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Conserved domains on  [gi|110668273|ref|YP_658084|]
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hypothetical protein HQ2347A [Haloquadratum walsbyi DSM 16790]

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
85-192 5.78e-12

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.


The actual alignment was detected with superfamily member pfam01163:

Pssm-ID: 276297  Cd Length: 186  Bit Score: 61.47  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273   85 EGEGFFEHFAT-PLEM----AEHEFTAAKRMRKLGLNTPKPIETfevdNLGILVSEY-------LPDFQTLDsLNQQAET 152
Cdd:pfam01163  33 DGDFRFRDSKTsWRYLvrlwAEKEFRNLKRLYEAGVPVPKPIAV----NRHVLVMEFigddgvpAPRLKDVE-LEEEAEE 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 110668273  153 DVAPIIFKMLRQMHEDGLYHGDLRAENILLYEDDVYFIDV 192
Cdd:pfam01163 108 IYDEIIREMRRLYQEAGLVHGDLSEYNVLVDDDKPVIIDV 147
 
Name Accession Description Interval E-value
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
85-192 5.78e-12

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 250410  Cd Length: 186  Bit Score: 61.47  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273   85 EGEGFFEHFAT-PLEM----AEHEFTAAKRMRKLGLNTPKPIETfevdNLGILVSEY-------LPDFQTLDsLNQQAET 152
Cdd:pfam01163  33 DGDFRFRDSKTsWRYLvrlwAEKEFRNLKRLYEAGVPVPKPIAV----NRHVLVMEFigddgvpAPRLKDVE-LEEEAEE 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 110668273  153 DVAPIIFKMLRQMHEDGLYHGDLRAENILLYEDDVYFIDV 192
Cdd:pfam01163 108 IYDEIIREMRRLYQEAGLVHGDLSEYNVLVDDDKPVIIDV 147
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
100-192 7.56e-11

Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins; RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270696  Cd Length: 189  Bit Score: 58.72  E-value: 7.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 100 AEHEFTAAKRMRKLGLNTPKPIETFEvdnlGILVSEYL-------PDFQTLDSLNQQAE---TDVAPIIFKMLrqmHEDG 169
Cdd:cd05145   65 ARKEFRNLKRLYEAGVRVPEPIAVYR----NVLVMEFIgddgspaPRLKDVELEEEDAEelyEQVVEQMRRMY---CKAG 137
                         90       100
                 ....*....|....*....|...
gi 110668273 170 LYHGDLRAENILLYEDDVYFIDV 192
Cdd:cd05145  138 LVHGDLSEYNILYYDGKPVIIDV 160
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
109-191 1.78e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 57.99  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 109 RMRKLGLNTPKPietFEVD-NLGILVSEYLpDFQTLDSLNQQAETDVAPIIFKMLRQ---MHEDGLYHGDLRAENILLYE 184
Cdd:PRK14879  55 RARKAGVNVPAV---YFVDpENFIIVMEYI-EGEPLKDLINSNGMEELELSREIGRLvgkLHSAGIIHGDLTTSNMILSG 130

                 ....*..
gi 110668273 185 DDVYFID 191
Cdd:PRK14879 131 GKIYLID 137
Probable_serine/threonine-protein_kinase TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
103-191 2.47e-10

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


Pssm-ID: 274749  Cd Length: 199  Bit Score: 57.22  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273  103 EFTAAKRMRKLGLNTPKPietFEVD-NLGILVSEYLPDFQTLDSLNQQaETDVAPIIFKMLRQMHEDGLYHGDLRAENIL 181
Cdd:TIGR03724  47 EARLLSRARKAGVNTPVI---YDVDpDNKTIVMEYIEGKPLKDVIEEN-GDELAREIGRLVGKLHKAGIVHGDLTTSNII 122
                          90
                  ....*....|
gi 110668273  182 LYEDDVYFID 191
Cdd:TIGR03724 123 VRDDKVYLID 132
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
103-232 8.68e-10

