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Conserved domains on  [gi|1131742490|ref|NP_001335123|]
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serine/threonine-protein kinase RIO1 isoform 3 [Homo sapiens]

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 ...
 78-267 6.38e-150

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: 424.29  E-value: 6.38e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  78 INGCISTGKEANVYHASTANGESRAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKGNPRKMVKTWAEKEMRNLIRLNTAE 157
Cdd:cd05147     1 INGCISTGKEANVYHATTKNGGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 158 IPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRRMYQDARLVHADLSEFNMLYHGGGVYIID 237
Cdd:cd05147    81 IPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYIID 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1131742490 238 VSQSVEHDHPHALEFLRKDCANVNDFFMRH 267
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 ...
 78-267 6.38e-150

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: 424.29  E-value: 6.38e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  78 INGCISTGKEANVYHASTANGESRAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKGNPRKMVKTWAEKEMRNLIRLNTAE 157
Cdd:cd05147     1 INGCISTGKEANVYHATTKNGGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 158 IPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRRMYQDARLVHADLSEFNMLYHGGGVYIID 237
Cdd:cd05147    81 IPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYIID 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1131742490 238 VSQSVEHDHPHALEFLRKDCANVNDFFMRH 267
Cdd:cd05147   161 VSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO smart00090
RIO-like kinase;
47-283 6.46e-115

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 337.35  E-value: 6.46e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490   47 DKADRATVEQVLDPRTRMILFKMLTRGIITEINGCISTGKEANVYHAS--TANGESRAIKIYKTSILVFKDRDKYVSGEF 124
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHALdfDGSGKERAVKIYRTGTLEFKRRDRYVDGDF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  125 RFRhgYCKGNPRKMVKTWAEKEMRNLIRLNTAEIPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELYLQVI 204
Cdd:smart00090  81 RFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEEFELYDDIL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742490  205 QYMRRMYQDARLVHADLSEFNMLYHGGGVYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMRHSVAVMTVRELFEFVTD 283
Cdd:smart00090 159 EEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDEEELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 89-276 5.12e-98

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: 292.22  E-value: 5.12e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  89 NVYHASTANGESRAIKIYKTSILVFKDRDKYVSGEFRFRHGycKGNPRKMVKTWAEKEMRNLIRLNTAEIPCPEPIMLRS 168
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 169 HVLVMSFIGKDDMPAPLLKNVQLSEskARELYLQVIQYMRRMYQDARLVHADLSEFNMLYHGGGVYIIDVSQSVEHDHPH 248
Cdd:pfam01163  79 HVLVMEFIGKDGVPAPKLKDVELEE--AEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHPN 156

                         170       180
                  ....*....|....*....|....*...
gi 1131742490 249 ALEFLRKDCANVNDFFMRHSVAVMTVRE 276
Cdd:pfam01163 157 ALEFLERDVENIINFFRRKGVDEVDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
36-282 1.06e-90

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 275.91  E-value: 1.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  36 RQKEADMYRIKDKADRATVEQVLDPRTRMILFKMLTRGIITEINGCISTGKEANVYHASTANGESRAIKIYKTSILVFKD 115
Cdd:COG1718     8 REIDKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTATSSFKR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 116 RDKYVSGEFRFRHgycKG--NPRKMVKTWAEKEMRNLIRLNTAEIPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSE 193
Cdd:COG1718    88 MAQYIEGDPRFMG---KGsfGRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVELEP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 194 SKARELYLQVIQYMRRMYqDARLVHADLSEFNMLYHGGGVYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMRHSVAVMT 273
Cdd:COG1718   165 EEAEELYEQLIEYIVRLY-KAGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPELDP 243


                  ....*....
gi 1131742490 274 vRELFEFVT 282
Cdd:COG1718   244 -EELLKEIW 251
PRK14879 PRK14879
Kae1-associated kinase Bud32;
145-237 1.00e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 43.36  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 145 KEMRNLIRLNTAEIPCPEPIM--LRSHVLVMSFIgkddmPAPLLKNVQLS-ESKARELYLQVIQYMRRMYQdARLVHADL 221
Cdd:PRK14879   48 REARIMSRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKDLINSnGMEELELSREIGRLVGKLHS-AGIIHGDL 121

                          90
                  ....*....|....*.
gi 1131742490 222 SEFNMLYHGGGVYIID 237
Cdd:PRK14879  122 TTSNMILSGGKIYLID 137
 
Name Accession Description Interval E-value
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 78-267 6.38e-150

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: 424.29  E-value: 6.38e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  78 INGCISTGKEANVYHASTANGESRAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKGNPRKMVKTWAEKEMRNLIRLNTAE 157
Cdd:cd05147     1 INGCISTGKEANVYHATTKNGGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 158 IPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRRMYQDARLVHADLSEFNMLYHGGGVYIID 237
Cdd:cd05147    81 IPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYIID 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1131742490 238 VSQSVEHDHPHALEFLRKDCANVNDFFMRH 267
Cdd:cd05147   161 VSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO smart00090
RIO-like kinase;
47-283 6.46e-115

