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Conserved domains on  [gi|502860856|ref|WP_013095832|]
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MULTISPECIES: tRNA guanosine(34) transglycosylase Tgt [Enterobacter]

Protein Classification

tRNA guanosine(34) transglycosylase Tgt( domain architecture ID 11417414)

tRNA guanosine(34) transglycosylase Tgt 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

CATH:  3.20.20.105
EC:  2.4.2.-
Gene Ontology:  GO:0008479|GO:0046872
PubMed:  19925456

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tgt COG0343
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
1-368 0e+00

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: 787.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   1 MKFELDTTD-GRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDF 79
Cdd:COG0343    3 MKFELLATDpGKARRGRLTTPHGTIETPAFMPVGTQATVKALTPEELKEIGAQIILGNTYHLYLRPGAEVIAKAGGLHKF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  80 MQWKGPILTDSGGFQVFSLGDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSM 159
Cdd:COG0343   83 MNWDGPILTDSGGFQVFSLAKLRKITEEGVTFRSHIDGSKHFLTPEKSMEIQRALGSDIIMAFDECTPYPATYEYAKKSM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 160 EMSLRWAKRSRDRFDSlQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADK 239
Cdd:COG0343  163 ERTLRWAERCKAAHKR-LPDQALFGIVQGGMYEDLRKESAEALVELDFDGYAIGGLSVGEPKEEMYEILEYTTPLLPEDK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 240 PRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLD 319
Cdd:COG0343  242 PRYLMGVGTPEDLLEAVARGVDMFDCVLPTRNARNGTAFTSQGRINIRNARYKEDFRPLDPECDCYTCRNYSRAYLRHLF 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 502860856 320 RCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRT 368
Cdd:COG0343  322 KAGEILGARLLTIHNLHFYLRLMREIREAIEEGRFAEFKAEFLAKYGRG 370
 
Name Accession Description Interval E-value
Tgt COG0343
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
1-368 0e+00

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: 787.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   1 MKFELDTTD-GRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDF 79
Cdd:COG0343    3 MKFELLATDpGKARRGRLTTPHGTIETPAFMPVGTQATVKALTPEELKEIGAQIILGNTYHLYLRPGAEVIAKAGGLHKF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  80 MQWKGPILTDSGGFQVFSLGDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSM 159
Cdd:COG0343   83 MNWDGPILTDSGGFQVFSLAKLRKITEEGVTFRSHIDGSKHFLTPEKSMEIQRALGSDIIMAFDECTPYPATYEYAKKSM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 160 EMSLRWAKRSRDRFDSlQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADK 239
Cdd:COG0343  163 ERTLRWAERCKAAHKR-LPDQALFGIVQGGMYEDLRKESAEALVELDFDGYAIGGLSVGEPKEEMYEILEYTTPLLPEDK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 240 PRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLD 319
Cdd:COG0343  242 PRYLMGVGTPEDLLEAVARGVDMFDCVLPTRNARNGTAFTSQGRINIRNARYKEDFRPLDPECDCYTCRNYSRAYLRHLF 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 502860856 320 RCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRT 368
Cdd:COG0343  322 KAGEILGARLLTIHNLHFYLRLMREIREAIEEGRFAEFKAEFLAKYGRG 370
Q_tRNA_tgt TIGR00430
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange ...
3-370 0e+00

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: 711.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856    3 FELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQW 82
Cdd:TIGR00430   1 FELQKTDKHARVGKLNTPHGSVETPVFMPVGTLGTVKGLTPEELEATGAEIILANTYHLWLRPGQKIVKELGGLHKFMQW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   83 KGPILTDSGGFQVFSLGDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMS 162
Cdd:TIGR00430  81 DGPILTDSGGFQVFSLSDLRKIEEEGVHFKSPIDGSKIFLTPEKSMEIQYALGSDIIMAFDECTPYPADRDYAEKSTERT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  163 LRWAKRSRDRFDSLQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRY 242
Cdd:TIGR00430 161 LRWAERCLEAHDRRGNKQALFGIVQGGTYEDLRSQSAEGLIELDFPGYAIGGLSVGEPKEDMLRILEHTAPLLPKDKPRY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  243 LMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCN 322
Cdd:TIGR00430 241 LMGVGTPEDLLNAIRRGIDMFDCVMPTRNARNGTLFVTEGRINIKNAKYKDDTRPLDEECDCYTCKNYSRAYLRHLIRCN 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 502860856  323 EILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRTVP 370
Cdd:TIGR00430 321 ELLGARLATLHNLHFYLRLMEKIRQAILEDRFLSFRTEFLERYGEEVP 368
TGT pfam01702
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
9-367 0e+00

