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Q92GM6 (TGT_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Queuine tRNA-ribosyltransferase

EC=2.4.2.29
Alternative name(s):
Guanine insertion enzyme
tRNA-guanine transglycosylase
Gene names
Name:tgt
Ordered Locus Names:RC1097
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and -Tyr). After this exchange, a cyclopentendiol moiety is attached to the 7-aminomethyl group of 7-deazaguanine, resulting in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) By similarity. HAMAP-Rule MF_00168

Catalytic activity

Guanine34 in tRNA + queuine = queuosine34 in tRNA + guanine. HAMAP-Rule MF_00168

Guanine34 in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7-carbaguanine34 in tRNA + guanine. HAMAP-Rule MF_00168

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00168

Pathway

tRNA modification; tRNA-queuosine biosynthesis. HAMAP-Rule MF_00168

Sequence similarities

Belongs to the queuine tRNA-ribosyltransferase family.

Ontologies

Keywords
   Biological processQueuosine biosynthesis
tRNA processing
   LigandMetal-binding
Zinc
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processqueuosine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

queuine tRNA-ribosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361Queuine tRNA-ribosyltransferase HAMAP-Rule MF_00168
PRO_0000135513

Sites

Active site921Nucleophile By similarity
Metal binding3041Zinc By similarity
Metal binding3061Zinc By similarity
Metal binding3091Zinc By similarity
Metal binding3351Zinc By similarity
Binding site931Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92GM6 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 1BEC5C2C39341A84

FASTA36140,590
        10         20         30         40         50         60 
MSKFSFNIHH QHKKARSGII VTAHGEMRTP AFMPVGTRGT VKAMLPESVA ETGADILLGN 

        70         80         90        100        110        120 
TYHLMLQPTA ERIVQLGGLH KFMNWDKPIL TDSGGFQVMS LSKLCKITEE GVSFSSHING 

       130        140        150        160        170        180 
DKYMLTPERS TEIQYLLGST ITMAFDECTP YPATFEEAKT SMQLTTRWAN RSRNAFVKRE 

       190        200        210        220        230        240 
GYAQFGIIQG SVYEELREQS AKDLVELDFE GYAIGGLAVG EGQELMFKVL DYAPEFLPQN 

       250        260        270        280        290        300 
KPRYLMGVGK PVDIIGAVSR GIDMFDCVIP TRSGRNGQAF TKYGTVNIRN SKYADDNKPL 

       310        320        330        340        350        360 
EHDCLCPACR NYSKAYLHHL VRIGEILGSM LMTWHNLTYF QNLMSRIRAY IKLGKDFDFD 


S 

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References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL03635.1.
PIRA97837.
RefSeqNP_360734.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92GM6.
SMRQ92GM6. Positions 3-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC1097.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL03635; AAL03635; RC1097.
GeneID928246.
KEGGrco:RC1097.
PATRIC17889654. VBIRicCon45613_1260.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0343.
HOGENOMHOG000223473.
KOK00773.
OMATPRFMPV.
OrthoDBEOG6SNDVG.
ProtClustDBPRK00112.

Enzyme and pathway databases

UniPathwayUPA00392.

Family and domain databases

Gene3D3.20.20.105. 1 hit.
HAMAPMF_00168. Q_tRNA_Tgt.
InterProIPR004803. Queuine_tRNA-ribosylTrfase.
IPR002616. tRNA_ribo_trans-like.
[Graphical view]
PANTHERPTHR11962. PTHR11962. 1 hit.
PfamPF01702. TGT. 1 hit.
[Graphical view]
SUPFAMSSF51713. SSF51713. 1 hit.
TIGRFAMsTIGR00430. Q_tRNA_tgt. 1 hit.
TIGR00449. tgt_general. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTGT_RICCN
AccessionPrimary (citable) accession number: Q92GM6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Rickettsia conorii

(strain Malish 7): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways