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Conserved domains on  [gi|25146502|ref|NP_741662|]
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Queuine tRNA-ribosyltransferase accessory subunit 2 [Caenorhabditis elegans]

Protein Classification

tRNA guanosine transglycosylase family protein( domain architecture ID 139675)

tRNA guanosine transglycosylase family protein similar to the catalytic and accessory subunits of TGT, which catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 in tRNAs with GU(N) anticodons resulting in the hypermodified nucleoside queuosine

Gene Ontology:  GO:0046872
PubMed:  19925456

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TGT super family cl46131
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
13-369 4.17e-45

Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine. It catalyzes the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues.


The actual alignment was detected with superfamily member pfam01702:

Pssm-ID: 460299  Cd Length: 358  Bit Score: 158.41  E-value: 4.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502    13 GRLGKIDT-WGSVEvnhqTPSFQTYLRAGHIPHLTWEVAEN---QLKLEQTHIFQMTlPTLvsnaKIIEKFGkGAAKFCG 88
Cdd:pfam01702   4 ARLGRLTTpHGVIE----TPAFMPVGTQGTVKGLTPDELKElgaQIILGNTYHLYLR-PGL----ELVAKAG-GLHKFMG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502    89 MPAGAavhLTpfD-------PLGKLPGgyNDSKSVAIWTAN--GKVSLDVK--MwrEIINSFGcgS-IETLVDYDTPKDV 156
Cdd:pfam01702  74 WDGPI---LT--DsggfqvfSLAKLRK--ITEEGVTFRSHIdgSKHFLTPEesM--EIQEALG--SdIAMALDECTPYPA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   157 GQKKLVKAVDRTKTFQEQLFQQDEKVNGER---IVSlgGGFSKYHRRKCAVDV------GLAenIAGYTVEfreftEGKE 227
Cdd:pfam01702 143 SRKRAEKSVERTLRWAERCLEAHKRPEDQAlfgIVQ--GGLYPDLREESAEELaeldfdGYA--IGGLSVG-----EPKE 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   228 tddkEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEEGHAFclsddfpTSskYEVVDFNNE 307
Cdd:pfam01702 214 ----EMYEIVEATTPLLPEDKPRYLMGVGTPEDILEAVALGVDMFDCVYPTRNARNGRAL-------TS--EGTLNLRNA 280
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25146502   308 KFADDFTALFDGCACYTCTKYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLEN 369
Cdd:pfam01702 281 KYAEDFRPLDEGCSCYTCRNYSRAYLRHLLKAKEMLGARLLTIHNLHFYLELMREIRQAIKE 342
 
Name Accession Description Interval E-value
TGT pfam01702
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
13-369 4.17e-45

Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine. It catalyzes the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues.


Pssm-ID: 460299  Cd Length: 358  Bit Score: 158.41  E-value: 4.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502    13 GRLGKIDT-WGSVEvnhqTPSFQTYLRAGHIPHLTWEVAEN---QLKLEQTHIFQMTlPTLvsnaKIIEKFGkGAAKFCG 88
Cdd:pfam01702   4 ARLGRLTTpHGVIE----TPAFMPVGTQGTVKGLTPDELKElgaQIILGNTYHLYLR-PGL----ELVAKAG-GLHKFMG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502    89 MPAGAavhLTpfD-------PLGKLPGgyNDSKSVAIWTAN--GKVSLDVK--MwrEIINSFGcgS-IETLVDYDTPKDV 156
Cdd:pfam01702  74 WDGPI---LT--DsggfqvfSLAKLRK--ITEEGVTFRSHIdgSKHFLTPEesM--EIQEALG--SdIAMALDECTPYPA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   157 GQKKLVKAVDRTKTFQEQLFQQDEKVNGER---IVSlgGGFSKYHRRKCAVDV------GLAenIAGYTVEfreftEGKE 227
Cdd:pfam01702 143 SRKRAEKSVERTLRWAERCLEAHKRPEDQAlfgIVQ--GGLYPDLREESAEELaeldfdGYA--IGGLSVG-----EPKE 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   228 tddkEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEEGHAFclsddfpTSskYEVVDFNNE 307
Cdd:pfam01702 214 ----EMYEIVEATTPLLPEDKPRYLMGVGTPEDILEAVALGVDMFDCVYPTRNARNGRAL-------TS--EGTLNLRNA 280
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25146502   308 KFADDFTALFDGCACYTCTKYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLEN 369
Cdd:pfam01702 281 KYAEDFRPLDEGCSCYTCRNYSRAYLRHLLKAKEMLGARLLTIHNLHFYLELMREIRQAIKE 342
tgt_general TIGR00449
tRNA-guanine family transglycosylase; Different tRNA-guanine transglycosylases catalyze ...
134-369 4.05e-28

