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Conserved domains on  [gi|1039744181|ref|XP_017171095|]
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serine/threonine-protein kinase RIO1 isoform X1 [Mus musculus]

Protein Classification

serine/threonine-protein kinase RIO1( domain architecture ID 10142323)

serine/threonine protein kinase RIO1 is an atypical protein kinase that catalyzes the ATP-dependent phosphorylation of serine residues in substrate proteins; it acts predominantly as an ATPase and is required for 18S rRNA processing, ribosome assembly, proper cell cycle progression, and chromosome maintenance

CATH:  1.10.510.10
EC:  2.7.11.1|3.6.3.-
Gene Ontology:  GO:0005524|GO:0004674|GO:0006468
PubMed:  16183636|16182620|12135737|19614568|16244704

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 15-204 4.39e-146

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: 411.96  E-value: 4.39e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  15 IHGCISTGKEANVYYASTPSGESRAIKIYKTSILMFKDRDKYVTGEFRFRRGYCKGNPRKMVRTWAEKEMRNLCRLKTAN 94
Cdd:cd05147     1 INGCISTGKEANVYHATTKNGGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  95 IPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYQDARLVHADLSEFNMLYHGGDVYIID 174
Cdd:cd05147    81 IPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYIID 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039744181 175 VSQSVEHDHPHALEFLRKDCTNVNDFFSKH 204
Cdd:cd05147   161 VSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
 
Name Accession Description Interval E-value
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 15-204 4.39e-146

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: 411.96  E-value: 4.39e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  15 IHGCISTGKEANVYYASTPSGESRAIKIYKTSILMFKDRDKYVTGEFRFRRGYCKGNPRKMVRTWAEKEMRNLCRLKTAN 94
Cdd:cd05147     1 INGCISTGKEANVYHATTKNGGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  95 IPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYQDARLVHADLSEFNMLYHGGDVYIID 174
Cdd:cd05147    81 IPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYIID 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039744181 175 VSQSVEHDHPHALEFLRKDCTNVNDFFSKH 204
Cdd:cd05147   161 VSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO smart00090
RIO-like kinase;
1-220 2.04e-104

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 308.07  E-value: 2.04e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181    1 MILFKLLHKDHISEIHGCISTGKEANVYYAS--TPSGESRAIKIYKTSILMFKDRDKYVTGEFRFRrgYCKGNPRKMVRT 78
Cdd:smart00090  18 LALYSLLNRGILSAIGGCISTGKEANVYHALdfDGSGKERAVKIYRTGTLEFKRRDRYVDGDFRFK--YRKINPRKLVRL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181   79 WAEKEMRNLCRLKTANIPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYQDARLVHADL 158
Cdd:smart00090  96 WAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEEFELYDDILEEMRKLYKEGELVHGDL 175

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039744181  159 SEFNMLYHGGDVYIIDVSQSVEHDHPHALEFLRKDCTNVNDFFSKHAVAVMTVRELFDFVTD 220
Cdd:smart00090 176 SEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDEEELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 26-213 6.07e-95

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: 460091 [Multi-domain]  Cd Length: 184  Bit Score: 282.20  E-value: 6.07e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  26 NVYYASTPSGESRAIKIYKTSILMFKDRDKYVTGEFRFRRGycKGNPRKMVRTWAEKEMRNLCRLKTANIPCPEPIRLRS 105
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181 106 HVLLMGFIGKDDMPAPLLKNVQLSEskARELYLQVIQYMRKMYQDARLVHADLSEFNMLYHGGDVYIIDVSQSVEHDHPH 185
Cdd:pfam01163  79 HVLVMEFIGKDGVPAPKLKDVELEE--AEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHPN 156

                         170       180
                  ....*....|....*....|....*...
gi 1039744181 186 ALEFLRKDCTNVNDFFSKHAVAVMTVRE 213
Cdd:pfam01163 157 ALEFLERDVENIINFFRRKGVDEVDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
1-219 7.31e-85

Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];


