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Conserved domains on  [gi|22299030|ref|NP_682277|]
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hypothetical protein tll1487, partial [Thermosynechococcus elongatus BP-1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
1-88 1.62e-14

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


:

Pssm-ID: 224630  Cd Length: 191  Bit Score: 71.14  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030   1 MITLTLLHPVQATPVQSWTFEN------ENVIRIGRAVDNHVVLYSAVVSRHHVELRRHGLQWEVVNLG-TNGTYLDGKR 73
Cdd:COG1716  60 LEPGVLTALDGPLAVTIGLDEGsvivlgEPVTTIGRDPDNDIVLDDDVVSRRHAELRREGNEVFLEDLGsTNGTYVNGEK 139
                        90
                ....*....|....*.
gi 22299030  74 IQQA-TLTDGGILRLA 88
Cdd:COG1716 140 VRQRvLLQDGDVIRLG 155
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
213-339 2.32e-14

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14014:

Pssm-ID: 328722  Cd Length: 260  Bit Score: 71.85  E-value: 2.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 213 NYQIIRALGQ---SNIYLGWRSGLTA-----VIRgHSLAASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVS 284
Cdd:cd14014   1 RYRLVRLLGRggmGEVYRARDTLLGRpvaikVLR-PELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22299030 285 EMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLI 339
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAG--IVHRDIKPANIL 132
 
Name Accession Description Interval E-value
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
1-88 1.62e-14

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 224630  Cd Length: 191  Bit Score: 71.14  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030   1 MITLTLLHPVQATPVQSWTFEN------ENVIRIGRAVDNHVVLYSAVVSRHHVELRRHGLQWEVVNLG-TNGTYLDGKR 73
Cdd:COG1716  60 LEPGVLTALDGPLAVTIGLDEGsvivlgEPVTTIGRDPDNDIVLDDDVVSRRHAELRREGNEVFLEDLGsTNGTYVNGEK 139
                        90
                ....*....|....*.
gi 22299030  74 IQQA-TLTDGGILRLA 88
Cdd:COG1716 140 VRQRvLLQDGDVIRLG 155
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
26-87 1.93e-14

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 306897  Cd Length: 66  Bit Score: 68.37  E-value: 1.93e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22299030    26 IRIGRAVDNHVVLYSAVVSRHHVELRRH-GLQWEVVNLG-TNGTYLDGKRIQQ--ATLTDGGILRL 87
Cdd:pfam00498   1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLGsTNGTFVNGQRLGPepVRLKDGDVIRL 66
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
213-339 2.32e-14

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  Cd Length: 260  Bit Score: 71.85  E-value: 2.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 213 NYQIIRALGQ---SNIYLGWRSGLTA-----VIRgHSLAASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVS 284
Cdd:cd14014   1 RYRLVRLLGRggmGEVYRARDTLLGRpvaikVLR-PELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22299030 285 EMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLI 339
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAG--IVHRDIKPANIL 132
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
13-100 3.32e-11

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017  Cd Length: 102  Bit Score: 60.09  E-value: 3.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030  13 TPVQSWTFENENVIRIGRAVDNH-VVLYSAVVSRHHVELRRHGLQ--WEVVNLGTNGTYLDGKRIQQAT---LTDGGILR 86
Cdd:cd00060  11 ASGRRYYLDPGGTYTIGRDSDNCdIVLDDPSVSRRHAVIRYDGDGgvVLIDLGSTNGTFVNGQRVSPGEpvrLRDGDVIR 90
                        90
                ....*....|....
gi 22299030  87 LarSGPNIQIRLGS 100
Cdd:cd00060  91 L--GNTSISFRFES 102
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
26-74 4.58e-08

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578  Cd Length: 52  Bit Score: 50.25  E-value: 4.58e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 22299030     26 IRIGRAV-DNHVVLYSAVVSRHHVELRRH-GLQWEVVNLG-TNGTYLDGKRI 74
Cdd:smart00240   1 VTIGRSSeDCDIQLDGPSISRRHAVIVYDgGGRFYLIDLGsTNGTFVNGKRI 52
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
214-338 1.37e-07

