ID   QTRT2_PONAB             Reviewed;         415 AA.
AC   Q5R998;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-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; CR859492; CAH91662.1; -; mRNA.
DR   RefSeq; NP_001129001.1; NM_001135529.1.
DR   AlphaFoldDB; Q5R998; -.
DR   SMR; Q5R998; -.
DR   STRING; 9601.ENSPPYP00000015129; -.
DR   GeneID; 100190841; -.
DR   KEGG; pon:100190841; -.
DR   CTD; 79691; -.
DR   eggNOG; KOG3909; Eukaryota.
DR   InParanoid; Q5R998; -.
DR   Proteomes; UP000001595; 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; 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_0000295634"
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;  46829 MW;  521DEABF459C9B4E CRC64;
     MRLSLTKVVN GCRLGKIINL GKTGDHTMDI PGCLLYTKTG SAPHLTHHTL HNIHGVPAMA
     QLTLSSLAEH HEVLREYKEG VGKFIGMPES LLYCSLHDPV SPCPAGYVTN KSVSVWSVAG
     RVEMTVSKFM AIQQALQPDW FQCLSDGEVS CKEATSIKRV RKSVDRSLLF LDNCLRLQEE
     SEVLQKSVII GVIEGGDVME ERLRSARETA KRPVGGFLLD GFQGNPTTLE TRLRLLSSVT
     AELPEDKPRL ISGVSRPDEV LECIERGVDL FESFFPYQVT ERGCALTFSF DYQPNPEETL
     LQQNGTQEEI KCMDQIKKME TTGCNQEITS FEINLKEKKY QEDFNPLVRG CSCYCCKNHT
     RAYIHHLLVT NELLAGVLLM MHNFEHYFGF FHYIREALKS DKLAQLKELI HRQAS