Pssm-ID: 441324  Cd Length: 252  Bit Score: 258.97  E-value: 7.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181   1 MILFKLLHKDHISEIHGCISTGKEANVYYASTPSGESRAIKIYKTSILMFKDRDKYVTGEFRF--RRGYckgNPRKMVRT 78
Cdd:COG1718    36 KALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTATSSFKRMAQYIEGDPRFmgKGSF---GRRQLIFA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  79 WAEKEMRNLCRLKTANIPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYqDARLVHADL 158
Cdd:COG1718   113 WARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVELEPEEAEELYEQLIEYIVRLY-KAGLVHGDL 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039744181 159 SEFNMLYHGGDVYIIDVSQSVEHDHPHALEFLRKDCTNVNDFFSKHAVAVMTvRELFDFVT 219
Cdd:COG1718   192 SEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPELDP-EELLKEIW 251
PRK14879 PRK14879
Kae1-associated kinase Bud32;
77-180 4.76e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 44.13  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  77 RTwaEKEMRNLCRLKTANIPCPEP--IRLRSHVLLMGFIgkddmPAPLLKNV-QLSESKARELYLQVIQYMRKMYQdARL 153
Cdd:PRK14879   45 RT--RREARIMSRARKAGVNVPAVyfVDPENFIIVMEYI-----EGEPLKDLiNSNGMEELELSREIGRLVGKLHS-AGI 116

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039744181 154 VHADLSEFNMLYHGGDVYIID-----VSQSVE 180
Cdd:PRK14879  117 IHGDLTTSNMILSGGKIYLIDfglaeFSKDLE 148
 
Name Accession Description Interval E-value
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 15-204 4.39e-146

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: 411.96  E-value: 4.39e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  15 IHGCISTGKEANVYYASTPSGESRAIKIYKTSILMFKDRDKYVTGEFRFRRGYCKGNPRKMVRTWAEKEMRNLCRLKTAN 94
Cdd:cd05147     1 INGCISTGKEANVYHATTKNGGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  95 IPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYQDARLVHADLSEFNMLYHGGDVYIID 174
Cdd:cd05147    81 IPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYIID 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1039744181 175 VSQSVEHDHPHALEFLRKDCTNVNDFFSKH 204
Cdd:cd05147   161 VSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO smart00090
RIO-like kinase;
1-220 2.04e-104

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 308.07  E-value: 2.04e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181    1 MILFKLLHKDHISEIHGCISTGKEANVYYAS--TPSGESRAIKIYKTSILMFKDRDKYVTGEFRFRrgYCKGNPRKMVRT 78
Cdd:smart00090  18 LALYSLLNRGILSAIGGCISTGKEANVYHALdfDGSGKERAVKIYRTGTLEFKRRDRYVDGDFRFK--YRKINPRKLVRL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181   79 WAEKEMRNLCRLKTANIPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYQDARLVHADL 158
Cdd:smart00090  96 WAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEEFELYDDILEEMRKLYKEGELVHGDL 175

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039744181  159 SEFNMLYHGGDVYIIDVSQSVEHDHPHALEFLRKDCTNVNDFFSKHAVAVMTVRELFDFVTD 220
Cdd:smart00090 176 SEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDEEELFERITG 237
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 17-204 2.70e-102

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 [Multi-domain]  Cd Length: 189  Bit Score: 301.01  E-value: 2.70e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  17 GCISTGKEANVYYASTPSGESRAIKIYKTSILMFKDRDKYVTGEFRFRrGYCKGNPRKMVRTWAEKEMRNLCRLKTANIP 96
Cdd:cd05145     3 GVISTGKEANVYLARGGDGEPVAVKIYRTSTSSFKKMAKYIEGDPRFE-SRRRGNRRKLIFAWARKEFRNLKRLYEAGVR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  97 CPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYQDARLVHADLSEFNMLYHGGDVYIIDVS 176
Cdd:cd05145    82 VPEPIAVYRNVLVMEFIGDDGSPAPRLKDVELEEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNILYYDGKPVIIDVS 161

                         170       180
                  ....*....|....*....|....*...
gi 1039744181 177 QSVEHDHPHALEFLRKDCTNVNDFFSKH 204
Cdd:cd05145   162 QAVTLDHPNAEEFLRRDIRNINRFFSRK 189
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 26-213 6.07e-95

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: 460091 [Multi-domain]  Cd Length: 184  Bit Score: 282.20  E-value: 6.07e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  26 NVYYASTPSGESRAIKIYKTSILMFKDRDKYVTGEFRFRRGycKGNPRKMVRTWAEKEMRNLCRLKTANIPCPEPIRLRS 105
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181 106 HVLLMGFIGKDDMPAPLLKNVQLSEskARELYLQVIQYMRKMYQDARLVHADLSEFNMLYHGGDVYIIDVSQSVEHDHPH 185
Cdd:pfam01163  79 HVLVMEFIGKDGVPAPKLKDVELEE--AEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHPN 156