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 55.75  E-value: 8.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 103 EFTAAKRMRKLGLNTPKpieTFEVD-NLGILVSEYLPDFQTLDSLNQqAETDVAPIIFKMLRQMHEDGLYHGDLRAENIL 181
Cdd:COG3642   49 EARILAKAREAGVPVPI---VYDVDpDNGLIVMEYIEGELLKDALEE-ARPDLLREVGRLVGKLHKAGIVHGDLTTSNII 124
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 110668273 182 LYEDDVYFID--VTNVNEEsvADAMAYDIACALGALEP-HLGAKSTIDAALSSY 232
Cdd:COG3642  125 LSGGRIYFIDfgLGEFSDE--VEDKAVDLHVLERALEStHEKAEELFAAFLEGY 176
RIO smart00090
RIO-like kinase;
100-192 1.38e-08

RIO-like kinase;


Pssm-ID: 214511  Cd Length: 237  Bit Score: 53.07  E-value: 1.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273   100 AEHEFTAAKRMRKLGLNTPKPIETfevdNLGILVSEYL-------PDFQTLDSLNQQAEtdvaPIIFKMLRQM----HED 168
Cdd:smart00090  97 AEKEFRNLQRLYEAGVPVPKPIAW----RRNVLVMEFIggdglpaPRLKDVEPEEEEEF----ELYDDILEEMrklyKEG 168
                           90       100
                   ....*....|....*....|....
gi 110668273   169 GLYHGDLRAENILLYEDDVYFIDV 192
Cdd:smart00090 169 ELVHGDLSEYNILVHDGKVVIIDV 192
RIO1 COG1718
Serine/threonine protein kinase involved in cell cycle control [Signal transduction mechanisms ...
100-192 2.83e-11

Serine/threonine protein kinase involved in cell cycle control [Signal transduction mechanisms / Cell division and chromosome partitioning]


Pssm-ID: 224632 [Multi-domain]  Cd Length: 268  Bit Score: 61.18  E-value: 2.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 100 AEHEFTAAKRMRKLGLNTPKPIETFEvdnlGILVSEYL-------PDFQTLDSLNQQAETDVAPIIFKMLRQMHEDGLYH 172
Cdd:COG1718  115 ARKEFRNLKRAYEAGVRVPEPIAFRN----NVLVMEFIgddglpaPRLKDVPLELEEAEGLYEDVVEYMRRLYKEAGLVH 190
                         90       100
                 ....*....|....*....|
gi 110668273 173 GDLRAENILLYEDDVYFIDV 192
Cdd:COG1718  191 GDLSEYNILVHDGEPYIIDV 210
PRK09605 PRK09605
bifunctional UGMP family protein/serine/threonine protein kinase; Validated
103-191 1.56e-05

bifunctional UGMP family protein/serine/threonine protein kinase; Validated


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 44.49  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 103 EFTAAKRMRKLGLNTPKpIETFEVDNlGILVSEYLPDFQTLDSLNqqAETDVAPIIFKMLRQMHEDGLYHGDLRAENILL 182
Cdd:PRK09605 386 EARLLSEARRAGVPTPV-IYDVDPEE-KTIVMEYIGGKDLKDVLE--GNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIV 461

                 ....*....
gi 110668273 183 YEDDVYFID 191
Cdd:PRK09605 462 RDDRLYLID 470
 
Name Accession Description Interval E-value
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
85-192 5.78e-12

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 250410  Cd Length: 186  Bit Score: 61.47  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273   85 EGEGFFEHFAT-PLEM----AEHEFTAAKRMRKLGLNTPKPIETfevdNLGILVSEY-------LPDFQTLDsLNQQAET 152
Cdd:pfam01163  33 DGDFRFRDSKTsWRYLvrlwAEKEFRNLKRLYEAGVPVPKPIAV----NRHVLVMEFigddgvpAPRLKDVE-LEEEAEE 107
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 110668273  153 DVAPIIFKMLRQMHEDGLYHGDLRAENILLYEDDVYFIDV 192
Cdd:pfam01163 108 IYDEIIREMRRLYQEAGLVHGDLSEYNVLVDDDKPVIIDV 147
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
100-192 7.56e-11

Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar proteins; RIO1 is present in archaea, bacteria and eukaryotes. In addition, RIO3 is present in multicellular eukaryotes. Both RIO1 and RIO3 are associated with precursors of 40S ribosomal subunits, just like RIO2. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. The specific function of RIO3 is unknown. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270696  Cd Length: 189  Bit Score: 58.72  E-value: 7.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 100 AEHEFTAAKRMRKLGLNTPKPIETFEvdnlGILVSEYL-------PDFQTLDSLNQQAE---TDVAPIIFKMLrqmHEDG 169
Cdd:cd05145   65 ARKEFRNLKRLYEAGVRVPEPIAVYR----NVLVMEFIgddgspaPRLKDVELEEEDAEelyEQVVEQMRRMY---CKAG 137
                         90       100
                 ....*....|....*....|...
gi 110668273 170 LYHGDLRAENILLYEDDVYFIDV 192
Cdd:cd05145  138 LVHGDLSEYNILYYDGKPVIIDV 160
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
109-191 1.78e-10

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 57.99  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 109 RMRKLGLNTPKPietFEVD-NLGILVSEYLpDFQTLDSLNQQAETDVAPIIFKMLRQ---MHEDGLYHGDLRAENILLYE 184
Cdd:PRK14879  55 RARKAGVNVPAV---YFVDpENFIIVMEYI-EGEPLKDLINSNGMEELELSREIGRLvgkLHSAGIIHGDLTTSNMILSG 130

                 ....*..
gi 110668273 185 DDVYFID 191
Cdd:PRK14879 131 GKIYLID 137
Probable_serine/threonine-protein_kinase TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
103-191 2.47e-10

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


Pssm-ID: 274749  Cd Length: 199  Bit Score: 57.22  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273  103 EFTAAKRMRKLGLNTPKPietFEVD-NLGILVSEYLPDFQTLDSLNQQaETDVAPIIFKMLRQMHEDGLYHGDLRAENIL 181
Cdd:TIGR03724  47 EARLLSRARKAGVNTPVI---YDVDpDNKTIVMEYIEGKPLKDVIEEN-GDELAREIGRLVGKLHKAGIVHGDLTTSNII 122
                          90
                  ....*....|
gi 110668273  182 LYEDDVYFID 191
Cdd:TIGR03724 123 VRDDKVYLID 132
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
103-191 2.53e-10

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in Escherichia coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 253661  Cd Length: 206  Bit Score: 57.37  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273  103 EFTAAKRMRKLGLNTPKPIETFEV-DNLG---ILVSEYLPDFQTLDSLNQQAETDVAPI-------IFKMLRQMHEDGLY 171
Cdd:pfam06293  61 EFRLLRRLREAGVPVPKPVAAGAVkVGGEyqaDLLTERLEGAQDLVTWLAQWADPAEELrralwraVGRLIARMHRAGVN 140
                          90       100
                  ....*....|....*....|....
gi 110668273  172 HGDLRAENILLYED----DVYFID 191
Cdd:pfam06293 141 HTDLNAHNILLDTGeggfKVWLID 164
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
103-232 8.68e-10

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 55.75  E-value: 8.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 103 EFTAAKRMRKLGLNTPKpieTFEVD-NLGILVSEYLPDFQTLDSLNQqAETDVAPIIFKMLRQMHEDGLYHGDLRAENIL 181
Cdd:COG3642   49 EARILAKAREAGVPVPI---VYDVDpDNGLIVMEYIEGELLKDALEE-ARPDLLREVGRLVGKLHKAGIVHGDLTTSNII 124
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 110668273 182 LYEDDVYFID--VTNVNEEsvADAMAYDIACALGALEP-HLGAKSTIDAALSSY 232
Cdd:COG3642  125 LSGGRIYFIDfgLGEFSDE--VEDKAVDLHVLERALEStHEKAEELFAAFLEGY 176
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
97-191 1.13e-09

Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270700  Cd Length: 152  Bit Score: 54.48  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273  97 LEMAEHEFTAAKRMRKLGLNtPKPIETFEvdNLGILVSEYLPDFQTLDslNQQAETDVAPIIFKMLRQMHEDGLY----- 171
Cdd:cd05151   36 LIDRENEKANSKAAAELGIA-PEVIYFDP--ETGVKITEFIEGATLLT--NDFSDPENLERIAALLRKLHSSPLEdlvlc 110
                         90       100
                 ....*....|....*....|
gi 110668273 172 HGDLRAENILLYEDDVYFID 191
Cdd:cd05151  111 HNDLVPGNFLLDDDRLYLID 130
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
103-191 4.17e-09

3-deoxy-D-manno-octulosonic-acid kinase; Reviewed


Pssm-ID: 234975  Cd Length: 239  Bit Score: 54.50  E-value: 4.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 103 EFTAAKRMRKLGLNTPKPIE--------TFEVDnlgiLVSEYLPDFQTLDSLNQQAETDVAPI--IFKMLRQMHEDGLYH 172
Cdd:PRK01723  90 EFRLLAQLYEAGLPVPRPIAarvvrhglFYRAD----ILIERIEGARDLVALLQEAPLSEEQWqaIGQLIARFHDAGVYH 165
                         90       100
                 ....*....|....*....|
gi 110668273 173 GDLRAENILLYEDD-VYFID 191
Cdd:PRK01723 166 ADLNAHNILLDPDGkFWLID 185
RIO smart00090
RIO-like kinase;
100-192 1.38e-08

RIO-like kinase;


Pssm-ID: 214511  Cd Length: 237  Bit Score: 53.07  E-value: 1.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273   100 AEHEFTAAKRMRKLGLNTPKPIETfevdNLGILVSEYL-------PDFQTLDSLNQQAEtdvaPIIFKMLRQM----HED 168
Cdd:smart00090  97 AEKEFRNLQRLYEAGVPVPKPIAW----RRNVLVMEFIggdglpaPRLKDVEPEEEEEF----ELYDDILEEMrklyKEG 168
                           90       100
                   ....*....|....*....|....
gi 110668273   169 GLYHGDLRAENILLYEDDVYFIDV 192
Cdd:smart00090 169 ELVHGDLSEYNILVHDGKVVIIDV 192
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
101-191 1.55e-08

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: 51.29  E-value: 1.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 101 EHEFTAAKRMRKLGLNTPKPIETFEVDNLGILVSEYLPDFQTLDSLN--QQAETDVAPIIFKMLRQM---HEDGLYHGDL 175
Cdd:cd13968   38 ESEMDILRRLKGLELNIPKVLVTEDVDGPNILLMELVKGGTLIAYTQeeELDEKDVESIMYQLAECMrllHSFHLIHRDL 117
                         90
                 ....*....|....*..
gi 110668273 176 RAENILLYED-DVYFID 191
Cdd:cd13968  118 NNDNILLSEDgNVKLID 134
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
100-192 3.43e-08

Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is present in archaea, bacteria and eukaryotes. This subfamily is composed of RIO1 proteins from eukaryotes. RIO1 is essential for survival and is required for 18S rRNA processing, proper cell cycle progression and chromosome maintenance. It is associated with precursors of 40S ribosomal subunits, just like RIO2. Although depletion of either RIO1 and RIO2 results in similar effects, the two kinases are not fully interchangeable. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270698  Cd Length: 190  Bit Score: 51.03  E-value: 3.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 100 AEHEFTAAKRMRKLGLNTPKPIETFEVdnlgILVSEY----------LPDFQTLDSLNQQAETDVapiiFKMLRQM-HED 168
Cdd:cd05147   66 AEKEMRNLKRLNQAGIPCPEPILLRSH----VLVMEFigkdgwpaprLKDAKLSESKWRELYLQV----IKIMRRMyQKC 137
                         90       100
                 ....*....|....*....|....
gi 110668273 169 GLYHGDLRAENILLYEDDVYFIDV 192
Cdd:cd05147  138 RLVHADLSEYNLLYHKGKVYIIDV 161
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
95-190 1.42e-07