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 51.76  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030    214 YQIIRALGQ---SNIYLGW--RSGLTAVIRGHSLAASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIY 288
Cdd:smart00220   1 YEILEKLGEgsfGKVYLARdkKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 22299030    289 GQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNL 338
Cdd:smart00220  81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENI 128
Pkinase pfam00069
Protein kinase domain;
247-341 1.16e-05

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 46.05  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030   247 DEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDp 326
Cdd:pfam00069  40 KKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNG- 118
                          90
                  ....*....|....*.
gi 22299030   327 pVLHLHIRPSN-LIHP 341
Cdd:pfam00069 119 -IIHRDLKPENiLIDE 133
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
2-113 1.03e-03

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537  Cd Length: 396  Bit Score: 40.43  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030     2 ITLTLLHPVQATPVQ--SWTFEnENVIRIGRAVDNHVVLYSA--VVSRHHVELRRHGLQWEVVNLGTNGTYLD--GKRIQ 75
Cdd:TIGR03354   1 LVLTVLNAHQLTPGIaaQKTFG-TNGGTIGRSEDCDWVLPDPerHVSGRHARIRYRDGAYLLTDLSTNGVFLNgsGSPLG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 22299030    76 QAT---LTDGGILRLarsGP-NIQIRLGSDQRPT-TPSARMET 113
Cdd:TIGR03354  80 RGNpvrLEQGDRLRL---GDyEIRVSLGDPLVSRqASESRADT 119
 
Name Accession Description Interval E-value
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
1-88 1.62e-14

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 224630  Cd Length: 191  Bit Score: 71.14  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030   1 MITLTLLHPVQATPVQSWTFEN------ENVIRIGRAVDNHVVLYSAVVSRHHVELRRHGLQWEVVNLG-TNGTYLDGKR 73
Cdd:COG1716  60 LEPGVLTALDGPLAVTIGLDEGsvivlgEPVTTIGRDPDNDIVLDDDVVSRRHAELRREGNEVFLEDLGsTNGTYVNGEK 139
                        90
                ....*....|....*.
gi 22299030  74 IQQA-TLTDGGILRLA 88
Cdd:COG1716 140 VRQRvLLQDGDVIRLG 155
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
26-87 1.93e-14

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 306897  Cd Length: 66  Bit Score: 68.37  E-value: 1.93e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22299030    26 IRIGRAVDNHVVLYSAVVSRHHVELRRH-GLQWEVVNLG-TNGTYLDGKRIQQ--ATLTDGGILRL 87
Cdd:pfam00498   1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDgGGRFYLEDLGsTNGTFVNGQRLGPepVRLKDGDVIRL 66
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
213-339 2.32e-14

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  Cd Length: 260  Bit Score: 71.85  E-value: 2.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 213 NYQIIRALGQ---SNIYLGWRSGLTA-----VIRgHSLAASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVS 284
Cdd:cd14014   1 RYRLVRLLGRggmGEVYRARDTLLGRpvaikVLR-PELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVM 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22299030 285 EMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLI 339
Cdd:cd14014  80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAG--IVHRDIKPANIL 132
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
13-100 3.32e-11

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017  Cd Length: 102  Bit Score: 60.09  E-value: 3.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030  13 TPVQSWTFENENVIRIGRAVDNH-VVLYSAVVSRHHVELRRHGLQ--WEVVNLGTNGTYLDGKRIQQAT---LTDGGILR 86
Cdd:cd00060  11 ASGRRYYLDPGGTYTIGRDSDNCdIVLDDPSVSRRHAVIRYDGDGgvVLIDLGSTNGTFVNGQRVSPGEpvrLRDGDVIR 90
                        90
                ....*....|....
gi 22299030  87 LarSGPNIQIRLGS 100
Cdd:cd00060  91 L--GNTSISFRFES 102
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
26-74 4.58e-08

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578  Cd Length: 52  Bit Score: 50.25  E-value: 4.58e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 22299030     26 IRIGRAV-DNHVVLYSAVVSRHHVELRRH-GLQWEVVNLG-TNGTYLDGKRI 74
Cdd:smart00240   1 VTIGRSSeDCDIQLDGPSISRRHAVIVYDgGGRFYLIDLGsTNGTFVNGKRI 52
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
254-339 1.26e-07