                         170       180
                  ....*....|....*....|....*...
gi 1039744181 186 ALEFLRKDCTNVNDFFSKHAVAVMTVRE 213
Cdd:pfam01163 157 ALEFLERDVENIINFFRRKGVDEVDERK 184
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 15-203 1.68e-91

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: 273.86  E-value: 1.68e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  15 IHGCISTGKEANVYYASTPSGESR------AIKIYKTSILMFKDRDKYVTGEFRFRRGYCKGNPRKMVRTWAEKEMRNLC 88
Cdd:cd05146     1 VNGCISTGKEAVVFHANGGSMEEVllppecAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKEMHNLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  89 RLKTANIPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYQDARLVHADLSEFNMLYHGG 168
Cdd:cd05146    81 RMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNILWHEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039744181 169 DVYIIDVSQSVEHDHPHALEFLRKDCTNVNDFFSK 203
Cdd:cd05146   161 KVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQK 195
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
1-219 7.31e-85

Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];


Pssm-ID: 441324  Cd Length: 252  Bit Score: 258.97  E-value: 7.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181   1 MILFKLLHKDHISEIHGCISTGKEANVYYASTPSGESRAIKIYKTSILMFKDRDKYVTGEFRF--RRGYckgNPRKMVRT 78
Cdd:COG1718    36 KALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTATSSFKRMAQYIEGDPRFmgKGSF---GRRQLIFA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  79 WAEKEMRNLCRLKTANIPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRKMYqDARLVHADL 158
Cdd:COG1718   113 WARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVELEPEEAEELYEQLIEYIVRLY-KAGLVHGDL 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039744181 159 SEFNMLYHGGDVYIIDVSQSVEHDHPHALEFLRKDCTNVNDFFSKHAVAVMTvRELFDFVT 219
Cdd:COG1718   192 SEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPELDP-EELLKEIW 251
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 15-204 1.61e-34

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: 126.68  E-value: 1.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  15 IHGCISTGKEANVYYA-STPSGE--SRAIKIYKTSILMFKDRDKYVTGEFRFrrGYCKGNPRKMVRTWAEKEMRNLCRLK 91
Cdd:cd05119     1 IGGVISTGKEANVFYAdGVFDGKpvACAVKIYRIETSEFDKVDEYLYGDERF--DYRRISPKEKVFIWTEKEFRNLERAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  92 TANIPCPEPIRLRSHVLLMGFIGKDDMPAPLLKNV--QLSESKARELYLQVIQYMRKMYQDARLVHADLSEFNMLYHGGd 169
Cdd:cd05119    79 EAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELgrELKELDVEGIFNDVVENVKRLYQEAELVHADLSEYNILYIDK- 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1039744181 170 VYIIDVSQSVEHDHPHALEFLRKDCTNVNDFFSKH 204
Cdd:cd05119   158 VYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSKY 192
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 19-204 2.24e-31

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 [Multi-domain]  Cd Length: 183  Bit Score: 117.61  E-value: 2.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  19 ISTGKEANVYYASTPSGESRAIKIYK---TSilmFKdrdkyvtgEFRFRRGYCKGNPRK----MVRTWAEKEMRNLCRLK 91
Cdd:cd05144     8 IGVGKESDVYLALDEDGNPVVLKFHRlgrTS---FR--------KVKRKRDYLKHRKHAswlyLSRLAAEKEFAALKALY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  92 TANIPCPEPIRLRSHVLLMGFIgkddmPAPLLKNVQLSEsKARELYLQVIQYMRKMYQdARLVHADLSEFN-MLYHGGDV 170
Cdd:cd05144    77 EEGFPVPKPIDWNRHAVVMELI-----DGYPLYQVRLLE-DPEEVLDEILELIVKLAK-HGLIHGDFSEFNiLVDEDEKI 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1039744181 171 YIIDVSQSVEHDHPHALEFLRKDCTNVNDFFSKH 204
Cdd:cd05144   150 TVIDFPQMVSTSHPNAEEYFDRDVECIIKFFRRK 183
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 32-220 1.68e-26

