ID   QTRT2_DROER             Reviewed;         418 AA.
AC   B3NCH1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-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=GG14034;
OS   Drosophila erecta (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7220;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14021-0224.01;
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}.
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DR   EMBL; CH954178; EDV51201.1; -; Genomic_DNA.
DR   RefSeq; XP_001972175.1; XM_001972139.2.
DR   AlphaFoldDB; B3NCH1; -.
DR   SMR; B3NCH1; -.
DR   STRING; 7220.FBpp0132580; -.
DR   EnsemblMetazoa; FBtr0134088; FBpp0132580; FBgn0106296.
DR   GeneID; 6545822; -.
DR   KEGG; der:6545822; -.
DR   eggNOG; KOG3909; Eukaryota.
DR   HOGENOM; CLU_037350_0_0_1; -.
DR   OMA; AKEMTAW; -.
DR   OrthoDB; 883398at2759; -.
DR   PhylomeDB; B3NCH1; -.
DR   Proteomes; UP000008711; 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; tRNA processing; Zinc.
FT   CHAIN           1..418
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000383934"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         327
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         356
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   418 AA;  46519 MW;  3A62A20EF84176B5 CRC64;
     MKFAIESISK NSGRLGQLRI KDGGPELKTP LLLQTTKGGS IPWLSADVFE SHVSQKPQVL
     QFTLSTMDQM TEALTHWNSG GGNGLSGYVG LPGHLNILMV RDPCETTLSG GNDRDIMPLF
     TRRGKESLSS ERYMEMVASF KPDIYQGLCD ADTNLDSAKK RIQKSVDRTE KFMHYIYEHR
     CKVNSTLLAP IVGGYNTFAR TQSIKHAREQ PAGSYGGYIF EGFHTNGLTA TTLDTSKLLP
     IVEHCVKQLE EDKPRILPGA YTPLTILELI RQGIDVFDSS YAYCASLNFK ALTFSFVQDA
     VEHVPFLDIT DEAIKEDFTP PLSECSCLTC QKHTRAYLHH LYKTNELLGP ILLMVHNIHH
     YMAFFEEIRE SVAKDALPQL TELVRNQNGK TQVDYSIAAN NKVISKATMG KGFAAAAV