ID   QTRT2_XENLA             Reviewed;         415 AA.
AC   Q6DF96;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
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};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) 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; BC076845; AAH76845.1; -; mRNA.
DR   RefSeq; NP_001086589.1; NM_001093120.1.
DR   AlphaFoldDB; Q6DF96; -.
DR   SMR; Q6DF96; -.
DR   BioGRID; 103284; 1.
DR   DNASU; 446424; -.
DR   GeneID; 446424; -.
DR   KEGG; xla:446424; -.
DR   CTD; 446424; -.
DR   Xenbase; XB-GENE-6256231; qtrt2.L.
DR   OrthoDB; 883398at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 446424; Expressed in oocyte and 19 other tissues.
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; 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   2: Evidence at transcript level;
KW   Cytoplasm; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion outer membrane; Reference proteome; tRNA processing; Zinc.
FT   CHAIN           1..415
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000295635"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         353
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"
FT   BINDING         382
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   415 AA;  45980 MW;  CFEB3B5E3E44EC41 CRC64;
     MKLSLSKVTS GARLGVISNF GRNGDKTLEV PGCLLYTKTA SPPHLTHDTL QTIEGVPAVT
     HITLSTLAEH QEVLEEYKEG IGKFAGLPDA VFYCSTHDPV SPCPTGYNTN KAVSLWGSGG
     RIEMTTQKFI SAQRVLRPDW FQCLSDGEVT PGGNSRKRIK KSVDRSLVFL DECLQLLSEH
     EELKPCVLIG AVEGGDLLDE RLRSARETAK RPVGGFLLDG FHGISAGNEA KLSLVSAVTA
     ELPEDKPRFI HGVGRPDEVL EFIQRGVDLF DSCFPYQVTE RGCALIFTHC HRPDPETAVL
     EKSEMSDTER NGDVGAEIEE PDADQAEMTP FEICLKEKRF REDFGPLLEG CTCYCCRNHS
     RAYVHHLLMA KELLAGILLM IHNFQHYFSF FSSIRAALRD GEIKALAELI RKQNS