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Conserved domains on  [gi|21356879|ref|NP_648489|]
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RIO kinase 1, isoform A [Drosophila melanogaster]

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

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 ...
205-395 2.61e-143

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: 2.61e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 205 INGCISTGKEANVYHAVSKNGEEeFAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVRTWAEKEMRNYLRMRNA 284
Cdd:cd05147   1 INGCISTGKEANVYHATTKNGGE-LAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 285 GVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDVELSTSKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDGQLVII 364
Cdd:cd05147  80 GIPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYII 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 21356879 365 DVSQSVEHDHPHSFDFLRKDCTNISEFFRKR 395
Cdd:cd05147 160 DVSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
 
Name Accession Description Interval E-value
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
205-395 2.61e-143

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: 2.61e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 205 INGCISTGKEANVYHAVSKNGEEeFAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVRTWAEKEMRNYLRMRNA 284
Cdd:cd05147   1 INGCISTGKEANVYHATTKNGGE-LAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 285 GVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDVELSTSKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDGQLVII 364
Cdd:cd05147  80 GIPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYII 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 21356879 365 DVSQSVEHDHPHSFDFLRKDCTNISEFFRKR 395
Cdd:cd05147 160 DVSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO smart00090
RIO-like kinase;
174-411 2.71e-111

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 332.34  E-value: 2.71e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879    174 DKHDRATAEQVMDPRTRMILFKLLNRGMIQEINGCISTGKEANVYHAVSKNGE-EEFAIKIYKTSILVFKDRDKYVSGEF 252
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHALDFDGSgKERAVKIYRTGTLEFKRRDRYVDGDF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879    253 RFRhgYCKHNPRKMVRTWAEKEMRNYLRMRNAGVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDVELSTSKARELYRDCV 332
Cdd:smart00090  81 RFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEEFELYDDIL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356879    333 VIMWRIYNQCRLVHADLSEFNILLQDGQLVIIDVSQSVEHDHPHSFDFLRKDCTNISEFFRKRAVATMTVKELFDFITD 411
Cdd:smart00090 159 EEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDEEELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
216-404 3.92e-97

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: 293.76  E-value: 3.92e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879   216 NVYHAVSKNGEEeFAIKIYKTSILVFKDRDKYVSGEFRFRHGycKHNPRKMVRTWAEKEMRNYLRMRNAGVPVPEPILLR 295
Cdd:pfam01163   1 NVYHAVSEDGKE-VAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879   296 SHVLVMRFCGRDGWPAPKLKDVELStsKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDGQLVIIDVSQSVEHDHP 375
Cdd:pfam01163  78 RHVLVMEFIGKDGVPAPKLKDVELE--EAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHP 155
                         170       180
                  ....*....|....*....|....*....
gi 21356879   376 HSFDFLRKDCTNISEFFRKRAVATMTVKE 404
Cdd:pfam01163 156 NALEFLERDVENIINFFRRKGVDEVDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
153-410 1.71e-80

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 253.19  E-value: 1.71e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 153 MSAQAANRLVnfdRRDRTQVRDKHDRATAEQVMDPRTRMILFKLLNRGMIQEINGCISTGKEANVYHAVSKnGEEEFAIK 232
Cdd:COG1718   1 MKDRRLDREI---DKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLARRP-GGELVAAK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 233 IYKTSILVFKDRDKYVSGEFRFRHgycK--HNPRKMVRTWAEKEMRNYLRMRNAGVPVPEPILLRSHVLVMRFCGRDGWP 310
Cdd:COG1718  77 IYRTATSSFKRMAQYIEGDPRFMG---KgsFGRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 311 APKLKDVELSTSKARELYRDCVVIMWRIYNqCRLVHADLSEFNILLQDGQLVIIDVSQSVEHDHPHSFDFLRKDCTNISE 390
Cdd:COG1718 154 APRLKDVELEPEEAEELYEQLIEYIVRLYK-AGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIAR 232
                       250       260
                ....*....|....*....|
gi 21356879 391 FFRKRAVATMTvKELFDFIT 410
Cdd:COG1718 233 FFARFGPELDP-EELLKEIW 251
PRK14879 PRK14879
Kae1-associated kinase Bud32;
209-371 1.46e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 40.28  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879  209 ISTGKEANVYHAvskngeEEFAIKIyktsilVFKDR-DKyvsgefRFRHGYCKHNPRKMvRTwaEKEMRNYLRMRNAGVP 287
Cdd:PRK14879   4 IKRGAEAEIYLG------DFLGIKA------VIKWRiPK------RYRHPELDERIRRE-RT--RREARIMSRARKAGVN 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879  288 VPEPIL--LRSHVLVMRFCgrDGwpaPKLKDV-ELSTSKARELYRDCVVIMWRIYNQcRLVHADLSEFNILLQDGQLVII 364
Cdd:PRK14879  63 VPAVYFvdPENFIIVMEYI--EG---EPLKDLiNSNGMEELELSREIGRLVGKLHSA-GIIHGDLTTSNMILSGGKIYLI 136
                        170
                 ....*....|..
gi 21356879  365 D-----VSQSVE 371
Cdd:PRK14879 137 DfglaeFSKDLE 148
 