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


Pssm-ID: 440246 [Multi-domain]  Cd Length: 183  Bit Score: 104.60  E-value: 1.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  32 TPSGESRAIKIYKTSILMFK-------DRDKYV-TGEFRFRrgyckgnprkmvrtwAEKEMRNLCRLKTANIPCPEPIRL 103
Cdd:COG0478     5 SPGGGPVALKFHREGRTSFRkvrreraDKEHYSwLYAARTR---------------AEREFRALERLYPAGLPVPRPIAA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181 104 RSHVLLMGFIgkddmPAPLLKNVQLSESKarELYLQVIQYMRKMYqDARLVHADLSEFN-MLYHGGDVYIIDVSQSVEHD 182
Cdd:COG0478    70 NRHAIVMERI-----EGVELARLKLEDPE--EVLDKILEEIRRAH-DAGIVHADLSEYNiLVDDDGGVWIIDWPQAVPRD 141

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1039744181 183 HPHALEFLRKDCTNVNDFFSKHAVAVMTVRELFDFVTD 220
Cdd:COG0478   142 HPNAEELLERDLENLLRSFRKKYGLEVDLDEVWAALLG 179
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 77-186 5.91e-09

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 54.58  E-value: 5.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  77 RTWAEkeMRNLCRLKTANIPCPEPI--RLRSHVLLMGFIgkddmPAPLLKNVQLSESKARELYLQVIQYMRKMYqDARLV 154
Cdd:COG3642     2 RTRRE--ARLLRELREAGVPVPKVLdvDPDDADLVMEYI-----EGETLADLLEEGELPPELLRELGRLLARLH-RAGIV 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039744181 155 HADLSEFNMLYHGGDVYIIDVSQSVEHDHPHA 186
Cdd:COG3642    74 HGDLTTSNILVDDGGVYLIDFGLARYSDPLED 105
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 19-174 8.02e-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 [Multi-domain]  Cd Length: 136  Bit Score: 50.90  E-value: 8.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  19 ISTGKEANVYYAST-PSGESRAIKIYKtsilmfkdrdkyvtgefrfrrgyckgNPRKMVRTWAEKEMRNLCRLKTANIPC 97
Cdd:cd13968     1 MGEGASAKVFWAEGeCTTIGVAVKIGD--------------------------DVNNEEGEDLESEMDILRRLKGLELNI 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  98 PEPIRLRSH----VLLMGFIGKDDMPAPLLKnVQLSESKARELYLQVIQYMRKMYQDaRLVHADLSEFNMLY-HGGDVYI 172
Cdd:cd13968    55 PKVLVTEDVdgpnILLMELVKGGTLIAYTQE-EELDEKDVESIMYQLAECMRLLHSF-HLIHRDLNNDNILLsEDGNVKL 132


                  ..
gi 1039744181 173 ID 174
Cdd:cd13968   133 ID 134
PRK14879 PRK14879
Kae1-associated kinase Bud32;
77-180 4.76e-05

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 44.13  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  77 RTwaEKEMRNLCRLKTANIPCPEP--IRLRSHVLLMGFIgkddmPAPLLKNV-QLSESKARELYLQVIQYMRKMYQdARL 153
Cdd:PRK14879   45 RT--RREARIMSRARKAGVNVPAVyfVDPENFIIVMEYI-----EGEPLKDLiNSNGMEELELSREIGRLVGKLHS-AGI 116

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1039744181 154 VHADLSEFNMLYHGGDVYIID-----VSQSVE 180
Cdd:PRK14879  117 IHGDLTTSNMILSGGKIYLIDfglaeFSKDLE 148
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
82-181 8.46e-04

bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 41.41  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039744181  82 KEMRNLCRLKTANIPCP--EPIRLRSHVLLMGFIGKDDMPAPLLKNVQLSESKARELylqviqymRKMYqDARLVHADLS 159
Cdd:PRK09605  385 AEARLLSEARRAGVPTPviYDVDPEEKTIVMEYIGGKDLKDVLEGNPELVRKVGEIV--------AKLH-KAGIVHGDLT 455

                          90       100
                  ....*....|....*....|....*..
gi 1039744181 160 EFNMLYHGGDVYIID-----VSQSVEH 181
Cdd:PRK09605  456 TSNFIVRDDRLYLIDfglgkYSDLIED 482
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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