NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1128/IAI.73.10.6407-6418.2005; PubMed=16177312 [NCBI, ExPASy, EBI, Israel, Japan]
Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
"Comparative genomic analysis of Chlamydia trachomatis oculotropic and genitotropic strains.";
Infect. Immun. 73:6407-6418(2005).

Comments

FUNCTION: Exchanges the guanine residue with 7-aminomethyl-7-deazaguanine in tRNAs with GU(N) 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).
CATALYTIC ACTIVITY: [tRNA]-guanine + queuine = [tRNA]-queuine + guanine.
CATALYTIC ACTIVITY: [tRNA]-guanine + 7-aminomethyl-7-carbaguanine = [tRNA]-7-aminomethyl-7-carbaguanine + guanine.
COFACTOR: Binds 1 zinc ion per subunit (By similarity).
PATHWAY: tRNA modification; queuosine-tRNA biosynthesis .
SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.

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

CP000051; AAX50453.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_328001.1; -.

3D structure databases

ModBase

Q3KMG9.

Enzyme and pathway databases

BioCyc

CTRA315277-1:CTA_0211-MON; -.

Ontologies

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.

Genome annotation databases

GeneID

3687237; -.

GenomeReviews

CP000051_GR; CTA_0211.

KEGG

cta:CTA_0211; -.

Phylogenomic databases

HOGENOM

Q3KMG9; -.

Genome annotation databases

CMR

Q3KMG9; CTA_0211.

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

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 372`	`372`	`Queuine tRNA-ribosyltransferase.`	`PRO_1000016775`
`ACT_SITE`	`89 89`		`Nucleophile (By similarity).`
`METAL`	`319 319`		`Zinc (By similarity).`
`METAL`	`321 321`		`Zinc (By similarity).`
`METAL`	`324 324`		`Zinc (By similarity).`
`METAL`	`351 351`		`Zinc (By similarity).`
`BINDING`	`90 90`		`Substrate (By similarity).`

Sequence information

Length: 372 AA [This is the length of the unprocessed precursor]

Molecular weight: 40932 Da [This is the MW of the unprocessed precursor]

CRC64: B4F7FF3B79D294DB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALRFEILHQ SKKSRARVGR IETAHGYIDT PAFVPVATNG ALKGVLDHSN IPLMFCNTYH 

        70         80         90        100        110        120 
LIVHPGAEAI AAMGGLHQFI GRNAPIITDS GGFQIFSLAY GSVAEEIKSC GKKKGGNTII 

       130        140        150        160        170        180 
KVNDDGVHFK SYRDGRKLFL SPEISVQAQK DLGADIILPL DELLPFHADP TYFHQSSQRT 

       190        200        210        220        230        240 
YVWEKRSLDY HLKNPGIQSM YGVIHGGTFP DQRKLGCKFV EDLPFDGSAI GGSLGKNLQD 

       250        260        270        280        290        300 
IVEVVGVTAA NLSAERPRHL LGIGDLPSIW ATVGFGIDSF DSSYPTKAAR HGMILTLQGP 

       310        320        330        340        350        360 
LKINNQRYSS DLNPIEPGCS CLACSQGITR AYLRHLFKVH EPNAGIWASI HNMHHMQKVM 

       370 
REIREGILND RI

Q3KMG9 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 submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools