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Conserved domains on  [gi|21223155|ref|NP_628934|]
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Ser/Thr protein kinase [Streptomyces coelicolor A3(2)]

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
107-201 1.33e-15

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: 304357 [Multi-domain]  Cd Length: 260  Bit Score: 76.86  E-value: 1.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQ-TLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:cd14014  58 SHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADLLRERgPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG 137
                        90
                ....*....|....*...
gi 21223155 186 RVMLT--GLAVGAAEEAL 201
Cdd:cd14014 138 RVKLTdfGIARALGDSGL 155
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
589-670 5.30e-10

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: 304357 [Multi-domain]  Cd Length: 260  Bit Score: 59.91  E-value: 5.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 589 APEQAgpvhenwqLAAPIGPATDLWALGALLFRAVQGHAPYPEESTAE-LVQIVCAEPPAFAEEC----GPLRPVVESLL 663
Cdd:cd14014 169 APEQA--------RGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAvLAKHLQEAPPPPSPLNpdvpPALDAIILRAL 240

                ....*..
gi 21223155 664 RQDPTER 670
Cdd:cd14014 241 AKDPEER 247
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
107-201 1.33e-15

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 76.86  E-value: 1.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQ-TLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:cd14014  58 SHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADLLRERgPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG 137
                        90
                ....*....|....*...
gi 21223155 186 RVMLT--GLAVGAAEEAL 201
Cdd:cd14014 138 RVKLTdfGIARALGDSGL 155
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
589-670 5.30e-10

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 59.91  E-value: 5.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 589 APEQAgpvhenwqLAAPIGPATDLWALGALLFRAVQGHAPYPEESTAE-LVQIVCAEPPAFAEEC----GPLRPVVESLL 663
Cdd:cd14014 169 APEQA--------RGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAvLAKHLQEAPPPPSPLNpdvpPALDAIILRAL 240

                ....*..
gi 21223155 664 RQDPTER 670
Cdd:cd14014 241 AKDPEER 247
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
107-193 6.52e-11

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 62.55  E-value: 6.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155    107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQ-TLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:smart00220  55 KHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKKRgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG 134
                           90
                   ....*....|
gi 21223155    186 RVMLT--GLA 193
Cdd:smart00220 135 HVKLAdfGLA 144
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
314-558 1.05e-10

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 64.24  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  314 RAALPGARPAPDGATQAGGPGTSGGRPGLAPGPGSSYDDDDgagRPPHGSAPGGARPGHGVEAAGGAPGARPGQGSGRAA 393
Cdd:PRK07764 585 EAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPA---APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  394 FAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPGQitdpygvgttawhgatprtPGDPASSAARPTGDPAFPAP 473
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA-------------------PAPAATPPAGQADDPAAQPP 722
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  474 RPAGEPAAGSG-PAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAADPEREGGPRPAAGWD 552
Cdd:PRK07764 723 QAAQGASAPSPaADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAE 802

                 ....*.
gi 21223155  553 DLAGRA 558
Cdd:PRK07764 803 EVAMEL 808
Sporozoite_P67 pfam05642
Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. ...
318-494 1.54e-08

Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. A stage specific surface antigen of Theileria parva, p67, is the basis for the development of an anti-sporozoite vaccine for the control of East Coast fever (ECF) in cattle. The antigen has been shown to contain five distinct linear peptide sequences recognized by sporozoite-neutralizing murine monoclonal antibodies.


Pssm-ID: 253298 [Multi-domain]  Cd Length: 727  Bit Score: 57.38  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   318 PGARPAPDGATQAGGPGTSGGRPGLAPGpGSSYDDDDGAGRPPHGSAPGGARPGHGVEAAGGApGARPGQGSGRAAFAAG 397
Cdd:pfam05642 144 PGVSTSSGSTTSGTDLNTKQSQTGLGAS-GSHAQQDPAVSQSGVVGVPGLGVPGVGVPGGGGA-GALPGVGVGRAGVSPG 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   398 SGQAPYAIGPDA---ASGAPWDEDSVGDPAT--SGAAVPPGQITDPYGVGTTAWHGATPRTPGD-----PASSAARPTGD 467
Cdd:pfam05642 222 VGVGGLGGVPGVgilASNTSREGQTQDDQERdgDGRVIEPGVGLPGVRVGDSTSSPSTTRPSGStttttPASSGPSAPGG 301
                         170       180
                  ....*....|....*....|....*....
gi 21223155   468 PAfPAPRPAGEPAAGS--GPAAGRALPGA 494
Cdd:pfam05642 302 PG-SSSRNAVTRSTDSisGPIPSPGAPRA 329
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
114-187 4.80e-03

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 38.95  E-value: 4.80e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21223155 114 VFDVFAEGGSLWIASELVAARPLAALL----TEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:COG0515  63 LYDFFQDEGSLYLVMEYVDGGSLEDLLkkigRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRV 140
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
107-201 1.33e-15

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 76.86  E-value: 1.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQ-TLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:cd14014  58 SHPNIVRVYDVGEDDGRPYIVMEYVEGGSLADLLRERgPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG 137
                        90
                ....*....|....*...
gi 21223155 186 RVMLT--GLAVGAAEEAL 201
Cdd:cd14014 138 RVKLTdfGIARALGDSGL 155
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
589-670 5.30e-10

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 59.91  E-value: 5.30e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 589 APEQAgpvhenwqLAAPIGPATDLWALGALLFRAVQGHAPYPEESTAE-LVQIVCAEPPAFAEEC----GPLRPVVESLL 663
Cdd:cd14014 169 APEQA--------RGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAvLAKHLQEAPPPPSPLNpdvpPALDAIILRAL 240

                ....*..
gi 21223155 664 RQDPTER 670
Cdd:cd14014 241 AKDPEER 247
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
608-676 6.79e-10

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 59.61  E-value: 6.79e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21223155 608 PATDLWALGALLFRAVQGHAPYPEESTAELV-QIVCAEPPA----FAEECGP-LRPVVESLLRQDPTERIDFEEL 676
Cdd:cd14010 189 FASDLWALGCVLYEMFTGKPPFVAESFTELVeKILNEDPPPpppkVSSKPSPdFKSLLKGLLEKDPAKRLSWDEL 263
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
107-193 8.18e-10

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 58.44  E-value: 8.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQ--TLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd00180  49 NHPNIVKLYDVFETENFLYLVMEYCEGGSLKDLLKENkgPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSD 128
                        90
                ....*....|.
gi 21223155 185 GRVMLT--GLA 193
Cdd:cd00180 129 GTVKLAdfGLA 139
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
107-194 3.15e-09

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 57.60  E-value: 3.15e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALL--TEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd05122  55 KHPNIVKYYGSYLKKDELWIVMEFCSGGSLKDLLknTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSD 134
                        90
                ....*....|..
gi 21223155 185 GRVMLT--GLAV 194
Cdd:cd05122 135 GEVKLIdfGLSA 146
PK_MviN-like cd13973
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
107-197 1.58e-08

Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.


Pssm-ID: 270875 [Multi-domain]  Cd Length: 236  Bit Score: 55.03  E-value: 1.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGR 186
Cdd:cd13973  59 NDPGLARVLDAVAYRGGVYVVAEWVPGSSLADVAESGPLDPEAAARAVAELAEALAAAHRAGLALGIDHPDRVRISSDGR 138
                        90
                ....*....|.
gi 21223155 187 VMLTGLAVGAA 197
Cdd:cd13973 139 VVLAFPAVLAA 149
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
108-190 3.10e-08

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 54.76  E-value: 3.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:cd06648  63 HPNIVEMYSSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRV 142

                ...
gi 21223155 188 MLT 190
Cdd:cd06648 143 KLS 145
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
607-675 3.54e-08

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


Pssm-ID: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 54.22  E-value: 3.54e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELV-QIVCAEP---PAFAEECGPLRPVVESLLRQDPTERIDFEE 675
Cdd:cd14121 174 DARVDLWSVGVILYECLFGRAPFASRSFEELEeKIRSSKPieiPTRPELSADCRDLLLRLLQRDPDRRISFEE 246
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
611-676 8.42e-08

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 53.00  E-value: 8.42e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223155 611 DLWALGALLFRAVQGHAPYPEESTAELVQIV--CAEPPAFAEECG---PLRPVVESLLRQDPTERIDFEEL 676
Cdd:cd14009 176 DLWSVGAILFEMLVGKPPFRGSNHVQLLRNIerSDAVIPFPIAAQlspDCKDLLRRLLRRDPAERISFEEF 246
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
108-190 8.73e-08

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 53.39  E-value: 8.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:cd06647  63 NPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSV 142

                ...
gi 21223155 188 MLT 190
Cdd:cd06647 143 KLT 145
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
108-194 1.66e-07

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 52.21  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLT--EQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:cd06614  55 HPNIVDYYDSYLVGDELWVVMEYMDGGSLTDIITqnPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDG 134
                        90
                ....*....|.
gi 21223155 186 RVMLT--GLAV 194
Cdd:cd06614 135 SVKLAdfGFAA 145
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
121-196 2.61e-07

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 52.09  E-value: 2.61e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 121 GGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRVMLTGLAVGA 196
Cdd:cd06917  74 GPSLWIIMDYCEGGSIRTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAA 149
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
107-192 2.68e-07

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 52.30  E-value: 2.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLteQTLTPYRAAEVA-----SDVLLALRVLHSYGWVHRNITARTVLV 181
Cdd:cd08216  57 QHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLL--KTHFPEGLPELAiafilRDVLNALEYIHSKGYIHRSVKASHILI 134
                        90
                ....*....|.
gi 21223155 182 CDDGRVMLTGL 192
Cdd:cd08216 135 SGDGKVVLSGL 145
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
118-196 3.55e-07

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 51.48  E-value: 3.55e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21223155 118 FAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRVMLTGLAVGA 196
Cdd:cd06609  68 FLKGSKLWIIMEYCGGGSVLDLLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSG 146
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
108-190 4.38e-07

