ID   QTRT2_DANRE             Reviewed;         416 AA.
AC   Q7ZVJ6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 99.
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   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH45519.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC045519; AAH45519.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q7ZVJ6; -.
DR   SMR; Q7ZVJ6; -.
DR   STRING; 7955.ENSDARP00000106901; -.
DR   PaxDb; Q7ZVJ6; -.
DR   ZFIN; ZDB-GENE-060427-4; qtrt2.
DR   eggNOG; KOG3909; Eukaryota.
DR   InParanoid; Q7ZVJ6; -.
DR   PhylomeDB; Q7ZVJ6; -.
DR   PRO; PR:Q7ZVJ6; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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..416
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000383926"
FT   BINDING         350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         352
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         355
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   416 AA;  46090 MW;  2E9C3A2B1D039A1C CRC64;
     MKLELSRVVQ GCRLGVLTGL GKSGQHSLEV PGCLLHTRCA TVPHLTQDTL LTLSDLPAVT
     QVSVDSLAEH HEVLEEFKEG VRKFAGLHDT VIFCSLHDSA SPSPAGHVTN KTVSVWGSGG
     RIELTAARFM SIQAAVQPDC YQSMADGETW QANTSRKRVR KAVDRTLAHL DECLVLHQKT
     QELKHAEIFG VVEGGDILEE RLRSARETAK RPVGGFVLDG FHSSAMDQDV RAQLIQETSA
     ELPQEKPRLV LGVGRPDEVI SCVEAGVDLF ESFFPFQVTE RGCALSFNYT IDPDPETAGT
     SASTVLECNG ETPEVKKPSA NEDVENMTPF EINLKDKRYR DDFRPLVEGC VCYCCQKHMR
     AYVHHLLVTN ELLAGVLLML HNMAHYLGFF KALRDAITSD RLQDFKNTVL HRRQGD