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  Cd Length: 247  Bit Score: 51.88  E-value: 1.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 254 RQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHI 333
Cdd:cd14006  38 REISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHH--ILHLDL 115

                ....*.
gi 22299030 334 RPSNLI 339
Cdd:cd14006 116 KPENIL 121
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
214-338 1.37e-07

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 51.76  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030    214 YQIIRALGQ---SNIYLGW--RSGLTAVIRGHSLAASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIY 288
Cdd:smart00220   1 YEILEKLGEgsfGKVYLARdkKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 22299030    289 GQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNL 338
Cdd:smart00220  81 GGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENI 128
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
22-87 2.16e-07

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 318828  Cd Length: 91  Bit Score: 49.13  E-value: 2.16e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22299030    22 NENVIRIGRAVDNHVVLYSAVVSRHHVELRRHGLQWEVVNLG-TNGTYLDGKRIQQaTLTDGGILRL 87
Cdd:pfam16697  15 EGGRYRIGSDPDCDIVLSDKEVSRVHLKLEVDDEGVRLTDLGsRNGTLVNGQRVEL-ELRPGDVIEL 80
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
245-339 2.87e-07

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  Cd Length: 257  Bit Score: 51.10  E-value: 2.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWlipVCEL---LEVL 321
Cdd:cd05578  40 EKDSVRNVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDLRYHLQQKVKFSEETVKFY---ICEIvlaLDYL 116
                        90
                ....*....|....*...
gi 22299030 322 HQQDppVLHLHIRPSNLI 339
Cdd:cd05578 117 HSKN--IIHRDIKPDNIL 132
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
263-349 8.27e-07

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077  Cd Length: 291  Bit Score: 49.64  E-value: 8.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 263 QHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLIHPY 342
Cdd:cd14175  53 QHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQG--VVHRDLKPSNILYVD 130

                ....*...
gi 22299030 343 VSG-PASL 349
Cdd:cd14175 131 ESGnPESL 138
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
243-347 2.26e-06

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  Cd Length: 261  Bit Score: 48.46  E-value: 2.26e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 243 AASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSY----LVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELL 318
Cdd:cd14033  38 KLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRGHkciiLVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGL 117
                        90       100
                ....*....|....*....|....*....
gi 22299030 319 EVLHQQDPPVLHLHIRPSNLihpYVSGPA 347
Cdd:cd14033 118 HFLHSRCPPILHRDLKCDNI---FITGPT 143
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
261-337 4.23e-06

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  Cd Length: 250  Bit Score: 47.22  E-value: 4.23e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22299030 261 KIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRV-QEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSN 337
Cdd:cd14103  46 QLRHPRLLQLYDAFETPREMVLVMEYVAGGELFERVvDDDFELTERDCILFMRQICEGVQYMHKQG--ILHLDLKPEN 121
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
245-346 4.50e-06

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  Cd Length: 275  Bit Score: 47.41  E-value: 4.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIRAFQRQAQQLCKIQHPVLPQF---WEAFQCGSDS-YLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEV 320
Cdd:cd14031  49 TKAEQQRFKEEAEMLKGLQHPNIVRFydsWESVLKGKKCiVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQF 128
                        90       100
                ....*....|....*....|....*.
gi 22299030 321 LHQQDPPVLHLHIRPSNLihpYVSGP 346
Cdd:cd14031 129 LHTRTPPIIHRDLKCDNI---FITGP 151
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
244-338 4.69e-06

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  Cd Length: 258  Bit Score: 47.09  E-value: 4.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 244 ASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQ 323
Cdd:cd05117  38 LKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHS 117
                        90
                ....*....|....*
gi 22299030 324 QDppVLHLHIRPSNL 338
Cdd:cd05117 118 QG--IVHRDLKPENI 130
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
245-346 5.06e-06

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  Cd Length: 289  Bit Score: 47.35  E-value: 5.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDS----YLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEV 320
Cdd:cd14030  64 SKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKGkkciVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQF 143
                        90       100
                ....*....|....*....|....*.
gi 22299030 321 LHQQDPPVLHLHIRPSNLihpYVSGP 346
Cdd:cd14030 144 LHTRTPPIIHRDLKCDNI---FITGP 166
Pkinase pfam00069
Protein kinase domain;
247-341 1.16e-05

