
                         170       180
                  ....*....|....*....|....
gi 442620116 1920 GeEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd14221   179 G-RSYDEKVDVFSFGIVLCEIIGR 201
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
1805-1948 8.05e-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: 65.19  E-value: 8.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 LALVLELAPLGGLDALLRHyrrsgahMGPHTFQ---TLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedspRN 1881
Cdd:cd05611    72 LYLVMEYLNGGDCASLIKT-------LGGLPEDwakQYIAEVVLGVEDLHQRGIIHRDIKPENLLI------------DQ 132
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1882 LVHIKIADYGISRQT-APSGAKGFGGTEGFMAPEIIRYNGEeeyTEKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd05611   133 TGHLKLTDFGLSRNGlEKRHNKKFVGTPDYLAPETILGVGD---DKMSDWWSLGCVIFEFLFGYPPFH 197
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
1781-1948 9.30e-11

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: 64.84  E-value: 9.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGG---LDALLRHYRRSgahmgPHTFQTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd14111    48 QEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGkelLHSLIDRFRYS-----EDDVVGYLVQILQGLEYLHGRRVLH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd14111   123 LDIKPDNIMV------------TNLNAIKIVDFGSAQSFNPLSLRQLGrrtGTLEYMAPEMVK---GEPVGPPADIWSIG 187
                         170
                  ....*....|....
gi 442620116 1935 MFIYENISLRQPFE 1948
Cdd:cd14111   188 VLTYIMLSGRSPFE 201
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
1778-1955 9.58e-11

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: 65.22  E-value: 9.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGIC--IKPLALVLELaplggLDALLRHYRRSGAHMG--PHTFQTLVLQAARAIEYLHRR 1853
Cdd:cd07860    45 TAIREISLLKELNHPNIVKLLDVIhtENKLYLVFEF-----LHQDLKKFMDASALTGipLPLIKSYLFQLLQGLAFCHSH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVWELPqphtedsprnlvHIKIADYGISRqtapsgakGFG----------GTEGFMAPEIIRynGEEE 1923
Cdd:cd07860   120 RVLHRDLKPQNLLINTEG------------AIKLADFGLAR--------AFGvpvrtythevVTLWYRAPEILL--GCKY 177
                         170       180       190
                  ....*....|....*....|....*....|..
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07860   178 YSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQ 209
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
1788-1938 1.05e-10

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: 65.14  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPLGGL--DALLR-HYRRSGAhmgPHTFQtlvlQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd14086    56 LLKHPNIVRLHDSISEEgfHYLVFDLVTGGELfeDIVAReFYSEADA---SHCIQ----QILESVNHCHQNGIVHRDLKP 128
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1863 ENVLVwelpQPHTEDSPrnlvhIKIADYG--ISRQTAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIY 1938
Cdd:cd14086   129 ENLLL----ASKSKGAA-----VKLADFGlaIEVQGDQQAWFGFAGTPGYLSPEVLR---KDPYGKPVDIWACGVILY 194
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
1781-2001 1.32e-10

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: 64.42  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLT-LKHPNIVPLVGICIK-PLALVLELAPLGGLDALLRhyrRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd05037    50 FETASLMSqISHKHLVKLYGVCVAdENIMVQEYVRYGPLDKYLR---RMGNNVPLSWKLQVAKQLASALHYLEDKKLIHG 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphTEDSPRNLV-HIKIADYGISRqtaPSGAKGFGGTEG-FMAPEIIRyNGEEEYTEKVDCFSFGMF 1936
Cdd:cd05037   127 NVRGRNILL-------AREGLDGYPpFIKLSDPGVPI---TVLSREERVDRIpWIAPECLR-NLQANLTIAADKWSFGTT 195
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1937 IYE-------NISLRQPFEGHESIKE-CILegsrPALTQRETqfptccLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05037   196 LWEicsggeePLSALSSQEKLQFYEDqHQL----PAPDCAEL------AELIMQCWTYEPTKRPSFRAILRDL 258
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
1753-1999 1.33e-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: 64.45  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1753 ALMAFKVAVGKWDRDPLQHSCKAYCTARQELAVLLTLKHPNIVPLVGI--CIKPLALVLELAPLGGLdaLLRHYRRSgaH 1830
Cdd:cd14070    24 AVTGEKVAIKVIDKKKAKKDSYVTKNLRREGRIQQMIRHPNITQLLDIleTENSYYLVMELCPGGNL--MHRIYDKK--R 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1831 MGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISRQTA-PSGAKGFG---G 1906
Cdd:cd14070   100 LEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLL---------DENDN---IKLIDFGLSNCAGiLGYSDPFStqcG 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1907 TEGFMAPEIIrynGEEEYTEKVDCFSFGMFIYENISLRQPFEGHE-SIKECILEGSRPALTQRETQFPTCCLDLMVLCWH 1985
Cdd:cd14070   168 SPAYAAPELL---ARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfSLRALHQKMVDKEMNPLPTDLSPGAISFLRSLLE 244
                         250
                  ....*....|....
gi 442620116 1986 EQPRRRPTASQIVS 1999
Cdd:cd14070   245 PDPLKRPNIKQALA 258
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
1771-1947 1.34e-10

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 64.28  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1771 HSCKAYC---------TARQELAVLLTLKHPNIVPLVGICI--KPLALVLELAPlgG---LDALLRHyrrsgAHMGPHTF 1836
Cdd:cd14088    29 YTCKKFLkrdgrkvrkAAKNEINILKMVKHPNILQLVDVFEtrKEYFIFLELAT--GrevFDWILDQ-----GYYSERDT 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1837 QTLVLQAARAIEYLHRRRIIYRDLKSENVLVWElpqpHTEDSprnlvHIKIADYGISRqTAPSGAKGFGGTEGFMAPEII 1916
Cdd:cd14088   102 SNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYN----RLKNS-----KIVISDFHLAK-LENGLIKEPCGTPEYLAPEVV 171
                         170       180       190
                  ....*....|....*....|....*....|.
gi 442620116 1917 rynGEEEYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd14088   172 ---GRQRYGRPVDCWAIGVIMYILLSGNPPF 199
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
904-1083 1.45e-10

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 62.31  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  904 KLMVVGVAGIGKSTLLD-LLRQGAGSGSSSsshrsrasenhwakrmgharstsrshrhssassaniSTVGVDIgtwiceK 982
Cdd:COG1100     5 KIVVVGTGGVGKTSLVNrLVGDIFSLEKYL------------------------------------STNGVTI------D 42
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  983 RKRAPGSHGPVVFRTWDFGGQKEYYATHQYF---LSKRSLYLVLWrisDGH--KGLAELLQWLGNIQARAPNSPVIIVGT 1057
Cdd:COG1100    43 KKELKLDGLDVDLVIWDTPGQDEFRETRQFYarqLTGASLYLFVV---DGTreETLQSLYELLESLRRLGKKSPIILVLN 119
                         170       180
                  ....*....|....*....|....*.
gi 442620116 1058 HFDAVGEsISPQKAEQLQQLIREKFI 1083
Cdd:COG1100   120 KIDLYDE-EEIEDEERLKEALSEDNI 144
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
1758-1949 1.75e-10

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: 63.87  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWDRdplQHSCKAYCTARQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDaLLRHYRRSGAHMGPHTFQ 1837
Cdd:cd14191    28 KVWAGKFFK---AYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEMVSGGE-LFERIIDEDFELTERECI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1838 TLVLQAARAIEYLHRRRIIYRDLKSENVLVWElpqphtedspRNLVHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEII 1916
Cdd:cd14191   104 KYMRQISEGVEYIHKQGIVHLDLKPENIMCVN----------KTGTKIKLIDFGLARRLENAGSlKVLFGTPEFVAPEVI 173
                         170       180       190
                  ....*....|....*....|....*....|...
gi 442620116 1917 RYngeEEYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd14191   174 NY---EPIGYATDMWSIGVICYILVSGLSPFMG 203
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
1781-1949 1.78e-10

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: 64.27  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14194    57 REVSILKEIQHPNVITLHEVYENKtdVILILELVAGGELFDFLAEKES----LTEEEATEFLKQILNGVYYLHSLQIAHF 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELPQPHtedsPRnlvhIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFI 1937
Cdd:cd14194   133 DLKPENIMLLDRNVPK----PR----IKIIDFGLAHKIDFGNEfKNIFGTPEFVAPEIVNY---EPLGLEADMWSIGVIT 201
                         170
                  ....*....|..
gi 442620116 1938 YENISLRQPFEG 1949
Cdd:cd14194   202 YILLSGASPFLG 213
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
1711-1934 1.81e-10

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: 64.64  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARsfkpVAMKMLqpvppgarakesalmafkvavgkwdrdpLQHSCK--AYCTARQELAVLLT 1788
Cdd:cd07866    16 LGEGTFGEVYKARQIKTGRV----VALKKI----------------------------LMHNEKdgFPITALREIKILKK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKPLALVLELAPL---------GGLDALLRHYRrsgAHMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd07866    64 LKHPNVVPLIDMAVERPDKSKRKRGSvymvtpymdHDLSGLLENPS---VKLTESQIKCYMLQLLEGINYLHENHILHRD 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphteDSPRNLvhiKIADYGISR---QTAPSGAKGFGG----------TEGFMAPEIIRynGEEEYTE 1926
Cdd:cd07866   141 IKAANILI---------DNQGIL---KIADFGLARpydGPPPNPKGGGGGgtrkytnlvvTRWYRPPELLL--GERRYTT 206

                  ....*...
gi 442620116 1927 KVDCFSFG 1934
Cdd:cd07866   207 AVDIWGIG 214
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
1844-1947 1.92e-10

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: 64.65  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1844 ARAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISRQ-TAPSGAKG-FGGTEGFMAPEIIRyngE 1921
Cdd:cd05575   106 ASALGYLHSLNIIYRDLKPENILL---------DSQG---HVVLTDFGLCKEgIEPSDTTStFCGTPEYLAPEVLR---K 170
                          90       100
                  ....*....|....*....|....*.
gi 442620116 1922 EEYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd05575   171 QPYDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
1706-1950 1.92e-10

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: 64.36  E-value: 1.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1706 IKGSLLGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVPPGARAKesalmAFKVAvgkwdrdPLQHSCKAyctarqelav 1785
Cdd:cd14090     5 LTGELLGEGAYASVQTCINLYTG----KEYAVKIIEKHPGHSRSR-----VFREV-------ETLHQCQG---------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 lltlkHPNIVPLVGIC--IKPLALVLELApLGGldALLRHYRRSGaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14090    59 -----HPNILQLIEYFedDERFYLVFEKM-RGG--PLLSHIEKRV-HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPE 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphteDSPRNLVHIKIADYGISrqtapSGAKGFG---------------GTEGFMAPEIIR-YNGEE-EYTE 1926
Cdd:cd14090   130 NILC---------ESMDKVSPVKICDFDLG-----SGIKLSStsmtpvttpelltpvGSAEYMAPEVVDaFVGEAlSYDK 195
                         250       260
                  ....*....|....*....|....
gi 442620116 1927 KVDCFSFGMFIYENISLRQPFEGH 1950
Cdd:cd14090   196 RCDLWSLGVILYIMLCGYPPFYGR 219
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
1708-1934 1.96e-10

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


Pssm-ID: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 63.89  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKA-NCKVRGArsfkpVAMKMLQpvppgarakesalmaFKVAVGKWDRDplqhsckayctARQELAVL 1786
Cdd:cd14069     6 VQTLGEGAFGEVFLAvNRNTEEA-----VAVKFVD---------------MKRAPGDCPEN-----------IKKEVCIQ 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIKP--LALVLELAPLGGL-DALLRHYrrsgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSE 1863
Cdd:cd14069    55 KMLSHKNVVRFYGHRREGefQYLFLEYASGGELfDKIEPDV-----GMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPE 129
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1864 NVLVwelpqphteDSPRNLvhiKIADYGISRQTAPSGAK----GFGGTEGFMAPEIIRynGEEEYTEKVDCFSFG 1934
Cdd:cd14069   130 NLLL---------DENDNL---KISDFGLATVFRYKGKErllnKMCGTLPYVAPELLA--KKKYRAEPVDVWSCG 190
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1711-1999 2.41e-10

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: 63.79  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLQPVPPGarakesalmafkvavgkwdRDplqhsCKAycTARQELAVL-LTL 1789
Cdd:cd14198    16 LGRGKFAVVRQCISKSTG----QEYAAKFLKKRRRG-------------------QD-----CRA--EILHEIAVLeLAK 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPL--VGICIKPLALVLELAPLGgldALLRHYRRSGAHMGPHTFQT-LVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14198    66 SNPRVVNLheVYETTSEIILILEYAAGG---EIFNLCVPDLAEMVSENDIIrLIRQILEGVYYLHQNNIVHLDLKPQNIL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VWELpqphtedSPrnLVHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYENISLRQ 1945
Cdd:cd14198   143 LSSI-------YP--LGDIKIVDFGMSRKIGHACElREIMGTPEYLAPEILNY---DPITTATDMWNIGVIAYMLLTHES 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1946 PFEGHESiKECILEGSRPALTQRETQFPTC---CLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14198   211 PFVGEDN-QETFLNISQVNVDYSEETFSSVsqlATDFIQKLLVKNPEKRPTAEICLS 266
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
1709-1949 2.44e-10

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: 64.63  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKANCKVRGARsfkpVAMKMLQPvppgarakesalmafkvavgkwdrdpLQHSckAYC--TARqELAVL 1786
Cdd:cd07849    11 SYIGEGAYGMVCSAVHKPTGQK----VAIKKISP--------------------------FEHQ--TYClrTLR-EIKIL 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGIcIKPLA--------LVLELAPLGgLDALLRHYRRSGAHMGPHTFQTLvlqaaRAIEYLHRRRIIYR 1858
Cdd:cd07849    58 LRFKHENIIGILDI-QRPPTfesfkdvyIVQELMETD-LYKLIKTQHLSNDHIQYFLYQIL-----RGLKYIHSANVLHR 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWElpqphTEDsprnlvhIKIADYGISRQTAP-SGAKGF----GGTEGFMAPEIIRynGEEEYTEKVDCFSF 1933
Cdd:cd07849   131 DLKPSNLLLNT-----NCD-------LKICDFGLARIADPeHDHTGFlteyVATRWYRAPEIML--NSKGYTKAIDIWSV 196
                         250
                  ....*....|....*.
gi 442620116 1934 GMFIYENISLRQPFEG 1949
Cdd:cd07849   197 GCILAEMLSNRPLFPG 212
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
1778-2010 2.78e-10

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: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKH-PNIVPLvgICI-------KP-LALVLELaplggLDALLRH----YRRSGAH-MGPHTFQTLVLQA 1843
Cdd:cd07837    46 TALREVSLLQMLSQsIYIVRL--LDVehveengKPlLYLVFEY-----LDTDLKKfidsYGRGPHNpLPAKTIQSFMYQL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1844 ARAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNLvhIKIADYGISRQ-TAPsgAKGFGG---TEGFMAPEIIRyn 1919
Cdd:cd07837   119 CKGVAHCHSHGVMHRDLKPQNLLV---------DKQKGL--LKIADLGLGRAfTIP--IKSYTHeivTLWYRAPEVLL-- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 GEEEYTEKVDCFSFGMfIYENISLRQP-FEGHESIKEcILEGSRPALTQRETQFPtcclDLMVLC-WHEQPRRRPT-ASQ 1996
Cdd:cd07837   184 GSTHYSTPVDMWSVGC-IFAEMSRKQPlFPGDSELQQ-LLHIFRLLGTPNEEVWP----GVSKLRdWHEYPQWKPQdLSR 257
                         250
                  ....*....|....
gi 442620116 1997 IVSILSaPECIHLL 2010
Cdd:cd07837   258 AVPDLE-PEGVDLL 270
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
1710-1947 3.44e-10

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: 64.21  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPVPPGARAKESALMAfkvavgkwdrdplqhsckayctarqELAVLL-T 1788
Cdd:cd05604     3 VIGKGSFGKVLLA----KRKRDGKYYAVKVLQKKVILNRKEQKHIMA-------------------------ERNVLLkN 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPL--VGICIKPLALVLELAPLGgldALLRHYRRSGAHMGPHTfQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd05604    54 VKHPFLVGLhySFQTTDKLYFVLDFVNGG---ELFFHLQRERSFPEPRA-RFYAAEIASALGYLHSINIVYRDLKPENIL 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphteDSprnLVHIKIADYGISRQ--TAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLR 1944
Cdd:cd05604   130 L---------DS---QGHIVLTDFGLCKEgiSNSDTTTTFCGTPEYLAPEVIR---KQPYDNTVDWWCLGSVLYEMLYGL 194

                  ...
gi 442620116 1945 QPF 1947
Cdd:cd05604   195 PPF 197
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
1711-1938 3.70e-10

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: 63.11  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGArsfkPVAMKMLqpvppgaRAKESALMAFkvavgkwdrdplqhsckayctaRQELAVLLTLK 1790
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGT----KMALKFV-------PKPSTKLKDF----------------------LREYNISLELS 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 -HPNIVPLVGICIKP---LALVLELAPLGGLDALLRhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd13987    48 vHPHIIKTYDVAFETedyYVFAQEYAPYGDLFSIIP----PQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVL 123
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1867 VWElpqphtedspRNLVHIKIADYGISRQTApSGAKGFGGTEGFMAPEIIRYNGEEEYT--EKVDCFSFGMFIY 1938
Cdd:cd13987   124 LFD----------KDCRRVKLCDFGLTRRVG-STVKRVSGTIPYTAPEVCEAKKNEGFVvdPSIDVWAFGVLLF 186
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
1781-1998 3.94e-10

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 63.49  E-value: 3.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTL-KHPNIVPLVGICI--KPLALVLELApLGG--LDALLRHyrrsgAHMGPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd14178    45 EEIEILLRYgQHPNIITLKDVYDdgKFVYLVMELM-RGGelLDRILRQ-----KCFSEREASAVLCTITKTVEYLHSQGV 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphtEDSPRNLVHIKIADYGISRQTAPSGAKGFGG--TEGFMAPEIIRYNGeeeYTEKVDCFSF 1933
Cdd:cd14178   119 VHRDLKPSNILY--------MDESGNPESIRICDFGFAKQLRAENGLLMTPcyTANFVAPEVLKRQG---YDAACDIWSL 187
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1934 GMFIYENISLRQPF-EGHESIKECILE--GS-RPALTQRE-TQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14178   188 GILLYTMLAGFTPFaNGPDDTPEEILAriGSgKYALSGGNwDSISDAAKDIVSKMLHVDPHQRLTAPQVL 257
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1815-1998 4.26e-10

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: 62.97  E-value: 4.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1815 GGLDAllrhYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedSPRNlvHIKIADYGISR 1894
Cdd:cd06619    84 GSLDV----YRK----IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLV----------NTRG--QVKLCDFGVST 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1895 QTAPSGAKGFGGTEGFMAPEiiRYNGeEEYTEKVDCFSF---------GMFIYENISLRQPFEGHESIKECILEGSRPAL 1965
Cdd:cd06619   144 QLVNSIAKTYVGTNAYMAPE--RISG-EQYGIHSDVWSLgisfmelalGRFPYPQIQKNQGSLMPLQLLQCIVDEDPPVL 220
                         170       180       190
                  ....*....|....*....|....*....|...
gi 442620116 1966 TqrETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06619   221 P--VGQFSEKFVHFITQCMRKQPKERPAPENLM 251
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
456-710 4.73e-10

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 65.10  E-value: 4.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  456 ITRIDFSHNVLTSIPQELFhlVSLRYLNVAQNKITDLPAPIGQTygcpvLDELFLQDNQLTTLPAaifHLP-ALSILDVS 534
Cdd:PRK15370  201 ITTLILDNNELKSLPENLQ--GNIKTLYANSNQLTSIPATLPDT-----IQEMELSINRITELPE---RLPsALQSLDLF 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  535 NNKLQQLPFDLwrAPKLRELNVAFNLLRDLPvppmqtsssllsldklnlqsfEEPPSNkprnvtqqrLTHrnlwsatldi 614
Cdd:PRK15370  271 HNKISCLPENL--PEELRYLSVYDNSIRTLP---------------------AHLPSG---------ITH---------- 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  615 tdndmkwqheqdlgdgktagvgssqlssLNIANNLFTSIPAALPclaVNLTRLNMSYNSLRSMGhvTSYPATLKQLDLSH 694
Cdd:PRK15370  309 ----------------------------LNVQSNSLTALPETLP---PGLKTLEAGENALTSLP--ASLPPELQVLDVSK 355
                         250
                  ....*....|....*...
gi 442620116  695 NEISCWPSL--PRITESD 710
Cdd:PRK15370  356 NQITVLPETlpPTITTLD 373
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1708-1999 5.16e-10

