NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1159/000079829; PubMed=15383718 [NCBI, ExPASy, EBI, Israel, Japan]
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential.";
J. Mol. Microbiol. Biotechnol. 7:204-211(2004).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1186/gb-2004-5-10-r77; PubMed=15461803 [NCBI, ExPASy, EBI, Israel, Japan]
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species.";
Genome Biol. 5:RESEARCH077.1-RESEARCH077.12(2004).

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

AE017333; AAU41765.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CP000002; AAU24402.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_080040.1; -.
YP_092458.1; -.

3D structure databases

ModBase

Q65GP9.

Enzyme and pathway databases

BioCyc

BLIC279010:BL01140-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.

ProtoNet

Q65GP9.

Genome annotation databases

GeneID

3028240; -.
3098221; -.

GenomeReviews

CP000002_GR; BL01140.
AE017333_GR; BLi02897.

KEGG

bld:BLi02897; -.
bli:BL01140; -.

NMPDR

fig|279010.5.peg.3224; -.

Phylogenomic databases

HOGENOM

Q65GP9; -.

Genome annotation databases

CMR

Q65GP9; BLi02897.

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`	`1 381`	`381`	`Queuine tRNA-ribosyltransferase.`	`PRO_0000135450`
`ACT_SITE`	`96 96`		`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`	`97 97`		`Substrate (By similarity).`

Sequence information

Length: 381 AA [This is the length of the unprocessed precursor]

Molecular weight: 43615 Da [This is the MW of the unprocessed precursor]

CRC64: 235D1C594D363823 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQQPIRYEF IKACKQTGAR LGRVHTPHGS FETPVFMPVG TLATVKTMSP EELKEMGADI 

        70         80         90        100        110        120 
ILSNTYHLWL RPGHDIVKEA GGLHQFMNWN RAILTDSGGF QVFSLSEFRK IEEEGVHFRN 

       130        140        150        160        170        180 
HLNGDKLFLS PEKAMEIQNA LGSDIMMAFD ECPPYPAEYD YMKKSVERTS RWAERCLKAH 

       190        200        210        220        230        240 
NRPDEQGLFG IVQGGEYENL RKQSAKDLIS LDFPGYAIGG LSVGEPKDVM NRVLEFTTPL 

       250        260        270        280        290        300 
LPADKPRYLM GVGSPDSLID GAIRGVDMFD CVLPTRIARN GTLMTSEGRL VVKNAKYERD 

       310        320        330        340        350        360 
FRPIDEQCDC YTCRNYSRAY IRHLIRCNET FGIRLTSYHN LYFLLKLMGQ VRDAIREDRL 

       370        380 
GDFREEFFER YGFNKPNAKS F

Q65GP9 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