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Conserved domains on  [gi|22325377|ref|NP_003822|]
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serine/threonine-protein kinase RIO3 isoform 1 [Homo sapiens]

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 1.61e-151

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: 430.63  E-value: 1.61e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 253 ITGCISTGKESVVFHAYGGSMEDekedsKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 332
Cdd:cd05146   1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 333 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 412
Cdd:cd05146  76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22325377 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 1.61e-151

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: 430.63  E-value: 1.61e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 253 ITGCISTGKESVVFHAYGGSMEDekedsKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 332
Cdd:cd05146   1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 333 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 412
Cdd:cd05146  76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22325377 413 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:cd05146 156 LWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO smart00090
RIO-like kinase;
222-470 5.31e-119

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 349.68  E-value: 5.31e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377    222 EKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYggsmedekeDSKVIPTECAIKVFKTTLNEFKN 301
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAL---------DFDGSGKERAVKIYRTGTLEFKR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377    302 RDKYIKDDFRFKdrFSKLNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEE 381
Cdd:smart00090  72 RDRYVDGDFRFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377    382 MKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSE 461
Cdd:smart00090 150 EFELYDDILEEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDE-LDE 228


                   ....*....
gi 22325377    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 ...
 264-463 4.49e-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: 271.03  E-value: 4.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377   264 VVFHAYGgsmEDEKEdskvipteCAIKVFKTTLNEFKNRDKYIKDDFRFKDRfsKLNPRKIIRMWAEKEMHNLARMQRAG 343
Cdd:pfam01163   1 NVYHAVS---EDGKE--------VAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377   344 IPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLnsEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLID 423
Cdd:pfam01163  68 VPVPKPIDVNRHVLVMEFIGKDGVPAPKLKDVEL--EEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIID 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 22325377   424 VSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSERE 463
Cdd:pfam01163 146 VPQAVETDHPNALEFLERDVENIINFFRRKGVDE-VDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
214-468 9.09e-70

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 223.53  E-value: 9.09e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 214 ERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAyggsmedEKEDSKVIptecAIKVFK 293
Cdd:COG1718  11 DKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLA-------RRPGGELV----AAKIYR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 294 TTLNEFKNRDKYIKDDFRFKDRFSKlNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLK 373
Cdd:COG1718  80 TATSSFKRMAQYIEGDPRFMGKGSF-GRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 374 EVKLNSEEMKEAYYQTLHLMRQLYhECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:COG1718 159 DVELEPEEAEELYEQLIEYIVRLY-KAGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237

                       250
                ....*....|....*
gi 22325377 454 GVKeaLSERELFNAV 468
Cdd:COG1718 238 GPE--LDPEELLKEI 250
PRK14879 PRK14879
Kae1-associated kinase Bud32;
302-441 3.15e-10

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 59.92  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377  302 RDKYIKDDFRFKDRFSK--LNPR---KIIRMWAEKEMHNLARMQRAGIPCPTVVL--LKKHILVMSFIghdqvPAPKLKE 374
Cdd:PRK14879  14 LGDFLGIKAVIKWRIPKryRHPEldeRIRRERTRREARIMSRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377  375 VkLNSEEMKEA-YYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP--------------THPH 434
Cdd:PRK14879  89 L-INSNGMEELeLSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDfglaeFSKDLEDravdlhvllrslesTHPD 167


                 ....*..
gi 22325377  435 GLEFLFR 441
Cdd:PRK14879 168 WAEELFE 174
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 322-430 2.28e-07

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: 51.44  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377   322 RKIIRMWAEKEMHNLARMQRAGIPCPTV--VLLKKHILVMSFIghdqvPAPKLKEVklnSEEMKEAYYQTLHLMRQLYHE 399
Cdd:TIGR03724  37 ERLRKERTRREARLLSRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDV---IEENGDELAREIGRLVGKLHK 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22325377   400 CTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP 430
Cdd:TIGR03724 109 AGIVHGDLTTSNIIVRDDKVYLIDfglgkYSDEIED 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 1.61e-151

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: 430.63  E-value: 1.61e-151
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 253 ITGCISTGKESVVFHAYGGSMEDekedsKVIPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 332
Cdd:cd05146   1 VNGCISTGKEAVVFHANGGSMEE-----VLLPPECAIKVFKTTLNEFKNRDKYIKDDYRFKDRFSKQNPRKIIRLWAEKE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 333 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 412
Cdd:cd05146  76 MHNLKRMQKAGIPCPEVVLLKKHVLVMSFIGKDQVPAPKLKDAKLSSADLKLAYEQVVQMMKTMYNECHLVHADLSEYNI 155

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22325377 413 LWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:cd05146 156 LWHEGKVWFIDVSQSVEPTHPHALEFLLRDCRNVSNFFQKR 196
RIO smart00090
RIO-like kinase;
222-470 5.31e-119