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 46.05  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030   247 DEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDp 326
Cdd:pfam00069  40 KKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNG- 118
                          90
                  ....*....|....*.
gi 22299030   327 pVLHLHIRPSN-LIHP 341
Cdd:pfam00069 119 -IIHRDLKPENiLIDE 133
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
239-337 2.31e-05

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  Cd Length: 254  Bit Score: 45.04  E-value: 2.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 239 GHSLAASRDEIRAFQRQAQQLCKIQHPVLPQFwEAFQC----GSDS---YLVSEMIYGQSLKQRVQEQGSMNMIEVSRWL 311
Cdd:cd14012  32 YFKTSNGKKQIQLLEKELESLKKLRHPNLVSY-LAFSIerrgRSDGwkvYLLTEYAPGGSLSELLDSVGSVPLDTARRWT 110
                        90       100
                ....*....|....*....|....*.
gi 22299030 312 IPVCELLEVLHQQDppVLHLHIRPSN 337
Cdd:cd14012 111 LQLLEALEYLHRNG--VVHKSLHAGN 134
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
242-338 2.39e-05

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  Cd Length: 255  Bit Score: 44.96  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 242 LAASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIE--VSRWLIPVCelLE 319
Cdd:cd08219  35 LPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLMQKIKLQRGKLFPEdtILQWFVQMC--LG 112
                        90
                ....*....|....*....
gi 22299030 320 VLHQQDPPVLHLHIRPSNL 338
Cdd:cd08219 113 VQHIHEKRVLHRDIKSKNI 131
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
259-340 3.24e-05

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  Cd Length: 263  Bit Score: 44.63  E-value: 3.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 259 LCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHqqDPPVLHLHIRPSNL 338
Cdd:cd14167  55 LHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLH--DMGIVHRDLKPENL 132

                ..
gi 22299030 339 IH 340
Cdd:cd14167 133 LY 134
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
229-339 6.61e-05

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  Cd Length: 253  Bit Score: 43.58  E-value: 6.61e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 229 WRSGLTAVirghSLAASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVS 308
Cdd:cd14058  14 WRNQIVAV----KIIESESEKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVLHGKEPKPIYTAA 89
                        90       100       110
                ....*....|....*....|....*....|....*
gi 22299030 309 ---RWLIPVCELLEVLHQQDP-PVLHLHIRPSNLI 339
Cdd:cd14058  90 hamSWALQCAKGVAYLHSMKPkALIHRDLKPPNLL 124
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
248-346 8.57e-05

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  Cd Length: 266  Bit Score: 43.53  E-value: 8.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 248 EIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDS----YLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQ 323
Cdd:cd14032  43 ERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKGkrciVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHT 122
                        90       100
                ....*....|....*....|...
gi 22299030 324 QDPPVLHLHIRPSNLihpYVSGP 346
Cdd:cd14032 123 RTPPIIHRDLKCDNI---FITGP 142
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
253-339 9.00e-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  Cd Length: 259  Bit Score: 43.34  E-value: 9.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 253 QRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQG-SMNMIEVSRWLIPVCELLEVLHQQDppVLHL 331
Cdd:cd14114  47 RKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFLSGGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENN--IVHL 124

                ....*...
gi 22299030 332 HIRPSNLI 339
Cdd:cd14114 125 DIKPENIM 132
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
263-349 9.39e-05

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  Cd Length: 339  Bit Score: 43.47  E-value: 9.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 263 QHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLIHPY 342
Cdd:cd14176  71 QHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYVD 148

                ....*...
gi 22299030 343 VSG-PASL 349
Cdd:cd14176 149 ESGnPESI 156
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
213-338 9.76e-05

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  Cd Length: 257  Bit Score: 43.41  E-value: 9.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 213 NYQIIRALGQSN---IYL--GWRSGLTAVIRGHSLAA-SRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEM 286
Cdd:cd08225   1 RYEIIKKIGEGSfgkIYLakAKSDSEHCVIKEIDLTKmPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEY 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 22299030 287 IYGQSLKQRVQEQGSMNMIE--VSRWLIPVCelLEVLHQQDPPVLHLHIRPSNL 338
Cdd:cd08225  81 CDGGDLMKRINRQRGVLFSEdqILSWFVQIS--LGLKHIHDRKILHRDIKSQNI 132
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
245-341 9.78e-05