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 62.64  E-value: 5.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANcKVRGARsfkPVAMKMLQpvppgarakesalmafKVAVGKWDRDPLQHSCKAyctarqELAVLL 1787
Cdd:cd14005     5 GDLLGKGGFGTVYSGV-RIRDGL---PVAVKFVP----------------KSRVTEWAMINGPVPVPL------EIALLL 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 ---TLKHPNIVPLVGICIKP--LALVLEL-APLGGLDALLRHYRRSGAHMGPHTFQtlvlQAARAIEYLHRRRIIYRDLK 1861
Cdd:cd14005    59 kasKPGVPGVIRLLDWYERPdgFLLIMERpEPCQDLFDFITERGALSENLARIIFR----QVVEAVRHCHQRGVLHRDIK 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphtedsprNLV--HIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIR---YNGEEEYTekvdcFSFGMF 1936
Cdd:cd14005   135 DENLLI-------------NLRtgEVKLIDFGCGALLKDSVYTDFDGTRVYSPPEWIRhgrYHGRPATV-----WSLGIL 196
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1937 IYENISLRQPFEGHESIkecilegsrpalTQRETQFP----TCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14005   197 LYDMLCGDIPFENDEQI------------LRGNVLFRprlsKECCDLISRCLQFDPSKRPSLEQILS 251
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
1711-1947 5.21e-10

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 63.36  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKanckVRGARSFKPVAMKMLqpvppgarAKESALMAFKVAVGKWDRDPLQhsckayCTARQELAVLLTLK 1790
Cdd:cd05586     1 IGKGTFGQVYQ----VRKKDTRRIYAMKVL--------SKKVIVAKKEVAHTIGERNILV------RTALDESPFIVGLK 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPlvgiciKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLqaarAIEYLHRRRIIYRDLKSENVLVwel 1870
Cdd:cd05586    63 FSFQTP------TDLYLVTDYMSGGELFWHLQKEGRFSEDRAKFYIAELVL----ALEHLHKNDIVYRDLKPENILL--- 129
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1871 pqphteDSPRnlvHIKIADYGISRQ--TAPSGAKGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd05586   130 ------DANG---HIALCDFGLSKAdlTDNKTTNTFCGTTEYLAPEVLL--DEKGYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
1711-1935 5.24e-10

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 63.09  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSfkpvAMKMLQPVPPGARAKESalmafkvavgkwdrdplqhsckayctarqELAVLLTL- 1789
Cdd:cd06639    30 IGKGTYGKVYKVTNKKDGSLA----AVKILDPISDVDEEIEA-----------------------------EYNILRSLp 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP-------LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd06639    77 NHPNVVKFYGMFYKAdqyvggqLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKG 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1863 ENVLVwelpqpHTEDSprnlvhIKIADYGISRQTAPSGAKGFG--GTEGFMAPEIIRYNGEEEYTEKVDC--FSFGM 1935
Cdd:cd06639   157 NNILL------TTEGG------VKLVDFGVSAQLTSARLRRNTsvGTPFWMAPEVIACEQQYDYSYDARCdvWSLGI 221
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
1740-1953 5.35e-10

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: 63.59  E-value: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1740 LQPVPPGAR----AKESALMAFKVAVGKWDRdPLQ---HSCKAYctarQELAVLLTLKHPNIVPLVGiCIKP-------- 1804
Cdd:cd07850     5 LKPIGSGAQgivcAAYDTVTGQNVAIKKLSR-PFQnvtHAKRAY----RELVLMKLVNHKNIIGLLN-VFTPqksleefq 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 -LALVLELaplggLDA--------LLRHYRRSgahmgphtfqTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqpht 1875
Cdd:cd07850    79 dVYLVMEL-----MDAnlcqviqmDLDHERMS----------YLLYQMLCGIKHLHSAGIIHRDLKPSNIVV-------- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1876 edspRNLVHIKIADYGISRqTApsgakgfgGTEGFMAPEII-RYNGEEE------YTEKVDCFSFGMFIYENISLRQPFE 1948
Cdd:cd07850   136 ----KSDCTLKILDFGLAR-TA--------GTSFMMTPYVVtRYYRAPEvilgmgYKENVDIWSVGCIMGEMIRGTVLFP 202

                  ....*
gi 442620116 1949 GHESI 1953
Cdd:cd07850   203 GTDHI 207
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
1776-1998 5.43e-10

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: 62.76  E-value: 5.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1776 YCTARQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGlDALLRHYRRSGAhMGPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd06645    52 FAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGG-GSLQDIYHVTGP-LSESQIAYVSRETLQGLYYLHSKGK 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYNGEEEYTEKVDCFSF 1933
Cdd:cd06645   130 MHRDIKGANILL-------TDNG-----HVKLADFGVSAQITATIAkrKSFIGTPYWMAPEVAAVERKGGYNQLCDIWAV 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1934 GMFIYENISLRQP-FEGHESIKECILEGS--RPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06645   198 GITAIELAELQPPmFDLHPMRALFLMTKSnfQPPKLKDKMKWSNSFHHFVKMALTKNPKKRPTAEKLL 265
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
1781-1949 5.62e-10

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


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 62.67  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14196    57 REVSILRQVLHPNIITLHDVYENRtdVVLILELVSGGELFDFLAQKES----LSEEEATSFIKQILDGVNYLHTKKIAHF 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELPQPhtedsprnLVHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFI 1937
Cdd:cd14196   133 DLKPENIMLLDKNIP--------IPHIKLIDFGLAHEIEDGVEfKNIFGTPEFVAPEIVNY---EPLGLEADMWSIGVIT 201
                         170
                  ....*....|..
gi 442620116 1938 YENISLRQPFEG 1949
Cdd:cd14196   202 YILLSGASPFLG 213
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
1846-1996 5.92e-10

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: 62.68  E-value: 5.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphtEDSprnlVHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRYNGEEE- 1923
Cdd:cd14181   128 AVSYLHANNIVHRDLKPENILL--------DDQ----LHIKLSDFGFSCHLEPGEKlRELCGTPGYLAPEILKCSMDETh 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1924 --YTEKVDCFSFGMFIYENISLRQPFEGHESI--KECILEG----SRPALTQRETQFPTCCLDLMVLCwheqPRRRPTAS 1995
Cdd:cd14181   196 pgYGKEVDLWACGVILFTLLAGSPPFWHRRQMlmLRMIMEGryqfSSPEWDDRSSTVKDLISRLLVVD----PEIRLTAE 271

                  .
gi 442620116 1996 Q 1996
Cdd:cd14181   272 Q 272
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
1704-1947 5.93e-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: 5.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1704 CIIKgsLLGRGAFGFVFKanckVRGARSFKPVAMKMLQpvppgaraKESALMAFKVAVGKWDRDPLQHS-----CKAYCT 1778
Cdd:cd05573     4 EVIK--VIGRGAFGEVWL----VRDKDTGQVYAMKILR--------KSDMLKREQIAHVRAERDILADAdspwiVRLHYA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQElavlltlKHpnivplvgicikpLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLqaarAIEYLHRRRIIYR 1858
Cdd:cd05573    70 FQDE-------DH-------------LYLVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVL----ALDSLHKLGFIHR 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAKGFG-------------------------------GT 1907
Cdd:cd05573   126 DIKPDNILL-------DADG-----HIKLADFGLCTKMNKSGDRESYlndsvntlfqdnvlarrrphkqrrvraysavGT 193
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 442620116 1908 EGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd05573   194 PDYIAPEVLR---GTGYGPECDWWSLGVILYEMLYGFPPF 230
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
1778-1959 6.15e-10

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: 62.67  E-value: 6.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGI--CIKPLALVLELAPLGGLDALLRHyrRSGAHmgPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd07870    44 TAIREASLLKGLKHANIVLLHDIihTKETLTFVFEYMHTDLAQYMIQH--PGGLH--PYNVRLFMFQLLRGLAYIHGQHI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISR-QTAPSgaKGFGG---TEGFMAPEIIRynGEEEYTEKVDCF 1931
Cdd:cd07870   120 LHRDLKPQNLLISYLGE------------LKLADFGLARaKSIPS--QTYSSevvTLWYRPPDVLL--GATDYSSALDIW 183
                         170       180
                  ....*....|....*....|....*...
gi 442620116 1932 SFGMFIYENISLRQPFEGHESIKECILE 1959
Cdd:cd07870   184 GAGCIFIEMLQGQPAFPGVSDVFEQLEK 211
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
1708-1998 6.48e-10

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: 62.19  E-value: 6.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGARsfkpVAMKMLQpvppgARAKESALMAFKVavgkwdrdplqhsckayctaRQELAVLL 1787
Cdd:cd14186     6 LNLLGKGSFACVYRARSLHTGLE----VAIKMID-----KKAMQKAGMVQRV--------------------RNEVEIHC 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFqtlVLQAARAIEYLHRRRIIYRDLKSENV 1865
Cdd:cd14186    57 QLKHPSILELYNYFEDSnyVYLVLEMCHNGEMSRYLKNRKKPFTEDEARHF---MHQIVTGMLYLHSHGILHRDLTLSNL 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphtedsPRNLvHIKIADYGISRQTAPSGAKGFG--GTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd14186   134 LL-----------TRNM-NIKIADFGLATQLKMPHEKHFTmcGTPNYISPEIAT---RSAHGLESDVWSLGCMFYTLLVG 198
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1944 RQPFEG---HESIKECIL-EGSRPALTQRETQfptcclDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14186   199 RPPFDTdtvKNTLNKVVLaDYEMPAFLSREAQ------DLIHQLLRKNPADRLSLSSVL 251
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
1711-1998 7.54e-10

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: 62.35  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGA-----RSFKPVAmkmlqpvppGARAKESALmafkvavgkwdRDPLQHsckayctarqelAV 1785
Cdd:cd14138    13 IGSGEFGSVFKCVKRLDGCiyaikRSKKPLA---------GSVDEQNAL-----------REVYAH------------AV 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLtlKHPNIVPLVGICIKPLALVL--ELAPLGGL-DALLRHYRRSGAHMGPHtFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd14138    61 LG--QHSHVVRYYSAWAEDDHMLIqnEYCNGGSLaDAISENYRIMSYFTEPE-LKDLLLQVARGLKYIHSMSLVHMDIKP 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVWELPQPHT---------EDSPRnlVHIKIADYG-ISRQTAPSGAKgfgGTEGFMAPEIIryngEEEYTE--KVDC 1930
Cdd:cd14138   138 SNIFISRTSIPNAaseegdedeWASNK--VIFKIGDLGhVTRVSSPQVEE---GDSRFLANEVL----QENYTHlpKADI 208
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1931 FSFGMFIYeNISLRQPFEGHESIKECILEGSRPALTQRETQFPTCCLDLMVlcwHEQPRRRPTASQIV 1998
Cdd:cd14138   209 FALALTVV-CAAGAEPLPTNGDQWHEIRQGKLPRIPQVLSQEFLDLLKVMI---HPDPERRPSAVALV 272
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
1774-1947 7.61e-10

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: 62.97  E-value: 7.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1774 KAYCTARQEL-------AVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDaLLRHYRRSGA-HMGPHTFQTLVLQAAr 1845
Cdd:cd05585    29 KAHIVSRSEVthtlaerTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGE-LFHHLQREGRfDLSRARFYTAELLCA- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 aIEYLHRRRIIYRDLKSENVLVwelpqPHTEdsprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRYNGeee 1923
Cdd:cd05585   107 -LECLHKFNVIYRDLKPENILL-----DYTG-------HIALCDFGLCKLNMKDDDKtnTFCGTPEYLAPELLLGHG--- 170
                         170       180
                  ....*....|....*....|....
gi 442620116 1924 YTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd05585   171 YTKAVDWWTLGVLLYEMLTGLPPF 194
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
1711-1998 7.95e-10

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: 62.25  E-value: 7.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGARSFKPVAMKMLQPvppGARAKESALMafkvavgkwdrdplqhsckayctaRQELAVLLTLK 1790
Cdd:cd05079    12 LGEGHFGKVELCRYDPEGDNTGEQVAVKSLKP---ESGGNHIADL------------------------KKEIEILRNLY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP----LALVLELAPLGGLDALLRhyrRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd05079    65 HENIVKYKGICTEDggngIKLIMEFLPSGSLKEYLP---RNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphtedspRNLVHIKIADYGISRqtAPSGAKGFGGTEGFMAPEIIRYNGE----EEYTEKVDCFSFGMFIYENIS 1942
Cdd:cd05079   142 V------------ESEHQVKIGDFGLTK--AIETDKEYYTVKDDLDSPVFWYAPEcliqSKFYIASDVWSFGVTLYELLT 207
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1943 --------------LRQPFEGHESIKECIL---EGSRpalTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd05079   208 ycdsesspmtlflkMIGPTHGQMTVTRLVRvleEGKR---LPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNLI 277
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
1781-2008 1.05e-09

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: 62.73  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTL-KHPNIVPLVGICI--KPLALVLELAPLGGL-DALLRHyrrsgAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd14176    61 EEIEILLRYgQHPNIITLKDVYDdgKYVYVVTELMKGGELlDKILRQ-----KFFSEREASAVLFTITKTVEYLHAQGVV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphtEDSPRNLVHIKIADYGISRQTAPSGAKGFGG--TEGFMAPEIIRYNGeeeYTEKVDCFSFG 1934
Cdd:cd14176   136 HRDLKPSNILY--------VDESGNPESIRICDFGFAKQLRAENGLLMTPcyTANFVAPEVLERQG---YDAACDIWSLG 204
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1935 MFIYENISLRQPF-EGHESIKECIL----EGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQivsILSAPECIH 2008
Cdd:cd14176   205 VLLYTMLTGYTPFaNGPDDTPEEILarigSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAAL---VLRHPWIVH 280
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
1777-2001 1.07e-09

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: 61.35  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1777 CTAR------QELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLrhYRRSGAHMGPHTFQTLVLQAARAIE 1848
Cdd:cd14057    31 VTTRisrdfnEEYPRLRIFSHPNVLPVLGACNSPpnLVVISQYMPYGSLYNVL--HEGTGVVVDQSQAVKFALDIARGMA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHR-RRIIYR-DLKSENVLVWElpqphtEDSPRnlvhIKIADYGISRQTapsgaKGFGGTEGFMAPEIIRYNGEEEYTE 1926
Cdd:cd14057   109 FLHTlEPLIPRhHLNSKHVMIDE------DMTAR----INMADVKFSFQE-----PGKMYNPAWMAPEALQKKPEDINRR 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1927 KVDCFSFGMFIYENISLRQPFEGHESIkEC----ILEGSRPALTQRETqfPTCClDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd14057   174 SADMWSFAILLWELVTREVPFADLSNM-EIgmkiALEGLRVTIPPGIS--PHMC-KLMKICMNEDPGKRPKFDMIVPIL 248
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
1782-1998 1.30e-09

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: 62.05  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVP-----LVGiciKPLALVLELAPLGGLDALLrhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd06655    66 EILVMKELKNPNIVNfldsfLVG---DELFVVMEYLAGGSLTDVV-----TETCMDEAQIAAVCRECLQALEFLHANQVI 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd06655   138 HRDIKSDNVLL------GMDGS------VKLTDFGFCAQITPEQSKrsTMVGTPYWMAPEVVT---RKAYGPKVDIWSLG 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1935 MFIYENISLRQPFEGHESIKECILEGSR--PALTQRETQFPTcCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06655   203 IMAIEMVEGEPPYLNENPLRALYLIATNgtPELQNPEKLSPI-FRDFLNRCLEMDVEKRGSAKELL 267
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
1781-1932 1.39e-09

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 61.37  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK-PLALVL-ELAPLGGLDALLRHYRRSGAHMGPHtfqtLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd13991    47 EELMACAGLTSPRVVPLYGAVREgPWVNIFmDLKEGGSLGQLIKEQGCLPEDRALH----YLGQALEGLEYLHSRKILHG 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphTEDSPRNLvhikIADYGISRQTAPSG-------AKGFGGTEGFMAPEIIRyngEEEYTEKVDCF 1931
Cdd:cd13991   123 DVKADNVLL-------SSDGSDAF----LCDFGHAECLDPDGlgkslftGDYIPGTETHMAPEVVL---GKPCDAKVDVW 188

                  .
gi 442620116 1932 S 1932
Cdd:cd13991   189 S 189
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
1781-1974 1.41e-09

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: 61.54  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGI--CIKPLALVLELAPLGGLDALLRHYRrsgaHMGPHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14010    43 NEVRLTHELKHPNVLKFYEWyeTSNHLWLVVEYCTGGDLETLLRQDG----NLPESSVRKFGRDLVRGLHYIHSKGIIYC 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphteDSPRNLvhiKIADYGISRQTAPSGAKGFG------------------GTEGFMAPEIIRyng 1920
Cdd:cd14010   119 DLKPSNILL---------DGNGTL---KLSDFGLARREGEILKELFGqfsdegnvnkvskkqakrGTPYYMAPELFQ--- 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1921 EEEYTEKVDCFSFGMFIYENISLRQPF--EGHESIKECILEGSRPALTQRETQFPT 1974
Cdd:cd14010   184 GGVHSFASDLWALGCVLYEMFTGKPPFvaESFTELVEKILNEDPPPPPPKVSSKPS 239
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
1705-1997 1.41e-09

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: 61.16  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1705 IIKGSLLGRGAFGFVFKANCKVRGARsfkpVAMKMLQPVppgaRAKESALMAFKvavgkwdrdPlqhsckayctarQELA 1784
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCK----VAIKIVSKK----KAPEDYLQKFL---------P------------REIE 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVGiCIKP---LALVLELAPLGgldALLRHYRRSGAHMGPHT---FQTLVLqaarAIEYLHRRRIIYR 1858
Cdd:cd14162    53 VIKGLKHPNLICFYE-AIETtsrVYIIMELAENG---DLLDYIRKNGALPEPQArrwFRQLVA----GVEYCHSKGVVHR 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphtedsPRNLvHIKIADYGISRQT--APSG----AKGFGGTEGFMAPEIIR---YNGEEEytekvD 1929
Cdd:cd14162   125 DLKCENLLL-----------DKNN-NLKITDFGFARGVmkTKDGkpklSETYCGSYAYASPEILRgipYDPFLS-----D 187
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1930 CFSFGMFIYENISLRQPFEGhESIKECILEgsrpalTQRETQFPTC------CLDLM--VLCWHEqprRRPTASQI 1997
Cdd:cd14162   188 IWSMGVVLYTMVYGRLPFDD-SNLKVLLKQ------VQRRVVFPKNptvseeCKDLIlrMLSPVK---KRITIEEI 253
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
1771-2002 1.42e-09

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: 61.48  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1771 HSCKAYCTARQELAVL---LTL---KHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHyrrsgaHMGPHTFQTLV-- 1840
Cdd:cd05064    39 HTLRAGCSDKQRRGFLaeaLTLgqfDHSNIVRLEGVITRgnTMMIVTEYMSNGALDSFLRK------HEGQLVAGQLMgm 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1841 LQA-ARAIEYLHRRRIIYRDLKSENVLVwelpqphtedsPRNLVhIKIADYG-ISRQTAPSGAKGFGGTEGFM--APEII 1916
Cdd:cd05064   113 LPGlASGMKYLSEMGYVHKGLAAHKVLV-----------NSDLV-CKISGFRrLQEDKSEAIYTTMSGKSPVLwaAPEAI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1917 RYNgeeEYTEKVDCFSFGMFIYENISL-RQPF--EGHESIKECILEGSR-PAltqretqfPTCCLD----LMVLCWHEQP 1988
Cdd:cd05064   181 QYH---HFSSASDVWSFGIVMWEVMSYgERPYwdMSGQDVIKAVEDGFRlPA--------PRNCPNllhqLMLDCWQKER 249
                         250
                  ....*....|....
gi 442620116 1989 RRRPTASQIVSILS 2002
Cdd:cd05064   250 GERPRFSQIHSILS 263
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
1782-2007 1.44e-09

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: 61.59  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVP-----LVGiciKPLALVLELAPLGGLDALLRHYRrsgahMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd06658    69 EVVIMRDYHHENVVDmynsyLVG---DELWVVMEFLEGGALTDIVTHTR-----MNEEQIATVCLSVLRALSYLHNQGVI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPS--GAKGFGGTEGFMAPEIIrynGEEEYTEKVDCFSFG 1934
Cdd:cd06658   141 HRDIKSDSILL-------TSDG-----RIKLSDFGFCAQVSKEvpKRKSLVGTPYWMAPEVI---SRLPYGTEVDIWSLG 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1935 MFIYENISLRQPFEGHESIKEC--ILEGSRPAL--TQRETQFPTCCLDLMVLcwhEQPRRRPTASQIVS-----ILSAPE 2005
Cdd:cd06658   206 IMVIEMIDGEPPYFNEPPLQAMrrIRDNLPPRVkdSHKVSSVLRGFLDLMLV---REPSQRATAQELLQhpflkLAGPPS 282

