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Conserved domains on  [gi|157822659|ref|NP_001101893|]
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serine/threonine-protein kinase RIO3 [Rattus norvegicus]

Protein Classification

serine/threonine-protein kinase RIO3( domain architecture ID 10142321)

serine/threonine-protein kinase RIO3 is an atypical protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 253-453 4.33e-150

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: 427.17  E-value: 4.33e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 253 ITGCISTGKESVVFHAYGGSLEDekedgKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 332
Cdd:cd05146    1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 333 MHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLSEEEMKDAYHQTLHLMQQLYKECTLVHADLSEYNM 412
Cdd:cd05146   76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157822659 413 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:cd05146  156 LWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
 
Name Accession Description Interval E-value
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 253-453 4.33e-150

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: 427.17  E-value: 4.33e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 253 ITGCISTGKESVVFHAYGGSLEDekedgKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 332
Cdd:cd05146    1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 333 MHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLSEEEMKDAYHQTLHLMQQLYKECTLVHADLSEYNM 412
Cdd:cd05146   76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157822659 413 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:cd05146  156 LWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO smart00090
RIO-like kinase;
222-470 4.62e-117

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 344.67  E-value: 4.62e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659   222 EKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYggsledekeDGKVIPTECAIKVFKTTLNEFKN 301
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAL---------DFDGSGKERAVKIYRTGTLEFKR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659   302 RDKYIKDDFRFKdrFSKLNPRKIIRMWAEKEMHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLSEEE 381
Cdd:smart00090  72 RDRYVDGDFRFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659   382 MKDAYHQTLHLMQQLYKECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEALnE 461
Cdd:smart00090 150 EFELYDDILEEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELD-E 228


                   ....*....
gi 157822659   462 RELFNAVSG 470
Cdd:smart00090 229 EELFERITG 237
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 264-457 7.13e-89

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: 270.64  E-value: 7.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659  264 VVFHAYGgsledekEDGKviptECAIKVFKTTLNEFKNRDKYIKDDFRFKDRfsKLNPRKIIRMWAEKEMHNLTRMQKAG 343
Cdd:pfam01163   1 NVYHAVS-------EDGK----EVAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659  344 IPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLseEEMKDAYHQTLHLMQQLYKECTLVHADLSEYNMLWHAGKVWLID 423
Cdd:pfam01163  68 VPVPKPIDVNRHVLVMEFIGKDGVPAPKLKDVEL--EEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIID 145

                         170       180       190
                  ....*....|....*....|....*....|....
gi 157822659  424 VSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKE 457
Cdd:pfam01163 146 VPQAVETDHPNALEFLERDVENIINFFRRKGVDE 179
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
214-468 9.03e-73

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 231.62  E-value: 9.03e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 214 ERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAyggsledEKEDGKVIptecAIKVFK 293
Cdd:COG1718   11 DKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLA-------RRPGGELV----AAKIYR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 294 TTLNEFKNRDKYIKDDFRFKDRFSKlNPRKIIRMWAEKEMHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLK 373
Cdd:COG1718   80 TATSSFKRMAQYIEGDPRFMGKGSF-GRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 374 EVKLSEEEMKDAYHQTLHLMQQLYKeCTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:COG1718  159 DVELEPEEAEELYEQLIEYIVRLYK-AGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237

                        250
                 ....*....|....*
gi 157822659 454 GVKeaLNERELFNAV 468
Cdd:COG1718  238 GPE--LDPEELLKEI 250
PRK14879 PRK14879
Kae1-associated kinase Bud32;
302-441 1.06e-07

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 52.60  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 302 RDKYIKDDFRFKDRFSK--LNPR---KIIRMWAEKEMHNLTRMQKAGIPCPTVVL--LKKHILVMSFIghdqvPAPKLKE 374
Cdd:PRK14879  14 LGDFLGIKAVIKWRIPKryRHPEldeRIRRERTRREARIMSRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 375 VkLSEEEM------KDAYHQT--LHlmqqlykECTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP----------- 430
Cdd:PRK14879  89 L-INSNGMeelelsREIGRLVgkLH-------SAGIIHGDLTTSNMILSGGKIYLIDfglaeFSKDLEDravdlhvllrs 160