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  Cd Length: 257  Bit Score: 43.34  E-value: 9.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIRAFQRQaQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQ 324
Cdd:cd14107  39 SSTRARAFQER-DILARLSHRRLTCLLDQFETRKTLILILELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGM 117
                        90
                ....*....|....*....
gi 22299030 325 DppVLHLHIRPSN--LIHP 341
Cdd:cd14107 118 N--ILHLDIKPDNilMVSP 134
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
263-349 9.93e-05

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  Cd Length: 293  Bit Score: 43.46  E-value: 9.93e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 263 QHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLIHPY 342
Cdd:cd14178  55 QHPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQG--VVHRDLKPSNILYMD 132

                ....*...
gi 22299030 343 VSG-PASL 349
Cdd:cd14178 133 ESGnPESI 140
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
214-339 1.07e-04

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  Cd Length: 265  Bit Score: 43.23  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 214 YQIIRALGQ---SNIYLG-------WRSglTAVIRGHSLAASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLV 283
Cdd:cd14098   2 YQIIDRLGSgtfAEVKKAvevetgkMRA--IKQIVKRKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLV 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 22299030 284 SEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLI 339
Cdd:cd14098  80 MEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMG--ITHRDLKPENIL 133
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
262-339 1.24e-04

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  Cd Length: 259  Bit Score: 43.07  E-value: 1.24e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22299030 262 IQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQR-VQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLI 339
Cdd:cd14191  56 LHHPKLVQCVDAFEEKANIVMVLEMVSGGELFERiIDEDFELTERECIKYMRQISEGVEYIHKQG--IVHLDLKPENIM 132
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
245-330 1.43e-04

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  Cd Length: 258  Bit Score: 42.60  E-value: 1.43e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSY--LVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLH 322
Cdd:cd13983  40 PKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEviFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLH 119

                ....*...
gi 22299030 323 QQDPPVLH 330
Cdd:cd13983 120 TRDPPIIH 127
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
259-340 1.83e-04

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  Cd Length: 277  Bit Score: 42.57  E-value: 1.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 259 LCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNL 338
Cdd:cd14169  55 LRRINHENIVSLEDIYESPTHLYLAMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLG--IVHRDLKPENL 132

                ..
gi 22299030 339 IH 340
Cdd:cd14169 133 LY 134
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
246-338 1.86e-04

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  Cd Length: 256  Bit Score: 42.49  E-value: 1.86e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 246 RDEIRafqRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIE--VSRWLIPVCelLEVLHQ 323
Cdd:cd08218  43 REESR---KEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLYKRINAQRGVLFPEdqILDWFVQLC--LALKHV 117
                        90
                ....*....|....*
gi 22299030 324 QDPPVLHLHIRPSNL 338
Cdd:cd08218 118 HDRKILHRDIKSQNI 132
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
259-340 2.04e-04

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  Cd Length: 259  Bit Score: 42.36  E-value: 2.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 259 LCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNL 338
Cdd:cd14083  55 LRKIKHPNIVQLLDIYESKSHLYLVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLG--IVHRDLKPENL 132

                ..
gi 22299030 339 IH 340
Cdd:cd14083 133 LY 134
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
257-340 2.69e-04

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  Cd Length: 277  Bit Score: 42.15  E-value: 2.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 257 QQLCK--------IQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQG-SMNMIEVSRWLIPVCELLEVLHQQDpp 327
Cdd:cd14104  40 QVLVKkeisilniARHRNILRLHESFESHEELVMIFEFISGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKN-- 117
                        90
                ....*....|...
gi 22299030 328 VLHLHIRPSNLIH 340
Cdd:cd14104 118 IGHFDIRPENIIY 130
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
243-339 2.92e-04