                  ..
gi 442620116 2006 CI 2007
Cdd:cd06658   283 CI 284
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
1776-1939 1.73e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 62.60  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1776 YCTARQELAVLLTLKHPNIVPLvgicikplalvLELAPLGGLDAL-LRHYRRS-----GAHMGP-HTFQTLVL--QAARA 1846
Cdd:PHA03211  204 YASSVHEARLLRRLSHPAVLAL-----------LDVRVVGGLTCLvLPKYRSDlytylGARLRPlGLAQVTAVarQLLSA 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNlvhIKIADYG---ISRQTAPSGAK-GFGGTEGFMAPEIIrynGEE 1922
Cdd:PHA03211  273 IDYIHGEGIIHRDIKTENVLV---------NGPED---ICLGDFGaacFARGSWSTPFHyGIAGTVDTNAPEVL---AGD 337
                         170
                  ....*....|....*..
gi 442620116 1923 EYTEKVDCFSFGMFIYE 1939
Cdd:PHA03211  338 PYTPSVDIWSAGLVIFE 354
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
1847-1947 1.77e-09

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: 61.08  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNlvhIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRYNGEEE-- 1923
Cdd:cd14182   123 ICALHKLNIVHRDLKPENILL---------DDDMN---IKLTDFGFSCQLDPGEKlREVCGTPGYLAPEIIECSMDDNhp 190
                          90       100
                  ....*....|....*....|....*
gi 442620116 1924 -YTEKVDCFSFGMFIYENISLRQPF 1947
Cdd:cd14182   191 gYGKEVDMWSTGVIMYTLLAGSPPF 215
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
1789-1949 1.78e-09

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 62.89  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIV---------PLVGIcikplalVLELAPlgGLDalLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:NF033483   64 LSHPNIVsvydvgedgGIPYI-------VMEYVD--GRT--LKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphTEDSprnlvHIKIADYGISR--------QTApsgakGFGGTEGFMAPEIIRYngeEEYTEKVDCF 1931
Cdd:NF033483  133 IKPQNILI-------TKDG-----RVKVTDFGIARalssttmtQTN-----SVLGTVHYLSPEQARG---GTVDARSDIY 192
                         170
                  ....*....|....*...
gi 442620116 1932 SFGMFIYENISLRQPFEG 1949
Cdd:NF033483  193 SLGIVLYEMLTGRPPFDG 210
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
1837-1994 1.93e-09

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: 61.10  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1837 QTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphTEDSPrnLVHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEI 1915
Cdd:cd14197   114 KRLMKQILEGVSFLHNNNVVHLDLKPQNILL-------TSESP--LGDIKIVDFGLSRILKNSEElREIMGTPEYVAPEI 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1916 IRYngeEEYTEKVDCFSFGMFIYENISLRQPFEGHESiKECILEGSRPALTQRETQF---PTCCLDLMVLCWHEQPRRRP 1992
Cdd:cd14197   185 LSY---EPISTATDMWSIGVLAYVMLTGISPFLGDDK-QETFLNISQMNVSYSEEEFehlSESAIDFIKTLLIKKPENRA 260

                  ..
gi 442620116 1993 TA 1994
Cdd:cd14197   261 TA 262
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
1782-1949 2.87e-09

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: 60.32  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSgAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLK 1861
Cdd:cd14190    51 EIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELFERIVDED-YHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLK 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphtedSPRNLVHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRYngeEEYTEKVDCFSFGMFIYEN 1940
Cdd:cd14190   130 PENILC----------VNRTGHQVKIIDFGLARRYNPREKlKVNFGTPEFLSPEVVNY---DQVSFPTDMWSMGVITYML 196

                  ....*....
gi 442620116 1941 ISLRQPFEG 1949
Cdd:cd14190   197 LSGLSPFLG 205
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
1780-1996 2.96e-09

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: 61.02  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSGAHMgphTFQTLVL-----QAARAIEYLHRRR 1854
Cdd:cd14094    53 KREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGF---VYSEAVAshymrQILEALRYCHDNN 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphteDSPRNLVHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIRyngEEEYTEKVDCFS 1932
Cdd:cd14094   130 IIHRDVKPHCVLL---------ASKENSAPVKLGGFGVAIQLGESGlvAGGRVGTPHFMAPEVVK---REPYGKPVDVWG 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1933 FGMFIYENISLRQPFEGH-ESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd14094   198 CGVILFILLSGCLPFYGTkERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYE 262
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
1855-1997 3.02e-09

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: 60.63  E-value: 3.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRY---NGEEEYTEKVDCF 1931
Cdd:cd06622   124 IIHRDVKPTNVLVNGNGQ------------VKLCDFGVSGNLVASLAKTNIGCQSYMAPERIKSggpNQNPTYTVQSDVW 191
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1932 SFGMFIYENISLRQPF--EGHESI---KECILEGSRPALTqreTQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd06622   192 SLGLSILEMALGRYPYppETYANIfaqLSAIVDGDPPTLP---SGYSDDAQDFVAKCLNKIPNRRPTYAQL 259
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
1780-1999 3.29e-09

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: 60.43  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVG--ICIKPLALVLELAPLGGLDALlrhYRRSG-------AHMGPHTFQTLVlqaaraieYL 1850
Cdd:cd06646    54 QQEIFMVKECKHCNIVAYFGsyLSREKLWICMEYCGGGSLQDI---YHVTGplselqiAYVCRETLQGLA--------YL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYNGEEEYTEKV 1928
Cdd:cd06646   123 HSKGKMHRDIKGANILL-------TDNG-----DVKLADFGVAAKITATIAkrKSFIGTPYWMAPEVAAVEKNGGYNQLC 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1929 DCFSFGMFIYENISLRQP-FEGHESIKECILEGS--RPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd06646   191 DIWAVGITAIELAELQPPmFDLHPMRALFLMSKSnfQPPKLKDKTKWSSTFHNFVKISLTKNPKKRPTAERLLT 264
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
447-714 3.60e-09

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 62.41  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  447 RLNEVALTAITridfshnvlTSIPQELFHLVslrylnVAQNKITDLPAPIGQTygcpvLDELFLQDNQLTTLPAAI---- 522
Cdd:PRK15370  184 RLKILGLTTIP---------ACIPEQITTLI------LDNNELKSLPENLQGN-----IKTLYANSNQLTSIPATLpdti 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  523 --------------FHLP-ALSILDVSNNKLQQLPFDLwrAPKLRELNVAFNLLRDLP--VPPMQTsssllsldKLNLQ- 584
Cdd:PRK15370  244 qemelsinritelpERLPsALQSLDLFHNKISCLPENL--PEELRYLSVYDNSIRTLPahLPSGIT--------HLNVQs 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  585 -SFEEPPSNKPRNVTqqrlthrnlwsaTLDITDNDMKWQHEQDlgdgktagvgSSQLSSLNIANNLFTSIPAALPclaVN 663
Cdd:PRK15370  314 nSLTALPETLPPGLK------------TLEAGENALTSLPASL----------PPELQVLDVSKNQITVLPETLP---PT 368
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442620116  664 LTRLNMSYNSLRSMGHvtSYPATLKQLDLSHNEiscwpsLPRITESDPHLL 714
Cdd:PRK15370  369 ITTLDVSRNALTNLPE--NLPAALQIMQASRNN------LVRLPESLPHFR 411
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
1711-1955 3.69e-09

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: 61.30  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKanckVRGARSFKPVAMKMLQPVppgarakesalmaFKVAVgkwdrdplqhSCKaycTARQELAVLLTLK 1790
Cdd:cd07853     8 IGYGAFGVVWS----VTDPRDGKRVALKKMPNV-------------FQNLV----------SCK---RVFRELKMLCFFK 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGI-------CIKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLvlqaaRAIEYLHRRRIIYRDLKSE 1863
Cdd:cd07853    58 HDNVLSALDIlqpphidPFEEIYVVTELMQSDLHKIIVSPQPLSSDHVKVFLYQIL-----RGLKYLHSAGILHRDIKPG 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphtedsPRNLVhIKIADYGISRQTAPSGAKGFGG---TEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYEN 1940
Cdd:cd07853   133 NLLV-----------NSNCV-LKICDFGLARVEEPDESKHMTQevvTQYYRAPEILM--GSRHYTSAVDIWSVGCIFAEL 198
                         250
                  ....*....|....*
gi 442620116 1941 ISLRQPFEGHESIKE 1955
Cdd:cd07853   199 LGRRILFQAQSPIQQ 213
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
1841-2001 4.06e-09

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 59.81  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1841 LQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtEDSPRNlvhiKIADYGISRQTAP-SGAkgFGGTEGFMAPEIirYN 1919
Cdd:cd13975   109 LDVVEGIRFLHSQGLVHRDIKLKNVLL--------DKKNRA----KITDLGFCKPEAMmSGS--IVGTPIHMAPEL--FS 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 GEeeYTEKVDCFSFG-MFIY---ENISLRQPFE---GHESIKECILEGSRPaltQRETQFPTCCLDLMVLCWHEQPRRRP 1992
Cdd:cd13975   173 GK--YDNSVDVYAFGiLFWYlcaGHVKLPEAFEqcaSKDHLWNNVRKGVRP---ERLPVFDEECWNLMEACWSGDPSQRP 247

                  ....*....
gi 442620116 1993 TASQIVSIL 2001
Cdd:cd13975   248 LLGIVQPKL 256
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
1779-1953 4.15e-09

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: 60.88  E-value: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLK-HPNIVPLVGICI------KPLALVLELaplggLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLH 1851
Cdd:cd07857    48 ALRELKLLRHFRgHKNITCLYDMDIvfpgnfNELYLYEEL-----MEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPsgakGFGGTEGFM----------APEIIRYNge 1921
Cdd:cd07857   123 SANVLHRDLKPGNLLV-------NADC-----ELKICDFGLARGFSE----NPGENAGFMteyvatrwyrAPEIMLSF-- 184
                         170       180       190
                  ....*....|....*....|....*....|..
gi 442620116 1922 EEYTEKVDCFSFGMFIYENISLRQPFEGHESI 1953
Cdd:cd07857   185 QSYTKAIDVWSVGCILAELLGRKPVFKGKDYV 216
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
1781-1948 4.36e-09

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 59.62  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIKP---LALVLELAPLGGL-DALLrhyrrsgaHMGP---HTFQTLVLQAARAIEYLHRR 1853
Cdd:cd14163    49 RELQIVERLDHKNIIHVYEMLESAdgkIYLVMELAEDGDVfDCVL--------HGGPlpeHRAKALFRQLVEAIRYCHGC 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVwelpqphtedSPRNLvhiKIADYGISRQTAPSG---AKGFGGTEGFMAPEIIRynGEEEYTEKVDC 1930
Cdd:cd14163   121 GVAHRDLKCENALL----------QGFTL---KLTDFGFAKQLPKGGrelSQTFCGSTAYAAPEVLQ--GVPHDSRKGDI 185
                         170
                  ....*....|....*...
gi 442620116 1931 FSFGMFIYENISLRQPFE 1948
Cdd:cd14163   186 WSMGVVLYVMLCAQLPFD 203
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
1774-1998 4.75e-09

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: 59.95  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1774 KAYCTARQELAVLLTL-KHPNIVPLVGICI--KPLALVLELAPlGG--LDALLRHY----RRSGAHMgphtfQTLvlqaA 1844
Cdd:cd14091    35 KSKRDPSEEIEILLRYgQHPNIITLRDVYDdgNSVYLVTELLR-GGelLDRILRQKffseREASAVM-----KTL----T 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1845 RAIEYLHRRRIIYRDLKSENVLVwelpqphtEDSPRNLVHIKIADYGISRQ-TAPSG---AKGFggTEGFMAPEIIRYNG 1920
Cdd:cd14091   105 KTVEYLHSQGVVHRDLKPSNILY--------ADESGDPESLRICDFGFAKQlRAENGllmTPCY--TANFVAPEVLKKQG 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1921 eeeYTEKVDCFSFGMFIYENISLRQPF-----EGHESIKECILEG------------SRPA--LTQRetqfptccldlMV 1981
Cdd:cd14091   175 ---YDAACDIWSLGVLLYTMLAGYTPFasgpnDTPEVILARIGSGkidlsggnwdhvSDSAkdLVRK-----------ML 240
                         250
                  ....*....|....*..
gi 442620116 1982 lcwHEQPRRRPTASQIV 1998
Cdd:cd14091   241 ---HVDPSQRPTAAQVL 254
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
1711-1947 5.29e-09

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: 59.98  E-value: 5.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKAnckvRGARSFKPVAMKMLQpVPPGarakESALmafkvavgkwdrdPLQhsckaycTARqELAVLLTLK 1790
Cdd:cd07863     8 IGVGAYGTVYKA----RDPHSGHFVALKSVR-VQTN----EDGL-------------PLS-------TVR-EVALLKRLE 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 ---HPNIVPLVGICIK-------PLALVLElaplgGLDALLRHYRRSGAHMG--PHTFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd07863    58 afdHPNIVRLMDVCATsrtdretKVTLVFE-----HVDQDLRTYLDKVPPPGlpAETIKDLMRQFLRGLDFLHANCIVHR 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWELPQphtedsprnlvhIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMfI 1937
Cdd:cd07863   133 DLKPENILVTSGGQ------------VKLADFGLARIYSCQMAlTPVVVTLWYRAPEVLL---QSTYATPVDMWSVGC-I 196
                         250
                  ....*....|
gi 442620116 1938 YENISLRQPF 1947
Cdd:cd07863   197 FAEMFRRKPL 206
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
1709-1944 5.33e-09

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: 60.07  E-value: 5.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1709 SLLGRGAFGFVFKanckvrGARSFKPVAMKMLqpvppgarakesalmafkvavgkwdrdPLQHscKAYCTARQELAVLLT 1788
Cdd:cd14054     1 QLIGQGRYGTVWK------GSLDERPVAVKVF---------------------------PARH--RQNFQNEKDIYELPL 45
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKPLA-------LVLELAPLGGLDALLRHYRRSGahmgpHTFQTLVLQAARAIEYLH--RRR----- 1854
Cdd:cd14054    46 MEHSNILRFIGADERPTAdgrmeylLVLEYAPKGSLCSYLRENTLDW-----MSSCRMALSLTRGLAYLHtdLRRgdqyk 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 --IIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISrqTAPSGAKGFG--------------GTEGFMAPEI--- 1915
Cdd:cd14054   121 paIAHRDLNSRNVLV------------KADGSCVICDFGLA--MVLRGSSLVRgrpgaaenasisevGTLRYMAPEVleg 186
                         250       260       270
                  ....*....|....*....|....*....|
gi 442620116 1916 -IRYNGEEEYTEKVDCFSFGMFIYEnISLR 1944
Cdd:cd14054   187 aVNLRDCESALKQVDVYALGLVLWE-IAMR 215
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
1803-1949 5.97e-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: 5.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1803 KPLALVLELAPLGGLDALLRHyrrsgahMGPHTFQTLVLQAAR---AIEYLHRRRIIYRDLKSENVLVwelpqphtedsp 1879
Cdd:cd05609    73 RHLCMVMEYVEGGDCATLLKN-------IGPLPVDMARMYFAEtvlALEYLHSYGIVHRDLKPDNLLI------------ 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1880 RNLVHIKIADYGIS-----------------RQTAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENIS 1942
Cdd:cd05609   134 TSMGHIKLTDFGLSkiglmslttnlyeghieKDTREFLDKQVCGTPEYIAPEVILRQG---YGKPVDWWAMGIILYEFLV 210

                  ....*..
gi 442620116 1943 LRQPFEG 1949
Cdd:cd05609   211 GCVPFFG 217
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
1805-1952 8.09e-09

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: 59.37  E-value: 8.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 LALVLELAPLGGLdallrHYrrsgaHMGPH---TFQTLVLQAARAI---EYLHRRRIIYRDLKSENVLVWELPqphteds 1878
Cdd:cd05606    73 LCFILDLMNGGDL-----HY-----HLSQHgvfSEAEMRFYAAEVIlglEHMHNRFIVYRDLKPANILLDEHG------- 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1879 prnlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNgeEEYTEKVDCFSFGMFIYENISLRQPFEGHES 1952
Cdd:cd05606   136 -----HVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKG--VAYDSSADWFSLGCMLYKLLKGHSPFRQHKT 202
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
1711-1955 8.64e-09

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 59.32  E-value: 8.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKMLqpvppgaRAKESALMAFkvavgkwdrdplqhsckaycTARQELAVLLTLK 1790
Cdd:cd07869    13 LGEGSYATVYKGKSKVNG----KLVALKVI-------RLQEEEGTPF--------------------TAIREASLLKGLK 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGI--CIKPLALVLELAPLGGLDALLRHyrRSGAHmgPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVW 1868
Cdd:cd07869    62 HANIVLLHDIihTKETLTLVFEYVHTDLCQYMDKH--PGGLH--PENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLIS 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 ELPQphtedsprnlvhIKIADYGISR-QTAPSGA-KGFGGTEGFMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd07869   138 DTGE------------LKLADFGLARaKSVPSHTySNEVVTLWYRPPDVLL--GSTEYSTCLDMWGVGCIFVEMIQGVAA 203

                  ....*....
gi 442620116 1947 FEGHESIKE 1955
Cdd:cd07869   204 FPGMKDIQD 212
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
1779-2001 9.02e-09

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: 58.88  E-value: 9.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTL-KHPNIVPLVG---ICIKPLALVL---ELAPlGGLDALLRHyrrsgahMGPHTFQ-----TLVLQAARA 1846
Cdd:cd13985    44 AIKEIEIMKRLcGHPNIVQYYDsaiLSSEGRKEVLllmEYCP-GSLVDILEK-------SPPSPLSeeevlRIFYQICQA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHR--RRIIYRDLKSENVLVwelpqphteDSPRNlvhIKIADYG-ISRQT-APSGAKGFGGTEG---------FMAP 1913
Cdd:cd13985   116 VGHLHSqsPPIIHRDIKIENILF---------SNTGR---FKLCDFGsATTEHyPLERAEEVNIIEEeiqknttpmYRAP 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1914 EIIRYNGEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIKECILEGSRPAlTQRETQFPTCCLDLMVlcwHEQPRRRPT 1993
Cdd:cd13985   184 EMIDLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVAGKYSIPE-QPRYSPELHDLIRHML---TPDPAERPD 259

                  ....*...
gi 442620116 1994 ASQIVSIL 2001
Cdd:cd13985   260 IFQVINII 267
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
1793-1950 9.28e-09

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


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 59.27  E-value: 9.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1793 NIVPLVGICIKPLALVLELAPLGGlDALLRHYRRSgAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpq 1872
Cdd:cd14174    61 NILELIEFFEDDTRFYLVFEKLRG-GSILAHIQKR-KHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILC----- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1873 phteDSPRNLVHIKIADYGISRQ----------TAPSGAKGFGGTEgFMAPEIIRYNGEEE--YTEKVDCFSFGMFIYEN 1940
Cdd:cd14174   134 ----ESPDKVSPVKICDFDLGSGvklnsactpiTTPELTTPCGSAE-YMAPEVVEVFTDEAtfYDKRCDLWSLGVILYIM 208
                         170
                  ....*....|
gi 442620116 1941 ISLRQPFEGH 1950
Cdd:cd14174   209 LSGYPPFVGH 218
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
1838-2003 9.38e-09

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 60.04  E-value: 9.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1838 TLVLQAARAIEYLHRRRIIYRDLKSENVLvweLPQPHTedsprnlvhIKIADYGISRQTAPSGAKGFGGTE----GFMAP 1913
Cdd:cd05105   241 SFTYQVARGMEFLASKNCVHRDLAARNVL---LAQGKI---------VKICDFGLARDIMHDSNYVSKGSTflpvKWMAP 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1914 EIIRYNgeeEYTEKVDCFSFGMFIYENISL-RQPFEG---HESIKECILEGSRPALTQRETQFptcCLDLMVLCWHEQPR 1989
Cdd:cd05105   309 ESIFDN---LYTTLSDVWSYGILLWEIFSLgGTPYPGmivDSTFYNKIKSGYRMAKPDHATQE---VYDIMVKCWNSEPE 382
                         170
                  ....*....|....
gi 442620116 1990 RRPTASQIVSILSA 2003
Cdd:cd05105   383 KRPSFLHLSDIVES 396
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
1805-1954 9.62e-09

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: 59.63  E-value: 9.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 LALVLELAPLGGLDALL-RHYRRSGAHMGPHTFQTLVLqaarAIEYLHRRRIIYRDLKSENVLVwelpqphteDSprnLV 1883
Cdd:cd05601    76 LYLVMEYHPGGDLLSLLsRYDDIFEESMARFYLAELVL----AIHSLHSMGYVHRDIKPENILI---------DR---TG 139
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1884 HIKIADYGISRQTAPSGAKGFG---GTEGFMAPEI---IRYNGEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIK 1954
Cdd:cd05601   140 HIKLADFGSAAKLSSDKTVTSKmpvGTPDYIAPEVltsMNGGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIK 216
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
1707-1934 1.11e-08

