ID   QTRT2_TRIAD             Reviewed;         369 AA.
AC   B3RNT0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=TRIADDRAFT_53275;
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Trichoplacidae; Trichoplax.
OX   NCBI_TaxID=10228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999;
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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; DS985242; EDV28066.1; -; Genomic_DNA.
DR   RefSeq; XP_002109900.1; XM_002109864.1.
DR   AlphaFoldDB; B3RNT0; -.
DR   SMR; B3RNT0; -.
DR   STRING; 10228.TriadP53275; -.
DR   PRIDE; B3RNT0; -.
DR   EnsemblMetazoa; TriadT53275; TriadP53275; TriadG53275.
DR   GeneID; 6750565; -.
DR   KEGG; tad:TRIADDRAFT_53275; -.
DR   CTD; 6750565; -.
DR   eggNOG; KOG3909; Eukaryota.
DR   HOGENOM; CLU_037350_0_0_1; -.
DR   InParanoid; B3RNT0; -.
DR   OMA; MAGSRMK; -.
DR   OrthoDB; 883398at2759; -.
DR   PhylomeDB; B3RNT0; -.
DR   Proteomes; UP000009022; 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; IBA:GO_Central.
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; 2.
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..369
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000383945"
FT   REGION          263..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         308
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         339
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   369 AA;  41705 MW;  D40293D97A7D2415 CRC64;
     MNFKVRVIDL AGSCCRLGAL QFGTKVVETP GCLIYNRSGV VPHLTPDILE TLDNVPPIMH
     TPLASIIEEP GLIKLRGYGK GLASFIGYKD NSVYISASDY QGEAMYQYNE NKSISVWTKT
     GRTKVTPDDY SKFVEVCRPS WYQSLCDTVP ANASIKRTRK SVDRTLEFLD QCLKYREKHD
     SLKTSELWAA VEGGGLVDER QRSAKESATR PVFGFTLEGF GSDQMNVETI FELLPLTTQN
     LPVEKPRLIH AIGSPTINSL SRSSKLTEVE EENGNDSSND QDRTATFSLL NLREDRYNED
     FSPLVSGCKC FVCSNHTRAY IHHLIINNEM LGGVLLMTHN LFQYIEFFRC IRTSLKNNKW
     KELRKLFDA