ID   QTRT2_CULQU             Reviewed;         429 AA.
AC   B0WAN0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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=CPIJ003941;
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB;
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA   Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS231873; EDS41584.1; -; Genomic_DNA.
DR   RefSeq; XP_001845764.1; XM_001845712.1.
DR   AlphaFoldDB; B0WAN0; -.
DR   SMR; B0WAN0; -.
DR   STRING; 7176.CPIJ003941-PA; -.
DR   GeneID; 6035615; -.
DR   KEGG; cqu:CpipJ_CPIJ003941; -.
DR   VEuPathDB; VectorBase:CPIJ003941; -.
DR   VEuPathDB; VectorBase:CQUJHB017870; -.
DR   eggNOG; KOG3909; Eukaryota.
DR   HOGENOM; CLU_037350_0_0_1; -.
DR   InParanoid; B0WAN0; -.
DR   OMA; MAGSRMK; -.
DR   OrthoDB; 883398at2759; -.
DR   PhylomeDB; B0WAN0; -.
DR   Proteomes; UP000002320; Partially assembled 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..429
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000383932"
FT   BINDING         330
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         332
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         335
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         361
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   429 AA;  47602 MW;  EEA3697BC74F7ECF CRC64;
     MKFVLETVSK CSGRLGSLSG VDRLASSAKF QTPTLVLHTK GGSVPHLSKE VLHYLTGAEP
     QLMQYSLNGT VHMEEAVRGC GDGLSGFVAQ KESVSLLVLR DPAEPCQPGY HEKDVVPVFG
     RSGRKNFTAE SYMSLVEAFR PDVYVPLFDG DTDGGSSKKR EQRSQERTET FVEQCLEVHR
     KSEKLKGASV LGPIVGGYNK KLREKSVQFV ERLKDDFAGY FIAGLHSYGS SASEVKEAPL
     LDIVSSVCQQ LPLEKPKFLF GAFTPQLVLE LVVRGVDIFD TSYPYLKTQQ NRALNFSFDT
     SDSNVVARKN ELDLTDACWA EDFTGFVDGC QCLACTKHTK AYTHHLYNTR EMLAPILLMI
     HNLHHYFEFF KAIRRHVAQD TVGELIAHIN KHVVLPVTDG VVKEPGKSLD GVELKESASV
     QVEAKRVKV