Name Accession Description Interval E-value
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
205-395 2.61e-143

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: 2.61e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 205 INGCISTGKEANVYHAVSKNGEEeFAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVRTWAEKEMRNYLRMRNA 284
Cdd:cd05147   1 INGCISTGKEANVYHATTKNGGE-LAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKEMRNLKRLNQA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 285 GVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDVELSTSKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDGQLVII 364
Cdd:cd05147  80 GIPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNLLYHKGKVYII 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 21356879 365 DVSQSVEHDHPHSFDFLRKDCTNISEFFRKR 395
Cdd:cd05147 160 DVSQSVEHDHPHALEFLRRDCVNVNDFFRKK 190
RIO smart00090
RIO-like kinase;
174-411 2.71e-111

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 332.34  E-value: 2.71e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879    174 DKHDRATAEQVMDPRTRMILFKLLNRGMIQEINGCISTGKEANVYHAVSKNGE-EEFAIKIYKTSILVFKDRDKYVSGEF 252
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHALDFDGSgKERAVKIYRTGTLEFKRRDRYVDGDF 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879    253 RFRhgYCKHNPRKMVRTWAEKEMRNYLRMRNAGVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDVELSTSKARELYRDCV 332
Cdd:smart00090  81 RFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEEEFELYDDIL 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21356879    333 VIMWRIYNQCRLVHADLSEFNILLQDGQLVIIDVSQSVEHDHPHSFDFLRKDCTNISEFFRKRAVATMTVKELFDFITD 411
Cdd:smart00090 159 EEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELDEEELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
216-404 3.92e-97

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: 293.76  E-value: 3.92e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879   216 NVYHAVSKNGEEeFAIKIYKTSILVFKDRDKYVSGEFRFRHGycKHNPRKMVRTWAEKEMRNYLRMRNAGVPVPEPILLR 295
Cdd:pfam01163   1 NVYHAVSEDGKE-VAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAGVPVPKPIDVN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879   296 SHVLVMRFCGRDGWPAPKLKDVELStsKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDGQLVIIDVSQSVEHDHP 375
Cdd:pfam01163  78 RHVLVMEFIGKDGVPAPKLKDVELE--EAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIIDVPQAVETDHP 155
                         170       180
                  ....*....|....*....|....*....
gi 21356879   376 HSFDFLRKDCTNISEFFRKRAVATMTVKE 404
Cdd:pfam01163 156 NALEFLERDVENIINFFRRKGVDEVDERK 184
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
205-395 6.39e-93

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: 283.29  E-value: 6.39e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 205 INGCISTGKEANVYHAVSKNGEEeFAIKIYKTSILVFKDRDKYVSGEFRFRHGyCKHNPRKMVRTWAEKEMRNYLRMRNA 284
Cdd:cd05145   1 LGGVISTGKEANVYLARGGDGEP-VAVKIYRTSTSSFKKMAKYIEGDPRFESR-RRGNRRKLIFAWARKEFRNLKRLYEA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 285 GVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDVELSTSKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDGQLVII 364
Cdd:cd05145  79 GVRVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVELEEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNILYYDGKPVII 158
                       170       180       190
                ....*....|....*....|....*....|.
gi 21356879 365 DVSQSVEHDHPHSFDFLRKDCTNISEFFRKR 395
Cdd:cd05145 159 DVSQAVTLDHPNAEEFLRRDIRNINRFFSRK 189
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
205-395 2.09e-89