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 51.56  E-value: 4.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:cd06657  76 HENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRV 155

                ...
gi 21223155 188 MLT 190
Cdd:cd06657 156 KLS 158
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
107-197 1.06e-06

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


Pssm-ID: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 50.05  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALL----TEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVC 182
Cdd:cd06610  57 NHPNVVSYYTSFVVGDELWLVMPLLSGGSLLDIMkssyPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLG 136
                        90
                ....*....|....*
gi 21223155 183 DDGRVMLTGLAVGAA 197
Cdd:cd06610 137 EDGSVKIADFGVSAS 151
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
603-680 1.10e-06

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 49.64  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 603 AAP--------IGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAE----PPAFAEECGPLrpvVESLLRQDPTER 670
Cdd:cd14075 167 AAPelfkdehyIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGtytiPSYVSEPCQEL---IRGILQPVPSDR 243
                        90
                ....*....|..
gi 21223155 671 IDFEEL--SGWL 680
Cdd:cd14075 244 YSIDEIknSEWL 255
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
607-680 1.24e-06

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 49.72  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAE-LVQIV-C--AEPPAFAEECgplRPVVESLLRQDPTERIDFEELSG--WL 680
Cdd:cd14074 182 APAVDIWSLGVILYMLVCGQPPFQEANDSEtLTMIMdCkyTVPAHVSPEC---KDLIRRMLIRDPKKRASLEEIENhpWL 258
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
108-190 1.54e-06

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


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 49.72  E-value: 1.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:cd06654  76 NPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSV 155

                ...
gi 21223155 188 MLT 190
Cdd:cd06654 156 KLT 158
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
107-196 2.38e-06

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 49.25  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTE--QTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd06643  60 DHPNIVKLLDAFYYENNLWILIEFCAGGAVDAVMLEleRPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLD 139
                        90
                ....*....|..
gi 21223155 185 GRVMLTGLAVGA 196
Cdd:cd06643 140 GDIKLADFGVSA 151
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
108-190 3.31e-06

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


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 48.50  E-value: 3.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:cd06658  78 HENVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRI 157

                ...
gi 21223155 188 MLT 190
Cdd:cd06658 158 KLS 160
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
108-190 3.34e-06

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


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 48.56  E-value: 3.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:cd06656  75 NPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSV 154

                ...
gi 21223155 188 MLT 190
Cdd:cd06656 155 KLT 157
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
107-196 3.35e-06

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 48.59  E-value: 3.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALL--TEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd06611  60 KHPNIVGLYEAYFYENKLWILIEFCDGGALDSIMleLERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLD 139
                        90
                ....*....|..
gi 21223155 185 GRVMLTGLAVGA 196
Cdd:cd06611 140 GDVKLADFGVSA 151
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
108-192 3.38e-06

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 48.71  E-value: 3.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVA---ARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd08226  58 HPNIMTHWTVFTEGSWLWVISPFMAygsARGLLKTYFPEGMNEALIGNILYGAIKALNYLHQNGCIHRSVKASHILISGD 137

                ....*...
gi 21223155 185 GRVMLTGL 192
Cdd:cd08226 138 GLVSLSGL 145
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
607-671 5.21e-06

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 47.51  E-value: 5.21e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGP-LRPVVESLLRQDPTERI 671
Cdd:cd05123 171 GKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPeAKSLISGLLQKDPTKRL 236
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
108-190 5.65e-06

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 48.06  E-value: 5.65e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:cd06659  77 HPNVVEMYKSYLVGEELWVLMEYLQGGALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRV 156

                ...
gi 21223155 188 MLT 190
Cdd:cd06659 157 KLS 159
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
107-196 7.62e-06

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 47.72  E-value: 7.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTE--QTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd06644  67 NHPYIVKLLGAFYWDGKLWIMIEFCPGGAVDAIMLEldRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLD 146
                        90
                ....*....|..
gi 21223155 185 GRVMLTGLAVGA 196
Cdd:cd06644 147 GDIKLADFGVSA 158
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
605-671 1.10e-05

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 46.82  E-value: 1.10e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223155 605 PIGPATDLWALGALLFRAVQGHAPYPEESTAELVQ-IVCAE---PPAFAEECGPLrpvVESLLRQDPTERI 671
Cdd:cd05581 194 PAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQkIVKLEyefPENFPPDAKDL---IQKLLVLDPSKRL 261
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
588-676 2.43e-05

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 45.54  E-value: 2.43e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 588 WAPEQ-AGPVHenwqlaapiGPATDLWALGALLFRAVQGHAPYPEESTAE-LVQIVCAE---PPAFAEECGPLrpvVESL 662
Cdd:cd14007 165 LPPEMvEGKEY---------DYKVDIWSLGVLCYELLVGKPPFESKSHQEtYKRIQNVDikfPSSVSPEAKDL---ISKL 232
                        90
                ....*....|....
gi 21223155 663 LRQDPTERIDFEEL 676
Cdd:cd14007 233 LQKDPSKRLSLEQV 246
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
577-676 3.29e-05

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 45.75  E-value: 3.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 577 RMAVVGpvTERW-APEQAgpvhenwqLAAPIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGPL 655
Cdd:cd06659 174 RKSLVG--TPYWmAPEVI--------SRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSPPPKLKNSHKA 243
                        90       100
                ....*....|....*....|....*
gi 21223155 656 RPV----VESLLRQDPTERIDFEEL 676
Cdd:cd06659 244 SPVlrdfLERMLVRDPQERATAQEL 268
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
607-676 4.93e-05

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 45.04  E-value: 4.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECgPLRPVVESLLRQ----DPTERIDFEEL 676
Cdd:cd14118 196 GKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPDDP-VVSEQLKDLILRmldkNPSERITLPEI 268
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
107-192 6.08e-05

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 44.93  E-value: 6.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVA---ARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCD 183
Cdd:cd08227  57 NHPNIVPYRATFIADNELWVVTSFMAygsAKDLICTHFMDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHILISV 136

                ....*....
gi 21223155 184 DGRVMLTGL 192
Cdd:cd08227 137 DGKVYLSGL 145
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
607-678 9.72e-05

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 44.13  E-value: 9.72e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAE----PPAFAEECgplRPVVESLLRQDPTERIDFEELSG 678
Cdd:cd05590 174 GPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDevvyPTWLSQDA---VDILKAFMTKNPTMRLGSLTLGG 246
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
606-678 9.92e-05

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 43.79  E-value: 9.92e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21223155 606 IGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCA----EPPAFAEECGPLRpvveSLLRQDPTERIDFEELSG 678
Cdd:cd14161 179 IGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSgayrEPTKPSDACGLIR----WLLMVNPERRATLEDVAS 251
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
108-190 1.19e-04

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 43.94  E-value: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRV 187
Cdd:cd06655  75 NPNIVNFLDSFLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSV 154

                ...
gi 21223155 188 MLT 190
Cdd:cd06655 155 KLT 157
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
107-196 1.25e-04

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 43.50  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGR 186
Cdd:cd06640  60 DSPYVTKYYGSYLKGTKLWIIMEYLGGGSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGD 139
                        90
                ....*....|
gi 21223155 187 VMLTGLAVGA 196
Cdd:cd06640 140 VKLADFGVAG 149
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
105-194 1.44e-04

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 43.14  E-value: 1.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 105 VPDHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQT----LTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVL 180
Cdd:cd13997  56 LGQHPNIVRYYSSWEEGGHLYIQMELCENGSLQDALEELSpiskLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIF 135
                        90
                ....*....|....*.
gi 21223155 181 VCDDGRVMLT--GLAV 194
Cdd:cd13997 136 ISNKGTCKIGdfGLAT 151
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
107-185 1.57e-04

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 43.08  E-value: 1.57e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYR-AAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:cd14095  56 KHPNIVQLIEEYDTDTELYLVMELVKGGDLFDAITSSTKFTERdASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHE 135
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
611-676 1.62e-04

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 43.08  E-value: 1.62e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 611 DLWALGALLFRAVQGHAPYPEESTAELVQIV----CAEPPAFAEECGPLRPVVESLLRQDPTERIDFEEL 676
Cdd:cd14202 191 DLWSIGTIIYQCLTGKAPFQASSPQDLRLFYeknkSLSPNIPRETSSHLRQLLLGLLQRNQKDRMDFDEF 260
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
603-676 1.70e-04

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 42.89  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 603 AAP--------IGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAE----PPAFAEECgplRPVVESLLRQDPTER 670
Cdd:cd14003 165 AAPevllgrkyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGkypiPSHLSPDA---RDLIRRMLVVDPSKR 241

                ....*.
gi 21223155 671 IDFEEL 676
Cdd:cd14003 242 ITIEEI 247
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
604-680 1.72e-04

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


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 43.15  E-value: 1.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 604 APIGPATDLWALGALLFRAVQGHAPYPEESTAELV--QIVCAE----PPAFAEECGPLRPVVESLLRQDPTERIDFEEL- 676
Cdd:cd14084 191 EGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLkeQILSGKytfiPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEAl 270

                ....*
gi 21223155 677 -SGWL 680
Cdd:cd14084 271 eHPWL 275
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
107-196 2.04e-04

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


Pssm-ID: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 43.12  E-value: 2.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGR 186
Cdd:cd06642  60 DSPYITRYYGSYLKGTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGD 139
                        90
                ....*....|
gi 21223155 187 VMLTGLAVGA 196
Cdd:cd06642 140 VKLADFGVAG 149
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
607-671 2.06e-04

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 43.37  E-value: 2.06e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEE----STAELVQIVCAEPPAFAEECGPL-RPVVESLLRQDPTERI 671
Cdd:cd05614 185 GKAVDWWSLGILMFELLTGASPFTLEgeknTQSEVSRRILKCDPPFPSFIGPVaRDLLQKLLCKDPKKRL 254
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
113-190 2.13e-04

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870  Cd Length: 136  Bit Score: 40.89  E-value: 2.13e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21223155 113 QVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRVMLT 190
Cdd:cd13968  56 KVLVTEDVDGPNILLMELVKGGTLIAYTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLI 133
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
609-671 2.45e-04

