QTRT2_DROPE
ID QTRT2_DROPE Reviewed; 417 AA.
AC B4H1X9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=GL17966;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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; CH479203; EDW30331.1; -; Genomic_DNA.
DR RefSeq; XP_002024858.1; XM_002024822.1.
DR AlphaFoldDB; B4H1X9; -.
DR SMR; B4H1X9; -.
DR STRING; 7234.FBpp0182073; -.
DR EnsemblMetazoa; FBtr0183581; FBpp0182073; FBgn0155569.
DR GeneID; 6599839; -.
DR KEGG; dpe:6599839; -.
DR eggNOG; KOG3909; Eukaryota.
DR HOGENOM; CLU_037350_0_0_1; -.
DR OMA; MAGSRMK; -.
DR PhylomeDB; B4H1X9; -.
DR Proteomes; UP000008744; 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; 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 3: Inferred from homology;
KW Cytoplasm; Metal-binding; Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..417
FT /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT /id="PRO_0000383938"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 329
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"
SQ SEQUENCE 417 AA; 46303 MW; B5FCC457D19D5195 CRC64;
MKFVIESLTK NSGRLGRLHI KDGAPGQRTP LLMQTTKGGS IPYLSADVFE SHVTETPQLL
ELTLSTIDHM SEALAQFNSA DRGLSDYIGF PGHLNVLLLR DPCETTPAGG NDRDIQPLFT
RRGKESLSPK RYMEMVASLR PDIYQGLCDA DTNAESAKKR VQKSVDRTEK FMHYIYEHKS
KVDSTLLAPI VGGYNTFART QSIKHALEQP SGSYGGYVFE GFHTNGLSAT ILDASKLLPI
VEHCVGQLEE EKPRMVPGAY TPLTTLELIG LGMDLFDTSY AYCAAVNFKA LTFTFVQDEV
VHVPFLDITD DAIKEDFSPL LKNCVCLSCQ KHTRAYVHHL YKTNELLGPI LLMVHNLHHY
MAFFEAIRES IARDGLPQLT ELVRRQNGDS QVDYSIAPNR KVISKATMGK GFAAAAV