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: 663.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856    9 DGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILT 88
Cdd:pfam01702   1 DGAARLGRLTTPHGVIETPAFMPVGTQGTVKGLTPDELKELGAQIILGNTYHLYLRPGLELVAKAGGLHKFMGWDGPILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   89 DSGGFQVFSLGDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKR 168
Cdd:pfam01702  81 DSGGFQVFSLAKLRKITEEGVTFRSHIDGSKHFLTPEESMEIQEALGSDIAMALDECTPYPASRKRAEKSVERTLRWAER 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  169 SRDRFDSlQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGK 248
Cdd:pfam01702 161 CLEAHKR-PEDQALFGIVQGGLYPDLREESAEELAELDFDGYAIGGLSVGEPKEEMYEIVEATTPLLPEDKPRYLMGVGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  249 PEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGAR 328
Cdd:pfam01702 240 PEDILEAVALGVDMFDCVYPTRNARNGRALTSEGTLNLRNAKYAEDFRPLDEGCSCYTCRNYSRAYLRHLLKAKEMLGAR 319
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 502860856  329 LNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGR 367
Cdd:pfam01702 320 LLTIHNLHFYLELMREIRQAIKEGRFEEFVEEFLRKYPS 358
PRK01008 PRK01008
queuine tRNA-ribosyltransferase; Provisional
1-354 2.50e-101

queuine tRNA-ribosyltransferase; Provisional


Pssm-ID: 134464  Cd Length: 372  Bit Score: 304.44  E-value: 2.50e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   1 MKFEL--DTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMtpeeVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHD 78
Cdd:PRK01008   3 LKFELlhQSKKSRARVGRIETAHGIIDTPAFVPVATNGALKGV----LDHSNIPLMFCNTYHLLVHPGTEAIAAMGGLHQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  79 FMQWKGPILTDSGGFQVFSL------------------GDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVM 140
Cdd:PRK01008  79 FIGRNAPIITDSGGFQIFSLaygsvaeeikscgkkkggSSILKITDEGVWFKSYRDGRKLFLSPEISVQAQKDLGADIII 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 141 IFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGlAVGEP 220
Cdd:PRK01008 159 PLDELLPFHADPTYFLQSCQRTYVWEKRSLDYHLKNPRHQSMYGVIHGGIDPDQRKIGCKFVEDLPFDGSAIGG-SLGKN 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 221 KEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDA 300
Cdd:PRK01008 238 LQEMVEVVGVTTSNLSKERPVHLLGIGDLPSIWATVGFGIDSFDSSYPTKAARHGLILTKQGPLKINNQRYSSDLNPIEP 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502860856 301 ECDCYTC-RNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKL 354
Cdd:PRK01008 318 GCSCLACsSGISRAYLRHLFKVHEPNAGIWASIHNLHHMQQVMKEIREQILNDRI 372
 
Name Accession Description Interval E-value
Tgt COG0343
Queuine/archaeosine tRNA-ribosyltransferase [Translation, ribosomal structure and biogenesis]; ...
1-368 0e+00