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 42.68  E-value: 2.45e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21223155 609 ATDLWALGALLFRAVQGHAPYP----EESTAELVQIVCAEPPAFAEECGPL-RPVVESLLRQDPTERI 671
Cdd:cd05613 188 AVDWWSLGVLMYELLTGASPFTvdgeKNSQAEISRRILKSEPPYPQEMSALaKDIIQRLLMKDPKKRL 255
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
63-194 2.47e-04

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 42.73  E-value: 2.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  63 GFTARdggvRHSGRRPTAAGGPRSPADPVVRRAVEAAQAaaavpDHP---RLDQVFDVFAEGgSLWIASELVAARPLAAL 139
Cdd:cd14118  37 GFFRR----PPPRRKPGALGKPLDPLDRVYREIAILKKL-----DHPnvvKLVEVLDDPNED-NLYMVFELVDKGAVMEV 106
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21223155 140 LTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRVMLTGLAV 194
Cdd:cd14118 107 PTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGV 161
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
108-193 2.59e-04

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 42.49  E-value: 2.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLT-----EQTLTPYRAAEVASDVLLALRVLH-SYGWVHRNITARTVLV 181
Cdd:cd08528  68 HPNIVRYYKTFLENDRLYIVMELIEGAPLGEHFSslkekNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIML 147
                        90
                ....*....|....
gi 21223155 182 CDDGRVMLT--GLA 193
Cdd:cd08528 148 GEDDKVTITdfGLA 161
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
590-670 2.61e-04

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 42.64  E-value: 2.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 590 PEQAGPvhENWQlAAPIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEE--CG---PLRPVVESLLR 664
Cdd:cd14115 155 PEFAAP--EVIQ-GTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfGDvsqAARDFINVILQ 231

                ....*.
gi 21223155 665 QDPTER 670
Cdd:cd14115 232 EDPRRR 237
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
602-676 2.68e-04

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 42.94  E-value: 2.68e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21223155 602 LAAPIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGPL----RPVVESLLRQDPTERIDFEEL 676
Cdd:cd05610 230 LGKPHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPEGEEELsvnaQNAIEILLTMDPTKRAGLKEL 308
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
607-680 2.70e-04

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 42.42  E-value: 2.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELVQIV---------CAEPPAfaeecgplRPVVESLLRQDPTERIDFEE-- 675
Cdd:cd13976 166 GKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIrrgqfaipeTLSPRA--------RCLIRSLLRREPSERLTAEDil 237

                ....*
gi 21223155 676 LSGWL 680
Cdd:cd13976 238 LHPWL 242
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
108-190 2.89e-04

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 42.56  E-value: 2.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTE--QTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:cd05113  58 HEKLVQLYGVCTKQRPIYIVTEYMSNGCLLNYLREhgKRFQPSQLLEMCKDVCEGMAYLESKQFIHRDLAARNCLVDDQG 137

                ....*
gi 21223155 186 RVMLT 190
Cdd:cd05113 138 CVKVS 142
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
108-184 3.11e-04

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 42.42  E-value: 3.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLT---EQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd05148  61 HKHLISLFAVCSVGEPVYIITELMEKGSLLAFLRspeGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGED 140
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
107-190 3.52e-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 [Multi-domain]  Cd Length: 259  Bit Score: 41.97  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQ-TLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVC--- 182
Cdd:cd14083  59 KHPNIVQLLDIYESKSHLYLVMELVTGGELFDRIVEKgSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYspd 138

                ....*...
gi 21223155 183 DDGRVMLT 190
Cdd:cd14083 139 EDSKIMIS 146
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
108-198 3.67e-04

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


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 41.94  E-value: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTL-TPYRAAEVASDVLLALRVLHSYGWVHRNITARTVL---VCD 183
Cdd:cd14167  60 HPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFyTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDE 139
                        90
                ....*....|....*
gi 21223155 184 DGRVMLTGLAVGAAE 198
Cdd:cd14167 140 DSKIMISDFGLSKIE 154
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
611-677 3.74e-04

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


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 42.13  E-value: 3.74e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21223155 611 DLWALGALLFRAVQGHAPYPEESTA----ELVQIVCAEPPAFAEECGP-LRPVVESLLRQDPTERIDFEELS 677
Cdd:cd05577 177 DWFALGCMLYEMIAGRSPFRQRKEKvdkeELKRRTLEMAVEYPDSFSPeARSLCEGLLQKDPERRLGCRGGS 248
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
590-676 4.20e-04

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 41.99  E-value: 4.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 590 PEQAGPvhENWQlAAPIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVC-----AEPPAFAEEcgpLRPVVESLLR 664
Cdd:cd08530 165 PLYAAP--EVWK-GRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCrgkfpPIPPVYSQD---LQQIIRSLLQ 238
                        90
                ....*....|..
gi 21223155 665 QDPTERIDFEEL 676
Cdd:cd08530 239 VNPKKRPSCDKL 250
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
572-676 4.34e-04

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


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 41.81  E-value: 4.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 572 RARQTRMAVVGpvTERW-APEQAgpvhenwqLAAPIGPATDLWALGALLFRAVQGHAPYPEESTAE-LVQIVCAEPPAF- 648
Cdd:cd06614 149 KEKSKRNSVVG--TPYWmAPEVI--------KRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRaLFLITTKGIPPLk 218
                        90       100       110
                ....*....|....*....|....*....|
gi 21223155 649 -AEECGP-LRPVVESLLRQDPTERIDFEEL 676
Cdd:cd06614 219 nPEKWSPeFKDFLNKCLVKDPEKRPSAEEL 248
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
107-196 4.49e-04

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


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 41.98  E-value: 4.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGR 186
Cdd:cd06641  60 DSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGE 139
                        90
                ....*....|
gi 21223155 187 VMLTGLAVGA 196
Cdd:cd06641 140 VKLADFGVAG 149
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
107-196 4.99e-04

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 41.52  E-value: 4.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTE-QTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:cd06613  55 RHPNIVAYFGSYLRRDKLWIVMEYCGGGSLQDIYQVtGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDG 134
                        90
                ....*....|.
gi 21223155 186 RVMLTGLAVGA 196
Cdd:cd06613 135 DVKLADFGVSA 145
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
609-671 4.99e-04

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 41.79  E-value: 4.99e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21223155 609 ATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAE-ECGPLRPVVESLLRQDPTERI 671
Cdd:cd05585 174 AVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDgFDRDAKDLLIGLLNRDPTKRL 237
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
606-676 5.59e-04

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 41.43  E-value: 5.59e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21223155 606 IGPATDLWALGALLFRAVQGHAPYPEESTAelVQIVCAEP-PAFAEECGPLRP-----VVESLLRQDPTERIDFEEL 676
Cdd:cd14131 191 IGRPSDVWSLGCILYQMVYGKTPFQHITNP--IAKLQAIIdPNHEIEFPDIPNpdlidVMKRCLQRDPKKRPSIPEL 265
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
611-675 6.60e-04

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


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 41.20  E-value: 6.60e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 611 DLWALGALLFRAVQGHAPY----PE------ESTAELVqivcaepPAFAEECGP-LRPVVESLLRQDPTERIDFEE 675
Cdd:cd14120 182 DLWSIGTIVYQCLTGKAPFqaqtPQelkafyEKNANLR-------PNIPSGTSPaLKDLLLGLLKRNPKDRIDFED 250
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
71-194 7.37e-04

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 41.10  E-value: 7.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  71 VRHSG--RRP------TAAGGPRSPADPVVRraVEAAQAAAAVPDHP---RLDQVFDVFAEGgSLWIASELVAARPLAAL 139
Cdd:cd14199  41 MRQAGfpRRPpprgarAAPEGCTQPRGPIER--VYQEIAILKKLDHPnvvKLVEVLDDPSED-HLYMVFELVKQGPVMEV 117
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21223155 140 LTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRVMLTGLAV 194
Cdd:cd14199 118 PTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGV 172
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
76-194 7.73e-04

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 41.09  E-value: 7.73e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  76 RRP------TAAGGPRSPADPVVRraVEAAQAAAAVPDH---PRLDQVFDVFAEGgSLWIASELVAARPLAALLTEQTLT 146
Cdd:cd14200  46 RRPpprgskAAQGEQAKPLAPLER--VYQEIAILKKLDHvniVKLIEVLDDPAED-NLYMVFDLLRKGPVMEVPSDKPFS 122
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 21223155 147 PYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRVMLTGLAV 194
Cdd:cd14200 123 EDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGV 170
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
606-676 8.52e-04

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


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 41.00  E-value: 8.52e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21223155 606 IGPATDLWALGALLFRAVQGHAPYPEESTAELVQ--IVCAEPPAFAEECGP-LRPVVESLLRQDPTERIDFEEL 676
Cdd:cd14008 188 SGKAADIWALGVTLYCLVFGRLPFNGDNILELYEaiQNQNDEFPIPPELSPeLKDLLRRMLEKDPEKRITLKEI 261
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
607-676 9.13e-04

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 40.80  E-value: 9.13e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGP-LRPVVESLLRQDPTERIDFEEL 676
Cdd:cd14023 166 GKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPkARCLIRSLLRREPSERLTAPEI 236
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
605-671 9.51e-04

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 41.14  E-value: 9.51e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223155 605 PIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIV----CAEPPAFAEECgplRPVVESLLRQDPTERI 671
Cdd:cd05616 177 PYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSImehnVAYPKSMSKEA---VAICKGLMTKHPGKRL 244
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
605-676 1.09e-03

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 40.50  E-value: 1.09e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 605 PIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGPLRPVVESLLRQ----DPTERIDFEEL 676
Cdd:cd06648 179 PYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEPPKLKNLHKVSPRLRSFLDRmlvrDPAQRATAAEL 254
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
107-183 1.10e-03