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  Cd Length: 261  Bit Score: 41.87  E-value: 2.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 243 AASRDEIRafqRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQgSMNMIEVSRWLIP--VCELLEV 320
Cdd:cd14192  42 AKEREEVK---NEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFDRITDE-SYQLTELDAILFTrqICEGVHY 117
                        90
                ....*....|....*....
gi 22299030 321 LHQQdpPVLHLHIRPSNLI 339
Cdd:cd14192 118 LHQH--YILHLDLKPENIL 134
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
250-340 3.17e-04

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  Cd Length: 294  Bit Score: 41.73  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 250 RAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVL 329
Cdd:cd14085  43 KIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENG--IV 120
                        90
                ....*....|.
gi 22299030 330 HLHIRPSNLIH 340
Cdd:cd14085 121 HRDLKPENLLY 131
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
245-339 3.91e-04

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  Cd Length: 271  Bit Score: 41.53  E-value: 3.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIrafQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQ 324
Cdd:cd14195  51 SREEI---EREVNILREIQHPNIITLHDIFENKTDVVLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSK 127
                        90
                ....*....|....*
gi 22299030 325 DppVLHLHIRPSNLI 339
Cdd:cd14195 128 R--IAHFDLKPENIM 140
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
244-338 4.08e-04

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  Cd Length: 257  Bit Score: 41.27  E-value: 4.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 244 ASRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGsDSYLVSEMIY--GQSLKQRVQEQGSMNMIE--VSRWLIPVCELLE 319
Cdd:cd08223  38 ASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGE-DGFLYIVMGFceGGDLYTRLKEQKGVLLEErqVVEWFVQIAMALQ 116
                        90
                ....*....|....*....
gi 22299030 320 VLHQQDppVLHLHIRPSNL 338
Cdd:cd08223 117 YMHERN--ILHRDLKTQNI 133
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
221-338 4.26e-04

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  Cd Length: 245  Bit Score: 40.98  E-value: 4.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 221 GQSNIYLG-WRSGLTAV--IRGHSLAAsrDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQ 297
Cdd:cd13999   5 SFGEVYKGkWRGTDVAIkkLKVEDDND--ELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLLH 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 22299030 298 EQ-GSMNMIEVSRWLIPVCELLEVLHQqdPPVLHLHIRPSNL 338
Cdd:cd13999  83 KKkIPLSWSLRLKIALDIARGMNYLHS--PPIIHRDLKSLNI 122
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
254-339 6.00e-04

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  Cd Length: 255  Bit Score: 40.66  E-value: 6.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 254 RQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYgQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHI 333
Cdd:cd14108  47 RELALLAELDHKSIVRFHDAFEKRRVVIIVTELCH-EELLERITKRPTVCESEVRSYMRQLLEGIEYLHQND--VLHLDL 123

                ....*.
gi 22299030 334 RPSNLI 339
Cdd:cd14108 124 KPENLL 129
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
263-355 6.05e-04

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  Cd Length: 295  Bit Score: 40.77  E-value: 6.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 263 QHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLIhpY 342
Cdd:cd14177  56 QHPNIITLKDVYDDGRYVYLVTELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQG--VVHRDLKPSNIL--Y 131
                        90
                ....*....|...
gi 22299030 343 VSGPASLYSQKSC 355
Cdd:cd14177 132 MDDSANADSIRIC 144
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
245-339 6.52e-04

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  Cd Length: 215  Bit Score: 40.33  E-value: 6.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQ-GSMNMIEVSRWLIPVCELLEVLHQ 323
Cdd:cd00180  31 LKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLKDLLKENkGPLSEEEALSILRQLLSALEYLHS 110
                        90
                ....*....|....*.
gi 22299030 324 QdpPVLHLHIRPSNLI 339
Cdd:cd00180 111 N--GIIHRDLKPENIL 124
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
264-339 9.45e-04

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  Cd Length: 289  Bit Score: 40.48  E-value: 9.45e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22299030 264 HPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNLI 339
Cdd:cd14090  59 HPNILQLIEYFEDDERFYLVFEKMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKG--IAHRDLKPENIL 132
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
2-113 1.03e-03