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: 58.92  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKanCKVRGARSFkpVAMKmlqpvppgaRAKESalmafkvavgkwDRDPLQHSckaycTARQELAVL 1786
Cdd:cd07847     5 KLSKIGEGSYGVVFK--CRNRETGQI--VAIK---------KFVES------------EDDPVIKK-----IALREIRML 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd07847    55 KQLKHPNLVNLIEVFRRKrkLHLVFEYCDHTVLNELEKNPRG----VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPEN 130
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1865 VLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRynGEEEYTEKVDCFSFG 1934
Cdd:cd07847   131 ILI-------TKQG-----QIKLCDFGFARILTGPGDDytDYVATRWYRAPELLV--GDTQYGPPVDVWAIG 188
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
1782-1996 1.26e-08

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 58.39  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGG---LDALLRHYRRSGAHMGPHTFQTLvlqaaRAIEYLHRRRIIYR 1858
Cdd:cd14110    49 EYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGpelLYNLAERNSYSEAEVTDYLWQIL-----SAVDYLHSRRILHL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVWElpqphtedspRNLVhiKIADYGISRQTAPSGA---KGFGGTEGFMAPEIIRYNGEEEYTekvDCFSFGM 1935
Cdd:cd14110   124 DLRSENMIITE----------KNLL--KIVDLGNAQPFNQGKVlmtDKKGDYVETMAPELLEGQGAGPQT---DIWAIGV 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116 1936 FIYENISLRQPF------EGHESIKECILEGSR--PALTQRETQF--PTCCldlmvlcwhEQPRRRPTASQ 1996
Cdd:cd14110   189 TAFIMLSADYPVssdlnwERDRNIRKGKVQLSRcyAGLSGGAVNFlkSTLC---------AKPWGRPTASE 250
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
1774-1996 1.27e-08

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 58.37  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1774 KAYCTARQELAVLLTLKHPNIVPLVGICIKPLALVLeLAPLGGLDALLRHYRRSGahMGPHTFQTLVLQAARAIEYLHRR 1853
Cdd:cd14108    40 KKKTSARRELALLAELDHKSIVRFHDAFEKRRVVII-VTELCHEELLERITKRPT--VCESEVRSYMRQLLEGIEYLHQN 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVWElpqpHTEDsprnlvHIKIADYGISRQTAPSGAKGFG-GTEGFMAPEIIrynGEEEYTEKVDCFS 1932
Cdd:cd14108   117 DVLHLDLKPENLLMAD----QKTD------QVRICDFGNAQELTPNEPQYCKyGTPEFVAPEIV---NQSPVSKVTDIWP 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1933 FGMFIYENISLRQPFEGhESIKECILEGSRPALTQRETQFPTCCLD-----LMVLCwheQPRRRPTASQ 1996
Cdd:cd14108   184 VGVIAYLCLTGISPFVG-ENDRTTLMNIRNYNVAFEESMFKDLCREakgfiIKVLV---SDRLRPDAEE 248
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
1791-1950 1.34e-08

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 58.89  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPLALVLELAPLGGLDALLRHYRRSgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwel 1870
Cdd:cd14173    59 HRNVLELIEFFEEEDKFYLVFEKMRGGSILSHIHRRR--HFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILC--- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1871 pqphteDSPRNLVHIKIADY----GI------SRQTAPSGAKGFGGTEgFMAPEIIRYNGEEE--YTEKVDCFSFGMFIY 1938
Cdd:cd14173   134 ------EHPNQVSPVKICDFdlgsGIklnsdcSPISTPELLTPCGSAE-YMAPEVVEAFNEEAsiYDKRCDLWSLGVILY 206
                         170
                  ....*....|..
gi 442620116 1939 ENISLRQPFEGH 1950
Cdd:cd14173   207 IMLSGYPPFVGR 218
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
1778-1999 1.42e-08

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: 58.14  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIKP--------LALVLELAPLGGLDALLRHYRrsgaHMGPHTFQTLVLQAARAIEY 1849
Cdd:cd14012    44 LLEKELESLKKLRHPNLVSYLAFSIERrgrsdgwkVYLLTEYAPGGSLSELLDSVG----SVPLDTARRWTLQLLEALEY 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1850 LHRRRIIYRDLKSENVLVwelpqphTEDSPRNLVhiKIADYGISRQTAPSGAKGFGGT---EGFMAPEIIRYNGeeEYTE 1926
Cdd:cd14012   120 LHRNGVVHKSLHAGNVLL-------DRDAGTGIV--KLTDYSLGKTLLDMCSRGSLDEfkqTYWLPPELAQGSK--SPTR 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1927 KVDCFSFGMFIYENISLRQPFEGHESIKECILEGSRPALTQretqfptcclDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14012   189 KTDVWDLGLLFLQMLFGLDVLEKYTSPNPVLVSLDLSASLQ----------DFLSKCLSLDPKKRPTALELLP 251
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1781-1939 1.51e-08

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: 58.60  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVG-------ICIkplalVLELAPLGGLDALLRHYRRSgahmgPHTFQTLVLQAA-RAIEYLH- 1851
Cdd:cd06615    48 RELKVLHECNSPYIVGFYGafysdgeISI-----CMEHMDGGSLDQVLKKAGRI-----PENILGKISIAVlRGLTYLRe 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 RRRIIYRDLKSENVLVwelpqphtedSPRNlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEiiRYNGeEEYTEKVDCF 1931
Cdd:cd06615   118 KHKIMHRDVKPSNILV----------NSRG--EIKLCDFGVSGQLIDSMANSFVGTRSYMSPE--RLQG-THYTVQSDIW 182

                  ....*...
gi 442620116 1932 SFGMFIYE 1939
Cdd:cd06615   183 SLGLSLVE 190
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
1791-1949 1.52e-08

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: 58.44  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP----LALVLELAPLGgLDALLRHYRRsgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd07831    57 HPNILRLIEVLFDRktgrLALVFELMDMN-LYELIKGRKR---PLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENIL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1867 VwelpqphtedsprNLVHIKIADYGISR---QTAPSGAkgFGGTEGFMAPEIIRYNGeeEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd07831   133 I-------------KDDILKLADFGSCRgiySKPPYTE--YISTRWYRAPECLLTDG--YYGPKMDIWAVGCVFFEILSL 195

                  ....*.
gi 442620116 1944 RQPFEG 1949
Cdd:cd07831   196 FPLFPG 201
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
1782-1948 1.58e-08

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: 58.02  E-value: 1.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLgglDALLRHYRRSGAHMGPHTfQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd14187    57 EIAIHRSLAHQHVVGFHGFFEDNdfVYVVLELCRR---RSLLELHKRRKALTEPEA-RYYLRQIILGCQYLHRNRVIHRD 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphTEDsprnlVHIKIADYGISRQTAPSG--AKGFGGTEGFMAPEIIrynGEEEYTEKVDCFSFGMFI 1937
Cdd:cd14187   133 LKLGNLFL-------NDD-----MEVKIGDFGLATKVEYDGerKKTLCGTPNYIAPEVL---SKKGHSFEVDIWSIGCIM 197
                         170
                  ....*....|.
gi 442620116 1938 YENISLRQPFE 1948
Cdd:cd14187   198 YTLLVGKPPFE 208
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
1710-1947 2.24e-08

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: 58.49  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPVPPGARAKESALMAfkvavgkwdrdplqhsckayctarqELAVLL-T 1788
Cdd:cd05602    14 VIGKGSFGKVLLA----RHKSDEKFYAVKVLQKKAILKKKEEKHIMS-------------------------ERNVLLkN 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKPLALVLELAPLGGLDaLLRHYRRSGAHMGPHTfQTLVLQAARAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd05602    65 VKHPFLVGLHFSFQTTDKLYFVLDYINGGE-LFYHLQRERCFLEPRA-RFYAAEIASALGYLHSLNIVYRDLKPENILL- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphteDSPRnlvHIKIADYGISRQT-APSGAKG-FGGTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISLRQP 1946
Cdd:cd05602   142 --------DSQG---HIVLTDFGLCKENiEPNGTTStFCGTPEYLAPEVLH---KQPYDRTVDWWCLGAVLYEMLYGLPP 207

                  .
gi 442620116 1947 F 1947
Cdd:cd05602   208 F 208
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
1815-1999 2.25e-08

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 57.80  E-value: 2.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1815 GGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVWELPQPH-----------TEDSPR-NL 1882
Cdd:cd14051    85 GSLADAISENEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVsseeeeedfegEEDNPEsNE 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1883 VHIKIADYGisRQTAPSGAKGFGGTEGFMAPEIIRyngeEEYTE--KVDCFSFGMFIYENI---SLrqPFEGHESIKecI 1957
Cdd:cd14051   165 VTYKIGDLG--HVTSISNPQVEEGDCRFLANEILQ----ENYSHlpKADIFALALTVYEAAgggPL--PKNGDEWHE--I 234
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 442620116 1958 LEGSRPALTQRETQFpTCCLDLMVlcwHEQPRRRPTASQIVS 1999
Cdd:cd14051   235 RQGNLPPLPQCSPEF-NELLRSMI---HPDPEKRPSAAALLQ 272
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
1710-1999 2.39e-08

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 57.69  E-value: 2.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKanckVRGARSFKPVAMKmlqpvppgarakesalmafKVavgkwdrdpLQHSCKAYCTARQELAVLLTL 1789
Cdd:cd13986     7 LLGEGGFSFVYL----VEDLSTGRLYALK-------------------KI---------LCHSKEDVKEAMREIENYRLF 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLA-------LVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLH---RRRIIYRD 1859
Cdd:cd13986    55 NHPNILRLLDSQIVKEAggkkevyLLLPYYKRGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRD 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVWELPQPHTED------SPRNLVH----IKIADYGISRQTAPsgakgfggtegFMAPEIIRYNGEEEYTEKVD 1929
Cdd:cd13986   135 IKPGNVLLSEDDEPILMDlgsmnpARIEIEGrreaLALQDWAAEHCTMP-----------YRAPELFDVKSHCTIDEKTD 203
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1930 CFSFGMFIYENISLRQPFEGHE----SIKECILEG-SRPaltQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd13986   204 IWSLGCTLYALMYGESPFERIFqkgdSLALAVLSGnYSF---PDNSRYSEELHQLVKSMLVVNPAERPSIDDLLS 275
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
1780-1998 2.78e-08

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 57.81  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKH-PNIVPLVGICIKP--------LALVLELAPLGGLDALLRHYRrsGAHMGPHTFQTLVLQAARAIEYL 1850
Cdd:cd06637    50 KQEINMLKKYSHhRNIATYYGAFIKKnppgmddqLWLVMEFCGAGSVTDLIKNTK--GNTLKEEWIAYICREILRGLSHL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIR--YNGEEEYTE 1926
Cdd:cd06637   128 HQHKVIHRDIKGQNVLL-------TENA-----EVKLVDFGVSAQLDRTVGRrnTFIGTPYWMAPEVIAcdENPDATYDF 195
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1927 KVDCFSFGMFIYENISLRQPFEGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06637   196 KSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPAPRLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLM 267
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
1710-2002 2.80e-08

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: 57.83  E-value: 2.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRgarsfkPVAMKMLQpvppgARAKESalmafkvavgkWDRDplqhsckayctarQELAVLLTL 1789
Cdd:cd13998     2 VIGKGRFGEVWKASLKNE------PVAVKIFS-----SRDKQS-----------WFRE-------------KEIYRTPML 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVG------ICIKPLALVLELAPLGGLDALLRHyrrsgahmgpHTFQT-----LVLQAARAIEYLH------- 1851
Cdd:cd13998    47 KHENILQFIAaderdtALRTELWLVTAFHPNGSL*DYLSL----------HTIDWvslcrLALSVARGLAHLHseipgct 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1852 --RRRIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFG------GTEGFMAPEI----IRYN 1919
Cdd:cd13998   117 qgKPAIAHRDLKSKNILV------------KNDGTCCIADFGLAVRLSPSTGEEDNanngqvGTKRYMAPEVlegaINLR 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 GEEEYtEKVDCFSFGMFIYENIS-----------LRQPFEGH-------ESIKECIL-EGSRPALTQRETQFPTCCL--D 1978
Cdd:cd13998   185 DFESF-KRVDIYAMGLVLWEMASrctdlfgiveeYKPPFYSEvpnhpsfEDMQEVVVrDKQRPNIPNRWLSHPGLQSlaE 263
                         330       340
                  ....*....|....*....|....
gi 442620116 1979 LMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd13998   264 TIEECWDHDAEARLTAQCIEERLS 287
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
1788-2002 2.95e-08

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: 57.65  E-value: 2.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRSGAhMGPH-------TFQTLVLQAARAIEYLHRRRIIYR 1858
Cdd:cd14206    53 SLQHPNILQCLGLCTEtiPFLLIMEFCQLGDLKRYLRAQRKADG-MTPDlptrdlrTLQRMAYEITLGLLHLHKNNYIHS 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1859 DLKSENVLVwelpqphTEDsprnlVHIKIADYGISRQTApsgAKGFGGTEG-------FMAPEII-RYNGE---EEYTEK 1927
Cdd:cd14206   132 DLALRNCLL-------TSD-----LTVRIGDYGLSHNNY---KEDYYLTPDrlwiplrWVAPELLdELHGNlivVDQSKE 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1928 VDCFSFGMFIYENISL-RQPFEgHES--------IKECILEGSRPALTQRETQFptcCLDLMVLCWHEqPRRRPTASQIV 1998
Cdd:cd14206   197 SNVWSLGVTIWELFEFgAQPYR-HLSdeevltfvVREQQMKLAKPRLKLPYADY---WYEIMQSCWLP-PSQRPSVEELH 271

                  ....
gi 442620116 1999 SILS 2002
Cdd:cd14206   272 LQLS 275
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1778-1949 3.28e-08

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 57.57  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIKPLA--LVLELAPLGgldALLRHYRRSgAHMGPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd14180    47 TQREVAALRLCQSHPNIVALHEVLHDQYHtyLVMELLRGG---ELLDRIKKK-ARFSESEASQLMRSLVSAVSFMHEAGV 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVWElpqpHTEDSPrnlvhIKIADYGISR----QTAPSGAKGFggTEGFMAPEIIRYNGeeeYTEKVDCF 1931
Cdd:cd14180   123 VHRDLKPENILYAD----ESDGAV-----LKVIDFGFARlrpqGSRPLQTPCF--TLQYAAPELFSNQG---YDESCDLW 188
                         170
                  ....*....|....*...
gi 442620116 1932 SFGMFIYENISLRQPFEG 1949
Cdd:cd14180   189 SLGVILYTMLSGQVPFQS 206
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
1789-1994 3.44e-08

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: 57.28  E-value: 3.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIK------PLALVLELAPLGGL-DALLRHyrrsgaHMGPHTFQTLVLQAARAIEYLH-----RRR-- 1854
Cdd:cd14056    46 LRHENILGFIAADIKstgswtQLWLITEYHEHGSLyDYLQRN------TLDTEEALRLAYSAASGLAHLHteivgTQGkp 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 -IIYRDLKSENVLVwelpqphtedsPRNLVhIKIADYGIS---RQTAPSGAKGFG---GTEGFMAPEII--RYNGE--EE 1923
Cdd:cd14056   120 aIAHRDLKSKNILV-----------KRDGT-CCIADLGLAvryDSDTNTIDIPPNprvGTKRYMAPEVLddSINPKsfES 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1924 YtEKVDCFSFGMFIYEnISLR-----------QPFEGH-------ESIKECI-LEGSRPALTQRETQFPtcCL----DLM 1980
Cdd:cd14056   188 F-KMADIYSFGLVLWE-IARRceiggiaeeyqLPYFGMvpsdpsfEEMRKVVcVEKLRPPIPNRWKSDP--VLrsmvKLM 263
                         250
                  ....*....|....
gi 442620116 1981 VLCWHEQPRRRPTA 1994
Cdd:cd14056   264 QECWSENPHARLTA 277
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
1782-1981 5.59e-08

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: 57.04  E-value: 5.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVP-----LVGiciKPLALVLELAPLGGLDALLrhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd06654    67 EILVMRENKNPNIVNyldsyLVG---DELWVVMEYLAGGSLTDVV-----TETCMDEGQIAAVCRECLQALEFLHSNQVI 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd06654   139 HRDIKSDNILL------GMDGS------VKLTDFGFCAQITPEQSKrsTMVGTPYWMAPEVVT---RKAYGPKVDIWSLG 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1935 MFIYENISLRQPFEGHESIKECILEGSR--PALTQRET------QFPTCCLDLMV 1981
Cdd:cd06654   204 IMAIEMIEGEPPYLNENPLRALYLIATNgtPELQNPEKlsaifrDFLNRCLEMDV 258
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
1755-1998 6.48e-08

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


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 56.56  E-value: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1755 MAFKVAV-GKWDRDPlqhsckayctaRQELAVLLTL-KHPNIVPLVGICI--KPLALVLELAPLGGL-DALLRHyrrsgA 1829
Cdd:cd14177    30 MEFAVKIiDKSKRDP-----------SEEIEILMRYgQHPNIITLKDVYDdgRYVYLVTELMKGGELlDRILRQ-----K 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1830 HMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVWelpqphteDSPRNLVHIKIADYGISRQTapsgaKGFGG--- 1906
Cdd:cd14177    94 FFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYM--------DDSANADSIRICDFGFAKQL-----RGENGlll 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1907 ----TEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQPFEG--HESIKECILEGSRPALTQRETQFPTC---CL 1977
Cdd:cd14177   161 tpcyTANFVAPEVLMRQG---YDAACDIWSLGVLLYTMLAGYTPFANgpNDTPEEILLRIGSGKFSLSGGNWDTVsdaAK 237
                         250       260
                  ....*....|....*....|.
gi 442620116 1978 DLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14177   238 DLLSHMLHVDPHQRYTAEQVL 258
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
1708-2001 7.09e-08

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: 57.22  E-value: 7.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANC-KVRGARSFKPVAMKMLQPvppGARAKE-SALMAfkvavgkwdrdplqhsckayctarqELAV 1785
Cdd:cd05104    40 GKTLGAGAFGKVVEATAyGLAKADSAMTVAVKMLKP---SAHSTErEALMS-------------------------ELKV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1786 LLTL-KHPNIVPLVGICI--KPLALVLELAPLGGLDALLR------------------HYR------------------- 1825
Cdd:cd05104    92 LSYLgNHINIVNLLGACTvgGPTLVITEYCCYGDLLNFLRrkrdsficpkfedlaeaaLYRnllhqremacdslneymdm 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1826 --------------RSGAHMGPHTFQTLVL--------------------QAARAIEYLHRRRIIYRDLKSENVLvwelp 1871
Cdd:cd05104   172 kpsvsyvvptkadkRRGVRSGSYVDQDVTSeileedelaldtedllsfsyQVAKGMEFLASKNCIHRDLAARNIL----- 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1872 qphtedsprnLVH---IKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRyngEEEYTEKVDCFSFGMFIYENISL- 1943
Cdd:cd05104   247 ----------LTHgriTKICDFGLARDIRNDSNYVVKGNArlpvKWMAPESIF---ECVYTFESDVWSYGILLWEIFSLg 313
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442620116 1944 RQPFEG---HESIKECILEGSR---PALTqretqfPTCCLDLMVLCWHEQPRRRPTASQIVSIL 2001
Cdd:cd05104   314 SSPYPGmpvDSKFYKMIKEGYRmdsPEFA------PSEMYDIMRSCWDADPLKRPTFKQIVQLI 371
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1708-1998 8.69e-08

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 55.63  E-value: 8.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGARsfkpVAMKMLqpvppgARAKesalmafkvaVGKWDRDPLQHSCKayctarQELAVLL 1787
Cdd:cd14101     5 GNLLGKGGFGTVYAGHRISDGLQ----VAIKQI------SRNR----------VQQWSKLPGVNPVP------NEVALLQ 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1788 TL----KHPNIVPLVGICIKP--LALVLElAPLGGLDaLLRHYRRSGAhMGPHTFQTLVLQAARAIEYLHRRRIIYRDLK 1861
Cdd:cd14101    59 SVgggpGHRGVIRLLDWFEIPegFLLVLE-RPQHCQD-LFDYITERGA-LDESLARRFFKQVVEAVQHCHSKGVVHRDIK 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphteDSPRNlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNGEEEYTEKVdcFSFGMFIYENI 1941
Cdd:cd14101   136 DENILV---------DLRTG--DIKLIDFGSGATLKDSMYTDFDGTRVYSPPEWILYHQYHALPATV--WSLGILLYDMV 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1942 SLRQPFEGHESIKECILEGSRPAltqretqFPTCClDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14101   203 CGDIPFERDTDILKAKPSFNKRV-------SNDCR-SLIRSCLAYNPSDRPSLEQIL 251
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
1779-1995 8.98e-08