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: 787.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   1 MKFELDTTD-GRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDF 79
Cdd:COG0343    3 MKFELLATDpGKARRGRLTTPHGTIETPAFMPVGTQATVKALTPEELKEIGAQIILGNTYHLYLRPGAEVIAKAGGLHKF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  80 MQWKGPILTDSGGFQVFSLGDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSM 159
Cdd:COG0343   83 MNWDGPILTDSGGFQVFSLAKLRKITEEGVTFRSHIDGSKHFLTPEKSMEIQRALGSDIIMAFDECTPYPATYEYAKKSM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 160 EMSLRWAKRSRDRFDSlQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADK 239
Cdd:COG0343  163 ERTLRWAERCKAAHKR-LPDQALFGIVQGGMYEDLRKESAEALVELDFDGYAIGGLSVGEPKEEMYEILEYTTPLLPEDK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 240 PRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLD 319
Cdd:COG0343  242 PRYLMGVGTPEDLLEAVARGVDMFDCVLPTRNARNGTAFTSQGRINIRNARYKEDFRPLDPECDCYTCRNYSRAYLRHLF 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 502860856 320 RCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRT 368
Cdd:COG0343  322 KAGEILGARLLTIHNLHFYLRLMREIREAIEEGRFAEFKAEFLAKYGRG 370
Q_tRNA_tgt TIGR00430
tRNA-guanine transglycosylase; This tRNA-guanine transglycosylase (tgt) catalyzes an exchange ...
3-370 0e+00

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: 711.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856    3 FELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQW 82
Cdd:TIGR00430   1 FELQKTDKHARVGKLNTPHGSVETPVFMPVGTLGTVKGLTPEELEATGAEIILANTYHLWLRPGQKIVKELGGLHKFMQW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   83 KGPILTDSGGFQVFSLGDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMS 162
Cdd:TIGR00430  81 DGPILTDSGGFQVFSLSDLRKIEEEGVHFKSPIDGSKIFLTPEKSMEIQYALGSDIIMAFDECTPYPADRDYAEKSTERT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  163 LRWAKRSRDRFDSLQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRY 242
Cdd:TIGR00430 161 LRWAERCLEAHDRRGNKQALFGIVQGGTYEDLRSQSAEGLIELDFPGYAIGGLSVGEPKEDMLRILEHTAPLLPKDKPRY 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  243 LMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCN 322
Cdd:TIGR00430 241 LMGVGTPEDLLNAIRRGIDMFDCVMPTRNARNGTLFVTEGRINIKNAKYKDDTRPLDEECDCYTCKNYSRAYLRHLIRCN 320
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 502860856  323 EILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRTVP 370
Cdd:TIGR00430 321 ELLGARLATLHNLHFYLRLMEKIRQAILEDRFLSFRTEFLERYGEEVP 368
tgt_general TIGR00449
tRNA-guanine family transglycosylase; Different tRNA-guanine transglycosylases catalyze ...
3-370 0e+00

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: 664.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856    3 FELDTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQW 82
Cdd:TIGR00449   1 FEIKKTDGHARVGRLKTPHGSVETPVFMPVGTLGTVKGLTPEELKKTGAQIILANTYHLYLRPGQKIVALLGGLHKFMQW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   83 KGPILTDSGGFQVFSLGDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMS 162
Cdd:TIGR00449  81 DGPILTDSGGFQVFSLGDLRKIEEEGVHFKSPIDGSKIFLTPEKIMEIQYALGSDIIMALDECTPPPADYDYAEESLERT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  163 LRWAKRSRDRFDSlQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRY 242
Cdd:TIGR00449 161 LRWAEESLEYHKR-RNENALFGIVQGGTYPDLRRQSAEGLAELDFDGYAIGGVSVGEPKRDMLRILEHVAPLLPKDKPRY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  243 LMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCN 322
Cdd:TIGR00449 240 LMGVGTPELLANAVSLGIDMFDCVAPTRYARNGTLLTTEGRIKIKNAKYKDDTRPLDEPCDCYVCKNYSRAYLRHLIRCN 319
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 502860856  323 EILGARLNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGRTVP 370
Cdd:TIGR00449 320 ELLGARLATEHNLHFSFRLIEKIRQAILEDRLLSFVEEFLEAYGRLLP 367
TGT pfam01702
Queuine tRNA-ribosyltransferase; This is a family of queuine tRNA-ribosyltransferases EC:2.4.2. ...
9-367 0e+00