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537  Cd Length: 396  Bit Score: 40.43  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030     2 ITLTLLHPVQATPVQ--SWTFEnENVIRIGRAVDNHVVLYSA--VVSRHHVELRRHGLQWEVVNLGTNGTYLD--GKRIQ 75
Cdd:TIGR03354   1 LVLTVLNAHQLTPGIaaQKTFG-TNGGTIGRSEDCDWVLPDPerHVSGRHARIRYRDGAYLLTDLSTNGVFLNgsGSPLG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 22299030    76 QAT---LTDGGILRLarsGP-NIQIRLGSDQRPT-TPSARMET 113
Cdd:TIGR03354  80 RGNpvrLEQGDRLRL---GDyEIRVSLGDPLVSRqASESRADT 119
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
244-340 1.17e-03

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  Cd Length: 285  Bit Score: 39.98  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 244 ASRDeiRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQ 323
Cdd:cd14166  41 LSRD--SSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHE 118
                        90
                ....*....|....*..
gi 22299030 324 QDppVLHLHIRPSNLIH 340
Cdd:cd14166 119 NG--IVHRDLKPENLLY 133
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
224-339 1.32e-03

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  Cd Length: 254  Bit Score: 39.82  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 224 NIYLG-WRSGLTAVIRGHSLA-ASRDEIRAFQRQAQQLCKIQHPVLPQFWEAfqCGSDSY---LVSEMIYGQSLKQRVQE 298
Cdd:cd14064   8 KVYKGrCRNKIVAIKRYRANTyCSKSDVDMFCREVSILCRLNHPCVIQFVGA--CLDDPSqfaIVTQYVSGGSLFSLLHE 85
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 22299030 299 QG-SMNMIEVSRWLIPVCELLEVLHQQDPPVLHLHIRPSNLI 339
Cdd:cd14064  86 QKrVIDLQSKLIIAVDVAKGMEYLHNLTQPIIHRDLNSHNIL 127
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
255-339 1.92e-03

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  Cd Length: 261  Bit Score: 39.13  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 255 QAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQR-VQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHI 333
Cdd:cd14190  51 EIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELFERiVDEDYHLTEVDAMVFVRQICEGIQFMHQMR--VLHLDL 128

                ....*.
gi 22299030 334 RPSNLI 339
Cdd:cd14190 129 KPENIL 134
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
245-339 1.92e-03

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  Cd Length: 269  Bit Score: 39.23  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIrafQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQ 324
Cdd:cd14194  51 SREDI---EREVSILKEIQHPNVITLHEVYENKTDVILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSL 127
                        90
                ....*....|....*
gi 22299030 325 DppVLHLHIRPSNLI 339
Cdd:cd14194 128 Q--IAHFDLKPENIM 140
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
259-348 2.00e-03

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  Cd Length: 259  Bit Score: 39.05  E-value: 2.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 259 LCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNL 338
Cdd:cd14087  51 LRRVRHTNIIQLIEVFETKERVYMVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLG--ITHRDLKPENL 128
                        90
                ....*....|
gi 22299030 339 IHpYVSGPAS 348
Cdd:cd14087 129 LY-YHPGPDS 137
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
253-339 2.35e-03

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  Cd Length: 310  Bit Score: 39.25  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 253 QRQ--AQQLCKiQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCEllEVLHQQDPPVLH 330
Cdd:cd14179  49 QREiaALKLCE-GHPNIVKLHEVYHDQLHTFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVS--AVSHMHDVGVVH 125

                ....*....
gi 22299030 331 LHIRPSNLI 339
Cdd:cd14179 126 RDLKPENLL 134
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
239-339 2.35e-03

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  Cd Length: 257  Bit Score: 39.13  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 239 GHSLAASRDEIRAFQRQA-----QQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIP 313
Cdd:cd14110  28 GQMLAAKIIPYKPEDKQLvlreyQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNLAERNSYSEAEVTDYLWQ 107
                        90       100
                ....*....|....*....|....*.
gi 22299030 314 VCELLEVLHQQDppVLHLHIRPSNLI 339
Cdd:cd14110 108 ILSAVDYLHSRR--ILHLDLRSENMI 131
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
238-339 4.46e-03