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


Pssm-ID: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 40.39  E-value: 1.10e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21223155 107 DHPRLDQVFDVFAEGGSLWI-ASELVAARPLAALLTEQT-LTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCD 183
Cdd:cd13987  48 VHPHIIKTYDVAFETEDYYVfAQEYAPYGDLFSIIPPQVgLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFD 126
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
607-671 1.15e-03

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 40.78  E-value: 1.15e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGP-LRPVVESLLRQDPTERI 671
Cdd:cd05594 204 GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPeAKSLLSGLLKKDPKQRL 269
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
108-196 1.15e-03

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 40.41  E-value: 1.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALL-TEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGR 186
Cdd:cd06645  67 HSNIVAYFGSYLRRDKLWICMEFCGGGSLQDIYhVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGH 146
                        90
                ....*....|
gi 21223155 187 VMLTGLAVGA 196
Cdd:cd06645 147 VKLADFGVSA 156
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
108-193 1.27e-03

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 40.41  E-value: 1.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVA---------ARPLAALLTEQTLtpyraaEVASDVLLALRVLHSYGWVHRNITART 178
Cdd:cd05039  59 HPNLVQLLGVVLEGNGLYIVTEYMAkgslvdylrSRGRAVITRKDQL------GFALDVCEGMEYLESKKFVHRDLAARN 132
                        90
                ....*....|....*..
gi 21223155 179 VLVCDDG--RVMLTGLA 193
Cdd:cd05039 133 VLVSEDNvaKVSDFGLA 149
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
610-683 1.63e-03

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 40.22  E-value: 1.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 610 TDLWALGALLFRAVQGHAPYPEEST----AELVQIVCAEPPAFAEECGP-LRPVVESLLRQDPTERIDFEELSG--WLRS 682
Cdd:cd06622 188 SDVWSLGLSILEMALGRYPYPPETYanifAQLSAIVDGDPPTLPSGYSDdAQDFVAKCLNKIPNRRPTYAQLLEhpWLVK 267

                .
gi 21223155 683 L 683
Cdd:cd06622 268 Y 268
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
147-189 1.64e-03

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 40.13  E-value: 1.64e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 21223155 147 PYRAAEVA---SDVLLALRVLHSYGWVHRNITARTVLVCDDGRVML 189
Cdd:cd06607  97 PLQEVEIAaicHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKL 142
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
608-676 1.73e-03

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


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 39.83  E-value: 1.73e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21223155 608 PATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAE-----PPAFAEEcgpLRPVVESLLRQDPTERIDFEEL 676
Cdd:cd08217 189 EKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGkfpriPSRYSSE---LNEVIKSMLNVDPDKRPSVEEL 259
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
575-651 1.82e-03

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


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 39.84  E-value: 1.82e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21223155 575 QTRMAVVGPvtERWAPEqagpVHENwqlaAPIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEE 651
Cdd:cd14104 154 KFRLQYTSA--EFYAPE----VHQH----ESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDE 220
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
106-196 1.99e-03

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 39.98  E-value: 1.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 106 PDHPRLDQVFDVFAE-----GGSLWIASELVAARPLAALLTE-----QTLTPYRAAEVASDVLLALRVLHSYGWVHRNIT 175
Cdd:cd06639  76 PNHPNVVKFYGMFYKadqyvGGQLWLVLELCNGGSVTELVKGllkcgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVK 155
                        90       100
                ....*....|....*....|.
gi 21223155 176 ARTVLVCDDGRVMLTGLAVGA 196
Cdd:cd06639 156 GNNILLTTEGGVKLVDFGVSA 176
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
108-184 2.03e-03

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 40.01  E-value: 2.03e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELV-AARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd14175  54 HPNIITLKDVYDDGKHVYLVTELMrGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDE 131
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
108-193 2.04e-03

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 39.77  E-value: 2.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTP-YRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGR 186
Cdd:cd14098  60 HPGIVRLIDWYEDDQHIYLVMEYVEGGDLMDFIMAWGAIPeQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDP 139
                        90
                ....*....|.
gi 21223155 187 VMLT----GLA 193
Cdd:cd14098 140 VIVKisdfGLA 150
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
108-193 2.04e-03

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 39.69  E-value: 2.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLteQTLTPYRAAEVAS---DVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd06632  61 HPNIVQYYGTEREEDNLYIFLEYVPGGSIHKLL--QRYGAFEEPVIRLytrQILSGLAYLHSRNTVHRDIKGANILVDTN 138
                        90
                ....*....|.
gi 21223155 185 GRVMLT--GLA 193
Cdd:cd06632 139 GVVKLAdfGMA 149
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
107-189 2.14e-03

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 39.56  E-value: 2.14e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAAL--LTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDD 184
Cdd:cd06612  56 DSPYIVKYYGSYFKNTDLWIVMEYCGAGSVSDImkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEE 135

                ....*
gi 21223155 185 GRVML 189
Cdd:cd06612 136 GQAKL 140
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
607-670 2.44e-03

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 39.29  E-value: 2.44e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELV-QIVCA---EPPAFAEECGPLRpvveSLLRQDPTER 670
Cdd:cd14073 179 GPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVkQISSGdyrEPTQPSDASGLIR----WMLTVNPKRR 242
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
605-675 2.65e-03

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 39.49  E-value: 2.65e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 605 PIGPATDLWALGALLFRAVQGHAPYPEESTAELV-QIVCAE----PPAFAEECGPLRPVVESLLRQDPTERIDFEE 675
Cdd:cd14169 178 PYGKAVDVWAIGVISYILLCGYPPFYDENDSELFnQILKAEyefdSPYWDDISESAKDFIRHLLERDPEKRFTCEQ 253
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
611-671 2.76e-03

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 39.62  E-value: 2.76e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 611 DLWALGALLFRAVQGHAPYPEESTA----ELVQIVCAEPPAFAEECGP-LRPVVESLLRQDPTERI 671
Cdd:cd05630 183 DWWALGCLLYEMIAGQSPFQQRKKKikreEVERLVKEVPEEYSEKFSPqARSLCSMLLCKDPAERL 248
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
156-193 2.77e-03

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 39.43  E-value: 2.77e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 21223155 156 DVLLALRVLHSYGWVHRNITARTVLVCDDGRVMLT--GLA 193
Cdd:cd06606 107 QILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLAdfGCA 146
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
589-681 2.78e-03

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 39.24  E-value: 2.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 589 APEQAGPvHENWqlaaPIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPafAEECGP-LRPVVESLLRQDP 667
Cdd:cd13985 182 APEMIDL-YSKK----PIGEKADIWALGCLLYKLCFFKLPFDESSKLAIVAGKYSIPE--QPRYSPeLHDLIRHMLTPDP 254
                        90
                ....*....|....
gi 21223155 668 TERIDFEELSGWLR 681
Cdd:cd13985 255 AERPDIFQVINIIT 268
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
605-676 2.81e-03

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 39.61  E-value: 2.81e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21223155 605 PIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEE-CGPLRPVVESLLRQDPTERI----DFEEL 676
Cdd:cd05602 184 PYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNiTNSARHLLEGLLQKDRTKRLgakdDFTEI 260
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
108-187 3.45e-03

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 38.97  E-value: 3.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQ--TLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:cd05059  58 HPNLVQLYGVCTKQRPIFIVTEYMANGCLLNYLRERkgKLGTEWLLDMCSDVCEAMEYLESNGFIHRDLAARNCLVGEDN 137

                ..
gi 21223155 186 RV 187
Cdd:cd05059 138 VV 139
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
107-183 3.51e-03

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 38.94  E-value: 3.51e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21223155 107 DHPRLDQVFDVFAEGgSLWIASELVAARPLAALLT--EQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCD 183
Cdd:cd05056  65 DHPHIVKLIGVITEN-PVWIVMELAPLGELRSYLQvnKYSLDLASLILYSYQLSTALAYLESKRFVHRDIAARNVLVSS 142
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
607-676 3.95e-03

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


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 38.86  E-value: 3.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGP-LRPVVESLLRQDPTERIDFEEL 676
Cdd:cd14022 166 GKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPkAKCLIRSILRREPSERLTSQEI 236
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
118-193 4.29e-03

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


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 38.67  E-value: 4.29e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21223155 118 FAEGGSLwiASELVAARPLAALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGRVMLT--GLA 193
Cdd:cd00192  77 YMEGGDL--LDFLRKSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISdfGLS 152
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
607-673 4.33e-03

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


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 38.74  E-value: 4.33e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 607 GPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCA---EPPAFAEECGPLRPVVESLLRQDPTERIDF 673
Cdd:cd05579 186 GKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNgkiEWPEDPEVSDEAKDLISKLLTPDPEKRLGA 255
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
605-676 4.41e-03

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 38.85  E-value: 4.41e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 605 PIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAE-PPAF--AEECGP-LRPVVESLLRQDPTERIDFEEL 676
Cdd:cd06657 192 PYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNlPPKLknLHKVSPsLKGFLDRLLVRDPAQRATAAEL 267
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
605-675 4.53e-03

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 38.40  E-value: 4.53e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 605 PIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCA-----EPPAFAEECGPLRPVVESLLRQDPTERIDFEE 675
Cdd:cd14006 166 PVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISAcrvdfSEEYFSSVSQEAKDFIRKLLVKEPRKRPTAQE 241
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
609-676 4.92e-03

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 38.73  E-value: 4.92e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21223155 609 ATDLWALGALLFRAVQGHAPYP---EESTAELVQIVCAEPPAF--AEECGP-LRPVVESLLRQDPTERIDFEEL 676
Cdd:cd06623 180 AADIWSLGLTLLECALGKFPFLppgQPSFFELMQAICDGPPPSlpAEEFSPeFRDFISACLQKDPKKRPSAAEL 253
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
108-186 5.15e-03

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 38.77  E-value: 5.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPL-AALLTEQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGR 186
Cdd:cd14091  53 HPNIITLRDVYDDGNSVYLVTELLRGGELlDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESG 132
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
611-676 5.46e-03

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 38.39  E-value: 5.46e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21223155 611 DLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGP-LRPVVESLLRQDPTERIDFEEL 676
Cdd:cd14002 181 DLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPeFKSFLQGLLNKDPSKRLSWPDL 247
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
607-676 5.61e-03

