QTRT2_DROMO
ID QTRT2_DROMO Reviewed; 416 AA.
AC B4KXI8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000255|HAMAP-Rule:MF_03043};
DE AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03043};
GN ORFNames=GI13356;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Non-catalytic subunit of the queuine tRNA-ribosyltransferase
CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-
CC Rule:MF_03043}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03043};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03043};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_03043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000255|HAMAP-Rule:MF_03043}.
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; CH933809; EDW18674.1; -; Genomic_DNA.
DR RefSeq; XP_002008198.1; XM_002008162.2.
DR AlphaFoldDB; B4KXI8; -.
DR SMR; B4KXI8; -.
DR STRING; 7230.FBpp0162573; -.
DR EnsemblMetazoa; FBtr0164081; FBpp0162573; FBgn0136113.
DR GeneID; 6582497; -.
DR KEGG; dmo:Dmoj_GI13356; -.
DR eggNOG; KOG3909; Eukaryota.
DR HOGENOM; CLU_037350_0_0_1; -.
DR InParanoid; B4KXI8; -.
DR OMA; AKEMTAW; -.
DR OrthoDB; 883398at2759; -.
DR PhylomeDB; B4KXI8; -.
DR Proteomes; UP000009192; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.105; -; 1.
DR HAMAP; MF_03043; QTRT2; 1.
DR InterPro; IPR028592; QTRTD1.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..416
FT /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT /id="PRO_0000383937"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ SEQUENCE 416 AA; 47104 MW; 7F5A26BB616245E5 CRC64;
MKFIIKSISK NSGRLGQLRI KDSKELQTPL LLQTTKGGSI PYLSADVFGM VTQEQQVLQL
TLCTMDQMAE SLAQWNRSLG AYVGYPEYNT LLLLRDPCEA TPTGGNDRDV VPLFTRRGKE
SLTAERYLQL VSSFAPDVYQ GLCDADTNPE STKKRVQKSV DRTERFMEHC YKQHRELDRL
KDSTLLAPIV GGYNTYARTQ SIKHAREQPK GSYGGYIFEG FHTNGLPATR LSPSQLLPIV
EHCVQQIEEE LPRLMPGPLT PVLMLELIRL GIDIFDTSYA YCAAVNYKAL TFSYTIDKEE
HSAFLDVTDE AIREEFKPML EGCKCLACQK HTRAYVHHLY KTNELLGPIL LMIHNLHHYM
GFFDVIRQSI AMDQLSLLLD YVRRQNMPND VNYCIEPNTK VVGKAAMGKG FITAAN