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: 663.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856    9 DGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMTPEEVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHDFMQWKGPILT 88
Cdd:pfam01702   1 DGAARLGRLTTPHGVIETPAFMPVGTQGTVKGLTPDELKELGAQIILGNTYHLYLRPGLELVAKAGGLHKFMGWDGPILT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   89 DSGGFQVFSLGDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVMIFDECTPYPADWDYAKRSMEMSLRWAKR 168
Cdd:pfam01702  81 DSGGFQVFSLAKLRKITEEGVTFRSHIDGSKHFLTPEESMEIQEALGSDIAMALDECTPYPASRKRAEKSVERTLRWAER 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  169 SRDRFDSlQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGLAVGEPKEDMHRILEHVCPQIPADKPRYLMGVGK 248
Cdd:pfam01702 161 CLEAHKR-PEDQALFGIVQGGLYPDLREESAEELAELDFDGYAIGGLSVGEPKEEMYEIVEATTPLLPEDKPRYLMGVGT 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  249 PEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDAECDCYTCRNYSRAYLHHLDRCNEILGAR 328
Cdd:pfam01702 240 PEDILEAVALGVDMFDCVYPTRNARNGRALTSEGTLNLRNAKYAEDFRPLDEGCSCYTCRNYSRAYLRHLLKAKEMLGAR 319
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 502860856  329 LNTIHNLRYYQRLMAGLRKAIEEGKLESFVTDFYQRQGR 367
Cdd:pfam01702 320 LLTIHNLHFYLELMREIRQAIKEGRFEEFVEEFLRKYPS 358
PRK01008 PRK01008
queuine tRNA-ribosyltransferase; Provisional
1-354 2.50e-101

queuine tRNA-ribosyltransferase; Provisional


Pssm-ID: 134464  Cd Length: 372  Bit Score: 304.44  E-value: 2.50e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856   1 MKFEL--DTTDGRARRGRLVFDRGVVETPAFMPVGTYGTVKGMtpeeVEATGAQIILGNTFHLWLRPGQEIMKLHGDLHD 78
Cdd:PRK01008   3 LKFELlhQSKKSRARVGRIETAHGIIDTPAFVPVATNGALKGV----LDHSNIPLMFCNTYHLLVHPGTEAIAAMGGLHQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856  79 FMQWKGPILTDSGGFQVFSL------------------GDIRKITEEGVHFRNPINGDPIFLDPEKSMEIQYDLGSDIVM 140
Cdd:PRK01008  79 FIGRNAPIITDSGGFQIFSLaygsvaeeikscgkkkggSSILKITDEGVWFKSYRDGRKLFLSPEISVQAQKDLGADIII 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 141 IFDECTPYPADWDYAKRSMEMSLRWAKRSRDRFDSLQNKNALFGIIQGSVYEDLRDISVKGLVEIGFDGYAVGGlAVGEP 220
Cdd:PRK01008 159 PLDELLPFHADPTYFLQSCQRTYVWEKRSLDYHLKNPRHQSMYGVIHGGIDPDQRKIGCKFVEDLPFDGSAIGG-SLGKN 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860856 221 KEDMHRILEHVCPQIPADKPRYLMGVGKPEDLVEGVRRGIDMFDCVMPTRNARNGHLFVTDGVVKIRNAKHKSDTSPLDA 300
Cdd:PRK01008 238 LQEMVEVVGVTTSNLSKERPVHLLGIGDLPSIWATVGFGIDSFDSSYPTKAARHGLILTKQGPLKINNQRYSSDLNPIEP 317
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502860856 301 ECDCYTC-RNYSRAYLHHLDRCNEILGARLNTIHNLRYYQRLMAGLRKAIEEGKL 354
Cdd:PRK01008 318 GCSCLACsSGISRAYLRHLFKVHEPNAGIWASIHNLHHMQQVMKEIREQILNDRI 372
 
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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