ID D2NPM3_ROTMD Unreviewed; 466 AA. AC D2NPM3; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 21-SEP-2011, entry version 14. DE RecName: Full=Queuine tRNA-ribosyltransferase; DE EC=2.4.2.29; GN OrderedLocusNames=RMDY18_17590; OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Micrococcaceae; Rothia. OX NCBI_TaxID=680646; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DY-18; RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H., RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., RA Fukushima H.; RT "Isolation and identification of Rothia mucilaginosa from persistent RT apical periodontitis lesions."; RL J Osaka Dent Univ 44:93-98(2010). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=DY-18; RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., RA Leung K.-P., Fukushima H.; RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical RT Isolate with Dense Meshwork-Like Structures from a Persistent Apical RT Periodontitis Lesion."; RL Sequencing 2010:457236-457236(2010). 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 + 7-aminomethyl-7-carbaguanine CC = [tRNA]-7-aminomethyl-7-carbaguanine + guanine. CC -!- CATALYTIC ACTIVITY: [tRNA]-guanine + queuine = [tRNA]-queuine + CC guanine. CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity). CC -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. 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; AP011540; BAI65591.1; -; Genomic_DNA. DR RefSeq; YP_003363411.1; NC_013715.1. DR GeneID; 8694711; -. DR GenomeReviews; AP011540_GR; RMDY18_17590. DR KEGG; rmu:RMDY18_17590; -. DR OMA; FMPVGTV; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; 2. 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 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Metal-binding; KW Queuosine biosynthesis; Transferase; tRNA processing; Zinc. SQ SEQUENCE 466 AA; 51371 MW; D80AECC5B94CCDA7 CRC64; MRTPPPAKEA GFSGRLGCRH SDGKQTIERR MSVLDNSFPT EDFGFTITSR LADTASPSAE RVEANGGQFR GRTGVITTPH GQIQTPAFTP VGTKATVKAV LPESMKELGA QALLSNAYHL YLQPGPEILD AAGGLGAFMN WDGPTFTDSG GFQVMSLGSG FKKVIDMGTV ADAKGADGRP LGDDDVAKGK ERLAHIDDDG VNFKSHIDGS IHRFTPEVSM QVQHQIGADV MFAFDELTTL YNSRGYQEEA LERTRLWALR CIAEHQRLTA ERVGKPYQAL FGVIQGAQYE DLRRKACQDL GSMPFDGFGI GGALEKENLG TIVRWCAEEL PESKPRHLLG ISEPDDIFVG IENGVDTFDC VSPTRVARNA AVYSPTGRYN ITNARFKADF SPIYEGCDCY TCTHYTRAYL RHLFKADERL AATLASIHNE RFIVRMVDDA REAIKDGTYF EYRDEFLGNY YSGKKP //