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UniProtKB/Swiss-Prot entry Q1RFD5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TGT_ECOUT
Primary accession number Q1RFD5
Secondary accession numbers None
Integrated into Swiss-Prot on January 15, 2008
Sequence was last modified on May 16, 2006 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 21)
Name and origin of the protein
Protein name Queuine tRNA-ribosyltransferase
Synonyms EC 2.4.2.29
tRNA-guanine transglycosylase
Guanine insertion enzyme
Gene name
Name: tgt
OrderedLocusNames: UTI89_C0428
From
Escherichia coli (strain UTI89 / UPEC) [TaxID: 364106] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0600938103; PubMed=16585510 [NCBI, ExPASy, EBI, Israel, Japan]
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.;
"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach.";
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CP000243; ABE05929.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_539460.1; -.
3D structure databases
ModBase Q1RFD5.
Enzyme and pathway databases
BioCyc ECOL364106:UTI89_C0428-MON; -.
Ontologies
GO
GO:0008479; Molecular function: queuine tRNA-ribosyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008616; Biological process: queuosine biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00168; -; 1.
PBIL [Tree]
InterPro IPR004803; QtRNA_ribo_trans.
IPR002616; tRNA_ribo_trans.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.105; tRNA_ribo_trans; 1.
PANTHER PTHR11962; tRNA_ribo_trans; 1.
Pfam PF01702; TGT; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00430; Q_tRNA_tgt; 1.
TIGR00449; tgt_general; 1.
BLOCKS Q1RFD5.
ProtoNet Q1RFD5.
Genome annotation databases
GeneID 3993726; -.
GenomeReviews CP000243_GR; UTI89_C0428.
KEGG eci:UTI89_C0428; -.
Phylogenomic databases
HOGENOM Q1RFD5; -.
Genome annotation databases
CMR Q1RFD5; UTI89_C0428.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Glycosyltransferase; Metal-binding; Queuosine biosynthesis; Transferase; tRNA processing; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   375  375     Queuine tRNA-ribosyltransferase. PRO_1000016789
ACT_SITE   89    89        Nucleophile (By similarity). 
METAL   302   302        Zinc (By similarity). 
METAL   304   304        Zinc (By similarity). 
METAL   307   307        Zinc (By similarity). 
METAL   333   333        Zinc (By similarity). 
BINDING   90    90        Substrate (By similarity). 
Sequence information
Length: 375 AA [This is the length of the unprocessed precursor] Molecular weight: 42594 Da [This is the MW of the unprocessed precursor] CRC64: 40271CA08D8A8820 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKFELDTTDG RARRGRLVFD RGVVETPCFM PVGTYGTVKG MTPEEVEATG AQIILGNTFH 

        70         80         90        100        110        120 
LWLRPGQEIM KLHGDLHDFM QWKGPILTDS GGFQVFSLGD IRKITEQGVH FRNPINGDPI 

       130        140        150        160        170        180 
FLDPEKSMEI QYDLGSDIVM IFDECTPYPA DWDYAKRSME MSLRWAKRSR ERFDSLGNKN 

       190        200        210        220        230        240 
ALFGIIQGSV YEDLRDISVK GLVDIGFDGY AVGGLAVGEP KADMHRILEH VCPQIPADKP 

       250        260        270        280        290        300 
RYLMGVGKPE DLVEGVRRGI DMFDCVMPTR NARNGHLFVT DGVVKIRNAK YKSDTGPLDP 

       310        320        330        340        350        360 
ECDCYTCRNY SRAYLHHLDR CNEILGARLN TIHNLRYYQR LMAGLRKAIE EGKLESFVTD 

       370 
FYQRQGREVP PLNVD 

Q1RFD5 in FASTA format

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