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 55.74  E-value: 8.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGL-DALLRHyrrsgAHMGPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd14115    36 AAHEAALLQHLQHPQYITLHDTYESPtsYILVLELMDDGRLlDYLMNH-----DELMEEKVAFYIRDIMEALQYLHNCRV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwELPQPhtedSPRnlvhIKIADYGISRQ-TAPSGAKGFGGTEGFMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd14115   111 AHLDIKPENLLI-DLRIP----VPR----VKLIDLEDAVQiSGHRHVHHLLGNPEFAAPEVIQ---GTPVSLATDIWSIG 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1935 MFIYENISLRQPF--EGHES--IKECILEGSRPalTQRETQFPTCCLDLMVLCWHEQPRRRPTAS 1995
Cdd:cd14115   179 VLTYVMLSGVSPFldESKEEtcINVCRVDFSFP--DEYFGDVSQAARDFINVILQEDPRRRPTAA 241
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
1703-1999 1.01e-07

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: 55.39  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1703 ECIIKGSLLGRGAFGFVFKANCKvrgarsfkpvamkmlqpvppgaraKESALMAFKVAVGKWDRDplQHSCKAYCTARQE 1782
Cdd:cd14050     1 QCFTILSKLGEGSFGEVFKVRSR------------------------EDGKLYAVKRSRSRFRGE--KDRKRKLEEVERH 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1783 LAVLltlKHPNIVPLVGICI--KPLALVLELAplgglDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDL 1860
Cdd:cd14050    55 EKLG---EHPNCVRFIKAWEekGILYIQTELC-----DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDI 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1861 KSENVLVwelpqphtedSPRNLVhiKIADYGISRQTAPSGAKgfGGTEG---FMAPEIIryNGeeEYTEKVDCFSFGMFI 1937
Cdd:cd14050   127 KPANIFL----------SKDGVC--KLGDFGLVVELDKEDIH--DAQEGdprYMAPELL--QG--SFTKAADIFSLGITI 188
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1938 YE---NISLrqPFEG-------HESIKECILEGSRPALtqretqfptccLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14050   189 LElacNLEL--PSGGdgwhqlrQGYLPEEFTAGLSPEL-----------RSIIKLMMDPDPERRPTAEDLLA 247
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
1700-2001 1.03e-07

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 56.94  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1700 IPSECIIKGSLLGRGAFGFVFKANCK-VRGARSFKPVAMKMLQPVppgARAKES-ALMAfkvavgkwdrdplqhsckayc 1777
Cdd:cd05107    34 MPRDNLVLGRTLGSGAFGRVVEATAHgLSHSQSTMKVAVKMLKST---ARSSEKqALMS--------------------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 tarqELAVLLTL-KHPNIVPLVGICIK--PLALVLELAPLGGL-DAL-------LRHY----RRSGA------------- 1829
Cdd:cd05107    90 ----ELKIMSHLgPHLNIVNLLGACTKggPIYIITEYCRYGDLvDYLhrnkhtfLQYYldknRDDGSlisggstplsqrk 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1830 -------------------------------------------HMGPH-----------------------TFQTLV--- 1840
Cdd:cd05107   166 shvslgsesdggymdmskdesadyvpmqdmkgtvkyadiessnYESPYdqylpsapertrrdtlinespalSYMDLVgfs 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1841 LQAARAIEYLHRRRIIYRDLKSENVLVWElpqphtedspRNLVhiKIADYGISRQTA-PSGAKGFGGT---EGFMAPEII 1916
Cdd:cd05107   246 YQVANGMEFLASKNCVHRDLAARNVLICE----------GKLV--KICDFGLARDIMrDSNYISKGSTflpLKWMAPESI 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1917 RYNgeeEYTEKVDCFSFGMFIYENISL-RQPFEG---HESIKECILEG---SRPALTQRETqfptccLDLMVLCWHEQPR 1989
Cdd:cd05107   314 FNN---LYTTLSDVWSFGILLWEIFTLgGTPYPElpmNEQFYNAIKRGyrmAKPAHASDEI------YEIMQKCWEEKFE 384
                         410
                  ....*....|..
gi 442620116 1990 RRPTASQIVSIL 2001
Cdd:cd05107   385 IRPDFSQLVHLV 396
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
1781-2003 1.08e-07

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 55.98  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLK-HPNIVPLVG-----------ICIKPLaLVLELAPLGGLDALLRHyrRSGAHMGPHTFQTLVLQAARAIE 1848
Cdd:cd14036    46 QEINFMKKLSgHPNIVQFCSaasigkeesdqGQAEYL-LLTELCKGQLVDFVKKV--EAPGPFSPDTVLKIFYQTCRAVQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1849 YLHRRR--IIYRDLKSENVLVWELPQ------------PHTEDSPRNLVHIKIADYGISRQTAPSgakgfggtegFMAPE 1914
Cdd:cd14036   123 HMHKQSppIIHRDLKIENLLIGNQGQiklcdfgsatteAHYPDYSWSAQKRSLVEDEITRNTTPM----------YRTPE 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1915 IIRYNGEEEYTEKVDCFSFGMFIYENISLRQPFEghESIKECILEGSRpALTQRETQFpTCCLDLMVLCWHEQPRRRPTA 1994
Cdd:cd14036   193 MIDLYSNYPIGEKQDIWALGCILYLLCFRKHPFE--DGAKLRIINAKY-TIPPNDTQY-TVFHDLIRSTLKVNPEERLSI 268

                  ....*....
gi 442620116 1995 SQIVSILSA 2003
Cdd:cd14036   269 TEIVEQLQE 277
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
1778-1949 1.09e-07

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: 55.95  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGI--CIKPLALVLELaplggLDALLRHYRRSGAHMG---PHTFQTLVLQAARAIEYLHR 1852
Cdd:cd07836    44 TAIREISLMKELKHENIVRLHDVihTENKLMLVFEY-----MDKDLKKYMDTHGVRGaldPNTVKSFTYQLLKGIAFCHE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 RRIIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRqtapsgakGFG----------GTEGFMAPEIIRynGEE 1922
Cdd:cd07836   119 NRVLHRDLKPQNLLINKRGE------------LKLADFGLAR--------AFGipvntfsnevVTLWYRAPDVLL--GSR 176
                         170       180
                  ....*....|....*....|....*..
gi 442620116 1923 EYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd07836   177 TYSTSIDIWSVGCIMAEMITGRPLFPG 203
pknD PRK13184
serine/threonine-protein kinase PknD;
1789-1947 1.19e-07

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 57.47  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKPLALVLELAPLGG--LDALLRHYRRSGAHMGPHTFQTLV-------LQAARAIEYLHRRRIIYRD 1859
Cdd:PRK13184   59 LIHPGIVPVYSICSDGDPVYYTMPYIEGytLKSLLKSVWQKESLSKELAEKTSVgaflsifHKICATIEYVHSKGVLHRD 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLV----------W--ELPQPHTEDsprNLVHIKIADYGI--SRQTAPSGAKgfgGTEGFMAPEIIRYNgeeEYT 1925
Cdd:PRK13184  139 LKPDNILLglfgevvildWgaAIFKKLEEE---DLLDIDVDERNIcySSMTIPGKIV---GTPDYMAPERLLGV---PAS 209
                         170       180
                  ....*....|....*....|..
gi 442620116 1926 EKVDCFSFGMFIYENISLRQPF 1947
Cdd:PRK13184  210 ESTDIYALGVILYQMLTLSFPY 231
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
1723-1973 1.21e-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: 55.96  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1723 NCKVRGARSFkPVAMKM--------------------LQPVPPGARAKESalmafkvavGKWDRDPLQhsckaycTARQE 1782
Cdd:cd14018     6 NAAVYEAALF-PLAIKMmwnisagssseailrsmgneLVPAPNVALLGEY---------GEVTRLGLQ-------NGRKL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1783 LAvlltlKHPNI----------VPLV--GICIKPLALVLELAPLG-----GLDALLRHYRRS------GAHMGPHTFQTL 1839
Cdd:cd14018    69 LA-----PHPNIirvqraftdsVPLLpgAIEDYPDVLPARLNPSGlghnrTLFLVMKNYPCTlrqylwVNTPSYRLARVM 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1840 VLQAARAIEYLHRRRIIYRDLKSENVLVwELpqpHTEDSPRnLVhikIADYGISRQTAPSGAK--------GFGGTEGFM 1911
Cdd:cd14018   144 ILQLLEGVDHLVRHGIAHRDLKSDNILL-EL---DFDGCPW-LV---IADFGCCLADDSIGLQlpfsswyvDRGGNACLM 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1912 APEIIRY----NGEEEYtEKVDCFSFGMFIYENISLRQPFEGHESikecileGSRPALTQRETQFP 1973
Cdd:cd14018   216 APEVSTAvpgpGVVINY-SKADAWAVGAIAYEIFGLSNPFYGLGD-------TMLESRSYQESQLP 273
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
1711-2007 1.24e-07

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: 55.76  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVfkanCKVRGARSFKPVAMKMLQpvppgARAKESALMAFkvavgkwdrdplqhsckayctarQELAVLLTLK 1790
Cdd:cd06659    29 IGEGSTGVV----CIAREKHSGRQVAVKMMD-----LRKQQRRELLF-----------------------NEVVIMRDYQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVP-----LVGiciKPLALVLELAPLGGLDALLRHYRRSGAHMgpHTFQTLVLQAaraIEYLHRRRIIYRDLKSENV 1865
Cdd:cd06659    77 HPNVVEmyksyLVG---EELWVLMEYLQGGALTDIVSQTRLNEEQI--ATVCEAVLQA---LAYLHSQGVIHRDIKSDSI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1866 LVwelpqphTEDSprnlvHIKIADYGISRQTAPS--GAKGFGGTEGFMAPEIIrynGEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd06659   149 LL-------TLDG-----RVKLSDFGFCAQISKDvpKRKSLVGTPYWMAPEVI---SRCPYGTEVDIWSLGIMVIEMVDG 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1944 RQPFEGHESIKECI-LEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIVS---ILSA--PECI 2007
Cdd:cd06659   214 EPPYFSDSPVQAMKrLRDSPPPKLKNSHKASPVLRDFLERMLVRDPQERATAQELLDhpfLLQTglPECL 283
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
1782-1998 1.29e-07

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: 55.88  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVP-----LVGiciKPLALVLELAPLGGLDALLrhyrrSGAHMGPHTFQTLVLQAARAIEYLHRRRII 1856
Cdd:cd06656    66 EILVMRENKNPNIVNyldsyLVG---DELWVVMEYLAGGSLTDVV-----TETCMDEGQIAAVCRECLQALDFLHSNQVI 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGISRQTAPSGAK--GFGGTEGFMAPEIIRyngEEEYTEKVDCFSFG 1934
Cdd:cd06656   138 HRDIKSDNILL------GMDGS------VKLTDFGFCAQITPEQSKrsTMVGTPYWMAPEVVT---RKAYGPKVDIWSLG 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1935 MFIYENISLRQPFEGHESIKECILEGSR--PALtQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06656   203 IMAIEMVEGEPPYLNENPLRALYLIATNgtPEL-QNPERLSAVFRDFLNRCLEMDVDRRGSAKELL 267
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
1710-1952 1.33e-07

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: 55.82  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPvpPGARAKESALMAFkvavgkwdrdplqhsckaycTARQELAVLLTL 1789
Cdd:cd14223     7 IIGRGGFGEVYGC----RKADTGKMYAMKCLDK--KRIKMKQGETLAL--------------------NERIMLSLVSTG 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKP--LALVLELAPLGGLdallrHYRRSgaHMGPHTFQTLVLQAARAI---EYLHRRRIIYRDLKSEN 1864
Cdd:cd14223    61 DCPFIVCMSYAFHTPdkLSFILDLMNGGDL-----HYHLS--QHGVFSEAEMRFYAAEIIlglEHMHSRFVVYRDLKPAN 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVWElpqpHTedsprnlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNgeEEYTEKVDCFSFGMFIYENISLR 1944
Cdd:cd14223   134 ILLDE----FG--------HVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKG--VAYDSSADWFSLGCMLFKLLRGH 199

                  ....*...
gi 442620116 1945 QPFEGHES 1952
Cdd:cd14223   200 SPFRQHKT 207
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
1710-1995 1.48e-07

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: 55.46  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGARSFKPVAMKMLQPVPPGARAKESALMAfkvavgkwdrDPlqhsckayctarqelavllTL 1789
Cdd:cd14055     2 LVGKGRFAEVWKAKLKQNASGQYETVAVKIFPYEEYASWKNEKDIFT----------DA-------------------SL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLA------LVLELAPLGGLDALLRHYRRSGAhmgphTFQTLVLQAARAIEYLHRRR--------- 1854
Cdd:cd14055    53 KHENILQFLTAEERGVGldrqywLITAYHENGSLQDYLTRHILSWE-----DLCKMAGSLARGLAHLHSDRtpcgrpkip 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPS------GAKGFGGTEGFMAPEII--RYNGEE-EYT 1925
Cdd:cd14055   128 IAHRDLKSSNILV------------KNDGTCVLADFGLALRLDPSlsvdelANSGQVGTARYMAPEALesRVNLEDlESF 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1926 EKVDCFSFGMFIYENIS----------LRQPFEGH-------ESIKECILEG-SRPALTQRETQFPTCCL--DLMVLCWH 1985
Cdd:cd14055   196 KQIDVYSMALVLWEMASrceasgevkpYELPFGSKvrerpcvESMKDLVLRDrGRPEIPDSWLTHQGMCVlcDTITECWD 275
                         330
                  ....*....|
gi 442620116 1986 EQPRRRPTAS 1995
Cdd:cd14055   276 HDPEARLTAS 285
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
1778-1894 1.60e-07

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


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 55.52  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICI--KPLALVLELAplgglDALLRHYRRS-GAHMGPHTFQTLVLQAARAIEYLHRRR 1854
Cdd:cd07839    45 SALREICLLKELKHKNIVRLYDVLHsdKKLTLVFEYC-----DQDLKKYFDScNGDIDPEIVKSFMFQLLKGLAFCHSHN 119
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 442620116 1855 IIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISR 1894
Cdd:cd07839   120 VLHRDLKPQNLLINKNGE------------LKLADFGLAR 147
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
1758-1951 1.75e-07

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: 55.68  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWDRdPLQHSCKAYcTARQELAVLLTLKHPNIVPLVGICIKPLA--------LVLelaPLGGLDalLRHYRrsGA 1829
Cdd:cd07879    42 KVAIKKLSR-PFQSEIFAK-RAYRELTLLKHMQHENVIGLLDVFTSAVSgdefqdfyLVM---PYMQTD--LQKIM--GH 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1830 HMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphTEDsprnlVHIKIADYGISRQtAPSGAKGFGGTEG 1909
Cdd:cd07879   113 PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAV-------NED-----CELKILDFGLARH-ADAEMTGYVVTRW 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 442620116 1910 FMAPEIIRynGEEEYTEKVDCFSFGMFIYENISLRQPFEGHE 1951
Cdd:cd07879   180 YRAPEVIL--NWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKD 219
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
1770-1973 2.07e-07

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: 55.06  E-value: 2.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1770 QHSCKAYCTARQelavlltLKHPNIVPL---VGICIKPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARA 1846
Cdd:cd14040    55 KHACREYRIHKE-------LDHPRIVKLydyFSLDTDTFCTVLEYCEGNDLDFYLKQHKL----MSEKEARSIVMQIVNA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHRRR--IIYRDLKSENVLVWElpqphtedsPRNLVHIKIADYGISR--QTAPSGAKGF------GGTEGFMAPEII 1916
Cdd:cd14040   124 LRYLNEIKppIIHYDLKPGNILLVD---------GTACGEIKITDFGLSKimDDDSYGVDGMdltsqgAGTYWYLPPECF 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 442620116 1917 RYNGEE-EYTEKVDCFSFGMFIYENISLRQPFeGHESIKECILEgSRPALTQRETQFP 1973
Cdd:cd14040   195 VVGKEPpKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQDILQ-ENTILKATEVQFP 250
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1817-1992 2.38e-07

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: 55.07  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1817 LDALLRhyrRSGAHMGPHTFQTLVLQAARAIEYLHRRR-IIYRDLKSENVLVWELPQphtedsprnlvhIKIADYGISRQ 1895
Cdd:cd06618   100 LDKLLK---RIQGPIPEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILLDESGN------------VKLCDFGISGR 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1896 TAPSGAKGFG-GTEGFMAPEIIRYNGEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIKEC---ILEGSRPALTQRETQ 1971
Cdd:cd06618   165 LVDSKAKTRSaGCAAYMAPERIDPPDNPKYDIRADVWSLGISLVELATGQFPYRNCKTEFEVltkILNEEPPSLPPNEGF 244
                         170       180
                  ....*....|....*....|.
gi 442620116 1972 FPTCClDLMVLCWHEQPRRRP 1992
Cdd:cd06618   245 SPDFC-SFVDLCLTKDHRYRP 264
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
1782-1960 2.48e-07

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 55.37  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICIKP--LALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLqaarAIEYLHRRRIIYRD 1859
Cdd:PTZ00426   81 ERKILNYINHPFCVNLYGSFKDEsyLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVL----IFEYLQSLNIVYRD 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphTEDSprnlvHIKIADYGISRqTAPSGAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYE 1939
Cdd:PTZ00426  157 LKPENLLL-------DKDG-----FIKMTDFGFAK-VVDTRTYTLCGTPEYIAPEILLNVG---HGKAADWWTLGIFIYE 220
                         170       180
                  ....*....|....*....|...
gi 442620116 1940 NISLRQPFEGHES--IKECILEG 1960
Cdd:PTZ00426  221 ILVGCPPFYANEPllIYQKILEG 243
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
1846-1952 2.49e-07

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: 55.45  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVWElpqpHTedsprnlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNgeEEYT 1925
Cdd:cd05633   120 GLEHMHNRFVVYRDLKPANILLDE----HG--------HVRISDLGLACDFSKKKPHASVGTHGYMAPEVLQKG--TAYD 185
                          90       100
                  ....*....|....*....|....*..
gi 442620116 1926 EKVDCFSFGMFIYENISLRQPFEGHES 1952
Cdd:cd05633   186 SSADWFSLGCMLFKLLRGHSPFRQHKT 212
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
1740-1955 2.50e-07

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: 55.48  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1740 LQPVPPGAR----AKESALMAFKVAVGKWDRdPLQ---HSCKAYctarQELAVLLTLKHPNIVPLVGIC--------IKP 1804
Cdd:cd07874    22 LKPIGSGAQgivcAAYDAVLDRNVAIKKLSR-PFQnqtHAKRAY----RELVLMKCVNHKNIISLLNVFtpqksleeFQD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 LALVLELaplggLDALLRHYRRsgAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedspRNLVH 1884
Cdd:cd07874    97 VYLVMEL-----MDANLCQVIQ--MELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVV------------KSDCT 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1885 IKIADYGISRQTAPS-GAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07874   158 LKILDFGLARTAGTSfMMTPYVVTRYYRAPEVILGMG---YKENVDIWSVGCIMGEMVRHKILFPGRDYIDQ 226
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1781-2026 2.70e-07

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 55.05  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRR-RIIY 1857
Cdd:cd06649    52 RELQVLHECNSPYIVGFYGAFYSdgEISICMEHMDGGSLDQVLKEAKR----IPEEILGKVSIAVLRGLAYLREKhQIMH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEiiRYNGeEEYTEKVDCFSFGMFI 1937
Cdd:cd06649   128 RDVKPSNILV------------NSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPE--RLQG-THYSVQSDIWSMGLSL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1938 YENISLRQPFEGHESiKECILEGSRPALTQRETQFPTccldlmvLCWHEQPRRRPTASQIVSILSAPECIHLLDVVAMPH 2017
Cdd:cd06649   193 VELAIGRYPIPPPDA-KELEAIFGRPVVDGEEGEPHS-------ISPRPRPPGRPVSGHGMDSRPAMAIFELLDYIVNEP 264

                  ....*....
gi 442620116 2018 SEKIVCGVF 2026
Cdd:cd06649   265 PPKLPNGVF 273
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
456-704 3.31e-07

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 56.01  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  456 ITRIDFSHNVLTS-IPQELFHLVSLRYLNVAQNKITD-LPAPIGQtygCPVLDELFLQDNQLT-TLPAAIFHLPALSILD 532
Cdd:PLN00113  358 LTVLDLSTNNLTGeIPEGLCSSGNLFKLILFSNSLEGeIPKSLGA---CRSLRRVRLQDNSFSgELPSEFTKLPLVYFLD 434
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  533 VSNNKLQ-QLPFDLWRAPKLRELNVAFNLLrdlpvppmqtsssllsldklnlqSFEEPPSNKPRNVTQQRLTHrNLWSAT 611
Cdd:PLN00113  435 ISNNNLQgRINSRKWDMPSLQMLSLARNKF-----------------------FGGLPDSFGSKRLENLDLSR-NQFSGA 490
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  612 LDITDNDMKWQHEQDLGDGKTAGVGSSQLSS------LNIANNLFT-SIPAALPCLAVnLTRLNMSYNSL-----RSMGH 679
Cdd:PLN00113  491 VPRKLGSLSELMQLKLSENKLSGEIPDELSSckklvsLDLSHNQLSgQIPASFSEMPV-LSQLDLSQNQLsgeipKNLGN 569
                         250       260
                  ....*....|....*....|....*
gi 442620116  680 VTSypatLKQLDLSHNEIScwPSLP 704
Cdd:PLN00113  570 VES----LVQVNISHNHLH--GSLP 588
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
1710-1998 3.81e-07