tRNA-guanine family transglycosylase; Different tRNA-guanine transglycosylases catalyze different tRNA base modifications. Two guanine base substitutions by different enzymes described by the model are involved in generating queuosine at position 34 in bacterial tRNAs and archaeosine at position 15 in archaeal tRNAs. This model is designed for fragment searching, so the superfamily is used loosely. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129541  Cd Length: 367  Bit Score: 112.88  E-value: 4.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   134 EIINSFGcGSIETLVDYDTPKDVGQKKLVKAVDRTKTFQEQLFQ-QDEKVNGERIVSLGGGFSKYHRRKCAVDVgLAENI 212
Cdd:TIGR00449 127 EIQYALG-SDIIMALDECTPPPADYDYAEESLERTLRWAEESLEyHKRRNENALFGIVQGGTYPDLRRQSAEGL-AELDF 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   213 AGYTVEFREFTEGKEtddkEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEEGHAFclsdd 292
Cdd:TIGR00449 205 DGYAIGGVSVGEPKR----DMLRILEHVAPLLPKDKPRYLMGVGTPELLANAVSLGIDMFDCVAPTRYARNGTLL----- 275
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25146502   293 fptsSKYEVVDFNNEKFADDFTALFDGCACYTCTKYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLEN 369
Cdd:TIGR00449 276 ----TTEGRIKIKNAKYKDDTRPLDEPCDCYVCKNYSRAYLRHLIRCNELLGARLATEHNLHFSFRLIEKIRQAILE 348
Tgt COG0343
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
224-369 2.29e-27

Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; Queuine/archaeosine tRNA-ribosyltransferase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440112  Cd Length: 370  Bit Score: 110.90  E-value: 2.29e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502 224 EGKEtddkEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEEGHAFclsddfpTSskYEVVD 303
Cdd:COG0343 221 EPKE----EMYEILEYTTPLLPEDKPRYLMGVGTPEDLLEAVARGVDMFDCVLPTRNARNGTAF-------TS--QGRIN 287
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25146502 304 FNNEKFADDFTALFDGCACYTCTKYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLEN 369
Cdd:COG0343 288 IRNARYKEDFRPLDPECDCYTCRNYSRAYLRHLFKAGEILGARLLTIHNLHFYLRLMREIREAIEE 353
PRK01008 PRK01008
queuine tRNA-ribosyltransferase; Provisional
231-371 4.97e-17

queuine tRNA-ribosyltransferase; Provisional


Pssm-ID: 134464  Cd Length: 372  Bit Score: 81.41  E-value: 4.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502  231 KEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEegHAFCLSDDFPtsskyevVDFNNEKFA 310
Cdd:PRK01008 239 QEMVEVVGVTTSNLSKERPVHLLGIGDLPSIWATVGFGIDSFDSSYPTKAAR--HGLILTKQGP-------LKINNQRYS 309
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25146502  311 DDFTALFDGCACYTCT-KYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLENSE 371
Cdd:PRK01008 310 SDLNPIEPGCSCLACSsGISRAYLRHLFKVHEPNAGIWASIHNLHHMQQVMKEIREQILNDR 371
 
Name Accession Description Interval E-value
TGT pfam01702
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
13-369 4.17e-45

Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2.29, also known as tRNA-guanine transglycosylase and guanine insertion enzyme. Queuine tRNA-ribosyltransferase modifies tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine. It catalyzes the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine, and the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA; giving a hypermodified base queuine in the wobble position. The aligned region contains a zinc binding motif C-x-C-x2-C-x29-H, and important tRNA and 7-aminomethyl-7deazaguanine binding residues.


Pssm-ID: 460299  Cd Length: 358  Bit Score: 158.41  E-value: 4.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502    13 GRLGKIDT-WGSVEvnhqTPSFQTYLRAGHIPHLTWEVAEN---QLKLEQTHIFQMTlPTLvsnaKIIEKFGkGAAKFCG 88
Cdd:pfam01702   4 ARLGRLTTpHGVIE----TPAFMPVGTQGTVKGLTPDELKElgaQIILGNTYHLYLR-PGL----ELVAKAG-GLHKFMG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502    89 MPAGAavhLTpfD-------PLGKLPGgyNDSKSVAIWTAN--GKVSLDVK--MwrEIINSFGcgS-IETLVDYDTPKDV 156
Cdd:pfam01702  74 WDGPI---LT--DsggfqvfSLAKLRK--ITEEGVTFRSHIdgSKHFLTPEesM--EIQEALG--SdIAMALDECTPYPA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   157 GQKKLVKAVDRTKTFQEQLFQQDEKVNGER---IVSlgGGFSKYHRRKCAVDV------GLAenIAGYTVEfreftEGKE 227
Cdd:pfam01702 143 SRKRAEKSVERTLRWAERCLEAHKRPEDQAlfgIVQ--GGLYPDLREESAEELaeldfdGYA--IGGLSVG-----EPKE 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   228 tddkEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEEGHAFclsddfpTSskYEVVDFNNE 307
Cdd:pfam01702 214 ----EMYEIVEATTPLLPEDKPRYLMGVGTPEDILEAVALGVDMFDCVYPTRNARNGRAL-------TS--EGTLNLRNA 280
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25146502   308 KFADDFTALFDGCACYTCTKYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLEN 369
Cdd:pfam01702 281 KYAEDFRPLDEGCSCYTCRNYSRAYLRHLLKAKEMLGARLLTIHNLHFYLELMREIRQAIKE 342
tgt_general TIGR00449
tRNA-guanine family transglycosylase; Different tRNA-guanine transglycosylases catalyze ...
134-369 4.05e-28