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 337.35  E-value: 6.46e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490   47 DKADRATVEQVLDPRTRMILFKMLTRGIITEINGCISTGKEANVYHAS--TANGESRAIKIYKTSILVFKDRDKYVSGEF 124
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHALdfDGSGKERAVKIYRTGTLEFKRRDRYVDGDF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  125 RFRhgYCKGNPRKMVKTWAEKEMRNLIRLNTAEIPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELYLQVI 204
Cdd:smart00090  81 RFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEEFELYDDIL 158

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1131742490  205 QYMRRMYQDARLVHADLSEFNMLYHGGGVYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMRHSVAVMTVRELFEFVTD 283
Cdd:smart00090 159 EEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDEEELFERITG 237
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 78-267 3.77e-106

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: 312.95  E-value: 3.77e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  78 INGCISTGKEANVYHASTANGESRAIKIYKTSILVFKDRDKYVSGEFRFRHGyCKGNPRKMVKTWAEKEMRNLIRLNTAE 157
Cdd:cd05145     1 LGGVISTGKEANVYLARGGDGEPVAVKIYRTSTSSFKKMAKYIEGDPRFESR-RRGNRRKLIFAWARKEFRNLKRLYEAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 158 IPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRRMYQDARLVHADLSEFNMLYHGGGVYIID 237
Cdd:cd05145    80 VRVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVELEEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNILYYDGKPVIID 159

                         170       180       190
                  ....*....|....*....|....*....|
gi 1131742490 238 VSQSVEHDHPHALEFLRKDCANVNDFFMRH 267
Cdd:cd05145   160 VSQAVTLDHPNAEEFLRRDIRNINRFFSRK 189
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 89-276 5.12e-98

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: 292.22  E-value: 5.12e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  89 NVYHASTANGESRAIKIYKTSILVFKDRDKYVSGEFRFRHGycKGNPRKMVKTWAEKEMRNLIRLNTAEIPCPEPIMLRS 168
Cdd:pfam01163   1 NVYHAVSEDGKEVAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVNR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 169 HVLVMSFIGKDDMPAPLLKNVQLSEskARELYLQVIQYMRRMYQDARLVHADLSEFNMLYHGGGVYIIDVSQSVEHDHPH 248
Cdd:pfam01163  79 HVLVMEFIGKDGVPAPKLKDVELEE--AEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHPN 156

                         170       180
                  ....*....|....*....|....*...
gi 1131742490 249 ALEFLRKDCANVNDFFMRHSVAVMTVRE 276
Cdd:pfam01163 157 ALEFLERDVENIINFFRRKGVDEVDERK 184
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 78-266 6.46e-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: 274.63  E-value: 6.46e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  78 INGCISTGKEANVYHASTANGESR------AIKIYKTSILVFKDRDKYVSGEFRFRHGYCKGNPRKMVKTWAEKEMRNLI 151
Cdd:cd05146     1 VNGCISTGKEAVVFHANGGSMEEVllppecAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKEMHNLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 152 RLNTAEIPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELYLQVIQYMRRMYQDARLVHADLSEFNMLYHGG 231
Cdd:cd05146    81 RMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNILWHEG 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1131742490 232 GVYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMR 266
Cdd:cd05146   161 KVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQK 195
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
36-282 1.06e-90

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 275.91  E-value: 1.06e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  36 RQKEADMYRIKDKADRATVEQVLDPRTRMILFKMLTRGIITEINGCISTGKEANVYHASTANGESRAIKIYKTSILVFKD 115
Cdd:COG1718     8 REIDKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLARRPGGELVAAKIYRTATSSFKR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 116 RDKYVSGEFRFRHgycKG--NPRKMVKTWAEKEMRNLIRLNTAEIPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNVQLSE 193
Cdd:COG1718    88 MAQYIEGDPRFMG---KGsfGRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLKDVELEP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 194 SKARELYLQVIQYMRRMYqDARLVHADLSEFNMLYHGGGVYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMRHSVAVMT 273
Cdd:COG1718   165 EEAEELYEQLIEYIVRLY-KAGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARFGPELDP 243


                  ....*....
gi 1131742490 274 vRELFEFVT 282
Cdd:COG1718   244 -EELLKEIW 251
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 78-267 3.43e-32

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: 121.28  E-value: 3.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  78 INGCISTGKEANVYHA-STANGE--SRAIKIYKTSILVFKDRDKYVSGEFRFRHGycKGNPRKMVKTWAEKEMRNLIRLN 154
Cdd:cd05119     1 IGGVISTGKEANVFYAdGVFDGKpvACAVKIYRIETSEFDKVDEYLYGDERFDYR--RISPKEKVFIWTEKEFRNLERAK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 155 TAEIPCPEPIMLRSHVLVMSFIGKDDMPAPLLKNV--QLSESKARELYLQVIQYMRRMYQDARLVHADLSEFNMLYhGGG 232
Cdd:cd05119    79 EAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELgrELKELDVEGIFNDVVENVKRLYQEAELVHADLSEYNILY-IDK 157

