ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q5HUF2


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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TGT_CAMJR
Primary accession number Q5HUF2
Secondary accession numbers None
Integrated into Swiss-Prot on June 7, 2005
Sequence was last modified on February 15, 2005 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 25)
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: CJE1090
From
Campylobacter jejuni (strain RM1221) [TaxID: 195099] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1371/journal.pbio.0030015; PubMed=15660156 [NCBI, ExPASy, EBI, Israel, Japan]
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M., Nelson K.E.;
"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species.";
PLoS Biol. 3:72-85(2005).
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
CP000025; AAW35418.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_179083.1; -.
3D structure databases
ModBase Q5HUF2.
Enzyme and pathway databases
BioCyc CJEJ195099:CJE_1090-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.
ProtoNet Q5HUF2.
Genome annotation databases
GeneID 3231599; -.
GenomeReviews CP000025_GR; CJE1090.
KEGG cjr:CJE1090; -.
NMPDR fig|195099.3.peg.1171; -.
TIGR CJE1090; -.
Phylogenomic databases
HOGENOM Q5HUF2; -.
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   373  373     Queuine tRNA-ribosyltransferase. PRO_0000135460
ACT_SITE   90    90        Nucleophile (By similarity). 
METAL   308   308        Zinc (By similarity). 
METAL   310   310        Zinc (By similarity). 
METAL   313   313        Zinc (By similarity). 
METAL   339   339        Zinc (By similarity). 
BINDING   91    91        Substrate (By similarity). 
Sequence information
Length: 373 AA [This is the length of the unprocessed precursor] Molecular weight: 42554 Da [This is the MW of the unprocessed precursor] CRC64: 23197D2141F32B18 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEFKLKHKDG MARVCEITTA HSTFLTPVFM PVGTVGAVKS LDANDMKNEL DAKIILANTY 

        70         80         90        100        110        120 
HMYLRPTSKV VKDFGGLHGF TKFDRSFLTD SGGFQAFSLS KNSKHFNEGI EFKSHIDGSR 

       130        140        150        160        170        180 
HLFTPKSVLD AQYDFNSDIM MILDDLVALP ATKERVKISV DRTILWAKEA ITYHKNMQNK 

       190        200        210        220        230        240 
GIGIGQNIFG IIQGGTDYEE RKRCALSLNE MPFDGLAIGG LSVGEENALM YETVQNLNPY 

       250        260        270        280        290        300 
LDENRPRYLM GVGTPEDLVE NVERGVDMFD CVMPTRNARN GTFFTSFGKF NIKKAEFIND 

       310        320        330        340        350        360 
HEVIDPTCSC YTCRNFSRGY LNHLFKAKEL TFFRLASLHN LHYYLELARK MREAILNNSF 

       370 
TQFKRNFYHL RGK 

Q5HUF2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!