QTRT2_DROWI
ID QTRT2_DROWI Reviewed; 428 AA.
AC B4N549;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GK20504;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH964101; EDW79488.1; -; Genomic_DNA.
DR RefSeq; XP_002068502.1; XM_002068466.2.
DR AlphaFoldDB; B4N549; -.
DR SMR; B4N549; -.
DR STRING; 7260.FBpp0249647; -.
DR EnsemblMetazoa; FBtr0251155; FBpp0249647; FBgn0222501.
DR GeneID; 6645802; -.
DR KEGG; dwi:6645802; -.
DR eggNOG; KOG3909; Eukaryota.
DR HOGENOM; CLU_037350_0_0_1; -.
DR InParanoid; B4N549; -.
DR OMA; AKEMTAW; -.
DR OrthoDB; 883398at2759; -.
DR PhylomeDB; B4N549; -.
DR Proteomes; UP000007798; 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..428
FT /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT /id="PRO_0000383942"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT BINDING 365
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ SEQUENCE 428 AA; 47757 MW; 100DCC256F8BA133 CRC64;
MKFLVENINK NSGRLGLLDL KAAGGGIQLK TPLLMQTTKG GSIPYLSADL FENYVQNKNG
QEPVPVLLQL TLSTMQQMAE SLALWPASLS HYLGFPGQGN VLLLRDPCES TPSGGNDRDV
APIFTRQGKE SLTPERYMEI IASFKPDIYQ GLCDADTNLE SSKKRVQKSV DRTERFMDYI
YEQHGKLQST SSSLLAPIVG GYNIFARTQS IKHARQQPEG KYSGYILEGF HNNGLSATAL
DGSQLLPIVE HCVKQLEENK IKMMPGAYSP LIILELIHIG VDVFDTSYAY CAAVNFKALV
FNYDEKSIEP RPTPFLDITD EAIKEEFVPL LDNCKCLTCQ KHTRAYVHHL YKTNELLGPI
LLMIHNLHHF MGFFETIRSS IAQDKLPKLI DLVCKQNGDS KVDYSIEKNV KVISKAVVGK
GFETTTES