RIO-like kinase;


Pssm-ID: 214511 [Multi-domain]  Cd Length: 237  Bit Score: 349.68  E-value: 5.31e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377    222 EKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAYggsmedekeDSKVIPTECAIKVFKTTLNEFKN 301
Cdd:smart00090   1 DKEDRATYEEVLDGRTRLALYSLLNRGILSAIGGCISTGKEANVYHAL---------DFDGSGKERAVKIYRTGTLEFKR 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377    302 RDKYIKDDFRFKdrFSKLNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEE 381
Cdd:smart00090  72 RDRYVDGDFRFK--YRKINPRKLVRLWAEKEFRNLQRLYEAGVPVPKPIAWRRNVLVMEFIGGDGLPAPRLKDVEPEEEE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377    382 MKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSE 461
Cdd:smart00090 150 EFELYDDILEEMRKLYKEGELVHGDLSEYNILVHDGKVVIIDVSQSVELDHPMALEFLERDIRNIIRFFRRKGVDE-LDE 228


                   ....*....
gi 22325377    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 1.39e-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: 308.35  E-value: 1.39e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 253 ITGCISTGKESVVFHAYGGSmedekedskviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRFSKLNPRKIIRMWAEKE 332
Cdd:cd05147   1 INGCISTGKEANVYHATTKN-----------GGELAIKVYKTSILVFKDRDKYVSGEFRFRHGYCKHNPRKMVKTWAEKE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 333 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 412
Cdd:cd05147  70 MRNLKRLNQAGIPCPEPILLRSHVLVMEFIGKDGWPAPRLKDAKLSESKWRELYLQVIKIMRRMYQKCRLVHADLSEYNL 149

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22325377 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 1.61e-98

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: 295.23  E-value: 1.61e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 253 ITGCISTGKESVVFHAYGGSmedekedskviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRfSKLNPRKIIRMWAEKE 332
Cdd:cd05145   1 LGGVISTGKEANVYLARGGD-----------GEPVAVKIYRTSTSSFKKMAKYIEGDPRFESR-RRGNRRKLIFAWARKE 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 333 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNM 412
Cdd:cd05145  69 FRNLKRLYEAGVRVPEPIAVYRNVLVMEFIGDDGSPAPRLKDVELEEEDAEELYEQVVEQMRRMYCKAGLVHGDLSEYNI 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22325377 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 ...
 264-463 4.49e-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: 271.03  E-value: 4.49e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377   264 VVFHAYGgsmEDEKEdskvipteCAIKVFKTTLNEFKNRDKYIKDDFRFKDRfsKLNPRKIIRMWAEKEMHNLARMQRAG 343
Cdd:pfam01163   1 NVYHAVS---EDGKE--------VAVKIYRTGTTSFKKRKRYRSGDFRFRDR--KTSWRYLVRLWAEKEFRNLKRLYEAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377   344 IPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVKLnsEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLID 423
Cdd:pfam01163  68 VPVPKPIDVNRHVLVMEFIGKDGVPAPKLKDVEL--EEAEEIYDEIIREMRRLYQEAGLVHGDLSEYNILVHDDKPVIID 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 22325377   424 VSQSVEPTHPHGLEFLFRDCRNVSQFFQKGGVKEaLSERE 463
Cdd:pfam01163 146 VPQAVETDHPNALEFLERDVENIINFFRRKGVDE-VDERK 184
RIO1 COG1718
Serine/threonine-protein kinase RIO1 [Signal transduction mechanisms];
214-468 9.09e-70

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


Pssm-ID: 441324  Cd Length: 252  Bit Score: 223.53  E-value: 9.09e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 214 ERRSARLHEKKEHSTAEKAVDPKTRLLMYKMVNSGMLETITGCISTGKESVVFHAyggsmedEKEDSKVIptecAIKVFK 293
Cdd:COG1718  11 DKLRKRIKDSDDFKVVDEVFDDSTPKALYKLVNDGLIDEVLGPLSTGKEANVFLA-------RRPGGELV----AAKIYR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 294 TTLNEFKNRDKYIKDDFRFKDRFSKlNPRKIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLK 373
Cdd:COG1718  80 TATSSFKRMAQYIEGDPRFMGKGSF-GRRQLIFAWARKEFRNLYRLYEAGVRVPEPIAFYGNVLLMEFIGDDGVPAPRLK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 374 EVKLNSEEMKEAYYQTLHLMRQLYhECTLVHADLSEYNMLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQKG 453
Cdd:COG1718 159 DVELEPEEAEELYEQLIEYIVRLY-KAGLVHGDLSEYNILVDDGGPVIIDLPQAVDVAHPNAKEFLERDVENIARFFARF 237