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: 274.24  E-value: 2.09e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 205 INGCISTGKEANVYHAVSKNGEE-----EFAIKIYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVRTWAEKEMRNYL 279
Cdd:cd05146   1 VNGCISTGKEAVVFHANGGSMEEvllppECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKEMHNLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 280 RMRNAGVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDVELSTSKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDG 359
Cdd:cd05146  81 RMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNILWHEG 160
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 21356879 360 QLVIIDVSQSVEHDHPHSFDFLRKDCTNISEFFRKR 395
Cdd:cd05146 161 KVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
153-410 1.71e-80

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 253.19  E-value: 1.71e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 153 MSAQAANRLVnfdRRDRTQVRDKHDRATAEQVMDPRTRMILFKLLNRGMIQEINGCISTGKEANVYHAVSKnGEEEFAIK 232
Cdd:COG1718   1 MKDRRLDREI---DKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLARRP-GGELVAAK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 233 IYKTSILVFKDRDKYVSGEFRFRHgycK--HNPRKMVRTWAEKEMRNYLRMRNAGVPVPEPILLRSHVLVMRFCGRDGWP 310
Cdd:COG1718  77 IYRTATSSFKRMAQYIEGDPRFMG---KgsFGRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 311 APKLKDVELSTSKARELYRDCVVIMWRIYNqCRLVHADLSEFNILLQDGQLVIIDVSQSVEHDHPHSFDFLRKDCTNISE 390
Cdd:COG1718 154 APRLKDVELEPEEAEELYEQLIEYIVRLYK-AGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIAR 232
                       250       260
                ....*....|....*....|
gi 21356879 391 FFRKRAVATMTvKELFDFIT 410
Cdd:COG1718 233 FFARFGPELDP-EELLKEIW 251
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
205-394 6.28e-30

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: 116.28  E-value: 6.28e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 205 INGCISTGKEANVYHAVSKNGEE--EFAIKIYKTSILVFKDRDKYVSGEFRFRHGycKHNPRKMVRTWAEKEMRNYLRMR 282
Cdd:cd05119   1 IGGVISTGKEANVFYADGVFDGKpvACAVKIYRIETSEFDKVDEYLYGDERFDYR--RISPKEKVFIWTEKEFRNLERAK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 283 NAGVPVPEPILLRSHVLVMRFCGRDGWPAPKLKDV--ELSTSKARELYRDCVVIMWRIYNQCRLVHADLSEFNILLQDGq 360
Cdd:cd05119  79 EAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELgrELKELDVEGIFNDVVENVKRLYQEAELVHADLSEYNILYIDK- 157
                       170       180       190
                ....*....|....*....|....*....|....
gi 21356879 361 LVIIDVSQSVEHDHPHSFDFLRKDCTNISEFFRK 394
Cdd:cd05119 158 VYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
209-395 2.99e-28

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: 111.44  E-value: 2.99e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 209 ISTGKEANVYHAVSKNGEEeFAIKIYK---TSilvFKdrdkyvsgEFRFRHGYCKHNPRK----MVRTWAEKEMRNYLRM 281
Cdd:cd05144   8 IGVGKESDVYLALDEDGNP-VVLKFHRlgrTS---FR--------KVKRKRDYLKHRKHAswlyLSRLAAEKEFAALKAL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 282 RNAGVPVPEPILLRSHVLVMRFCgrDGWPAPKLKDVElstsKARELYRDCVVIMWRIYNqCRLVHADLSEFNILL-QDGQ 360
Cdd:cd05144  76 YEEGFPVPKPIDWNRHAVVMELI--DGYPLYQVRLLE----DPEEVLDEILELIVKLAK-HGLIHGDFSEFNILVdEDEK 148
                       170       180       190
                ....*....|....*....|....*....|....*
gi 21356879 361 LVIIDVSQSVEHDHPHSFDFLRKDCTNISEFFRKR 395
Cdd:cd05144 149 ITVIDFPQMVSTSHPNAEEYFDRDVECIIKFFRRK 183
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
268-411 2.58e-23