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: 49.58  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273  95 TPLEMAEHEFTAAKRMRklGLNTPKPIETFEVDNLGILVSEYLP--DFQTLdsLNQQAETDVAPIIFKMLRQM------- 165
Cdd:cd00180   33 KLLEELLREIEILKKLN--HPNIVKLYDVFETENFLYLVMEYCEggSLKDL--LKENKGPLSEEEALSILRQLlsaleyl 108
                         90       100
                 ....*....|....*....|....*
gi 110668273 166 HEDGLYHGDLRAENILLYEDDVYFI 190
Cdd:cd00180  109 HSNGIIHRDLKPENILLDSDGTVKL 133
APH_ChoK_like cd05120
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed ...
111-212 1.96e-07

Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270690  Cd Length: 158  Bit Score: 48.45  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 111 RKLGLNTPKPIETFEVDNLGILVSEYLPDfQTLDS----LNQQAETDVAPIIFKMLRQMHE---DGLYHGDLRAENILLY 183
Cdd:cd05120   48 GKLSLPVPKVYGFGESDGWEYLLMERIEG-ETLSEvwprLSEEEKEKIADQLAEILAALHRidsSVLTHGDLHPGNILVK 126
                         90       100       110
                 ....*....|....*....|....*....|.
gi 110668273 184 EDD--VYFIDVtnvnEESVADAMAYDIACAL 212
Cdd:cd05120  127 PDGklSGIIDW----EFAGYGPPAFDYAAAL 153
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
100-193 6.73e-07

Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in multicellular eukaryotes. It is associated with precursors of 40S ribosomal subunits, just like RIO1 and RIO2. Its specific function is still unknown. Like RIO1 and RIO2, it may be involved in ribosomal subunit processing and maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO3 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270697  Cd Length: 196  Bit Score: 47.36  E-value: 6.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 100 AEHEFTAAKRMRKLGLNTPKPIetfeVDNLGILVSEYLPDFQTLDSLNQQAETDVAPI------IFKMLRQM-HEDGLYH 172
Cdd:cd05146   72 AEKEMHNLKRMQKAGIPCPEVV----LLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLklayeqVVQMMKTMyNECHLVH 147
                         90       100
                 ....*....|....*....|.
gi 110668273 173 GDLRAENILLYEDDVYFIDVT 193
Cdd:cd05146  148 ADLSEYNILWHEGKVWFIDVS 168
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
108-183 5.25e-06

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 45.42  E-value: 5.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 108 KRMRKLGLNTP--KPIETFEVDNLGILVSEYLPDFQTLDSLNQQAETDVAPI-----------IFKMLRQMHEDGLYHGD 174
Cdd:cd13981   52 SRLKNSRLRESisGAHSAHLFQDESILVMDYSSQGTLLDVVNKMKNKTGGGMdeplamfftieLLKVVEALHEVGIIHGD 131

                 ....*....
gi 110668273 175 LRAENILLY 183
Cdd:cd13981  132 IKPDNFLLR 140
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
100-191 6.60e-05

Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical protein serine kinases present in archaea, bacteria and eukaryotes. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. RIO kinases contain a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. Most organisms contain at least two RIO kinases, RIO1 and RIO2. A third protein, RIO3, is present in multicellular eukaryotes. In yeast, RIO1 and RIO2 are essential for survival. They function as non-ribosomal factors necessary for late 18S rRNA processing. RIO1 is also required for proper cell cycle progression and chromosome maintenance. The biological substrates for RIO kinases are still unknown. The RIO kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270689  Cd Length: 192  Bit Score: 41.55  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 100 AEHEFTAAKRMRKLGLNTPKPIETFEVDNLGILVSEYLPDFQTLDSLNQQ-AETDVAPIIFKMLRQM----HEDGLYHGD 174
Cdd:cd05119   67 TEKEFRNLERAKEAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELGRElKELDVEGIFNDVVENVkrlyQEAELVHAD 146
                         90
                 ....*....|....*..
gi 110668273 175 LRAENIlLYEDDVYFID 191
Cdd:cd05119  147 LSEYNI-LYIDKVYFID 162
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
100-191 3.30e-04