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  Cd Length: 269  Bit Score: 38.24  E-value: 4.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 238 RGHSLAASRDEIrafQRQAQQLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCEL 317
Cdd:cd14105  44 KASRRGVSREDI---EREVSILRQVLHPNIITLHDVFENKTDVVLILELVAGGELFDFLAEKESLSEEEATEFLKQILDG 120
                        90       100
                ....*....|....*....|..
gi 22299030 318 LEVLHQQDppVLHLHIRPSNLI 339
Cdd:cd14105 121 VNYLHTKN--IAHFDLKPENIM 140
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
213-338 4.85e-03

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  Cd Length: 253  Bit Score: 37.84  E-value: 4.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 213 NYQIIRALGQ---SNIYLGwRSgltavIRGHSLAA----SRDEIRAFQrQAQQL---CKIQ----HPVLPQFWEAFQCGS 278
Cdd:cd14007   1 DFEIGKPLGKgkfGNVYLA-RE-----KKSGFIVAlkviSKSQLQKSG-LEHQLrreIEIQshlrHPNILRLYGYFEDKK 73
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 279 DSYLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDppVLHLHIRPSNL 338
Cdd:cd14007  74 RIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKN--IIHRDIKPENI 131
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
235-339 5.61e-03

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  Cd Length: 299  Bit Score: 38.11  E-value: 5.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 235 AVIRGHSLAAS-RDEIRA-FQRQAQQLCKIQ----HPVLPQFWEAFQCGSDSY-LVSEMIYGQSLKQRVQEQGSMNMIEV 307
Cdd:cd14040  34 AAVKIHQLNKSwRDEKKEnYHKHACREYRIHkeldHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEA 113
                        90       100       110
                ....*....|....*....|....*....|..
gi 22299030 308 SRWLIPVCELLEVLHQQDPPVLHLHIRPSNLI 339
Cdd:cd14040 114 RSIVMQIVNALRYLNEIKPPIIHYDLKPGNIL 145
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
245-338 5.89e-03

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  Cd Length: 256  Bit Score: 37.76  E-value: 5.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIRAfqrqaqqLCKIQHPVLPQFWEAFQCGSDSYLVSEMIYGQSLKQRVQEQGSMNMI----EVSRWLIPVCELLEV 320
Cdd:cd08530  46 SVNEIRL-------LASVNHPNIIRYKEAFLDGNRLCIVMEYAPFGDLSKLISKRKKKRRLfpedDIWRIFIQMLRGLKA 118
                        90
                ....*....|....*...
gi 22299030 321 LHQQDppVLHLHIRPSNL 338
Cdd:cd08530 119 LHDQK--ILHRDLKSANI 134
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
211-339 7.16e-03

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  Cd Length: 262  Bit Score: 37.49  E-value: 7.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 211 LGNYQIIRALGQSNiYLGWRSGLTAVIrGHSLA--------ASRDE--IRAFQRQAQQLCKIQHPVLPQFWEAFQCGSDS 280
Cdd:cd14070   1 VGSYLIGRKLGEGS-FAKVREGLHAVT-GEKVAikvidkkkAKKDSyvTKNLRREGRIQQMIRHPNITQLLDILETENSY 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 22299030 281 YLVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHqqDPPVLHLHIRPSNLI 339
Cdd:cd14070  79 YLVMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLH--RAGVVHRDLKIENLL 135
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
261-339 8.02e-03

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  Cd Length: 309  Bit Score: 37.35  E-value: 8.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 261 KIQHPVLPQFWEAFQCGSDSY-LVSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLEVLHQQDPPVLHLHIRPSNLI 339
Cdd:cd14041  66 ELDHPRIVKLYDYFSLDTDSFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNIL 145
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
245-339 9.99e-03

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  Cd Length: 279  Bit Score: 36.91  E-value: 9.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22299030 245 SRDEIRAFQRQAQQLCKIQ----HPVLPQFWEAFQCGSDSYL-VSEMIYGQSLKQRVQEQGSMNMIEVSRWLIPVCELLE 319
Cdd:cd13990  40 SEEKKQNYIKHALREYEIHksldHPRIVKLYDVFEIDTDSFCtVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALK 119
                        90       100
                ....*....|....*....|
gi 22299030 320 VLHQQDPPVLHLHIRPSNLI 339
Cdd:cd13990 120 YLNEIKPPIIHYDLKPGNIL 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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