                        170
                 ....*....|....
gi 157822659 431 ---THPHGLEFLFR 441
Cdd:PRK14879 161 lesTHPDWAEELFE 174
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 322-430 5.44e-06

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


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 47.20  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659  322 RKIIRMWAEKEMHNLTRMQKAGIPCPTV--VLLKKHILVMSFIghdqvPAPKLKEV--KLSEEEMKDAYHQ--TLHlmqq 395
Cdd:TIGR03724  37 ERLRKERTRREARLLSRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDVieENGDELAREIGRLvgKLH---- 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 157822659  396 lykECTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP 430
Cdd:TIGR03724 108 ---KAGIVHGDLTTSNIIVRDDKVYLIDfglgkYSDEIED 144
 
Name Accession Description Interval E-value
RIO3_euk cd05146
Catalytic domain of the atypical protein serine kinase, RIO3 kinase; RIO3 is present only in ...
 253-453 4.33e-150

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: 427.17  E-value: 4.33e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 253 ITGCISTGKESVVFHAYGGSLEDekedgKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 332
Cdd:cd05146    1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 333 MHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLSEEEMKDAYHQTLHLMQQLYKECTLVHADLSEYNM 412
Cdd:cd05146   76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 157822659 413 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:cd05146  156 LWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO smart00090
RIO-like kinase;
222-470 4.62e-117

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 344.67  E-value: 4.62e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659   222 EKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYggsledekeDGKVIPTECAIKVFKTTLNEFKN 301
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAL---------DFDGSGKERAVKIYRTGTLEFKR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659   302 RDKYIKDDFRFKdrFSKLNPRKIIRMWAEKEMHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLSEEE 381
Cdd:smart00090  72 RDRYVDGDFRFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659   382 MKDAYHQTLHLMQQLYKECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEALnE 461
Cdd:smart00090 150 EFELYDDILEEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDELD-E 228


                   ....*....
gi 157822659   462 RELFNAVSG 470
Cdd:smart00090 229 EELFERITG 237
RIO1_euk cd05147
Catalytic domain of the atypical protein serine kinase, Eukaryotic RIO1 kinase; RIO1 is ...
 253-452 1.77e-103

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: 307.96  E-value: 1.77e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 253 ITGCISTGKESVVFHAYGGSledekedgkviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 332
Cdd:cd05147    1 INGCISTGKEANVYHATTKN-----------GGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 333 MHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLSEEEMKDAYHQTLHLMQQLYKECTLVHADLSEYNM 412
Cdd:cd05147   70 MRNLKRLNQAGIPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNL 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 157822659 413 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 452
Cdd:cd05147  150 LYHKGKVYIIDVSQSVEHDHPHALEFLRRDCVNVNDFFRK 189
RIO1_like cd05145
Catalytic domain of the atypical protein serine kinases, RIO1 and RIO3 kinases and similar ...
 253-452 1.08e-97

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: 293.30  E-value: 1.08e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 253 ITGCISTGKESVVFHAYGGSledekedgkviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRfSKLNPRKIIRMWAEKE 332
Cdd:cd05145    1 LGGVISTGKEANVYLARGGD-----------GEPVAVKIYRTSTSSFKKMAKYIEGDPRFESR-RRGNRRKLIFAWARKE 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 333 MHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLSEEEMKDAYHQTLHLMQQLYKECTLVHADLSEYNM 412
Cdd:cd05145   69 FRNLKRLYEAGVRVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVELEEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNI 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 157822659 413 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 452
Cdd:cd05145  149 LYYDGKPVIIDVSQAVTLDHPNAEEFLRRDIRNINRFFSR 188
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
 264-457 7.13e-89

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: 270.64  E-value: 7.13e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659  264 VVFHAYGgsledekEDGKviptECAIKVFKTTLNEFKNRDKYIKDDFRFKDRfsKLNPRKIIRMWAEKEMHNLTRMQKAG 343
Cdd:pfam01163   1 NVYHAVS-------EDGK----EVAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659  344 IPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLseEEMKDAYHQTLHLMQQLYKECTLVHADLSEYNMLWHAGKVWLID 423
Cdd:pfam01163  68 VPVPKPIDVNRHVLVMEFIGKDGVPAPKLKDVEL--EEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIID 145