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: 54.30  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKANCKVRGaRSFkpvAMKMLqPVPPGArakesalmafkvavgkwdrdplqhscKAYCTARQELAVLLTL 1789
Cdd:cd14046    13 VLGKGAFGQVVKVRNKLDG-RYY---AIKKI-KLRSES--------------------------KNNSRILREVMLLSRL 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIKPLALV--LELAPlgglDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd14046    62 NHQHVVRYYQAWIERANLYiqMEYCE----KSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 welpqphteDSPRNlvhIKIADYG--ISRQTAP-----------SGAKGFG-------GTEGFMAPEiIRYNGEEEYTEK 1927
Cdd:cd14046   138 ---------DSNGN---VKIGDFGlaTSNKLNVelatqdinkstSAALGSSgdltgnvGTALYVAPE-VQSGTKSTYNEK 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1928 VDCFSFGMFIYEnisLRQPFE-GHESIKecILEgsrpALTQRETQFP-TCCLDLM-----VLCW---HEqPRRRPTASQI 1997
Cdd:cd14046   205 VDMYSLGIIFFE---MCYPFStGMERVQ--ILT----ALRSVSIEFPpDFDDNKHskqakLIRWllnHD-PAKRPSAQEL 274

                  .
gi 442620116 1998 V 1998
Cdd:cd14046   275 L 275
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
1770-1973 3.82e-07

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: 54.30  E-value: 3.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1770 QHSCKAYCTARQelavlltLKHPNIVPL---VGICIKPLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARA 1846
Cdd:cd14041    55 KHACREYRIHKE-------LDHPRIVKLydyFSLDTDSFCTVLEYCEGNDLDFYLKQHKL----MSEKEARSIIMQIVNA 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1847 IEYLHRRR--IIYRDLKSENVLVWelpqphtedSPRNLVHIKIADYGISR-------------QTAPSGAkgfgGTEGFM 1911
Cdd:cd14041   124 LKYLNEIKppIIHYDLKPGNILLV---------NGTACGEIKITDFGLSKimdddsynsvdgmELTSQGA----GTYWYL 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1912 APEIIRYNGEE-EYTEKVDCFSFGMFIYENISLRQPFeGHESIKECILEgSRPALTQRETQFP 1973
Cdd:cd14041   191 PPECFVVGKEPpKISNKVDVWSVGVIFYQCLYGRKPF-GHNQSQQDILQ-ENTILKATEVQFP 251
LRR_8 pfam13855
Leucine rich repeat;
478-538 4.58e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 48.67  E-value: 4.58e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116   478 SLRYLNVAQNKITDLPApiGQTYGCPVLDELFLQDNQLTTL-PAAIFHLPALSILDVSNNKL 538
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDD--GAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
1696-2002 4.75e-07

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 54.47  E-value: 4.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1696 DKHTIPSECIIKGSLLGRGAFGFVFKANCKVRGAR-SFKPVAMKMLQPvppGARAKE-SALMAfkvavgkwdrdplqhsc 1773
Cdd:cd05106    31 EKWEFPRDNLQFGKTLGAGAFGKVVEATAFGLGKEdNVLRVAVKMLKA---SAHTDErEALMS----------------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1774 kayctarqELAVLLTL-KHPNIVPLVGICIK--PLALVLELAPLGGLDALLRH--------------------------- 1823
Cdd:cd05106    91 --------ELKILSHLgQHKNIVNLLGACTHggPVLVITEYCCYGDLLNFLRKkaetflnfvmalpeisetssdyknitl 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1824 ---YRRSGAHMGPHTFQTLV------------------------------------LQAARAIEYLHRRRIIYRDLKSEN 1864
Cdd:cd05106   163 ekkYIRSDSGFSSQGSDTYVemrpvsssssqssdskdeedtedswpldlddllrfsSQVAQGMDFLASKNCIHRDVAARN 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1865 VLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFGGTE----GFMAPEIIRYNgeeEYTEKVDCFSFGMFIYEN 1940
Cdd:cd05106   243 VLL------------TDGRVAKICDFGLARDIMNDSNYVVKGNArlpvKWMAPESIFDC---VYTVQSDVWSYGILLWEI 307
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1941 ISL-RQPFEG-------HESIKeCILEGSRPALTQRETqfptccLDLMVLCWHEQPRRRPTASQIVSILS 2002
Cdd:cd05106   308 FSLgKSPYPGilvnskfYKMVK-RGYQMSRPDFAPPEI------YSIMKMCWNLEPTERPTFSQISQLIQ 370
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
1842-1949 5.85e-07

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: 53.43  E-value: 5.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1842 QAARAIEYLHRRRIIYRDLKSENVLVWElpqpHTEDsprnlvHIKIADYGISRQTAP-SGAKGFGGTEGFMAPEIIRYng 1920
Cdd:cd14192   110 QICEGVHYLHQHYILHLDLKPENILCVN----STGN------QIKIIDFGLARRYKPrEKLKVNFGTPEFLAPEVVNY-- 177
                          90       100
                  ....*....|....*....|....*....
gi 442620116 1921 eEEYTEKVDCFSFGMFIYENISLRQPFEG 1949
Cdd:cd14192   178 -DFVSFPTDMWSVGVITYMLLSGLSPFLG 205
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
1711-1947 7.36e-07

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: 53.86  E-value: 7.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVfkanCKVRGARSFKPVAMKMLQpvppgaraKESALMAFKVAVGKWDRDPLQHsckayctARQELAVLLTL- 1789
Cdd:cd05598     9 IGVGAFGEV----SLVRKKDTNALYAMKTLR--------KKDVLKRNQVAHVKAERDILAE-------ADNEWVVKLYYs 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 ----KHpnivplvgicikpLALVLELAPLGGLDALLrhyrrsgahMGPHTFQT---------LVLqaarAIEYLHRRRII 1856
Cdd:cd05598    70 fqdkEN-------------LYFVMDYIPGGDLMSLL---------IKKGIFEEdlarfyiaeLVC----AIESVHKMGFI 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphTEDSprnlvHIKIADYGIS---RQTAPSG---AKGFGGTEGFMAPEIIRYNGeeeYTEKVDC 1930
Cdd:cd05598   124 HRDIKPDNILI-------DRDG-----HIKLTDFGLCtgfRWTHDSKyylAHSLVGTPNYIAPEVLLRTG---YTQLCDW 188
                         250
                  ....*....|....*..
gi 442620116 1931 FSFGMFIYENISLRQPF 1947
Cdd:cd05598   189 WSVGVILYEMLVGQPPF 205
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
1842-1951 8.47e-07

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: 52.99  E-value: 8.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1842 QAARAIEYLHRRRIIYRDLKSENVLVWElpqphtedspRNLVHIKIADYGISRQTAP-SGAKGFGGTEGFMAPEIIRYng 1920
Cdd:cd14193   110 QICEGIQYMHQMYILHLDLKPENILCVS----------REANQVKIIDFGLARRYKPrEKLRVNFGTPEFLAPEVVNY-- 177
                          90       100       110
                  ....*....|....*....|....*....|.
gi 442620116 1921 eEEYTEKVDCFSFGMFIYENISLRQPFEGHE 1951
Cdd:cd14193   178 -EFVSFPTDMWSLGVIAYMLLSGLSPFLGED 207
LRR_8 pfam13855
Leucine rich repeat;
503-561 9.45e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 47.90  E-value: 9.45e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442620116   503 PVLDELFLQDNQLTTLPAAIF-HLPALSILDVSNNKLQQL-PFDLWRAPKLRELNVAFNLL 561
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFkGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
1740-1955 1.01e-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: 53.51  E-value: 1.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1740 LQPVPPGAR----AKESALMAFKVAVGKWDRdPLQ---HSCKAYctarQELAVLLTLKHPNIVPLVGIC--------IKP 1804
Cdd:cd07875    29 LKPIGSGAQgivcAAYDAILERNVAIKKLSR-PFQnqtHAKRAY----RELVLMKCVNHKNIIGLLNVFtpqksleeFQD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1805 LALVLELAPLGGLDAL---LRHYRRSgahmgphtfqTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedspRN 1881
Cdd:cd07875   104 VYIVMELMDANLCQVIqmeLDHERMS----------YLLYQMLCGIKHLHSAGIIHRDLKPSNIVV------------KS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1882 LVHIKIADYGISRQtapsgakgfGGTEGFMAPEII-RYNGEEE------YTEKVDCFSFGMFIYENISLRQPFEGHESIK 1954
Cdd:cd07875   162 DCTLKILDFGLART---------AGTSFMMTPYVVtRYYRAPEvilgmgYKENVDIWSVGCIMGEMIKGGVLFPGTDHID 232

                  .
gi 442620116 1955 E 1955
Cdd:cd07875   233 Q 233
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
1738-1955 1.12e-06

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 53.49  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1738 KMLQPVPPGAR----AKESALMAFKVAVGKWDRdPLQ---HSCKAYctarQELAVLLTLKHPNIVPLVGIC--------I 1802
Cdd:cd07876    24 QQLKPIGSGAQgivcAAFDTVLGINVAVKKLSR-PFQnqtHAKRAY----RELVLLKCVNHKNIISLLNVFtpqksleeF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1803 KPLALVLELAPLGGLDAL---LRHYRRSgahmgphtfqTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedsp 1879
Cdd:cd07876    99 QDVYLVMELMDANLCQVIhmeLDHERMS----------YLLYQMLCGIKHLHSAGIIHRDLKPSNIVV------------ 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442620116 1880 RNLVHIKIADYGISRQTAPS-GAKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07876   157 KSDCTLKILDFGLARTACTNfMMTPYVVTRYYRAPEVILGMG---YKENVDIWSVGCIMGELVKGSVIFQGTDHIDQ 230
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
1791-1998 1.15e-06

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: 52.70  E-value: 1.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKP--------LALVLELAPLGGLDALLRHYRrsGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd06636    72 HRNIATYYGAFIKKsppghddqLWLVMEFCGAGSVTDLVKNTK--GNALKEDWIAYICREILRGLAHLHAHKVIHRDIKG 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphTEDSprnlvHIKIADYGISRQTAPSGAK--GFGGTEGFMAPEII--RYNGEEEYTEKVDCFSFGMFIY 1938
Cdd:cd06636   150 QNVLL-------TENA-----EVKLVDFGVSAQLDRTVGRrnTFIGTPYWMAPEVIacDENPDATYDYRSDIWSLGITAI 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1939 ENISLRQPFEGHESIKECILEGSRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd06636   218 EMAEGAPPLCDMHPMRALFLIPRNPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLL 277
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
1839-1951 1.22e-06

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 52.55  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1839 LVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedsPRNLVHIKIADYGISRqtaPSGAKG-FGGTEGFMAPEIIR 1917
Cdd:PHA03390  114 IIRQLVEALNDLHKHNIIHNDIKLENVLY-----------DRAKDRIYLCDYGLCK---IIGTPScYDGTLDYFSPEKIK 179
                          90       100       110
                  ....*....|....*....|....*....|....
gi 442620116 1918 yngEEEYTEKVDCFSFGMFIYENISLRQPFEGHE 1951
Cdd:PHA03390  180 ---GHNYDVSFDWWAVGVLTYELLTGKHPFKEDE 210
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
1782-1962 1.31e-06

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 53.97  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICI----KPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHR----- 1852
Cdd:PTZ00266   62 EVNVMRELKHKNIVRYIDRFLnkanQKLYILMEFCDAGDLSRNIQKCYKMFGKIEEHAIVDITRQLLHALAYCHNlkdgp 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1853 --RRIIYRDLKSENVL----VWELPQPHTEDSPRNLVHI-KIADYGISRQTA-PSGAKGFGGTEGFMAPEIIRYNgEEEY 1924
Cdd:PTZ00266  142 ngERVLHRDLKPQNIFlstgIRHIGKITAQANNLNGRPIaKIGDFGLSKNIGiESMAHSCVGTPYYWSPELLLHE-TKSY 220
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 442620116 1925 TEKVDCFSFGMFIYENISLRQPFEGHESIKECILEGSR 1962
Cdd:PTZ00266  221 DDKSDMWALGCIIYELCSGKTPFHKANNFSQLISELKR 258
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
1781-2026 1.47e-06

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: 52.75  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QELAVLLTLKHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHYRRsgahMGPHTFQTLVLQAARAIEYLHRR-RIIY 1857
Cdd:cd06650    52 RELQVLHECNSPYIVGFYGAFYSdgEISICMEHMDGGSLDQVLKKAGR----IPEQILGKVSIAVIKGLTYLREKhKIMH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVwelpqphtedSPRNlvHIKIADYGISRQTAPSGAKGFGGTEGFMAPEiiRYNGeEEYTEKVDCFSFGMFI 1937
Cdd:cd06650   128 RDVKPSNILV----------NSRG--EIKLCDFGVSGQLIDSMANSFVGTRSYMSPE--RLQG-THYSVQSDIWSMGLSL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1938 YENISLRQPFEghesikecilegsrPALTQRETQFPTCCLDLMVLCWHEQPRR--RPTASQIVSILSAPECIHLLDVVAM 2015
Cdd:cd06650   193 VEMAVGRYPIP--------------PPDAKELELMFGCQVEGDAAETPPRPRTpgRPLSSYGMDSRPPMAIFELLDYIVN 258
                         250
                  ....*....|.
gi 442620116 2016 PHSEKIVCGVF 2026
Cdd:cd06650   259 EPPPKLPSGVF 269
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
1710-1955 1.72e-06

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: 52.31  E-value: 1.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAnckvRGARSFKPVAMKMLQPVPPGARAKESALmafkvavgkwdrdplqhsckayctarQELAVLLTL 1789
Cdd:cd07848     8 VVGEGAYGVVLKC----RHKETKEIVAIKKFKDSEENEEVKETTL--------------------------RELKMLRTL 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIK--PLALVLELAPLGGLDALLRHyrRSGAHmgPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLV 1867
Cdd:cd07848    58 KQENIVELKEAFRRrgKLYLVFEYVEKNMLELLEEM--PNGVP--PEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLI 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1868 welpqphtedSPRNLvhIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRyngEEEYTEKVDCFSFGMFIYEnISLR 1944
Cdd:cd07848   134 ----------SHNDV--LKLCDFGFARNLSEGSNANYTeyvATRWYRSPELLL---GAPYGKAVDMWSVGCILGE-LSDG 197
                         250
                  ....*....|..
gi 442620116 1945 QP-FEGHESIKE 1955
Cdd:cd07848   198 QPlFPGESEIDQ 209
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1708-1999 2.29e-06

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 51.51  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1708 GSLLGRGAFGFVFKANCKVRGArsfkPVAMKMLQ--------PVPPGARAKESALMAFKVAVG--------KWDRDPLqh 1771
Cdd:cd14100     5 GPLLGSGGFGSVYSGIRVADGA----PVAIKHVEkdrvsewgELPNGTRVPMEIVLLKKVGSGfrgvirllDWFERPD-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1772 sckayctarqelAVLLTLKHPNIVP-LVGICIKPLALVLELAplggldallRHYRRsgahmgphtfqtlvlQAARAIEYL 1850
Cdd:cd14100    79 ------------SFVLVLERPEPVQdLFDFITERGALPEELA---------RSFFR---------------QVLEAVRHC 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1851 HRRRIIYRDLKSENVLVwelpqphtedsPRNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNGEEEYTEKVdc 1930
Cdd:cd14100   123 HNCGVLHRDIKDENILI-----------DLNTGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRFHRYHGRSAAV-- 189
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442620116 1931 FSFGMFIYENISLRQPFEGHESIKecileGSRPALTQRETqfpTCCLDLMVLCWHEQPRRRPTASQIVS 1999
Cdd:cd14100   190 WSLGILLYDMVCGDIPFEHDEEII-----RGQVFFRQRVS---SECQHLIKWCLALRPSDRPSFEDIQN 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
91-196 2.60e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.80  E-value: 2.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116    91 LYAAVHSGHLGIARLMLDHFPElIQQPTVERWLPLHAACINGHIKLLELLISYsypdylyqtyrdeegqwewrlpFDANA 170
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEH----------------------ADVNL 57
                           90       100
                   ....*....|....*....|....*.
gi 442620116   171 hDVTGQTSLYIASILGNKQLVGVLLK 196
Cdd:pfam12796   58 -KDNGRTALHYAARSGHLEIVKLLLE 82
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
1780-1959 2.90e-06

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: 51.40  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDaLLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRD 1859
Cdd:cd14104    44 KKEISILNIARHRNILRLHESFESHEELVMIFEFISGVD-IFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1860 LKSENVLVwelpqphtedSPRNLVHIKIADYGISRQTAPSGAKGFGGTEG-FMAPEIIRYngeEEYTEKVDCFSFGMFIY 1938
Cdd:cd14104   123 IRPENIIY----------CTRRGSYIKIIEFGQSRQLKPGDKFRLQYTSAeFYAPEVHQH---ESVSTATDMWSLGCLVY 189
                         170       180
                  ....*....|....*....|...
gi 442620116 1939 ENISLRQPFEG--HESIKECILE 1959
Cdd:cd14104   190 VLLSGINPFEAetNQQTIENIRN 212
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
453-698 2.93e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 52.93  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  453 LTAITRIDFSHNVLT-SIPQELFHLVSLRYLNVAQNKITD-LPAPIgqtYGCPVLDELFLQDNQLT-------------- 516
Cdd:PLN00113  235 LTSLNHLDLVYNNLTgPIPSSLGNLKNLQYLFLYQNKLSGpIPPSI---FSLQKLISLDLSDNSLSgeipelviqlqnle 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  517 -----------TLPAAIFHLPALSILDVSNNKLQ-QLPFDLWRAPKLRELNVAFN-LLRDLPvppmQTSSSLLSLDKLNL 583
Cdd:PLN00113  312 ilhlfsnnftgKIPVALTSLPRLQVLQLWSNKFSgEIPKNLGKHNNLTVLDLSTNnLTGEIP----EGLCSSGNLFKLIL 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  584 QS----FEEPPS-NKPRNVTQQRLTHRNLWSAT------------LDITDNDM-------KWQHEQ----DLGDGKTAG- 634
Cdd:PLN00113  388 FSnsleGEIPKSlGACRSLRRVRLQDNSFSGELpseftklplvyfLDISNNNLqgrinsrKWDMPSlqmlSLARNKFFGg 467
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442620116  635 ----VGSSQLSSLNIANNLFT-SIPAALPCLAvNLTRLNMSYNSLRsmGHVTSYPATLKQ---LDLSHNEIS 698
Cdd:PLN00113  468 lpdsFGSKRLENLDLSRNQFSgAVPRKLGSLS-ELMQLKLSENKLS--GEIPDELSSCKKlvsLDLSHNQLS 536
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
1713-1942 2.98e-06

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: 51.56  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1713 RGAFGFVFKANCkvrgarSFKPVAMKMLqpvppgarakesalmafkvavgkwdrdPLQHscKAYCTARQELAVLLTLKHP 1792
Cdd:cd14053     5 RGRFGAVWKAQY------LNRLVAVKIF---------------------------PLQE--KQSWLTEREIYSLPGMKHE 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1793 NIVPLVGI--CIKPLA----LVLELAPLGGLDALLRHYRRSGAHMgphtfQTLVLQAARAIEYLHRRR----------II 1856
Cdd:cd14053    50 NILQFIGAekHGESLEaeywLITEFHERGSLCDYLKGNVISWNEL-----CKIAESMARGLAYLHEDIpatngghkpsIA 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSG----AKGFGGTEGFMAPEIIryNGEEEYTE----KV 1928
Cdd:cd14053   125 HRDFKSKNVLL------------KSDLTACIADFGLALKFEPGKscgdTHGQVGTRRYMAPEVL--EGAINFTRdaflRI 190
                         250
                  ....*....|....
gi 442620116 1929 DCFSFGMFIYENIS 1942
Cdd:cd14053   191 DMYAMGLVLWELLS 204
PHA02875 PHA02875
ankyrin repeat protein; Provisional
61-300 3.14e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   61 ACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSGHLGIARLMLDH--FPElIQQPTVERwlPLHAACINGHIKLLE 138
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHgaIPD-VKYPDIES--ELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  139 -LLISYSYPDYLYqtYRDeegqwewrlpfdanahdvtGQTSLYIASILGNKQLVGVLLKWQlhcrrtlgdsassvSTPIT 217
Cdd:PHA02875   86 eLLDLGKFADDVF--YKD-------------------GMTPLHLATILKKLDIMKLLIARG--------------ADPDI 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  218 PTRKRISFGIQAIMSKlhisgesegpdDLASQESTECQRCPINVNLLCGAareTALLAAVRGGHLDVVQSLLQHGANPNI 297
Cdd:PHA02875  131 PNTDKFSPLHLAVMMG-----------DIKGIELLIDHKACLDIEDCCGC---TPLIIAMAKGDIAICKMLLDSGANIDY 196