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1131742490 233 VYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMRH 267
Cdd:cd05119   158 VYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSKY 192
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 82-267 4.48e-27

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: 106.82  E-value: 4.48e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490  82 ISTGKEANVYHASTANGESRAIKIYK---TSilvFKdRDKYVSGEFRFRHGYckgnprkmvkTW-------AEKEMRNLI 151
Cdd:cd05144     8 IGVGKESDVYLALDEDGNPVVLKFHRlgrTS---FR-KVKRKRDYLKHRKHA----------SWlylsrlaAEKEFAALK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 152 RLNTAEIPCPEPIMLRSHVLVMSFIgkddmPAPLLKNVQLSEsKARELYLQVIQYMRRMYQdARLVHADLSEFN-MLYHG 230
Cdd:cd05144    74 ALYEEGFPVPKPIDWNRHAVVMELI-----DGYPLYQVRLLE-DPEEVLDEILELIVKLAK-HGLIHGDFSEFNiLVDED 146

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1131742490 231 GGVYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMRH 267
Cdd:cd05144   147 EKITVIDFPQMVSTSHPNAEEYFDRDVECIIKFFRRK 183
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 143-283 8.00e-24

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: 98.05  E-value: 8.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 143 AEKEMRNLIRLNTAEIPCPEPIMLRSHVLVMSFIgkddmPAPLLKNVQLSESKarELYLQVIQYMRRMYqDARLVHADLS 222
Cdd:COG0478    46 AEREFRALERLYPAGLPVPRPIAANRHAIVMERI-----EGVELARLKLEDPE--EVLDKILEEIRRAH-DAGIVHADLS 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1131742490 223 EFN-MLYHGGGVYIIDVSQSVEHDHPHALEFLRKDCANVNDFFMRHSVAVMTVRELFEFVTD 283
Cdd:COG0478   118 EYNiLVDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSFRKKYGLEVDLDEVWAALLG 179
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 143-249 2.93e-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: 55.74  E-value: 2.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 143 AEKEMRNLIRLNTAEIPCPEPI--MLRSHVLVMSFIgkddmPAPLLKNVQLSESKARELYLQVIQYMRRMYqDARLVHAD 220
Cdd:COG3642     3 TRREARLLRELREAGVPVPKVLdvDPDDADLVMEYI-----EGETLADLLEEGELPPELLRELGRLLARLH-RAGIVHGD 76

                          90       100
                  ....*....|....*....|....*....
gi 1131742490 221 LSEFNMLYHGGGVYIIDVSQSVEHDHPHA 249
Cdd:COG3642    77 LTTSNILVDDGGVYLIDFGLARYSDPLED 105
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 112-237 1.13e-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: 53.60  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 112 VFKDRDKYVSGEFRFRHGYCKGNPrkmVKTWAEKEMRNLIRLNTAEIPCPEPIMLRS----HVLVMSFIGKDDMPAPLLK 187
Cdd:cd13968     9 VFWAEGECTTIGVAVKIGDDVNNE---EGEDLESEMDILRRLKGLELNIPKVLVTEDvdgpNILLMELVKGGTLIAYTQE 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1131742490 188 nVQLSESKARELYLQVIQYMRRMYQDaRLVHADLSEFNMLY-HGGGVYIID 237
Cdd:cd13968    86 -EELDEKDVESIMYQLAECMRLLHSF-HLIHRDLNNDNILLsEDGNVKLID 134
PRK14879 PRK14879
Kae1-associated kinase Bud32;
145-237 1.00e-04

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 43.36  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 145 KEMRNLIRLNTAEIPCPEPIM--LRSHVLVMSFIgkddmPAPLLKNVQLS-ESKARELYLQVIQYMRRMYQdARLVHADL 221
Cdd:PRK14879   48 REARIMSRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKDLINSnGMEELELSREIGRLVGKLHS-AGIIHGDL 121

                          90
                  ....*....|....*.
gi 1131742490 222 SEFNMLYHGGGVYIID 237
Cdd:PRK14879  122 TTSNMILSGGKIYLID 137
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
161-244 2.10e-03

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 40.64  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1131742490 161 PEPIM----LRSHVLVMSFIGKDDMPAPLLKNVQLSESKARELylqviqymRRMYqDARLVHADLSEFNMLYHGGGVYII 236
Cdd:PRK09605  399 PTPVIydvdPEEKTIVMEYIGGKDLKDVLEGNPELVRKVGEIV--------AKLH-KAGIVHGDLTTSNFIVRDDRLYLI 469

                          90
                  ....*....|...
gi 1131742490 237 D-----VSQSVEH 244
Cdd:PRK09605  470 DfglgkYSDLIED 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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