                         170       180       190
                  ....*....|....*....|....*....|....
gi 157822659  424 VSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKE 457
Cdd:pfam01163 146 VPQAVETDHPNALEFLERDVENIINFFRRKGVDE 179
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
214-468 9.03e-73

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 231.62  E-value: 9.03e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 214 ERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAyggsledEKEDGKVIptecAIKVFK 293
Cdd:COG1718   11 DKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLA-------RRPGGELV----AAKIYR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 294 TTLNEFKNRDKYIKDDFRFKDRFSKlNPRKIIRMWAEKEMHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLK 373
Cdd:COG1718   80 TATSSFKRMAQYIEGDPRFMGKGSF-GRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 374 EVKLSEEEMKDAYHQTLHLMQQLYKeCTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:COG1718  159 DVELEPEEAEELYEQLIEYIVRLYK-AGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237

                        250
                 ....*....|....*
gi 157822659 454 GVKeaLNERELFNAV 468
Cdd:COG1718  238 GPE--LDPEELLKEI 250
RIO cd05119
Catalytic domain of the atypical protein serine kinases, RIO kinases; RIO kinases are atypical ...
 253-452 2.72e-38

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: 138.62  E-value: 2.72e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 253 ITGCISTGKESVVFHAYGgsledeKEDGKviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRfsKLNPRKIIRMWAEKE 332
Cdd:cd05119    1 IGGVISTGKEANVFYADG------VFDGK--PVACAVKIYRIETSEFDKVDEYLYGDERFDYR--RISPKEKVFIWTEKE 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 333 MHNLTRMQKAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVK--LSEEEMKDAYHQTLHLMQQLYKECTLVHADLSEY 410
Cdd:cd05119   71 FRNLERAKEAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELGreLKELDVEGIFNDVVENVKRLYQEAELVHADLSEY 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 157822659 411 NMLWhAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 452
Cdd:cd05119  151 NILY-IDKVYFIDFGQAVTLRHPGAESYLERDVRNIIRFFSK 191
RIO2_C cd05144
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ...
 250-452 1.50e-24

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: 100.66  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 250 LETITGCISTGKESVVFHAYGgsledekEDGKviptECAIKV-------FKTTLNefkNRDkYIKDdfrfKDRFSKLNpr 322
Cdd:cd05144    1 ISSVGNQIGVGKESDVYLALD-------EDGN----PVVLKFhrlgrtsFRKVKR---KRD-YLKH----RKHASWLY-- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 323 kIIRMWAEKEMHNLTRMQKAGIPCPTVVLLKKHILVMSFIghdqvPAPKLKEVKLSEEEMKdAYHQTLHLMQQLYKeCTL 402
Cdd:cd05144   60 -LSRLAAEKEFAALKALYEEGFPVPKPIDWNRHAVVMELI-----DGYPLYQVRLLEDPEE-VLDEILELIVKLAK-HGL 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157822659 403 VHADLSEYN-MLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 452
Cdd:cd05144  132 IHGDFSEFNiLVDEDEKITVIDFPQMVSTSHPNAEEYFDRDVECIIKFFRR 182
RIO2 COG0478
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ...
 304-452 6.02e-22

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: 93.05  E-value: 6.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 304 KYIKDDFRFKDRFSKLN-PRKIirmwAEKEMHNLTRMQKAGIPCPTVVLLKKHILVMSFIghdqvPAPKLKEVKLSEEEm 382
Cdd:COG0478   24 RKVRRERADKEHYSWLYaARTR----AEREFRALERLYPAGLPVPRPIAANRHAIVMERI-----EGVELARLKLEDPE- 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822659 383 kDAYHQTLHLMQQLYkECTLVHADLSEYN-MLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 452
Cdd:COG0478   94 -EVLDKILEEIRRAH-DAGIVHADLSEYNiLVDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSFRK 162
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 326-427 6.71e-10

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: 57.66  E-value: 6.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 326 RMWAEKEMhnLTRMQKAGIPCPTVVLLKKH--ILVMSFIghdqvPAPKLKEVKLSEEEMKDAYHQTLHLMQQLYKeCTLV 403
Cdd:COG3642    2 RTRREARL--LRELREAGVPVPKVLDVDPDdaDLVMEYI-----EGETLADLLEEGELPPELLRELGRLLARLHR-AGIV 73

