QTRT2_DROGR
ID QTRT2_DROGR Reviewed; 419 AA.
AC B4IXD3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=GH16210;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH916366; EDV96370.1; -; Genomic_DNA.
DR RefSeq; XP_001984022.1; XM_001983986.1.
DR AlphaFoldDB; B4IXD3; -.
DR SMR; B4IXD3; -.
DR STRING; 7222.FBpp0150116; -.
DR EnsemblMetazoa; FBtr0151624; FBpp0150116; FBgn0123681.
DR GeneID; 6558174; -.
DR KEGG; dgr:6558174; -.
DR eggNOG; KOG3909; Eukaryota.
DR HOGENOM; CLU_037350_0_0_1; -.
DR InParanoid; B4IXD3; -.
DR OMA; AKEMTAW; -.
DR OrthoDB; 883398at2759; -.
DR PhylomeDB; B4IXD3; -.
DR Proteomes; UP000001070; 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..419
FT /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT /id="PRO_0000383935"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 357
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ SEQUENCE 419 AA; 47028 MW; C6ED4B75EBA95CEE CRC64;
MKFVIKSISK NSGRLGQLRI GKESNELQTP LLMQTTKGGS IPYLSGDVFD SVCKGQQQQQ
LLQLTLSTMD QMAESLVQWN RSLSEYVGLP GHATVLLLRD PCETTPAGGN DRDVVPLFTR
RGKESLTATR YLELVSSFAP DVYQGLCDAD TNPDSTKKRV QKSVDRTERF MEQCYERRVE
NSTLLAPIVG GYNTFARTQS IKHARQQPAG SYGGYILEGF HSNGLAATEL KATQLLPIVE
HCVQQLEEEQ PRLMPGAYTP LLMLELIRQG IDIFDTSYAY CAAVNYKALS FSYKLDEIRP
DDEHTPLLDM TAEEYKEQFK PLLSGCTCLA CEKHTRAYHH HLYKTHELLG PILLMIHNLH
HLMGFFDVIR ASIGTDQLPA LLEHLRMQNT STEINYRIEP NNKIVTKAAM GKGFIAPAV