C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270695  Cd Length: 183  Bit Score: 39.41  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 100 AEHEFTAAKRMRKLGLNTPKPIETfevdNLGILVSEYLPDFQtldsLNQQAET-DVAPI---IFKMLRQMHEDGLYHGDL 175
Cdd:cd05144   65 AEKEFAALKALYEEGFPVPKPIDW----NRHAVVMELIDGYP----LYQVRLLeDPEEVldeILELIVKLAKHGLIHGDF 136
                         90
                 ....*....|....*..
gi 110668273 176 RAENILLYEDD-VYFID 191
Cdd:cd05144  137 SEFNILVDEDEkITVID 153
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
121-194 7.53e-04

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


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 39.00  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 121 IETFEVDNLGILVSEYLPDFQTLD------SLNQQAETDVAPIIFKMLRQMHEDGLYHGDLRAENILLYEDDVYFIDVTN 194
Cdd:cd14098   67 IDWYEDDQHIYLVMEYVEGGDLMDfimawgAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVIVKISD 146
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
158-182 1.35e-03

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 38.00  E-value: 1.35e-03
                         10        20
                 ....*....|....*....|....*
gi 110668273 158 IFKMLRQMHEDGLYHGDLRAENILL 182
Cdd:cd13980  106 LLHALNQCHKRGVCHGDIKTENVLV 130
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
121-186 1.68e-03

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 37.84  E-value: 1.68e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110668273 121 IETFEVDNLGILVSEYLPD---FQTLDSLNQQAETDVAPIIFKMLR---QMHEDGLYHGDLRAENILLYEDD 186
Cdd:cd05117   65 YEVFEDDKNLYLVMELCTGgelFDRIVKKGSFSEREAAKIMKQILSavaYLHSQGIVHRDLKPENILLASKD 136
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
131-191 2.76e-03

Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and similar proteins; This family is composed of the atypical yeast protein kinase Abc1p, its human homolog ADCK3 (also called CABC1), and similar proteins. Abc1p (also called Coq8p) is required for the biosynthesis of Coenzyme Q (ubiquinone or Q), which is an essential lipid component in respiratory electron and proton transport. It is necessary for the formation of a multi-subunit Q-biosynthetic complex and may also function in the regulation of Q synthesis. Human ADCK3 is able to rescue defects in Q synthesis and the phosphorylation state of Coq proteins in yeast Abc1 (or Coq8) mutants. Mutations in ADCK3 cause progressive cerebellar ataxia and atrophy due to Q10 deficiency. Eukaryotes contain at least two more ABC1/ADCK3-like proteins: in humans, these are the putative atypical protein kinases named ADCK1 and ADCK2. In algae and higher plants, ABC1 kinases have proliferated to more than 15 subfamilies, most of which are located in plastids or mitochondria. Eight of these plant ABC1 kinase subfamilies (ABC1K1-8) are specific for photosynthetic organisms. ABC1 kinases are not related to the ATP-binding cassette (ABC) membrane transporter family.


Pssm-ID: 270691 [Multi-domain]  Cd Length: 247  Bit Score: 37.09  E-value: 2.76e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110668273 131 ILVSEYLP-----DFQTLDSLNQQAEtDVAPIIFKM-LRQMHEDGLYHGDLRAENILLYEDD-VYFID 191
Cdd:cd05121  147 VLVMEYIDgvkltDLEALRAAGIDRK-ELARRLVDAyLKQIFEDGFFHADPHPGNILVLPDGrIALLD 213
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
121-191 2.91e-03

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 36.94  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 121 IETFEVDNLGILVSEYLP--DFQTLDSLNQQAETDVAPI--IFKML----RQMHEDGLYHGDLRAENILL--YEDDVYFI 190
Cdd:cd13993   71 HDVFETEVAIYIVLEYCPngDLFEAITENRIYVGKTELIknVFLQLidavKHCHSLGIYHRDIKPENILLsqDEGTVKLC 150

                 .
gi 110668273 191 D 191
Cdd:cd13993  151 D 151
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
122-182 4.18e-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: 36.48  E-value: 4.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110668273 122 ETFEVDNLGILVSEYLPDFQTLDSLNQQA---ETDVAPIIFKML---RQMHEDGLYHGDLRAENILL 182
Cdd:cd14006   56 EAYESPTELVLILELCSGGELLDRLAERGslsEEEVRTYMRQLLeglQYLHNHHILHLDLKPENILL 122
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
97-191 7.78e-03