                       250
                ....*....|....*
gi 22325377 454 GVKeaLSERELFNAV 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 1.12e-37

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: 137.08  E-value: 1.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 253 ITGCISTGKESVVFHAYGgsmedeKEDSKviPTECAIKVFKTTLNEFKNRDKYIKDDFRFKDRfsKLNPRKIIRMWAEKE 332
Cdd:cd05119   1 IGGVISTGKEANVFYADG------VFDGK--PVACAVKIYRIETSEFDKVDEYLYGDERFDYR--RISPKEKVFIWTEKE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 333 MHNLARMQRAGIPCPTVVLLKKHILVMSFIGHDQVPAPKLKEVK--LNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEY 410
Cdd:cd05119  71 FRNLERAKEAGVSVPQPYTYEKNVLL*EFIGEDELPAPTLVELGreLKELDVEGIFNDVVENVKRLYQEAELVHADLSEY 150

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 22325377 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 7.15e-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: 98.73  E-value: 7.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 250 LETITGCISTGKESVVFHAYGGSMEdekedskviptECAIKV-------FKTTLNefkNRDkYIKDdfrfKDRFSKLNpr 322
Cdd:cd05144   1 ISSVGNQIGVGKESDVYLALDEDGN-----------PVVLKFhrlgrtsFRKVKR---KRD-YLKH----RKHASWLY-- 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 323 kIIRMWAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIghdqvPAPKLKEVKLNsEEMKEAYYQTLHLMRQLYhECTL 402
Cdd:cd05144  60 -LSRLAAEKEFAALKALYEEGFPVPKPIDWNRHAVVMELI-----DGYPLYQVRLL-EDPEEVLDEILELIVKLA-KHGL 131

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 22325377 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 1.66e-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: 94.59  E-value: 1.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 304 KYIKDDFRFKDRFSKLN-PRKIirmwAEKEMHNLARMQRAGIPCPTVVLLKKHILVMSFIghdqvPAPKLKEVKLNSEEm 382
Cdd:COG0478  24 RKVRRERADKEHYSWLYaARTR----AEREFRALERLYPAGLPVPRPIAANRHAIVMERI-----EGVELARLKLEDPE- 93

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22325377 383 kEAYYQTLHLMRQLyHECTLVHADLSEYN-MLWHAGKVWLIDVSQSVEPTHPHGLEFLFRDCRNVSQFFQK 452
Cdd:COG0478  94 -EVLDKILEEIRRA-HDAGIVHADLSEYNiLVDDDGGVWIIDWPQAVPRDHPNAEELLERDLENLLRSFRK 162
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
 326-427 7.38e-13

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: 66.52  E-value: 7.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 326 RMWAEKEMhnLARMQRAGIPCPTVVLLKKH--ILVMSFIghdqvPAPKLKEVKLNSEEMKEAYYQTLHLMRQLyHECTLV 403
Cdd:COG3642   2 RTRREARL--LRELREAGVPVPKVLDVDPDdaDLVMEYI-----EGETLADLLEEGELPPELLRELGRLLARL-HRAGIV 73

                        90       100
                ....*....|....*....|....
gi 22325377 404 HADLSEYNMLWHAGKVWLIDVSQS 427
Cdd:COG3642  74 HGDLTTSNILVDDGGVYLIDFGLA 97
PRK14879 PRK14879
Kae1-associated kinase Bud32;
302-441 3.15e-10

Kae1-associated kinase Bud32;


Pssm-ID: 237847 [Multi-domain]  Cd Length: 211  Bit Score: 59.92  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377  302 RDKYIKDDFRFKDRFSK--LNPR---KIIRMWAEKEMHNLARMQRAGIPCPTVVL--LKKHILVMSFIghdqvPAPKLKE 374
Cdd:PRK14879  14 LGDFLGIKAVIKWRIPKryRHPEldeRIRRERTRREARIMSRARKAGVNVPAVYFvdPENFIIVMEYI-----EGEPLKD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377  375 VkLNSEEMKEA-YYQTLHLMRQLYHECTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP--------------THPH 434
Cdd:PRK14879  89 L-INSNGMEELeLSREIGRLVGKLHSAGIIHGDLTTSNMILSGGKIYLIDfglaeFSKDLEDravdlhvllrslesTHPD 167


                 ....*..
gi 22325377  435 GLEFLFR 441
Cdd:PRK14879 168 WAEELFE 174
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
 322-430 2.28e-07

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: 51.44  E-value: 2.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377   322 RKIIRMWAEKEMHNLARMQRAGIPCPTV--VLLKKHILVMSFIghdqvPAPKLKEVklnSEEMKEAYYQTLHLMRQLYHE 399
Cdd:TIGR03724  37 ERLRKERTRREARLLSRARKAGVNTPVIydVDPDNKTIVMEYI-----EGKPLKDV---IEENGDELAREIGRLVGKLHK 108