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: 97.28  E-value: 2.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 268 RTWAEKEMRNYLRMRNAGVPVPEPILLRSHVLVMRfcgrdgwpapKLKDVELSTSKAR---ELYRDCVVIMWRIYNqCRL 344
Cdd:COG0478  43 RTRAEREFRALERLYPAGLPVPRPIAANRHAIVME----------RIEGVELARLKLEdpeEVLDKILEEIRRAHD-AGI 111
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21356879 345 VHADLSEFNILLQ-DGQLVIIDVSQSVEHDHPHSFDFLRKDCTNISEFFRKRAVATMTVKELFDFITD 411
Cdd:COG0478 112 VHADLSEYNILVDdDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSFRKKYGLEVDLDEVWAALLG 179
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
268-375 9.02e-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: 9.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 268 RTWAEkeMRNYLRMRNAGVPVPEPILLRSH--VLVMRFCgrdgwPAPKLKDVELSTSKARELYRDCVVIMWRIYNqCRLV 345
Cdd:COG3642   2 RTRRE--ARLLRELREAGVPVPKVLDVDPDdaDLVMEYI-----EGETLADLLEEGELPPELLRELGRLLARLHR-AGIV 73
                        90       100       110
                ....*....|....*....|....*....|
gi 21356879 346 HADLSEFNILLQDGQLVIIDVSQSVEHDHP 375
Cdd:COG3642  74 HGDLTTSNILVDDGGVYLIDFGLARYSDPL 103
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
209-365 1.69e-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: 53.21  E-value: 1.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 209 ISTGKEANVYHAVSKNGEEEFAIKIYKtsilvfkdrdkyvsgefrfrhgyckhNPRKMVRTWAEKEMRNYLRMRNAGVPV 288
Cdd:cd13968   1 MGEGASAKVFWAEGECTTIGVAVKIGD--------------------------DVNNEEGEDLESEMDILRRLKGLELNI 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 289 PEPILLRS----HVLVMRFCGRDGWPAPKLKdVELSTSKARELYRDCVVIMWRIYnQCRLVHADLSEFNILL-QDGQLVI 363
Cdd:cd13968  55 PKVLVTEDvdgpNILLMELVKGGTLIAYTQE-EELDEKDVESIMYQLAECMRLLH-SFHLIHRDLNNDNILLsEDGNVKL 132

                ..
gi 21356879 364 ID 365
Cdd:cd13968 133 ID 134
PRK14879 PRK14879
Kae1-associated kinase Bud32;
209-371 1.46e-03

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 40.28  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879  209 ISTGKEANVYHAvskngeEEFAIKIyktsilVFKDR-DKyvsgefRFRHGYCKHNPRKMvRTwaEKEMRNYLRMRNAGVP 287
Cdd:PRK14879   4 IKRGAEAEIYLG------DFLGIKA------VIKWRiPK------RYRHPELDERIRRE-RT--RREARIMSRARKAGVN 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879  288 VPEPIL--LRSHVLVMRFCgrDGwpaPKLKDV-ELSTSKARELYRDCVVIMWRIYNQcRLVHADLSEFNILLQDGQLVII 364
Cdd:PRK14879  63 VPAVYFvdPENFIIVMEYI--EG---EPLKDLiNSNGMEELELSREIGRLVGKLHSA-GIIHGDLTTSNMILSGGKIYLI 136
                        170
                 ....*....|..
gi 21356879  365 D-----VSQSVE 371
Cdd:PRK14879 137 DfglaeFSKDLE 148
ABC1_ADCK3-like cd05121
Activator of bc1 complex (ABC1) kinases (also called aarF domain containing kinase 3) and ...
217-365 7.68e-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: 38.25  E-value: 7.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 217 VYHAVSKNGEEeFAIKI--------YKTSILVFKDRDKYVSGEFRFRHGYckhNPRKMVRTWAE---------KEMRNYL 279
Cdd:cd05121  46 VHRARLKDGRE-VAVKVqrpgieeiIEADLRILRRLARLLERLSPLLRRL---DLVAIVDEFARslleeldfrREARNAE 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21356879 280 RMR-----NAGVPVPEPI--LLRSHVLVMRFCgrDGWpapKLKDVELSTSKARELyRDCVVIMWRIY----NQCRLVHAD 348
Cdd:cd05121 122 RFRknlkdSPDVYVPKVYpeLSTRRVLVMEYI--DGV---KLTDLEALRAAGIDR-KELARRLVDAYlkqiFEDGFFHAD 195
                       170
                ....*....|....*...
gi 21356879 349 LSEFNIL-LQDGQLVIID 365
Cdd:cd05121 196 PHPGNILvLPDGRIALLD 213
 
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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