tRNA-guanine family transglycosylase; Different tRNA-guanine transglycosylases catalyze different tRNA base modifications. Two guanine base substitutions by different enzymes described by the model are involved in generating queuosine at position 34 in bacterial tRNAs and archaeosine at position 15 in archaeal tRNAs. This model is designed for fragment searching, so the superfamily is used loosely. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129541  Cd Length: 367  Bit Score: 112.88  E-value: 4.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   134 EIINSFGcGSIETLVDYDTPKDVGQKKLVKAVDRTKTFQEQLFQ-QDEKVNGERIVSLGGGFSKYHRRKCAVDVgLAENI 212
Cdd:TIGR00449 127 EIQYALG-SDIIMALDECTPPPADYDYAEESLERTLRWAEESLEyHKRRNENALFGIVQGGTYPDLRRQSAEGL-AELDF 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   213 AGYTVEFREFTEGKEtddkEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEEGHAFclsdd 292
Cdd:TIGR00449 205 DGYAIGGVSVGEPKR----DMLRILEHVAPLLPKDKPRYLMGVGTPELLANAVSLGIDMFDCVAPTRYARNGTLL----- 275
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25146502   293 fptsSKYEVVDFNNEKFADDFTALFDGCACYTCTKYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLEN 369
Cdd:TIGR00449 276 ----TTEGRIKIKNAKYKDDTRPLDEPCDCYVCKNYSRAYLRHLIRCNELLGARLATEHNLHFSFRLIEKIRQAILE 348
Tgt COG0343
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
224-369 2.29e-27

Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; Queuine/archaeosine tRNA-ribosyltransferase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440112  Cd Length: 370  Bit Score: 110.90  E-value: 2.29e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502 224 EGKEtddkEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEEGHAFclsddfpTSskYEVVD 303
Cdd:COG0343 221 EPKE----EMYEILEYTTPLLPEDKPRYLMGVGTPEDLLEAVARGVDMFDCVLPTRNARNGTAF-------TS--QGRIN 287
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25146502 304 FNNEKFADDFTALFDGCACYTCTKYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLEN 369
Cdd:COG0343 288 IRNARYKEDFRPLDPECDCYTCRNYSRAYLRHLFKAGEILGARLLTIHNLHFYLRLMREIREAIEE 353
Q_tRNA_tgt TIGR00430
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange ...
134-369 1.04e-26

tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange for the guanine base at position 34 of many tRNAs; this nucleotide is subsequently modified to queuosine. The Archaea have a closely related enzyme that catalyzes a base exchange for guanine at position 15 in some tRNAs, a site that is subsequently converted to the archaeal-specific modified base archaeosine (7-formamidino-7-deazaguanosine), while Archaeoglobus fulgidus has both enzymes. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 129522  Cd Length: 368  Bit Score: 109.04  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   134 EIINSFGcGSIETLVDYDTPKDVGQKKLVKAVDRTKTFQEQLFQQDEKVNGER----IVSlgGGFSKYHRRKCAVDVgLA 209
Cdd:TIGR00430 127 EIQYALG-SDIIMAFDECTPYPADRDYAEKSTERTLRWAERCLEAHDRRGNKQalfgIVQ--GGTYEDLRSQSAEGL-IE 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   210 ENIAGYTVEFREFTEGKEtddkEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEEGHAFcl 289
Cdd:TIGR00430 203 LDFPGYAIGGLSVGEPKE----DMLRILEHTAPLLPKDKPRYLMGVGTPEDLLNAIRRGIDMFDCVMPTRNARNGTLF-- 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502   290 sddfpTSSkyEVVDFNNEKFADDFTALFDGCACYTCTKYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLEN 369
Cdd:TIGR00430 277 -----VTE--GRINIKNAKYKDDTRPLDEECDCYTCKNYSRAYLRHLIRCNELLGARLATLHNLHFYLRLMEKIRQAILE 349
PRK01008 PRK01008
queuine tRNA-ribosyltransferase; Provisional
231-371 4.97e-17

queuine tRNA-ribosyltransferase; Provisional


Pssm-ID: 134464  Cd Length: 372  Bit Score: 81.41  E-value: 4.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25146502  231 KEMKELLEETFSPLPPTKLRCISGPFNPKTVLFLVQQGIDLFDSSFPVKLAEegHAFCLSDDFPtsskyevVDFNNEKFA 310
Cdd:PRK01008 239 QEMVEVVGVTTSNLSKERPVHLLGIGDLPSIWATVGFGIDSFDSSYPTKAAR--HGLILTKQGP-------LKINNQRYS 309
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25146502  311 DDFTALFDGCACYTCT-KYTKGYLQHLLNTRELLASILLVIHNMTEYDKMFKLIRSSLENSE 371
Cdd:PRK01008 310 SDLNPIEPGCSCLACSsGISRAYLRHLFKVHEPNAGIWASIHNLHHMQQVMKEIREQILNDR 371
 
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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