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 38.37  E-value: 5.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21223155 607 GPATdLWALGALLFRAVQGHAPYPEEStaelvQIVCAE---PPAFAEECGPLrpvVESLLRQDPTERIDFEEL 676
Cdd:cd14005 186 RPAT-VWSLGILLYDMLCGDIPFENDE-----QILRGNvlfRPRLSKECCDL---ISRCLQFDPSKRPSLEQI 249
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
106-192 5.82e-03

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 38.24  E-value: 5.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 106 PDHPRL----DQVFDvFAEGGSLWIASELVAARPLAALLT--EQTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTV 179
Cdd:cd13975  55 PKHERIvslhGSVID-YSYGGGSSIAVLLIMERLHRDLYTgiKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNV 133
                        90
                ....*....|...
gi 21223155 180 LVCDDGRVMLTGL 192
Cdd:cd13975 134 LLDKKNRAKITDL 146
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
107-194 6.26e-03

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


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 37.97  E-value: 6.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLteQTLTPYRAAEVA---SDVLLALRVLHSYGWVHRNITARTVLVCD 183
Cdd:cd06627  57 NHPNIVKYIGSVKTKDSLYIILEYVENGSLASII--KKFGKFPESLVAvyiYQVLEGLAYLHEQGVIHRDIKGANILTTK 134
                        90
                ....*....|...
gi 21223155 184 DGRVMLT--GLAV 194
Cdd:cd06627 135 DGLVKLAdfGVAT 147
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
118-193 7.06e-03

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 37.88  E-value: 7.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 118 FAEGGSLW--IASELVaarplaalLTEQTLTPYrAAEVAsdvlLALRVLHSYGWVHRNITARTVLVCDDGRVMLT--GLA 193
Cdd:cd05123  74 YVPGGELFshLSKEGR--------FPEERARFY-AAEIV----LALEYLHSLGIIYRDLKPENILLDSDGHIKLTdfGLA 140
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
610-673 7.31e-03

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 38.14  E-value: 7.31e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 610 TDLWALGALLFRAVQ-GHAPYPEESTAELVQIVCA----EPPafaEEC-GPLRPVVESLLRQDPTERIDF 673
Cdd:cd05036 202 TDVWSFGVLLWEIFSlGYMPYPGKSNQEVMEFVTSggrmDPP---KNCpGPVYRIMTQCWQHIPEDRPNF 268
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
611-682 7.79e-03

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 37.84  E-value: 7.79e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21223155 611 DLWALGALLFRAVQGHAPYPEESTAELVQ-IVCAEPPAFAEE--CGPLRPVVESLLRQDPTERIDFEEL--SGWLRS 682
Cdd:cd06917 184 DIWSLGITTYEMATGNPPYSDVDALRAVMlIPKSKPPRLEGNgySPLLKEFVAACLDEEPKDRLSADELlkSKWIKQ 260
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
606-676 8.80e-03

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


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 37.66  E-value: 8.80e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21223155 606 IGPATDLWALGALLFRAVQGHAPY-PEESTAELVQI-VCAEPPAFAEECG---PLRPVVESLLRQDPTERIDFEEL 676
Cdd:cd13986 198 IDEKTDIWSLGCTLYALMYGESPFeRIFQKGDSLALaVLSGNYSFPDNSRyseELHQLVKSMLVVNPAERPSIDDL 273
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
109-186 9.11e-03

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


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 37.88  E-value: 9.11e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21223155 109 PRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQTLTPY-RAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDGR 186
Cdd:cd13991  58 PRVVPLYGAVREGPWVNIFMDLKEGGSLGQLIKEQGCLPEdRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGS 136
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
108-194 9.84e-03

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 37.79  E-value: 9.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155 108 HPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQT----LTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCD 183
Cdd:cd14052  62 HDNIVQLIDSWEYHGHLYIQTELCENGSLDVFLSELGllgrLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITF 141
                        90
                ....*....|...
gi 21223155 184 DGRVMLT--GLAV 194
Cdd:cd14052 142 EGTLKIGdfGMAT 154
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
107-193 6.52e-11

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 62.55  E-value: 6.52e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155    107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQ-TLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:smart00220  55 KHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKKRgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG 134
                           90
                   ....*....|
gi 21223155    186 RVMLT--GLA 193
Cdd:smart00220 135 HVKLAdfGLA 144
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
314-558 1.05e-10

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 64.24  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  314 RAALPGARPAPDGATQAGGPGTSGGRPGLAPGPGSSYDDDDgagRPPHGSAPGGARPGHGVEAAGGAPGARPGQGSGRAA 393
Cdd:PRK07764 585 EAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPA---APAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  394 FAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPGQitdpygvgttawhgatprtPGDPASSAARPTGDPAFPAP 473
Cdd:PRK07764 662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPA-------------------PAPAATPPAGQADDPAAQPP 722
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  474 RPAGEPAAGSG-PAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAADPEREGGPRPAAGWD 552
Cdd:PRK07764 723 QAAQGASAPSPaADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDEDRRDAE 802

                 ....*.
gi 21223155  553 DLAGRA 558
Cdd:PRK07764 803 EVAMEL 808
PHA03247 PHA03247
large tegument protein UL36; Provisional
261-583 3.09e-10

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 63.03  E-value: 3.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   261 PVPGTPVPGTAPAGLAPASLDAAADARAARAGAIAAYRAGARAAARIQEAQNGRAALPGARPAPDGATQAGGPGTSGGRP 340
Cdd:PHA03247 2622 HAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADP 2701
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   341 ------------------GLAPGPGSSYDDDDGAGRPPHGSAPGGARPGHGVEAAGGAPGARPGQGSGRAAFAAGSGQAP 402
Cdd:PHA03247 2702 ppppptpepaphalvsatPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR 2781
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   403 YAIGPDAASGAPWDEDSvgdPATSGAAVPPGQITDPYGVGTTAWHGATPRTPGDPASSAARPTGDPAFPAPRPAGEPAAG 482
Cdd:PHA03247 2782 RLTRPAVASLSESRESL---PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAP 2858
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   483 SGPAAGRALPGARPEDTAGSAVPWRETTAGPA-ARSRETASEAAAGPWRAAPPRAADPEREGGPRPAAGWDDLAGRAPGQ 561
Cdd:PHA03247 2859 GGDVRRRPPSRSPAAKPAAPARPPVRRLARPAvSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
                         330       340
                  ....*....|....*....|..
gi 21223155   562 RNPATALAAERARQTRMAVVGP 583
Cdd:PHA03247 2939 PQPPLAPTTDPAGAGEPSGAVP 2960
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
333-581 5.06e-10

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 61.82  E-value: 5.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  333 PGTSGGRPGLAPgpgssyddddgAGRPPHGSAPGGARPGHGVEAAGGAPGARPGQGSGRAAFAAGSGQAPYAIGPDAASG 412
Cdd:PRK12323 365 PGQSGGGAGPAT-----------AAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEAL 433
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  413 APWDEDSVGDPatsGAAVPPGQITDPYGVGTTAWHGATPRTPGDPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALP 492
Cdd:PRK12323 434 AAARQASARGP---GGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPA 510
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  493 GARPEDTAGSAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAADPEREGGPRP------------AAGWDDLAGRApg 560
Cdd:PRK12323 511 PAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPprasasglpdmfDGDWPALAARL-- 588
                        250       260
                 ....*....|....*....|.
gi 21223155  561 qrnPATALAAERARQTRMAVV 581
Cdd:PRK12323 589 ---PVRGLAQQLARQSELAGV 606
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
384-596 6.71e-10

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 61.43  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  384 RPGQGSGRAAFAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPGQITDPYGVGTTAWHGATPRTPGDPASSAAR 463
Cdd:PRK12323 364 RPGQSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARG 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  464 PTGDPAfPAPRPAGEPAAGSGPAAgralPGARPEDTAGSAVPWRETTAGPAARSREtaseaAAGPWRAAPPRAADPEREG 543
Cdd:PRK12323 444 PGGAPA-PAPAPAAAPAAAARPAA----AGPRPVAAAAAAAPARAAPAAAPAPADD-----DPPPWEELPPEFASPAPAQ 513
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 21223155  544 GPRPAAGWDDLAGRAPGQRNPATALAAerARQTRMAVVGPVTERWAPEQAGPV 596
Cdd:PRK12323 514 PDAAPAGWVAESIPDPATADPDDAFET--LAPAPAAAPAPRAAAATEPVVAPR 564
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
362-625 7.30e-10

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 61.40  E-value: 7.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  362 GSAPGGARPghgVEAAGGAPGARPGQGSGRAAFAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPGQITDPyGV 441
Cdd:PRK07003 365 GGAPGGGVP---ARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADR-GD 440
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  442 GTTAWHGATPRTPGDPASSAARPTGDPAFPAPRPAGEPA-AGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRET 520
Cdd:PRK07003 441 DAADGDAPVPAKANARASADSRCDERDAQPPADSGSASApASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASRED 520
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  521 ASEAAAGP----WRAAPPRAADPEREGGprPAAGWDDLagrapgqRNPATALAAERARQTRmAVVGPVTERWAPEQAGPV 596
Cdd:PRK07003 521 APAAAAPPapeaRPPTPAAAAPAARAGG--AAAALDVL-------RNAGMRVSSDRGARAA-AAAKPAAAPAAAPKPAAP 590
                        250       260
                 ....*....|....*....|....*....
gi 21223155  597 HENWQLAAPIGPATDLWALGALLFRAVQG 625
Cdd:PRK07003 591 RVAVQVPTPRARAATGDAPPNGAARAEQA 619
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
261-595 1.18e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 60.77  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  261 PVPGTPVPGTAPAGLAPASLDAAADARAARAGAIAAYRAGARAAARIQEAQNGRAALPGARPAPDGATQAGGPGTSGGRP 340
Cdd:PRK07764 401 AAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAP 480
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  341 glAPGPGSSYDDDDGAGRPPHGSAPGGARPGHGVE-----------------AAGGAPGARPGQGSG------------R 391
Cdd:PRK07764 481 --APAPPAAPAPAAAPAAPAAPAAPAGADDAATLRerwpeilaavpkrsrktWAILLPEATVLGVRGdtlvlgfstgglA 558
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  392 AAFAAGSG----------------QAPYAIGPDAASGAPWdedsvgDPATSGAAVPPGQITDPYGVGTTAWHGATPRTPG 455
Cdd:PRK07764 559 RRFASPGNaevlvtalaeelggdwQVEAVVGPAPGAAGGE------GPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGA 632
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  456 DPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGPWRAAPPR 535
Cdd:PRK07764 633 AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAG 712
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  536 AADPEREGGPRPAAGWDDLAGRAPGQRNPATALAAERARQTRMAVVGPVTERWAPEQAGP 595
Cdd:PRK07764 713 QADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAA 772
Sporozoite_P67 pfam05642
Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. ...
318-494 1.54e-08

Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. A stage specific surface antigen of Theileria parva, p67, is the basis for the development of an anti-sporozoite vaccine for the control of East Coast fever (ECF) in cattle. The antigen has been shown to contain five distinct linear peptide sequences recognized by sporozoite-neutralizing murine monoclonal antibodies.