                         90       100
                 ....*....|....*....|....
gi 157822659 404 HADLSEYNMLWHAGKVWLIDVSQS 427
Cdd:COG3642   74 HGDLTTSNILVDDGGVYLIDFGLA 97
PRK14879 PRK14879
Kae1-associated kinase Bud32;
302-441 1.06e-07

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 52.60  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 302 RDKYIKDDFRFKDRFSK--LNPR---KIIRMWAEKEMHNLTRMQKAGIPCPTVVL--LKKHILVMSFIghdqvPAPKLKE 374
Cdd:PRK14879  14 LGDFLGIKAVIKWRIPKryRHPEldeRIRRERTRREARIMSRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 375 VkLSEEEM------KDAYHQT--LHlmqqlykECTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP----------- 430
Cdd:PRK14879  89 L-INSNGMeelelsREIGRLVgkLH-------SAGIIHGDLTTSNMILSGGKIYLIDfglaeFSKDLEDravdlhvllrs 160

                        170
                 ....*....|....
gi 157822659 431 ---THPHGLEFLFR 441
Cdd:PRK14879 161 lesTHPDWAEELFE 174
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 322-430 5.44e-06

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


Pssm-ID: 274749 [Multi-domain]  Cd Length: 199  Bit Score: 47.20  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659  322 RKIIRMWAEKEMHNLTRMQKAGIPCPTV--VLLKKHILVMSFIghdqvPAPKLKEV--KLSEEEMKDAYHQ--TLHlmqq 395
Cdd:TIGR03724  37 ERLRKERTRREARLLSRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDVieENGDELAREIGRLvgKLH---- 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 157822659  396 lykECTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP 430
Cdd:TIGR03724 108 ---KAGIVHGDLTTSNIIVRDDKVYLIDfglgkYSDEIED 144
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 332-423 3.86e-05

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


Pssm-ID: 270700 [Multi-domain]  Cd Length: 152  Bit Score: 43.70  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 332 EMHNLTRMQKAGIpCPTVVLL--KKHILVMSFIghdqvPAPKLKEVKLSEEEMKdayHQTLHLMQQL----YKECTLVHA 405
Cdd:cd05151   42 EKANSKAAAELGI-APEVIYFdpETGVKITEFI-----EGATLLTNDFSDPENL---ERIAALLRKLhsspLEDLVLCHN 112

                         90
                 ....*....|....*...
gi 157822659 406 DLSEYNMLWHAGKVWLID 423
Cdd:cd05151  113 DLVPGNFLLDDDRLYLID 130
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 326-423 4.69e-05

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: 43.20  E-value: 4.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 326 RMWAEKEMHNLTRMQKAGIPCPTVVLLKKH----ILVMSFIGHDQVPAPkLKEVKLSEEEMKDAYHQTLHLMQQLYKEcT 401
Cdd:cd13968   34 GEDLESEMDILRRLKGLELNIPKVLVTEDVdgpnILLMELVKGGTLIAY-TQEEELDEKDVESIMYQLAECMRLLHSF-H 111

                         90       100
                 ....*....|....*....|...
gi 157822659 402 LVHADLSEYN-MLWHAGKVWLID 423
Cdd:cd13968  112 LIHRDLNNDNiLLSEDGNVKLID 134
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
301-429 2.18e-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: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822659 301 NRDKYIKDDFRFKDRFSKL--NP---RKIIRMWAEKEMHNLTRMQKAGIPCPTV--VLLKKHILVMSFIGhdqvpAPKLK 373
Cdd:PRK09605 350 KKGEYLGRDAVIKERVPKGyrHPeldERLRTERTRAEARLLSEARRAGVPTPVIydVDPEEKTIVMEYIG-----GKDLK 424

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822659 374 EV-KLSEEEMKDAYHQ--TLHlmqqlykECTLVHADLSEYNMLWHAGKVWLID-----VSQSVE 429
Cdd:PRK09605 425 DVlEGNPELVRKVGEIvaKLH-------KAGIVHGDLTTSNFIVRDDRLYLIDfglgkYSDLIE 481
 
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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