ID B2RAR3_HUMAN Unreviewed; 403 AA. AC B2RAR3; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 21-SEP-2011, entry version 27. DE RecName: Full=Queuine tRNA-ribosyltransferase; DE EC=2.4.2.29; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Amygdala; RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., RA Isogai T.; RT "NEDO functional analysis of protein and research application RT project."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Exchanges the guanine residue with 7-aminomethyl-7- CC deazaguanine in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His CC and -Tyr). After this exchange, a cyclopentendiol moiety is CC attached to the 7-aminomethyl group of 7-deazaguanine, resulting CC in the hypermodified nucleoside queuosine (Q) (7-(((4,5-cis- CC dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (By CC similarity). CC -!- CATALYTIC ACTIVITY: [tRNA]-guanine + queuine = [tRNA]-queuine + CC guanine. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK314308; BAG36960.1; -; mRNA. DR IPI; IPI00215974; -. DR UniGene; Hs.631638; -. DR ProteinModelPortal; B2RAR3; -. DR STRING; B2RAR3; -. DR HGNC; HGNC:23797; QTRT1. DR HOVERGEN; HBG101131; -. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00168; Q_tRNA_Tgt; 1; -. DR InterPro; IPR004803; Queuine_tRNA-ribosylTrfase. DR InterPro; IPR002616; tRNA_ribo_trans. DR Gene3D; G3DSA:3.20.20.105; tRNA_ribo_trans; 1. DR PANTHER; PTHR11962; tRNA_ribo_trans; 1. DR Pfam; PF01702; TGT; 1. DR SUPFAM; SSF51713; tRNA_ribo_trans; 1. DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1. DR TIGRFAMs; TIGR00449; Tgt_general; 1. PE 2: Evidence at transcript level; KW Glycosyltransferase; Queuosine biosynthesis; Transferase; KW tRNA processing; Zinc. SQ SEQUENCE 403 AA; 43990 MW; 1CCDDC17BF47A106 CRC64; MAGAATQASL ESAPRIMRLV AECSRSRARA GELWLPHGTV ATPVFMPVGT QATMKGITTE QLDALGCRIC LGNTYHLGLR PGPELIQKAN GLHGFMNWPH NLLTDSGGFQ MVSLVSLSEV TEEGVRFRSP YDGNETLLSP EKSVQIQNAL GSDIIMQLDD VVSSTVTGPR VEEAMYRSIR WLDRCIAAHQ RPDKQNLFAI IQGGLDADLR ATCLEEMTKR DVPGFAIGGL SGGESKSQFW RMVALSTSRL PKDKPRYLMG VGYATDLVVC VALGCDMFDC VFPTRTARFG SALVPTGNLQ LRKKVFEKDF GPIDPECTCP TCQKHSRAFL HALLHSDNTA ALHHLTVHNI AYQLQLMSAV RTSIVEKRFP GFVRDFMGAM YGDPTLCPTW ATDALASVGI TLG //