                  ...
gi 442620116  298 VAK 300
Cdd:PHA02875  197 FGK 199
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
1845-1992 4.30e-06

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 50.83  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1845 RAIEYLHRR-RIIYRDLKSENVLVwelpqphtedsPRNlVHIKIADYGISRQTAPSGAKGF-GGTEGFMAPEIIRYNGEE 1922
Cdd:cd06616   120 KALNYLKEElKIIHRDVKPSNILL-----------DRN-GNIKLCDFGISGQLVDSIAKTRdAGCRPYMAPERIDPSASR 187
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116 1923 E-YTEKVDCFSFGMFIYENISLRQPFEGHESIKECILE---GSRPAL-TQRETQFPTCCLDLMVLCWHEQPRRRP 1992
Cdd:cd06616   188 DgYDVRSDVWSLGITLYEVATGKFPYPKWNSVFDQLTQvvkGDPPILsNSEEREFSPSFVNFVNLCLIKDESKRP 262
Ank_2 pfam12796
Ankyrin repeats (3 copies);
23-109 4.57e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 4.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116    23 AVISGDERTVRVLLaalgtERQIIVNMAPSGANTLLFLACQSGYESITQRLLD-AGADGRSHAVTkysPLYAAVHSGHLG 101
Cdd:pfam12796    4 AAKNGNLELVKLLL-----ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGRT---ALHYAARSGHLE 75

                   ....*...
gi 442620116   102 IARLMLDH 109
Cdd:pfam12796   76 IVKLLLEK 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
273-374 4.71e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.03  E-value: 4.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   273 LLAAVRGGHLDVVQSLLQHGANPNIVAKpvedhndpkcceeiYGLSnvPIAEACKQRSLAMLDLLLKHGA---RDDNGTA 349
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK--------------NGRT--ALHLAAKNGHLEIVKLLLEHADvnlKDNGRTA 64
                           90       100
                   ....*....|....*....|....*
gi 442620116   350 IGMAITCGDEAILSRLLARRVHPDS 374
Cdd:pfam12796   65 LHYAARSGHLEIVKLLLEKGADINV 89
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
1710-2002 5.11e-06

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: 50.55  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVFKAncKVRGARsfkpVAMKMLqpvppgarakesalmaFKVAVGKWDRDplqhsckayctarQELAVLLTL 1789
Cdd:cd14144     2 SVGKGRYGEVWKG--KWRGEK----VAVKIF----------------FTTEEASWFRE-------------TEIYQTVLM 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNIVPLVGICIK------PLALVLELAPLGGLDALLRhyrrsGAHMGPHTFQTLVLQAARAIEYLH--------RRRI 1855
Cdd:cd14144    47 RHENILGFIAADIKgtgswtQLYLITDYHENGSLYDFLR-----GNTLDTQSMLKLAYSAACGLAHLHteifgtqgKPAI 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphtedsPRNLVhIKIADYGISRQTAPS------GAKGFGGTEGFMAPEI----IRYNGEEEYt 1925
Cdd:cd14144   122 AHRDIKSKNILV-----------KKNGT-CCIADLGLAVKFISEtnevdlPPNTRVGTKRYMAPEVldesLNRNHFDAY- 188
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1926 EKVDCFSFGMFIYEnISLR-----------QPF-------EGHESIKECI-LEGSRPALTQR--ETQFPTCCLDLMVLCW 1984
Cdd:cd14144   189 KMADMYSFGLVLWE-IARRcisggiveeyqLPYydavpsdPSYEDMRRVVcVERRRPSIPNRwsSDEVLRTMSKLMSECW 267
                         330
                  ....*....|....*...
gi 442620116 1985 HEQPRRRPTASQIVSILS 2002
Cdd:cd14144   268 AHNPAARLTALRVKKTLG 285
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1710-1947 5.64e-06

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: 51.15  E-value: 5.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVfkanCKVRGARSFKPVAMKMLQPVPPGARA------KESALMAFkvAVGKWdrdplqhSCKAYCTARQEl 1783
Cdd:cd05621    59 VIGRGAFGEV----QLVRHKASQKVYAMKLLSKFEMIKRSdsaffwEERDIMAF--ANSPW-------VVQLFCAFQDD- 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1784 avlltlkhpnivplvgiciKPLALVLELAPLGGLDALLRHYRRSGAHMGPHTFQTLVlqaarAIEYLHRRRIIYRDLKSE 1863
Cdd:cd05621   125 -------------------KYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVL-----ALDAIHSMGLIHRDVKPD 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphtedspRNLVHIKIADYGISRQTAPSG---AKGFGGTEGFMAPEIIRYNGEE-EYTEKVDCFSFGMFIYE 1939
Cdd:cd05621   181 NMLL------------DKYGHLKLADFGTCMKMDETGmvhCDTAVGTPDYISPEVLKSQGGDgYYGRECDWWSVGVFLFE 248

                  ....*...
gi 442620116 1940 NISLRQPF 1947
Cdd:cd05621   249 MLVGDTPF 256
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
1707-1939 6.75e-06

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 50.45  E-value: 6.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKAncKVRGARSFKPVAMKMLQpvppGARAKESAlmafkvavgkwdrdplqhsCKayctarqELAVL 1786
Cdd:cd07867     6 EGCKVGRGTYGHVYKA--KRKDGKDEKEYALKQIE----GTGISMSA-------------------CR-------EIALL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICI----KPLALVLELAPlGGLDALLRHYRRSGAHMGPHTF-----QTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd07867    54 RELKHPNVIALQKVFLshsdRKVWLLFDYAE-HDLWHIIKFHRASKANKKPMQLprsmvKSLLYQILDGIHYLHANWVLH 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVWelpqphTEDSPRNlvHIKIADYGISRQ-TAP----SGAKGFGGTEGFMAPEIIRynGEEEYTEKVDCFS 1932
Cdd:cd07867   133 RDLKPANILVM------GEGPERG--RVKIADMGFARLfNSPlkplADLDPVVVTFWYRAPELLL--GARHYTKAIDIWA 202

                  ....*..
gi 442620116 1933 FGMFIYE 1939
Cdd:cd07867   203 IGCIFAE 209
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
1705-1955 6.81e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 50.53  E-value: 6.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1705 IIKGSLLGRGAFGFVFKAnckvRGARSFKPVAMKMLQpvppgarakesalmAFKVAVGKWDRDPLQHSCKAYCTARQELA 1784
Cdd:PTZ00024   11 IQKGAHLGEGTYGKVEKA----YDTLTGKIVAIKKVK--------------IIEISNDVTKDRQLVGMCGIHFTTLRELK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1785 VLLTLKHPNIVPLVGICIKP--LALVLELAPlGGLDALL-RHYRRSGAHMgphtfQTLVLQAARAIEYLHRRRIIYRDLK 1861
Cdd:PTZ00024   73 IMNEIKHENIMGLVDVYVEGdfINLVMDIMA-SDLKKVVdRKIRLTESQV-----KCILLQILNGLNVLHKWYFMHRDLS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1862 SENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFGGTEGFM----------------APEIIRynGEEEYT 1925
Cdd:PTZ00024  147 PANIFI------------NSKGICKIADFGLARRYGYPPYSDTLSKDETMqrreemtskvvtlwyrAPELLM--GAEKYH 212
                         250       260       270
                  ....*....|....*....|....*....|
gi 442620116 1926 EKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:PTZ00024  213 FAVDMWSVGCIFAELLTGKPLFPGENEIDQ 242
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
1779-1992 7.13e-06

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 49.84  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1779 ARQELAVLLTLKHPNIVPLVGiCIKP---LALVLElaplgGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRI 1855
Cdd:cd14112    47 AVREFESLRTLQHENVQRLIA-AFKPsnfAYLVME-----KLQEDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphtedSPRNLVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIryNGEEEYTEKVDCFSFGM 1935
Cdd:cd14112   121 AHLDVQPDNIMF----------QSVRSWQVKLVDFGRAQKVSKLGKVPVDGDTDWASPEFH--NPETPITVQSDIWGLGV 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442620116 1936 FIYENISLRQPFEG----HESIKECIL-EGSRPALTQRE-TQFptcCLDLMVLCWHEQPRRRP 1992
Cdd:cd14112   189 LTFCLLSGFHPFTSeyddEEETKENVIfVKCRPNLIFVEaTQE---ALRFATWALKKSPTRRM 248
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1846-1973 9.01e-06

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 50.03  E-value: 9.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLvwelpqpHTEDSPRNLvhIKIADYGISRQTAPSGAKGFGG-TEGFMAPEIIrynGEEEY 1924
Cdd:cd14170   113 AIQYLHSINIAHRDVKPENLL-------YTSKRPNAI--LKLTDFGFAKETTSHNSLTTPCyTPYYVAPEVL---GPEKY 180
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 442620116 1925 TEKVDCFSFGMFIYENISLRQPFEGHESIkeCILEGSRPALTQRETQFP 1973
Cdd:cd14170   181 DKSCDMWSLGVIMYILLCGYPPFYSNHGL--AISPGMKTRIRMGQYEFP 227
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
1707-1939 9.24e-06

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 50.44  E-value: 9.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1707 KGSLLGRGAFGFVFKAncKVRGARSFKPVAMKMLQpvppGARAKESAlmafkvavgkwdrdplqhsCKayctarqELAVL 1786
Cdd:cd07868    21 EGCKVGRGTYGHVYKA--KRKDGKDDKDYALKQIE----GTGISMSA-------------------CR-------EIALL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1787 LTLKHPNIVPLVGICI----KPLALVLELAPlGGLDALLRHYRRSGAHMGPHTF-----QTLVLQAARAIEYLHRRRIIY 1857
Cdd:cd07868    69 RELKHPNVISLQKVFLshadRKVWLLFDYAE-HDLWHIIKFHRASKANKKPVQLprgmvKSLLYQILDGIHYLHANWVLH 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1858 RDLKSENVLVWelpqphTEDSPRNlvHIKIADYGISRQ-TAP----SGAKGFGGTEGFMAPEIIRynGEEEYTEKVDCFS 1932
Cdd:cd07868   148 RDLKPANILVM------GEGPERG--RVKIADMGFARLfNSPlkplADLDPVVVTFWYRAPELLL--GARHYTKAIDIWA 217

                  ....*..
gi 442620116 1933 FGMFIYE 1939
Cdd:cd07868   218 IGCIFAE 224
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
1789-2002 1.31e-05

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


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 49.48  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIK--PLALVLELAPLGGLDALLR----HYRRSGAHMgphTFQTLVLQAARAIEYLHRRRIIYRDLKS 1862
Cdd:cd05086    54 LQHPNILQCVGQCVEaiPYLLVFEFCDLGDLKTYLAnqqeKLRGDSQIM---LLQRMACEIAAGLAHMHKHNFLHSDLAL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1863 ENVLVwelpqphTEDsprnlVHIKIADYGIsrqtAPSGAKgfggtEGFM-------------APEII-RYNGE---EEYT 1925
Cdd:cd05086   131 RNCYL-------TSD-----LTVKVGDYGI----GFSRYK-----EDYIetddkkyaplrwtAPELVtSFQDGllaAEQT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1926 EKVDCFSFGMFIYENI-SLRQPFEgHESIKECILEgsrpALTQRETQFPTCCLDL---------MVLCWHeQPRRRPTAS 1995
Cdd:cd05086   190 KYSNIWSLGVTLWELFeNAAQPYS-DLSDREVLNH----VIKERQVKLFKPHLEQpysdrwyevLQFCWL-SPEKRPTAE 263

                  ....*..
gi 442620116 1996 QIVSILS 2002
Cdd:cd05086   264 EVHRLLT 270
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
1758-1990 1.35e-05

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: 49.78  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWD-RDPlqHSCKaycTARQELAVLLTLKHPNIVPLVGIC----------------IKPLALVLELAPlGGLDAL 1820
Cdd:cd07854    32 RVAVKKIVlTDP--QSVK---HALREIKIIRRLDHDNIVKVYEVLgpsgsdltedvgslteLNSVYIVQEYME-TDLANV 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1821 LRHYRRSGAHMGPHTFQTLvlqaaRAIEYLHRRRIIYRDLKSENVLVwelpqpHTEDsprnLVhIKIADYGISRQTAPS- 1899
Cdd:cd07854   106 LEQGPLSEEHARLFMYQLL-----RGLKYIHSANVLHRDLKPANVFI------NTED----LV-LKIGDFGLARIVDPHy 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1900 GAKGFGG----TEGFMAPEIIRYngEEEYTEKVDCFSFGMFIYENISLRQPFEGHESIKECILEGSRPALTQRETQfpTC 1975
Cdd:cd07854   170 SHKGYLSeglvTKWYRSPRLLLS--PNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILESVPVVREEDR--NE 245
                         250
                  ....*....|....*...
gi 442620116 1976 CLDLM---VLCWHEQPRR 1990
Cdd:cd07854   246 LLNVIpsfVRNDGGEPRR 263
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
1838-1956 1.43e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 49.87  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1838 TLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqpHTEDSprnlvhIKIADYGISR-QTAPSGAKGFGGTEGFMAPEII 1916
Cdd:PHA03209  161 IIEKQILEGLRYLHAQRIIHRDVKTENIFI------NDVDQ------VCIGDLGAAQfPVVAPAFLGLAGTVETNAPEVL 228
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 442620116 1917 rynGEEEYTEKVDCFSFGMFIYENISL------RQPFEGHESIKEC 1956
Cdd:PHA03209  229 ---ARDKYNSKADIWSAGIVLFEMLAYpstifeDPPSTPEEYVKSC 271
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
1815-1997 1.48e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. 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 Wee1b 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: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 49.16  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1815 GGLDALLRHYRRSGAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVW-----------ELPQPHTEDSPRNLV 1883
Cdd:cd14139    85 GSLQDAISENTKSGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIChkmqsssgvgeEVSNEEDEFLSANVV 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1884 HiKIADYGisRQTAPSGAKGFGGTEGFMAPEIIRyngeEEYTE--KVDCFSFGMFIYENISlRQPFEGHESIKECILEGS 1961
Cdd:cd14139   165 Y-KIGDLG--HVTSINKPQVEEGDSRFLANEILQ----EDYRHlpKADIFALGLTVALAAG-AEPLPTNGAAWHHIRKGN 236
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 442620116 1962 RPALTQretQFPTCCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14139   237 FPDVPQ---ELPESFSSLLKNMIQPDPEQRPSATAL 269
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
1825-1998 1.59e-05

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


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 48.77  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1825 RRSGAHM--GPHTF-----QTLVLQAARAIEYLHRRRIIYRDLKSENVLVWElpqphtedsprNLvHIKIADYGISRQTA 1897
Cdd:cd14189    85 RKSLAHIwkARHTLlepevRYYLKQIISGLKYLHLKGILHRDLKLGNFFINE-----------NM-ELKVGDFGLAARLE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1898 PSG--AKGFGGTEGFMAPEIIRYNGeeeYTEKVDCFSFGMFIYENISLRQPFEGHEsikeciLEGSRPALTQRETQFPTC 1975
Cdd:cd14189   153 PPEqrKKTICGTPNYLAPEVLLRQG---HGPESDVWSLGCVMYTLLCGNPPFETLD------LKETYRCIKQVKYTLPAS 223
                         170       180
                  ....*....|....*....|....*..
gi 442620116 1976 ----CLDLMVLCWHEQPRRRPTASQIV 1998
Cdd:cd14189   224 lslpARHLLAGILKRNPGDRLTLDQIL 250
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1778-1957 1.86e-05

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: 49.03  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGG-------LDALLRHYRRSG-AHMGPHTFQTLVLQAARAIEY 1849
Cdd:cd07864    52 TAIREIKILRQLNHRSVVNLKEIVTDKQDALDFKKDKGAfylvfeyMDHDLMGLLESGlVHFSEDHIKSFMKQLLEGLNY 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1850 LHRRRIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISRQTAPSGAKGFGG---TEGFMAPEIIRynGEEEYTE 1926
Cdd:cd07864   132 CHKKNFLHRDIKCSNILL------------NNKGQIKLADFGLARLYNSEESRPYTNkviTLWYRPPELLL--GEERYGP 197
                         170       180       190
                  ....*....|....*....|....*....|...
gi 442620116 1927 KVDCFSFGMFIYENISLRQPFEGHESIK--ECI 1957
Cdd:cd07864   198 AIDVWSCGCILGELFTKKPIFQANQELAqlELI 230
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1842-1997 1.94e-05

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 48.80  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1842 QAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedSPRNlVHIKIADYGISRQTAPSGAKGFGGTEGFMAPEIIRYNGE 1921
Cdd:cd14102   113 QVLEAVRHCYSCGVVHRDIKDENLLV----------DLRT-GELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRY 181
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442620116 1922 EEYTEKVdcFSFGMFIYENISLRQPFEGHESIKECILEGSRPALTQretqfptcCLDLMVLCWHEQPRRRPTASQI 1997
Cdd:cd14102   182 HGRSATV--WSLGVLLYDMVCGDIPFEQDEEILRGRLYFRRRVSPE--------CQQLIKWCLSLRPSDRPTLEQI 247
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
1842-1938 1.95e-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: 48.82  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1842 QAARAIEYLHRRRIIYRDLKSENVLvwelpqpHTEDSPRNLVhiKIADYGISRQTapSGAKGFGG---TEGFMAPEIIry 1918
Cdd:cd14089   108 QIGSAVAHLHSMNIAHRDLKPENLL-------YSSKGPNAIL--KLTDFGFAKET--TTKKSLQTpcyTPYYVAPEVL-- 174
                          90       100
                  ....*....|....*....|
gi 442620116 1919 nGEEEYTEKVDCFSFGMFIY 1938
Cdd:cd14089   175 -GPEKYDKSCDMWSLGVIMY 193
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
452-564 1.98e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 48.24  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  452 ALTAITRIDFSHNVLTSIpQELFHLVSLRYLNVAQNKIT---DLpapigqtYGCPVLDELFLQDNQL---TTL---PAAI 522
Cdd:cd21340    44 FLTNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNRISvveGL-------ENLTNLEELHIENQRLppgEKLtfdPRSL 115
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 442620116  523 FHL-PALSILDVSNNKLQQLPfDLWRAPKLRELNVAFNLLRDL 564
Cdd:cd21340   116 AALsNSLRVLNISGNNIDSLE-PLAPLRNLEQLDASNNQISDL 157
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
459-862 2.08e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 50.23  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  459 IDFSHNVLTS-IPQELFHLVSLRYLNVAQNKIT-DLPAPIGQTYGcpvLDELFLQDNQLT-TLPAAIFHLPALSILD-VS 534
Cdd:PLN00113  169 LDLGGNVLVGkIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKS---LKWIYLGYNNLSgEIPYEIGGLTSLNHLDlVY 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  535 NNKLQQLPFDLWRAPKLRELNVAFNLLRDlPVPP----MQTSSSLLSLDK----------LNLQSFE--EPPSNK----- 593
Cdd:PLN00113  246 NNLTGPIPSSLGNLKNLQYLFLYQNKLSG-PIPPsifsLQKLISLDLSDNslsgeipelvIQLQNLEilHLFSNNftgki 324
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  594 PRNVTQ-QRLTHRNLWSatlditdNDMKWQHEQDLGDgktagvgSSQLSSLNIA-NNLFTSIPAALpCLAVNLTRLNMSY 671
Cdd:PLN00113  325 PVALTSlPRLQVLQLWS-------NKFSGEIPKNLGK-------HNNLTVLDLStNNLTGEIPEGL-CSSGNLFKLILFS 389
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  672 NSL-----RSMGHVTSypatLKQLDLSHNEIScwPSLPRITESDP--HLLCYSCVQLpEGRDDDYKTASSKGSSSSATsf 744
Cdd:PLN00113  390 NSLegeipKSLGACRS----LRRVRLQDNSFS--GELPSEFTKLPlvYFLDISNNNL-QGRINSRKWDMPSLQMLSLA-- 460
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  745 RASVLKSVCRHRRHLRLEALRtliladnlLTRIQLSTDDATTLFNESEDADWSVVGVNRSKVIFPNLSM------LDMTN 818
Cdd:PLN00113  461 RNKFFGGLPDSFGSKRLENLD--------LSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSckklvsLDLSH 532
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 442620116  819 NCLK-EIPASLHELSSLSVLNISGNVNITELPPHLGLLSRLWNLN 862
Cdd:PLN00113  533 NQLSgQIPASFSEMPVLSQLDLSQNQLSGEIPKNLGNVESLVQVN 577
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
1846-1973 2.75e-05

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 48.45  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNLVHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIrynGEEEY 1924
Cdd:cd14172   115 AIQYLHSMNIAHRDVKPENLLY---------TSKEKDAVLKLTDFGFAKETTVQNAlQTPCYTPYYVAPEVL---GPEKY 182
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 442620116 1925 TEKVDCFSFGMFIYENISLRQPFegHESIKECILEGSRPALTQRETQFP 1973
Cdd:cd14172   183 DKSCDMWSLGVIMYILLCGFPPF--YSNTGQAISPGMKRRIRMGQYGFP 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
88-141 2.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 2.92e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 442620116    88 YSPLYAAVHSGHLGIARLMLDHFPELIQQPtVERWLPLHAACINGHIKLLELLI 141
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVD-GNGETALHFAASNGNVEVLKLLL 54
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
1780-1939 3.00e-05

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: 48.29  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1780 RQELAVLLTLKHPNIVPLVGICIKPL--ALVLELAPLGGLDALLRHyrRSGAHMGPHTFQ-TLVLQAARAIEYLHRRRII 1856
Cdd:cd14157    40 QTEVQICFRCCHPNILPLLGFCVESDchCLIYPYMPNGSLQDRLQQ--QGGSHPLPWEQRlSISLGLLKAVQHLHNFGIL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVWELPQPHTEDSPRNLVHI-KIADYGISRqtapsgAKGFGGTEGFMAPEIIRyNGeeEYTEKVDCFSFGM 1935
Cdd:cd14157   118 HGNIKSSNVLLDGNLLPKLGHSGLRLCPVdKKSVYTMMK------TKVLQISLAYLPEDFVR-HG--QLTEKVDIFSCGV 188

                  ....
gi 442620116 1936 FIYE 1939
Cdd:cd14157   189 VLAE 192
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
1693-1957 3.02e-05

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: 48.52  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1693 DIPDKHtIPSECIikgsllGRGAFGFVfkanCKVRGARSFKPVAMKMLqpvppgARAKESALMAFKvavgkwdrdplqhs 1772
Cdd:cd07858     2 EVDTKY-VPIKPI------GRGAYGIV----CSAKNSETNEKVAIKKI------ANAFDNRIDAKR-------------- 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1773 ckaycTARqELAVLLTLKHPNIVPLVGIcIKP--------LALVLELaplggLDALLRHYRRSGAHMGPHTFQTLVLQAA 1844
Cdd:cd07858    51 -----TLR-EIKLLRHLDHENVIAIKDI-MPPphreafndVYIVYEL-----MDTDLHQIIRSSQTLSDDHCQYFLYQLL 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1845 RAIEYLHRRRIIYRDLKSENVLVwelpqphteDSPRNLvhiKIADYGISRQTApsgakgfgGTEGFM----------APE 1914
Cdd:cd07858   119 RGLKYIHSANVLHRDLKPSNLLL---------NANCDL---KICDFGLARTTS--------EKGDFMteyvvtrwyrAPE 178
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 442620116 1915 IIRynGEEEYTEKVDCFSFGMfIYENISLRQP-FEGhesiKECI 1957
Cdd:cd07858   179 LLL--NCSEYTTAIDVWSVGC-IFAELLGRKPlFPG----KDYV 215
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
1712-1973 3.27e-05

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: 48.38  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1712 GRGAFGFV----FKANCKVrgarsfkpVAMKMLqpvppgaRAKEsalMAFKVAVG--KWDRDPLQHS-----CKAYCTAR 1780
Cdd:cd05599    10 GRGAFGEVrlvrKKDTGHV--------YAMKKL-------RKSE---MLEKEQVAhvRAERDILAEAdnpwvVKLYYSFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1781 QElavlltlkhpnivplvgiciKPLALVLELAPLGGLDALLrhyrrsgahMGPHTF-----QTLVLQAARAIEYLHRRRI 1855
Cdd:cd05599    72 DE--------------------ENLYLIMEFLPGGDMMTLL---------MKKDTLteeetRFYIAETVLAIESIHKLGY 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1856 IYRDLKSENVLVwelpqphteDSPRnlvHIKIADYGISrqtapsgaKGFG---------GTEGFMAPEIIRYNGeeeYTE 1926
Cdd:cd05599   123 IHRDIKPDNLLL---------DARG---HIKLSDFGLC--------TGLKkshlaystvGTPDYIAPEVFLQKG---YGK 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 442620116 1927 KVDCFSFGMFIYENISLRQPFEGHESIKECilegsRPALTQRET-QFP 1973
Cdd:cd05599   180 ECDWWSLGVIMYEMLIGYPPFCSDDPQETC-----RKIMNWRETlVFP 222
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
1768-1956 3.90e-05

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: 47.58  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1768 PLQHSCKAYcTARQELAVLLTLKHPNIVPLVGICIKPLALVLELAPLGGLDALLR----HYRRSGAHMGPHtfqtlVLQA 1843
Cdd:cd14114    36 MTPHESDKE-TVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELFERiaaeHYKMSEAEVINY-----MRQV 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1844 ARAIEYLHRRRIIYRDLKSENVLVwelpqphtedSPRNLVHIKIADYGISRQTAPSGA-KGFGGTEGFMAPEIIRYNGEE 1922
Cdd:cd14114   110 CEGLCHMHENNIVHLDIKPENIMC----------TTKRSNEVKLIDFGLATHLDPKESvKVTTGTAEFAAPEIVEREPVG 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 442620116 1923 EYTekvDCFSFGMFIYENISLRQPFEGH------ESIKEC 1956
Cdd:cd14114   180 FYT---DMWAVGVLSYVLLSGLSPFAGEnddetlRNVKSC 216
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
1711-1895 4.02e-05

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


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 47.84  E-value: 4.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1711 LGRGAFGFVFKANCKVRGarsfKPVAMKmlqpvppgarakesalmafkvavgkwdrdpLQHSCKAYCTARQELAVLLTLK 1790
Cdd:cd14016     8 IGSGSFGEVYLGIDLKTG----EEVAIK------------------------------IEKKDSKHPQLEYEAKVYKLLQ 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1791 HPNIVPLVGICIKPL---ALVLELapLG-GLDALLRHYRRsgaHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVL 1866
Cdd:cd14016    54 GGPGIPRLYWFGQEGdynVMVMDL--LGpSLEDLFNKCGR---KFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFL 128
                         170       180
                  ....*....|....*....|....*....
gi 442620116 1867 VwelpqpHTEDSpRNLVHikIADYGISRQ 1895
Cdd:cd14016   129 M------GLGKN-SNKVY--LIDFGLAKK 148
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
1789-1997 4.20e-05

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: 47.82  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1789 LKHPNIVPLVGICIKP------LALVLELAPLGGL-DALLRHyrrsgaHMGPHTFQTLVLQAARAIEYLH--------RR 1853
Cdd:cd14142    56 LRHENILGFIASDMTSrnsctqLWLITHYHENGSLyDYLQRT------TLDHQEMLRLALSAASGLVHLHteifgtqgKP 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVwelpqphtedsPRNLVHIkIADYGIS-RQTAPSGAKGFG-----GTEGFMAPEI----IRYNGEEE 1923
Cdd:cd14142   130 AIAHRDLKSKNILV-----------KSNGQCC-IADLGLAvTHSQETNQLDVGnnprvGTKRYMAPEVldetINTDCFES 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1924 YtEKVDCFSFGMFIYEnISLRQPFEG-------------------HESIKECILEGSRPALTQRETQFPTCCL--DLMVL 1982
Cdd:cd14142   198 Y-KRVDIYAFGLVLWE-VARRCVSGGiveeykppfydvvpsdpsfEDMRKVVCVDQQRPNIPNRWSSDPTLTAmaKLMKE 275
                         250
                  ....*....|....*
gi 442620116 1983 CWHEQPRRRPTASQI 1997
Cdd:cd14142   276 CWYQNPSARLTALRI 290
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
1842-1998 4.32e-05

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: 47.70  E-value: 4.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1842 QAARAIEYLHRRRIIYRDLKSENVLVWElpqphtedsprnLVHIKIADYGISRQTAPSGA--KGFGGTEGFMAPEIIRYN 1919
Cdd:cd14188   109 QIVSGLKYLHEQEILHRDLKLGNFFINE------------NMELKVGDFGLAARLEPLEHrrRTICGTPNYLSPEVLNKQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1920 GeeeYTEKVDCFSFGMFIYENISLRQPFEGhESIKE---CIlegsRPALTQRETQFPTCCLDLMVLCWHEQPRRRPTASQ 1996
Cdd:cd14188   177 G---HGCESDIWALGCVMYTMLLGRPPFET-TNLKEtyrCI----REARYSLPSSLLAPAKHLIASMLSKNPEDRPSLDE 248

                  ..
gi 442620116 1997 IV 1998
Cdd:cd14188   249 II 250
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
1758-1955 4.77e-05

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: 48.24  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1758 KVAVGKWdRDPLQHSCKAYCTARqELAVLLTLKHPNIVPLVGICIKP-------LALVLELaplggLDALLRHYRRSGAH 1830
Cdd:cd07859    27 KVAIKKI-NDVFEHVSDATRILR-EIKLLRLLRHPDIVEIKHIMLPPsrrefkdIYVVFEL-----MESDLHQVIKANDD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1831 MGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedspRNLVHIKIADYGISR---QTAPSGA--KGFG 1905
Cdd:cd07859   100 LTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILA------------NADCKLKICDFGLARvafNDTPTAIfwTDYV 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 442620116 1906 GTEGFMAPEIIrynGE--EEYTEKVDCFSFGMFIYENISLRQPFEGHESIKE 1955
Cdd:cd07859   168 ATRWYRAPELC---GSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQ 216
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
1778-1997 5.50e-05

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: 47.28  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1778 TARQELAVLLTLK-HPNIVPLVG---ICIKP----LALVLELAPLGGLDALLRHYRRSGAHmgphtfQTLVLQ----AAR 1845
Cdd:cd14037    46 VCKREIEIMKRLSgHKNIVGYIDssaNRSGNgvyeVLLLMEYCKGGGVIDLMNQRLQTGLT------ESEILKifcdVCE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1846 AIEYLHRRR--IIYRDLKSENVLVwelpqphtedSPRNlvHIKIADYG---------------------ISRQTAPSgak 1902
Cdd:cd14037   120 AVAAMHYLKppLIHRDLKVENVLI----------SDSG--NYKLCDFGsattkilppqtkqgvtyveedIKKYTTLQ--- 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1903 gfggtegFMAPEIIRYNGEEEYTEKVDCFSFGMFIYENISLRQPFEghESIKECILEGSrpaltqreTQFPT-------- 1974
Cdd:cd14037   185 -------YRAPEMIDLYRGKPITEKSDIWALGCLLYKLCFYTTPFE--ESGQLAILNGN--------FTFPDnsryskrl 247
                         250       260
                  ....*....|....*....|....
gi 442620116 1975 -CCLDLMVLcwhEQPRRRPTASQI 1997
Cdd:cd14037   248 hKLIRYMLE---EDPEKRPNIYQV 268
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
1782-1955 7.96e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 47.68  E-value: 7.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICI--KPLALVLelaPLGGLDalLRHY---RRSGAHMGPHTFQTLVLqaaRAIEYLHRRRII 1856
Cdd:PHA03212  133 EAHILRAINHPSIIQLKGTFTynKFTCLIL---PRYKTD--LYCYlaaKRNIAICDILAIERSVL---RAIQYLHENRII 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1857 YRDLKSENVLVwelpqPHTEDsprnlvhIKIADYGISRQTAPSGAK---GFGGTEGFMAPEIIrynGEEEYTEKVDCFSF 1933
Cdd:PHA03212  205 HRDIKAENIFI-----NHPGD-------VCLGDFGAACFPVDINANkyyGWAGTIATNAPELL---ARDPYGPAVDIWSA 269
                         170       180
                  ....*....|....*....|..
gi 442620116 1934 GMFIYENISlrqpfeGHESIKE 1955
Cdd:PHA03212  270 GIVLFEMAT------CHDSLFE 285
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
1807-1896 8.25e-05

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 47.18  E-value: 8.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1807 LVLELAPLGGLDALLRHYrrsgAHMGPHTFQTLVLQAARAIEYLHRRRIIYRDLKSENVLVwelpqphtedspRNLVHIK 1886
Cdd:cd05610    81 LVMEYLIGGDVKSLLHIY----GYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLI------------SNEGHIK 144
                          90
                  ....*....|
gi 442620116 1887 IADYGISRQT 1896
Cdd:cd05610   145 LTDFGLSKVT 154
Ank_2 pfam12796
Ankyrin repeats (3 copies);
125-297 8.73e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 8.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   125 LHAACINGHIKLLELLISYSYpdylyqtyrdeegqwewrlpfDANAHDVTGQTSLYIASILGNKQLVGVLLKwqlhcrrt 204
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGA---------------------DANLQDKNGRTALHLAAKNGHLEIVKLLLE-------- 51
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   205 lgdsassvstpitptrkrisfgiqaimsklhisgesegpddlasqestecqrcpiNVNLLCGAARETALLAAVRGGHLDV 284
Cdd:pfam12796   52 -------------------------------------------------------HADVNLKDNGRTALHYAARSGHLEI 76
                          170
                   ....*....|...
gi 442620116   285 VQSLLQHGANPNI 297
Cdd:pfam12796   77 VKLLLEKGADINV 89
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
270-300 9.68e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 9.68e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 442620116   270 ETAL-LAAVRGGHLDVVQSLLQHGANPNIVAK 300
Cdd:pfam00023    3 NTPLhLAAGRRGNLEIVKLLLSKGADVNARDK 34
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
1710-1979 1.30e-04

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 46.93  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1710 LLGRGAFGFVfkANCKVRGARsfKPVAMKMLQpvppgaraKESALMAFKVAVGKWDRDPLQHSCKAYCTARQelavlLTL 1789
Cdd:cd05623    79 VIGRGAFGEV--AVVKLKNAD--KVFAMKILN--------KWEMLKRAETACFREERDVLVNGDSQWITTLH-----YAF 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1790 KHPNivplvgicikPLALVLELAPLGGLDALLRHYR-RSGAHMGPHTFQTLVLqaarAIEYLHRRRIIYRDLKSENVLVw 1868
Cdd:cd05623   142 QDDN----------NLYLVMDYYVGGDLLTLLSKFEdRLPEDMARFYLAEMVL----AIDSVHQLHYVHRDIKPDNILM- 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1869 elpqphteDSPRnlvHIKIADYGISRQTAPSGAKGFG---GTEGFMAPEIIRY--NGEEEYTEKVDCFSFGMFIYENISL 1943
Cdd:cd05623   207 --------DMNG---HIRLADFGSCLKLMEDGTVQSSvavGTPDYISPEILQAmeDGKGKYGPECDWWSLGVCMYEMLYG 275
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 442620116 1944 RQPFEGhesikECILEGSRPALTQRET-QFPTCCLDL 1979
Cdd:cd05623   276 ETPFYA-----ESLVETYGKIMNHKERfQFPTQVTDV 307
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
809-850 1.56e-04

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 41.08  E-value: 1.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 442620116   809 PNLSMLDMTNNCLKEIPAsLHELSSLSVLNISGNVNITELPP 850
Cdd:pfam12799    1 PNLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNKITDLSD 41
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
1705-1947 2.11e-04

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: 46.22  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1705 IIKgsLLGRGAFGFVFKanckVRGARSFKPVAMKMLQPVPPGARAkESALMafkvavgkW-DRDPLQHsckayctARQEL 1783
Cdd:cd05596    30 VIK--VIGRGAFGEVQL----VRHKSTKKVYAMKLLSKFEMIKRS-DSAFF--------WeERDIMAH-------ANSEW 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1784 AVLLTLKHPNIvplvgiciKPLALVLELAPLGGLDALLRHYRRSgAHMGPHTFQTLVLqaarAIEYLHRRRIIYRDLKSE 1863
Cdd:cd05596    88 IVQLHYAFQDD--------KYLYMVMDYMPGGDLVNLMSNYDVP-EKWARFYTAEVVL----ALDAIHSMGFVHRDVKPD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1864 NVLVwelpqphteDSprnLVHIKIADYGISRQTapsGAKGFG------GTEGFMAPEIIR-YNGEEEYTEKVDCFSFGMF 1936
Cdd:cd05596   155 NMLL---------DA---SGHLKLADFGTCMKM---DKDGLVrsdtavGTPDYISPEVLKsQGGDGVYGRECDWWSVGVF 219
                         250
                  ....*....|.
gi 442620116 1937 IYENISLRQPF 1947
Cdd:cd05596   220 LYEMLVGDTPF 230
LRR_8 pfam13855
Leucine rich repeat;
764-842 3.13e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 3.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   764 LRTLILADNLLTRIqlstdDATTLFNesedadwsvvgvnrskviFPNLSMLDMTNNCLKEI-PASLHELSSLSVLNISGN 842
Cdd:pfam13855    3 LRSLDLSNNRLTSL-----DDGAFKG------------------LSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGN 59
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
809-858 5.29e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 45.61  E-value: 5.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 442620116  809 PNLSMLDMTNNCLK-EIPASLHELSSLSVLNISGNVNITELPPHLGLLSRL 858
Cdd:PLN00113  140 PNLETLDLSNNMLSgEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSL 190
LRR_8 pfam13855
Leucine rich repeat;
638-697 5.70e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.20  E-value: 5.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116   638 SQLSSLNIANNLFTSIPAA----LPclavNLTRLNMSYNSLRSM-GHVTSYPATLKQLDLSHNEI 697
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGafkgLS----NLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
453-489 1.37e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.04  E-value: 1.37e-03
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 442620116   453 LTAITRIDFSHNVLTSI-PQELFHLVSLRYLNVAQNKI 489
Cdd:pfam13855   24 LSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
453-561 1.42e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 44.07  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116  453 LTAITRIDFSHNVLT-SIPQELFHLV-SLRYLNVAQNKITDlPAPIGQTygcPVLDELFLQDNQLT-TLPAAIFHLPALS 529
Cdd:PLN00113   92 LPYIQTINLSNNQLSgPIPDDIFTTSsSLRYLNLSNNNFTG-SIPRGSI---PNLETLDLSNNMLSgEIPNDIGSFSSLK 167
                          90       100       110
                  ....*....|....*....|....*....|...
gi 442620116  530 ILDVSNNKLQ-QLPFDLWRAPKLRELNVAFNLL 561
Cdd:PLN00113  168 VLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQL 200
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
462-532 1.66e-03

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 42.47  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442620116  462 SHNVLTSIpQELFHLVSLRYLNVAQNKITDLPAPIGQTYGCPVLDELFLQDNQLTTLP----AAIFHLPALSILD 532
Cdd:cd21340   128 SGNNIDSL-EPLAPLRNLEQLDASNNQISDLEELLDLLSSWPSLRELDLTGNPVCKKPkyrdKIILASKSLEVLD 201
Ank_2 pfam12796
Ankyrin repeats (3 copies);
257-342 2.03e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.33  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   257 CPINVNLLCGaarETALLAAVRGGHLDVVQSLLQHgANPNIVAkpvedhndpkcceeiYGLSnvPIAEACKQRSLAMLDL 336
Cdd:pfam12796   21 ADANLQDKNG---RTALHLAAKNGHLEIVKLLLEH-ADVNLKD---------------NGRT--ALHYAARSGHLEIVKL 79

                   ....*.
gi 442620116   337 LLKHGA 342
Cdd:pfam12796   80 LLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
19-109 5.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 5.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116   19 ELRTAVISGDERTVRVLLAaLGTerqIIVNMAPSGANTLLFLACQSGYESITQRLLDAGADGRSHAVTKYSPLYAAVHSG 98
Cdd:PHA02875   71 ELHDAVEEGDVKAVEELLD-LGK---FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
                          90
                  ....*....|.
gi 442620116   99 HLGIARLMLDH 109
Cdd:PHA02875  147 DIKGIELLIDH 157
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
1782-1955 5.91e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.14  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1782 ELAVLLTLKHPNIVPLVGICI--KPLALVLELAPLGGLDALLRHY---RRsgahmgphtfQTLVLQAARAIEYLHRR--- 1853
Cdd:PLN00113  733 EIADMGKLQHPNIVKLIGLCRseKGAYLIHEYIEGKNLSEVLRNLsweRR----------RKIAIGIAKALRFLHCRcsp 802
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116 1854 RIIYRDLKSENVLVWELPQPHTEDSPRNLVHIKIADYGISrqtapsgakgfggteGFMAPEIiryNGEEEYTEKVDCFSF 1933
Cdd:PLN00113  803 AVVVGNLSPEKIIIDGKDEPHLRLSLPGLLCTDTKCFISS---------------AYVAPET---RETKDITEKSDIYGF 864
                         170       180
                  ....*....|....*....|....*.
gi 442620116 1934 GMFIYENISLRQP----FEGHESIKE 1955
Cdd:PLN00113  865 GLILIELLTGKSPadaeFGVHGSIVE 890
Ank_2 pfam12796
Ankyrin repeats (3 copies);
20-79 7.74e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 7.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 442620116    20 LRTAVISGDERTVRVLLAalgterQIIVNMAPSGaNTLLFLACQSGYESITQRLLDAGAD 79
Cdd:pfam12796   34 LHLAAKNGHLEIVKLLLE------HADVNLKDNG-RTALHYAARSGHLEIVKLLLEKGAD 86
 
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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