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 22325377   400 CTLVHADLSEYNMLWHAGKVWLID-----VSQSVEP 430
Cdd:TIGR03724 109 AGIVHGDLTTSNIIVRDDKVYLIDfglgkYSDEIED 144
PRK09605 PRK09605
bifunctional N(6)-L-threonylcarbamoyladenine synthase/serine/threonine protein kinase;
301-429 1.11e-05

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


Pssm-ID: 236586 [Multi-domain]  Cd Length: 535  Bit Score: 47.96  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377  301 NRDKYIKDDFRFKDRFSKL--NP---RKIIRMWAEKEMHNLARMQRAGIPCPTV--VLLKKHILVMSFIGhdqvpAPKLK 373
Cdd:PRK09605 350 KKGEYLGRDAVIKERVPKGyrHPeldERLRTERTRAEARLLSEARRAGVPTPVIydVDPEEKTIVMEYIG-----GKDLK 424

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22325377  374 EVKLNSEEMKEAYYQTLHLMrqlyHECTLVHADLSEYNMLWHAGKVWLID-----VSQSVE 429
Cdd:PRK09605 425 DVLEGNPELVRKVGEIVAKL----HKAGIVHGDLTTSNFIVRDDRLYLIDfglgkYSDLIE 481
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
 326-423 2.58e-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: 43.97  E-value: 2.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 326 RMWAEKEMHNLARMQRAGIPCPTVVLLKK----HILVMSFIGHDQVPAPkLKEVKLNSEEMKEAYYQTLHLMRQLyHECT 401
Cdd:cd13968  34 GEDLESEMDILRRLKGLELNIPKVLVTEDvdgpNILLMELVKGGTLIAY-TQEEELDEKDVESIMYQLAECMRLL-HSFH 111

                        90       100
                ....*....|....*....|...
gi 22325377 402 LVHADLSEYN-MLWHAGKVWLID 423
Cdd:cd13968 112 LIHRDLNNDNiLLSEDGNVKLID 134
ChoK-like cd05151
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ...
 332-423 4.41e-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: 4.41e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377 332 EMHNLARMQRAGIpCPTVVLL--KKHILVMSFIghdqVPAPKLKEVKLNSEEMKEAyyqtLHLMRQLYH----ECTLVHA 405
Cdd:cd05151  42 EKANSKAAAELGI-APEVIYFdpETGVKITEFI----EGATLLTNDFSDPENLERI----AALLRKLHSspleDLVLCHN 112

                        90
                ....*....|....*...
gi 22325377 406 DLSEYNMLWHAGKVWLID 423
Cdd:cd05151 113 DLVPGNFLLDDDRLYLID 130
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
 293-447 7.28e-05

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


Pssm-ID: 428872  Cd Length: 206  Bit Score: 43.92  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377   293 KTTLNEFkNRDKYikddfrfkdRFSKLNPRkiirmwAEKEMHNLARMQRAGIPCPTVV--------LLKKHILVMSFIGH 364
Cdd:pfam06293  37 GGMWGHL-NRDLY---------RYPLGRTR------AFREFRLIRRLREAGLPVPKPVaagevkvgGGYRADLLTERLEG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377   365 DQVPAPKLKEVKLNSEEMKEAYYQTLHLMRQLYHECTLVHADLSEYNMLWHAG-----KVWLIDVSQSVEPTHP-----H 434
Cdd:pfam06293 101 AQSLADWLADWAVPSGELRRAIWEAVGRLIRQMHRAGVQHGDLYAHHILLQQEgdegfEAWLIDLDKGRLRLPArrwrnK 180

                         170
                  ....*....|...
gi 22325377   435 GLEFLFRDCRNVS 447
Cdd:pfam06293 181 DLARLLRSFLNIG 193
PRK01723 PRK01723
3-deoxy-D-manno-octulosonic-acid kinase; Reviewed
 326-423 1.87e-03

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


Pssm-ID: 234975  Cd Length: 239  Bit Score: 39.87  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22325377  326 RMWAEkeMHNLARMQRAGIPCPTVV--------LLKKHILVMSFIGHDQVPAPKLKEVKLnSEEMkeaYYQTLHLMRQLy 397
Cdd:PRK01723  86 RAFAE--FRLLAQLYEAGLPVPRPIaarvvrhgLFYRADILIERIEGARDLVALLQEAPL-SEEQ---WQAIGQLIARF- 158

                         90       100
                 ....*....|....*....|....*..
gi 22325377  398 HECTLVHADLSEYNMLW-HAGKVWLID 423
Cdd:PRK01723 159 HDAGVYHADLNAHNILLdPDGKFWLID 185
 
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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