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

CP000885; ABX43791.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001560530.1; -.

3D structure databases

ModBase

A9KHU4.

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.

TIGRFAMs

TIGR00430; Q_tRNA_tgt; 1.
TIGR00449; tgt_general; 1.

ProtoNet

A9KHU4.

Genome annotation databases

GeneID

5743550; -.

GenomeReviews

CP000885_GR; Cphy_3438.

KEGG

cpy:Cphy_3438; -.

CMR

A9KHU4; Cphy_3438.

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`	`1 378`	`378`	`Queuine tRNA-ribosyltransferase.`	`PRO_1000077002`
`ACT_SITE`	`89 89`		`Nucleophile (By similarity).`
`METAL`	`309 309`		`Zinc (By similarity).`
`METAL`	`311 311`		`Zinc (By similarity).`
`METAL`	`314 314`		`Zinc (By similarity).`
`METAL`	`340 340`		`Zinc (By similarity).`
`BINDING`	`90 90`		`Substrate (By similarity).`

Sequence information

Length: 378 AA [This is the length of the unprocessed precursor]

Molecular weight: 42718 Da [This is the MW of the unprocessed precursor]

CRC64: 6A74358309962209 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYKLICKDGN AKRGEFTTVH GKIQTPVFMN VGTAAAIKGA VSTMDLQEIG TQVELSNTYH 

        70         80         90        100        110        120 
LHVRPGDEVV KKLGGLHKFM VWDKPILTDS GGFQVFSLAG LRKIKEEGVY FNSHIDGKKI 

       130        140        150        160        170        180 
FMGPEESMRI QSNLASTIAM AFDECPPHPA TREYMEDSVA RTTRWLLRCK NEMNRLNTLE 

       190        200        210        220        230        240 
DTINKHQMLF GINQGGTYTD IRVEHAKRIS ELDLDGYALG GLAVGESHSE MYRIIEETVP 

       250        260        270        280        290        300 
YLPEAKPTYL MGVGTPANIL EAVERGVDFF DCVYPARNGR HGHAYTNHGK MNLLNAKYEL 

       310        320        330        340        350        360 
DDRPIEEGCG CPVCKNYSRG YIRHLLKAKE MLGLRFLVTH NLYFYNKMME EIREAIENQN 

       370 
FASYKKKKLE GFAAEQGN

A9KHU4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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