Pssm-ID: 253298 [Multi-domain]  Cd Length: 727  Bit Score: 57.38  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   318 PGARPAPDGATQAGGPGTSGGRPGLAPGpGSSYDDDDGAGRPPHGSAPGGARPGHGVEAAGGApGARPGQGSGRAAFAAG 397
Cdd:pfam05642 144 PGVSTSSGSTTSGTDLNTKQSQTGLGAS-GSHAQQDPAVSQSGVVGVPGLGVPGVGVPGGGGA-GALPGVGVGRAGVSPG 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   398 SGQAPYAIGPDA---ASGAPWDEDSVGDPAT--SGAAVPPGQITDPYGVGTTAWHGATPRTPGD-----PASSAARPTGD 467
Cdd:pfam05642 222 VGVGGLGGVPGVgilASNTSREGQTQDDQERdgDGRVIEPGVGLPGVRVGDSTSSPSTTRPSGStttttPASSGPSAPGG 301
                         170       180
                  ....*....|....*....|....*....
gi 21223155   468 PAfPAPRPAGEPAAGS--GPAAGRALPGA 494
Cdd:pfam05642 302 PG-SSSRNAVTRSTDSisGPIPSPGAPRA 329
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
372-573 2.32e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 56.53  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  372 HGVEAAGGAPGARPGQGSGRAAFAAGSGQAPYAIGPDAASGAPwDEDSVGDPATSGAAVPPGQITDPYGVGTTAWHGATP 451
Cdd:PRK07764 582 WQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAP-AAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVP 660
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  452 RTPGDPASSAARPTGD-PAFPAPRPAGE-PAAGSGPAAGRALPGARPEDTAGSAV-PWRETTAGPAARSRETASEAAAGP 528
Cdd:PRK07764 661 DASDGGDGWPAKAGGAaPAAPPPAPAPAaPAAPAGAAPAQPAPAPAATPPAGQADdPAAQPPQAAQGASAPSPAADDPVP 740
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 21223155  529 WRAAPPRAADPEREGGPRPAAGWDDLAGRAPGQRNPATALAAERA 573
Cdd:PRK07764 741 LPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
Pkinase pfam00069
Protein kinase domain;
107-193 4.35e-08

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 54.14  E-value: 4.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTEQT-LTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLVCDDG 185
Cdd:pfam00069  56 NHPNIVRLYDVFEDKDHLYLVLEYVEGGSLFDLLSEKGaFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDG 135
                          90
                  ....*....|
gi 21223155   186 RVMLT--GLA 193
Cdd:pfam00069 136 NLKITdfGLA 145
PHA03247 PHA03247
large tegument protein UL36; Provisional
211-595 1.34e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   211 PDGEPDGAPERDAVSGAGGGVPRAGVFGPGDADPEAARRAAIEARGVGGL-PVPGTPVPGTAPAGLAPASLDAAADARAA 289
Cdd:PHA03247 2556 PPAAPPAAPDRSVPPPRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRgDPRGPAPPSPLPPDTHAPDPPPPSPSPAA 2635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   290 RAGAIAAYRAGARAAARIQEAQNGRAALPGARPAPDGATQAGGPGTSGGRPglapgpgssyddddgAGRPPHGSAPGGAR 369
Cdd:PHA03247 2636 NEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRR---------------AARPTVGSLTSLAD 2700
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   370 PghgvEAAGGAPGARPgqgsgraafAAGSGQAPYAIGPDAASGAPwdedsvgdPATSGAAVPPGQITDPYGVGTTAWHGA 449
Cdd:PHA03247 2701 P----PPPPPTPEPAP---------HALVSATPLPPGPAAARQAS--------PALPAAPAPPAVPAGPATPGGPARPAR 2759
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   450 TPRTPGDPASSAAR-PTGDPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGP 528
Cdd:PHA03247 2760 PPTTAGPPAPAPPAaPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAP 2839
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21223155   529 WRAAPPRAADPEREGGPRPAAgwdDLAGRAPGQRNPATALAAERARQTRMA--VVGPVTERWAPEQAGP 595
Cdd:PHA03247 2840 PPPPGPPPPSLPLGGSVAPGG---DVRRRPPSRSPAAKPAAPARPPVRRLArpAVSRSTESFALPPDQP 2905
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
309-594 2.45e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 53.64  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   309 EAQNGRAALPGARPAPDGATQAGGPGTSGGRPGLAPGPGSSYDDDDGAGRPPHGSAPGGARPGHGVEAAGGAPGARPGQG 388
Cdd:PHA03307  137 MLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISAS 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   389 SGRAAFAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPGQITDPYGVGTTAWHGATPRTPGDPASSAARPTGDP 468
Cdd:PHA03307  217 ASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSP 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   469 AfPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSavpwRETTAGPAARSRETASEAAAGPWRAAPPRAADPEREGGPRPA 548
Cdd:PHA03307  297 S-PSPSSPGSGPAPSSPRASSSSSSSRESSSSST----SSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRP 371
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 21223155   549 agwddlagrAPGQRNPATALAAERARQTRMAVVGPVTERWAPEQAG 594
Cdd:PHA03307  372 ---------SRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
380-574 6.99e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 51.77  E-value: 6.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  380 APGARPGQGSGRAAFAAGSGQAPyaiGPDAASGAPWDEDSVGDPATSGAAVPPGQitdpygvgttawHGATPRTPGDPAS 459
Cdd:PRK07003 361 AVTGGGAPGGGVPARVAGAVPAP---GARAAAAVGASAVPAVTAVTGAAGAALAP------------KAAAAAAATRAEA 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  460 SAARPT-GDPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAAD 538
Cdd:PRK07003 426 PPAAPApPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPA 505
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 21223155  539 PEREGGPRPAAGWDD----LAGRAPGQRNPATALAAERAR 574
Cdd:PRK07003 506 AVPDARAPAAASREDapaaAAPPAPEARPPTPAAAAPAAR 545
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
256-534 8.65e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 51.77  E-value: 8.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  256 GVGGLPVPGTP--VPGTAPA-GLAPASLDAAADARAARAGAIAAYRAGARAAARIQEAQngRAALPGARPAPDGATQAGG 332
Cdd:PRK07003 363 TGGGAPGGGVParVAGAVPApGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAAT--RAEAPPAAPAPPATADRGD 440
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  333 PGTSGGRPGLAPGPGSSYDDddgAGRPPHGSAPgGARPGHGVEAAGGAPGARPGQGSGRAAFAAGSGQAPYAIGPDAASG 412
Cdd:PRK07003 441 DAADGDAPVPAKANARASAD---SRCDERDAQP-PADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAA 516
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  413 APWDEDSVGDPATSGAAVP-PGQITDPYGVGTTAWHGATPRTPGDPASSaarPTGDPAFPAPRPAGEPAAGSGPAAGRAl 491
Cdd:PRK07003 517 SREDAPAAAAPPAPEARPPtPAAAAPAARAGGAAAALDVLRNAGMRVSS---DRGARAAAAAKPAAAPAAAPKPAAPRV- 592
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 21223155  492 pgARPEDTAGSAVPWRETTAGPAARSRETA-SEAAAGPWRAAPP 534
Cdd:PRK07003 593 --AVQVPTPRARAATGDAPPNGAARAEQAAeSRGAPPPWEDIPP 634
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
384-588 8.75e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 51.25  E-value: 8.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  384 RPGQGSGRAAFAAGSGQAPYAIGPDAASGAPwdedsvgDPATSGAAVPPgqitdpygvgttawhgatprtpgdPASSAAR 463
Cdd:PRK14951 365 KPAAAAEAAAPAEKKTPARPEAAAPAAAPVA-------QAAAAPAPAAA------------------------PAAAASA 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  464 PTGDPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAADPEREG 543
Cdd:PRK14951 414 PAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVALAPAPPAQAAPETVAIPVRVAPEPAVASAAPAPAAAPAAARLTPTEE 493
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 21223155  544 GPRPAAGWDDLAgrapgQRNPATALAAERARQTRMavVGPVTERW 588
Cdd:PRK14951 494 GDVWHATVQQLA-----AAEAITALARELALQSEL--VARDGDQW 531
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
589-676 6.33e-06

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 47.52  E-value: 6.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155    589 APEQAgpvhenwqLAAPIGPATDLWALGALLFRAVQGHAPYPEEST-AELVQIVCAEPPAFAEECGPLRP----VVESLL 663
Cdd:smart00220 164 APEVL--------LGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPEWDISPeakdLIRKLL 235
                           90
                   ....*....|...
gi 21223155    664 RQDPTERIDFEEL 676
Cdd:smart00220 236 VKDPEKRLTAEEA 248
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
310-490 6.69e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 48.72  E-value: 6.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  310 AQNGRAALPGARPAPDGATQAGGPGTSGGRPGLAPGPGSSYDDDDGAGRPPHGSAPGGARPGHGVEAAGGAPGARPGQGS 389
Cdd:PRK12323 389 AAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAG 468
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  390 GRAAfAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPGQITDPYGVGTTAWHGATPRTPGDPASSAARPTGDPA 469
Cdd:PRK12323 469 PRPV-AAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDPATADPDDAFETLAPAPAA 547
                        170       180
                 ....*....|....*....|.
gi 21223155  470 FPAPRPAGEPAAGSGPAAGRA 490
Cdd:PRK12323 548 APAPRAAAATEPVVAPRPPRA 568
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
355-484 7.62e-06

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 48.52  E-value: 7.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  355 GAGRPPHGSAPGGarPGHGVEAAGGAPGARPGQGSGRAAFAAGSGQAPYAIGPDAASG--APWDEDSVGDPATSGAAVPP 432
Cdd:PRK14959 376 GGASAPSGSAAEG--PASGGAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAPSprVPWDDAPPAPPRSGIPPRPA 453
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 21223155  433 GQItdpygvgttawhGATPRTPGDPASSA----ARPT-GDPAFPAPRPAGEPAAGSG 484
Cdd:PRK14959 454 PRM------------PEASPVPGAPDSVAsasdAPPTlGDPSDTAEHTPSGPRTWDG 498
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
190-579 8.99e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 48.44  E-value: 8.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  190 TGLAVGAAEEALCGYDPVPPPPDGEPDGAPERDAVSGAGGGVPRAGVFGPGDADPEAARRAAIEArgvgglPVPGTPVPG 269
Cdd:PRK07764 370 DERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPA------PAPAPAPPS 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  270 TAPAGLAPASLDAAADARAARAGAIAAYRAGARAAARIQEAQNGRAALPGARPAPDGATQAGGPGTSGGRP------GLA 343
Cdd:PRK07764 444 PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATLRErwpeilAAV 523
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  344 PG----------PGSSYDDDDGA----GRPPHGSAPGGARPGH----------------GVEAAGGAPGARPGQGSGRAA 393
Cdd:PRK07764 524 PKrsrktwaillPEATVLGVRGDtlvlGFSTGGLARRFASPGNaevlvtalaeelggdwQVEAVVGPAPGAAGGEGPPAP 603
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  394 FAAGSGQAPYAigPDAASGAPWDEDSVGDPATSGAAVPPGQITDPYGVGTTAWHGATPRTPGDPASSAARPTGDPAFPAP 473
Cdd:PRK07764 604 ASSGPPEEAAR--PAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAP 681
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  474 RPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAADPEREGGPRPAAGWDD 553
Cdd:PRK07764 682 PPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPP 761
                        410       420
                 ....*....|....*....|....*.
gi 21223155  554 LAGRAPGQRNPATALAAERARQTRMA 579
Cdd:PRK07764 762 PAPAPAAAPAAAPPPSPPSEEEEMAE 787
Pkinase pfam00069
Protein kinase domain;
605-676 9.59e-06

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 46.82  E-value: 9.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21223155   605 PIGPATDLWALGALLFRAVQGHAPYPEESTAELVQIVCAE-------PPAFAEECgplRPVVESLLRQDPTERIDFEEL 676
Cdd:pfam00069 173 PYGPKVDVWSLGCILYELLTGKPPFPGINGDTLYELIIDQldlssprPSSISEEA---KDLLKKLLKKDPSKRLTATQA 248
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
218-506 1.04e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 47.92  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  218 APERDAVSGAGGGVPRA---GVFGPGDADPEAARRAAIEARGvgglPVPGTPVPGTAPAGLAPAsldaaadaRAARAGAI 294
Cdd:PRK07003 359 EPAVTGGGAPGGGVPARvagAVPAPGARAAAAVGASAVPAVT----AVTGAAGAALAPKAAAAA--------AATRAEAP 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  295 AAYRAGARAAARIQEAQNGRAALPGARPAPdgATQAGGPGTSGGRPGLAPGPGSSyddddgagrpPHGSAPGGARPGHGV 374
Cdd:PRK07003 427 PAAPAPPATADRGDDAADGDAPVPAKANAR--ASADSRCDERDAQPPADSGSASA----------PASDAPPDAAFEPAP 494
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  375 EAAGGAPGARPGQGSGRAAFAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPGQITDPYGVGTTAWHGatpRTP 454
Cdd:PRK07003 495 RAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARAGGAAAALDVLRNAGMRVSSDRG---ARA 571
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 21223155  455 GDPASSAARPTGDPAFPAPRPA------GEPAAGSGPAAGRALPGARPEDTAGSAVPW 506
Cdd:PRK07003 572 AAAAKPAAAPAAAPKPAAPRVAvqvptpRARAATGDAPPNGAARAEQAAESRGAPPPW 629
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
215-534 1.18e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 47.86  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   215 PDGAPERDAVSGAGGGVPRAGVFGPGD-----ADPEAARRAAIEARGVGGLPVPGTPVPGTAPAGLAPASLDAAADARAA 289
Cdd:PHA03307  122 PPASPPPSPAPDLSEMLRPVGSPGPPPaasppAAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAA 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   290 RAGAIAAYRAGARAAARIQEAQNGRAALPGARPAPDGATQAGGPGTSGGRPGLAPGPGSSYDDDDGAGRPPHGSAPGGAR 369
Cdd:PHA03307  202 ASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSR 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   370 PGHGVEAAG-GAPGARPGQGSGRAAFAAGSGQAPYAIGPDAASGApwDEDSVGDPATSGAAVPPGQITDPygvgttawHG 448
Cdd:PHA03307  282 PGPASSSSSpRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSS--SSTSSSSESSRGAAVSPGPSPSR--------SP 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   449 ATPRTPGDPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALPG-ARPEDTAGSavpwreTTAGPAARSRETASEAAAG 527
Cdd:PHA03307  352 SPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGrARRRDATGR------FPAGRPRPSPLDAGAASGA 425

                  ....*..
gi 21223155   528 PWRAAPP 534
Cdd:PHA03307  426 FYARYPL 432
PHA03247 PHA03247
large tegument protein UL36; Provisional
357-567 1.58e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   357 GRPPHGSAPGGARPghgvEAAGGAPGARPGQGSGRAAFAAGSGQAPyAIGPDAASGAP-------W-------DEDSVGD 422
Cdd:PHA03247 2476 GAPVYRRPAEARFP----FAAGAAPDPGGGGPPDPDAPPAPSRLAP-AILPDEPVGEPvhprmltWirgleelASDDAGD 2550
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   423 PATSGAAVPPGQITD-----------PYGVGTTAW--------HGATPRTPGDPASSAARPTGDPAFPAPRPAGEPAAGS 483
Cdd:PHA03247 2551 PPPPLPPAAPPAAPDrsvppprpaprPSEPAVTSRarrpdappQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPS 2630
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   484 GPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAgPWRAAPPRAadPEREGGPRPAAGWDDLAGRAPGQRN 563
Cdd:PHA03247 2631 PSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRA-AQASSPPQR--PRRRAARPTVGSLTSLADPPPPPPT 2707

                  ....
gi 21223155   564 PATA 567
Cdd:PHA03247 2708 PEPA 2711
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
369-513 2.24e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 46.98  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  369 RPGHGVEAAGGApgARPGQGSGraafAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPgqitdpygvgttawhg 448
Cdd:PRK14959 373 PSGGGASAPSGS--AAEGPASG----GAATIPTPGTQGPQGTAPAAGMTPSSAAPATPAPSAAP---------------- 430
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21223155  449 aTPRTPGDPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAvPWRETTAGP 513
Cdd:PRK14959 431 -SPRVPWDDAPPAPPRSGIPPRPAPRMPEASPVPGAPDSVASASDAPPTLGDPSD-TAEHTPSGP 493
PRK12323 PRK12323
DNA polymerase III subunits gamma and tau; Provisional
457-680 4.29e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 46.02  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  457 PASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALPGArpedtagSAVPWRETTAGPAARSRETASEAAAgpwRAAPPRA 536
Cdd:PRK12323 374 PATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPA-------AAAAARAVAAAPARRSPAPEALAAA---RQASARG 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  537 ADPEREGGPRPAAGwddlagRAPGQRNPAT-------ALAAERARQTRMAVVGPVTERWAPEQAGPVHENWQLAAPIGPA 609
Cdd:PRK12323 444 PGGAPAPAPAPAAA------PAAAARPAAAgprpvaaAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAA 517
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223155  610 TDLWALGALLFRAVQGHAPYPEESTAELVQIVCAEPPAFAEECGPLRPVVESLLRQDPTERIDFEELSGWL 680
Cdd:PRK12323 518 PAGWVAESIPDPATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGDWPALAARL 588
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
421-583 6.25e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 45.36  E-value: 6.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  421 GDPATSGAAVPPGQITDPYGVGTTAwhgATPRTPGDPASSAARPTgdPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTA 500
Cdd:PRK07764 384 RLGVAGGAGAPAAAAPSAAAAAPAA---APAPAAAAPAAAAAPAP--AAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPP 458
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  501 GSAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAADPereggPRPAAGWDDLAGRAPGQRNPATALAAERARQTRMAV 580
Cdd:PRK07764 459 AAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAP-----AAPAAPAGADDAATLRERWPEILAAVPKRSRKTWAI 533

                 ...
gi 21223155  581 VGP 583
Cdd:PRK07764 534 LLP 536
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
355-494 1.11e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  355 GAGRPPHGSAPGGARPGHGVEAAGGAPGARPGQGSGRAAF-AAGSGQAPYAIGPDAASGAPWDEDSVGDPAtSGAAVPPG 433
Cdd:PRK07764 366 SASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAApAAAPAPAAAAPAAAAAPAPAAAPQPAPAPA-PAPAPPSP 444
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21223155  434 QITDPYGVGTTAWHGATPRTPGDPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALPGA 494
Cdd:PRK07764 445 AGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAG 505
Sporozoite_P67 pfam05642
Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. ...
231-440 1.17e-04

Sporozoite P67 surface antigen; This family consists of several Theileria P67 surface antigens. A stage specific surface antigen of Theileria parva, p67, is the basis for the development of an anti-sporozoite vaccine for the control of East Coast fever (ECF) in cattle. The antigen has been shown to contain five distinct linear peptide sequences recognized by sporozoite-neutralizing murine monoclonal antibodies.


