ID   QTRT2_XENTR             Reviewed;         413 AA.
AC   Q28DX0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Name=qtrt2 {ECO:0000255|HAMAP-Rule:MF_03043};
GN   Synonyms=qtrtd1 {ECO:0000255|HAMAP-Rule:MF_03043}; ORFNames=TEgg038e14.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
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 qtrt1 and an accessory
CC       subunit qtrt2. {ECO:0000255|HAMAP-Rule:MF_03043}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043}.
CC       Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03043};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03043};
CC       Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03043}. Note=May associate
CC       with the mitochondrion outer membrane. {ECO:0000255|HAMAP-
CC       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; CR848556; CAJ83627.1; -; mRNA.
DR   EMBL; BC135739; AAI35740.1; -; mRNA.
DR   RefSeq; NP_001016891.1; NM_001016891.2.
DR   AlphaFoldDB; Q28DX0; -.
DR   SMR; Q28DX0; -.
DR   STRING; 8364.ENSXETP00000006099; -.
DR   PaxDb; Q28DX0; -.
DR   GeneID; 549645; -.
DR   KEGG; xtr:549645; -.
DR   CTD; 79691; -.
DR   Xenbase; XB-GENE-1007716; qtrt2.
DR   eggNOG; KOG3909; Eukaryota.
DR   HOGENOM; CLU_037350_0_0_1; -.
DR   InParanoid; Q28DX0; -.
DR   OrthoDB; 883398at2759; -.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; 1.
DR   SUPFAM; SSF51713; SSF51713; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..413
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000383927"
FT   REGION          298..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         351
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"
FT   BINDING         380
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   413 AA;  45465 MW;  199BFD982765F0E4 CRC64;
     MKLSISKVAN GARLGVISNI GRNGDKTLEV PGCLLYTKTG SPPHLTHDTL QTIEGVPAVT
     HITLSTLAEH QEVLEEYKEG IGKFAGMPDA VLYCSTHDPV SPCPTGYNTN KAVSLWGAGG
     RIEMTAQKFI SAQRVLRPDW FQCLSDGEVT PGGNSRKRVK KSVDRTLAFL DECLQLLSGH
     EDLKPCVLIG AVEGGDLLEE RLRSARETAK RPVGGFLLDG FHGGSAEKEL SLISAVTAAL
     PEDKPRFIHG MGRPDEVLEC VQRGVDLFDS CFPYRVTERG CALIFSHCYR PDPETAVLEK
     SETSGAERNG DVGAESEEPD ADRAEMTSFE ICLKEKRFRE DFRPLLEGCS CYCCRNHSRA
     YVHHLLAAKE LLAGILLMIH NFQHYFRFFG SIRAALRDGE INALAELIRK QSS