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: 35.64  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273  97 LEMAEHEFTAAKRMRklGLNTPKPIETFEVDNLGILVSEYLpDFQTLDSLNQQAETDVAPIIFKMLRQM-------HEDG 169
Cdd:cd14014   44 RERFLREARALARLS--HPNIVRVYDVGEDDGRPYIVMEYV-EGGSLADLLRERGPLPPREALRILAQIadalaaaHRAG 120
                         90       100
                 ....*....|....*....|...
gi 110668273 170 LYHGDLRAENILLYEDD-VYFID 191
Cdd:cd14014  121 IVHRDIKPANILLTEDGrVKLTD 143
RIO1 COG1718
Serine/threonine protein kinase involved in cell cycle control [Signal transduction mechanisms ...
100-192 2.83e-11

Serine/threonine protein kinase involved in cell cycle control [Signal transduction mechanisms / Cell division and chromosome partitioning]


Pssm-ID: 224632 [Multi-domain]  Cd Length: 268  Bit Score: 61.18  E-value: 2.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 100 AEHEFTAAKRMRKLGLNTPKPIETFEvdnlGILVSEYL-------PDFQTLDSLNQQAETDVAPIIFKMLRQMHEDGLYH 172
Cdd:COG1718  115 ARKEFRNLKRAYEAGVRVPEPIAFRN----NVLVMEFIgddglpaPRLKDVPLELEEAEGLYEDVVEYMRRLYKEAGLVH 190
                         90       100
                 ....*....|....*....|
gi 110668273 173 GDLRAENILLYEDDVYFIDV 192
Cdd:COG1718  191 GDLSEYNILVHDGEPYIIDV 210
PRK09605 PRK09605
bifunctional UGMP family protein/serine/threonine protein kinase; Validated
103-191 1.56e-05

bifunctional UGMP family protein/serine/threonine protein kinase; Validated


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 44.49  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273 103 EFTAAKRMRKLGLNTPKpIETFEVDNlGILVSEYLPDFQTLDSLNqqAETDVAPIIFKMLRQMHEDGLYHGDLRAENILL 182
Cdd:PRK09605 386 EARLLSEARRAGVPTPV-IYDVDPEE-KTIVMEYIGGKDLKDVLE--GNPELVRKVGEIVAKLHKAGIVHGDLTTSNFIV 461

                 ....*....
gi 110668273 183 YEDDVYFID 191
Cdd:PRK09605 462 RDDRLYLID 470
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
90-191 2.53e-04

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 40.50  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273  90 FEHFATPLEMAEHEFTAAKRMRKLGlNTPKPIETFEVDNLGILVSEYLPDFQTLDSLNQQ------AETDVAPIIFKM-- 161
Cdd:COG0515   34 LESKSKEVERFLREIQILASLNHPP-NIVKLYDFFQDEGSLYLVMEYVDGGSLEDLLKKIgrkgplSESEALFILAQIls 112
                         90       100       110
                 ....*....|....*....|....*....|...
gi 110668273 162 -LRQMHEDGLYHGDLRAENILLYEDD--VYFID 191
Cdd:COG0515  113 aLEYLHSKGIIHRDIKPENILLDRDGrvVKLID 145
COG0478 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
91-191 4.24e-03

RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms]


Pssm-ID: 223554 [Multi-domain]  Cd Length: 304  Bit Score: 36.53  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110668273  91 EHFA---TPLEMAEHEFTAAKRMRKLGLNTPKPIETfevdNLGILVSEYLpDFQTLDSLNQQAEtDVAPIIFKMLRQM-- 165
Cdd:COG0478  144 EHGSwlyVSRLAAEREFEALQRLYPEGVKVPKPIAW----NRHAVVMEYI-EGVELYRLRLDVE-NPDEILDKILEEVrk 217
                         90       100
                 ....*....|....*....|....*...
gi 110668273 166 -HEDGLYHGDLRAENILLYED-DVYFID 191
Cdd:COG0478  218 aYRRGIVHGDLSEFNILVTEDgDIVVID 245
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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