Pssm-ID: 253298 [Multi-domain]  Cd Length: 727  Bit Score: 44.67  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   231 VPRAGVFGPGDADPEAARRAAIEARGVGGLPVPGTPVPGTAPAGLAPAsldaaadaraaragaiaayragaraaariqea 310
Cdd:pfam05642 163 QSQTGLGASGSHAQQDPAVSQSGVVGVPGLGVPGVGVPGGGGAGALPG-------------------------------- 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   311 qngrAALPGARPAPDGATqaGGPGTSGGRPGLAPGPGSSYDDDDGAGRPPHG--SAPGGARPGHGVEAAGGAPG-ARPGQ 387
Cdd:pfam05642 211 ----VGVGRAGVSPGVGV--GGLGGVPGVGILASNTSREGQTQDDQERDGDGrvIEPGVGLPGVRVGDSTSSPStTRPSG 284
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 21223155   388 GSGRAAFAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAvpPGQITDPYG 440
Cdd:pfam05642 285 STTTTTPASSGPSAPGGPGSSSRNAVTRSTDSISGPIPSPGA--PRAITGQMG 335
PRK12373 PRK12373
NADH dehydrogenase subunit E; Provisional
376-554 1.30e-04

NADH dehydrogenase subunit E; Provisional


Pssm-ID: 237082 [Multi-domain]  Cd Length: 400  Bit Score: 44.02  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  376 AAGGAPGARPGQGSGR--AAFAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSgaavppgqiTDPYGVGTTAWHGATPRT 453
Cdd:PRK12373 170 AAGKGPVVKPGPQIGRyaSEPAGGLTSLTEEAGKARYNASKALAEDIGDTVKR---------IDGTEVPLLAPWQGDAAP 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  454 PgdPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAArsretaseAAAGPWRAAP 533
Cdd:PRK12373 241 V--PPSEAARPKSADAETNAALKTPATAPKAAAKNAKAPEAQPVSGTAAAEPAPKEAAKAAA--------AAAKPALEDK 310
                        170       180
                 ....*....|....*....|.
gi 21223155  534 PRAADPEREGGPrpaagwDDL 554
Cdd:PRK12373 311 PRPLGIARPGGA------DDL 325
PHA03378 PHA03378
EBNA-3B; Provisional
432-669 1.38e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.29  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  432 PGQITDPYGVGTTAWHGATPRTPGDPASSAARPTGdpafPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTA 511
Cdd:PHA03378 654 PPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQ----WAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAA 729
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  512 GPAARSRETASEAAAGPWRAAPPRAADPEREGGP-RPAAGWDDLAGRAPGQRNPATALAAERARQTRMA--VVGP----V 584
Cdd:PHA03378 730 APGRARPPAAAPGRARPPAAAPGRARPPAAAPGRaRPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPppQAGPtsmqL 809
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  585 TERWAPEQAGPVHENWQLAAPIG-----PATDLWALGALLfrAVQGHAPYPEEST-AELVQIVCAEPPAFAE-----ECG 653
Cdd:PHA03378 810 MPRAAPGQQGPTKQILRQLLTGGvkrgrPSLKKPAALERQ--AAAGPTPSPGSGTsDKIVQAPVFYPPVLQPiqvmrQLG 887
                        250
                 ....*....|....*.
gi 21223155  654 PLRPVVESLLRQDPTE 669
Cdd:PHA03378 888 SVRAAAASTVTQAPTE 903
flhF PRK06995
flagellar biosynthesis regulator FlhF; Validated
472-585 5.42e-04

flagellar biosynthesis regulator FlhF; Validated


Pssm-ID: 235904 [Multi-domain]  Cd Length: 484  Bit Score: 42.26  E-value: 5.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  472 APRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGPwRAAPPRAADPEREGGPRPAAGW 551
Cdd:PRK06995  52 APPAAAAPAAAQPPPAAAPAAVSRPAAPAAEPAPWLVEHAKRLTAQREQLVARAAAP-AAPEAQAPAAPAERAAAENAAR 130
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 21223155  552 DDLAGRAPGQRNP---ATALAAERARQTRMAVVGPVT 585
Cdd:PRK06995 131 RLARAAAAAPRPRvpaDAAAAVADAVKARIERIVNDT 167
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
313-563 5.54e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   313 GRAALPGARPAPDGATQAGGPGTSGGRPGLAPGPGSSyDDDDGAGRPPH--GSAPGGARPGHGVEAAGGAPGARPGQGSG 390
Cdd:PHA03307   75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGP-SSPDPPPPTPPpaSPPPSPAPDLSEMLRPVGSPGPPPAASPP 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   391 RAAFAAGSGQAPYAIGPDAASGAPWDEDSVGDPATSGAAVPPgqITDPygvgttawhGATPRTPGDPASSAARPTGDpaf 470
Cdd:PHA03307  154 AAGASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPP--STPP---------AAASPRPPRRSSPISASASS--- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   471 PAPRPAGEPAAGSGPAAGRALPGARPEDTAG--SAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAADPEREGGPRPA 548
Cdd:PHA03307  220 PAPAPGRSAADDAGASSSDSSSSESSGCGWGpeNECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPS 299
                         250
                  ....*....|....*
gi 21223155   549 AGWDDLAGRAPGQRN 563
Cdd:PHA03307  300 PSSPGSGPAPSSPRA 314
kgd PRK12270
alpha-ketoglutarate decarboxylase; Reviewed
422-516 5.65e-04

alpha-ketoglutarate decarboxylase; Reviewed


Pssm-ID: 237030 [Multi-domain]  Cd Length: 1228  Bit Score: 42.57  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   422 DPATSGAAVPPGQITDPYGVGTTAwhgaTPRTPGDPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRAlpgARPEDTAG 501
Cdd:PRK12270   37 GPGSTAAPTAAAAAAAAAASAPAA----APAAKAPAAPAPAPPAAAAPAAPPKPAAAAAAAAAPAAPPA---AAAAAAPA 109
                          90
                  ....*....|....*..
gi 21223155   502 SAVPWRETTA--GPAAR 516
Cdd:PRK12270  110 AAAVEDEVTPlrGAAAA 126
PRK07003 PRK07003
DNA polymerase III subunits gamma and tau; Validated
422-611 6.42e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.14  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  422 DPATSGAAVPPGqitdpygvgttawhGATPRTPGDPASSAARPTGDPAFPAPRPAGePAAGSGPAAGRALPGARPEDTAG 501
Cdd:PRK07003 359 EPAVTGGGAPGG--------------GVPARVAGAVPAPGARAAAAVGASAVPAVT-AVTGAAGAALAPKAAAAAAATRA 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  502 SAVPWRETTAGPAARSRETASEAAAGPWRAAPPRAADP-EREGGPRPAAGWDDLAGRAPGQRNPATALAAERARQTRMAV 580
Cdd:PRK07003 424 EAPPAAPAPPATADRGDDAADGDAPVPAKANARASADSrCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAAT 503
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 21223155  581 VGPVTERWAP------EQAGPVHENWQLAAPIGPATD 611
Cdd:PRK07003 504 PAAVPDARAPaaasreDAPAAAAPPAPEARPPTPAAA 540
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
449-567 7.13e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 42.10  E-value: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  449 ATPRTPGDPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAAGP 528
Cdd:PRK14950 366 PQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPKEPVRETATPPPVPPRPVAPPVPHTPESAPKLTRAAIPVDEKPKYT 445
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 21223155  529 WRAAPP---RAADPEREGGPRPAAGWDDLAGRAPgQRNPATA 567
Cdd:PRK14950 446 PPAPPKeeeKALIADGDVLEQLEAIWKQILRDVP-PRSPAVQ 486
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
260-609 7.62e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.90  E-value: 7.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  260 LPVPGTPVPGTAPAGLAPASLDAAADARAARAGAIAAYRAGARAAARIQEAQNGRAALPGARPAPDGATQAGGPGTSGGR 339
Cdd:PRK07764 364 LPSASDDERGLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPS 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  340 PGLAPGPGSSYDDDDGAGRPPHGSAPGGARPGHGVEAAGGAPGARPGQGSGRAAFAAGSGQAPyaiGPDAASGAPWDE-- 417
Cdd:PRK07764 444 PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGA---DDAATLRERWPEil 520
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  418 DSVGD--PATSGAAVPPGQI-------------------------------------------------TDPYGVGTTAW 446
Cdd:PRK07764 521 AAVPKrsRKTWAILLPEATVlgvrgdtlvlgfstgglarrfaspgnaevlvtalaeelggdwqveavvgPAPGAAGGEGP 600
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  447 HGATPRTPGDPASSAARPTGDPAFPAPRPAGEPAAGSGPAAGRALPGARPEDTAGSAVPWRETTAGPAARSRETASEAAA 526
Cdd:PRK07764 601 PAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155  527 GPWRAAP--PRAADPEREGGPRPAAGWDDLAGRAPGQRNPATALAAERARQTRMAVVGPVTERWAPEQAGPVHENWQLAA 604
Cdd:PRK07764 681 PPPAPAPaaPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPP 760

                 ....*
gi 21223155  605 PIGPA 609
Cdd:PRK07764 761 PPAPA 765
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
107-193 8.99e-04

Protein tyrosine kinase;


Pssm-ID: 285015 [Multi-domain]  Cd Length: 258  Bit Score: 40.94  E-value: 8.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21223155   107 DHPRLDQVFDVFAEGGSLWIASELVAARPLAALLTE--QTLTPYRAAEVASDVLLALRVLHSYGWVHRNITARTVLV