ID A0A182GIG0_AEDAL Unreviewed; 423 AA.
AC A0A182GIG0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000256|HAMAP-Rule:MF_03043};
DE AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000256|HAMAP-Rule:MF_03043};
GN ORFNames=RP20_CCG010460 {ECO:0000313|EMBL:KXJ82951.1};
OS Aedes albopictus (Asian tiger mosquito) (Stegomyia albopicta).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7160 {ECO:0000313|EnsemblMetazoa:AALF010460-PA.1, ECO:0000313|Proteomes:UP000069940};
RN [1] {ECO:0000313|EMBL:KXJ82951.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ82951.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ82951.1};
RX PubMed=26483478; DOI=10.1073/pnas.1516410112;
RA Chen X.G., Jiang X., Gu J., Xu M., Wu Y., Deng Y., Zhang C., Bonizzoni M.,
RA Dermauw W., Vontas J., Armbruster P., Huang X., Yang Y., Zhang H., He W.,
RA Peng H., Liu Y., Wu K., Chen J., Lirakis M., Topalis P., Van Leeuwen T.,
RA Hall A.B., Jiang X., Thorpe C., Mueller R.L., Sun C., Waterhouse R.M.,
RA Yan G., Tu Z.J., Fang X., James A.A.;
RT "Genome sequence of the Asian Tiger mosquito, Aedes albopictus, reveals
RT insights into its biology, genetics, and evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E5907-E5915(2015).
RN [2] {ECO:0000313|EMBL:KXJ82951.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Foshan {ECO:0000313|EMBL:KXJ82951.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:KXJ82951.1};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:AALF010460-PA.1}
RP IDENTIFICATION.
RC STRAIN=Foshan {ECO:0000313|EnsemblMetazoa:AALF010460-PA.1};
RG EnsemblMetazoa;
RL Submitted (AUG-2022) to UniProtKB.
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:0000256|HAMAP-
CC Rule:MF_03043}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03043};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_03043};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03043}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03043}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000256|HAMAP-Rule:MF_03043}.
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DR EMBL; JXUM01011978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; JXUM01011979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KQ560342; KXJ82951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A182GIG0; -.
DR STRING; 7160.A0A182GIG0; -.
DR EnsemblMetazoa; AALF010460-RA; AALF010460-PA; AALF010460.
DR VEuPathDB; VectorBase:AALC636_005488; -.
DR VEuPathDB; VectorBase:AALF010460; -.
DR VEuPathDB; VectorBase:AALFPA_047329; -.
DR Proteomes; UP000069940; Unplaced.
DR Proteomes; UP000249989; 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:tRNA-guanosine(34) queuine transglycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.105; Queuine tRNA-ribosyltransferase-like; 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 NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR46064; QUEUINE TRNA-RIBOSYLTRANSFERASE ACCESSORY SUBUNIT 2; 1.
DR PANTHER; PTHR46064:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE ACCESSORY SUBUNIT 2; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03043};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03043};
KW Reference proteome {ECO:0000313|Proteomes:UP000249989};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03043};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_03043}.
FT DOMAIN 43..392
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 397..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT BINDING 361
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
SQ SEQUENCE 423 AA; 47986 MW; FD7D9F575290B6BF CRC64;
MKSVLITPYY YYQSLFDRFV IRYLNDSESL LSDLTVHRGG EGGSVPFLSK EVLQYLTSDP
PPMLHSLTNT DHMEEAIRAC GEGISSFVGQ KDSISLLVLK DPAELCKPSF HEKDFVPIFS
RSGRKNFTSE RYMQLVEAFK PDVFVPLFDG DTDPESSKKR LQKSLDRTEK FVEQCIEAHR
KSTNLKQSSL LGPIVGGYNL KLRKESVKFL EPFKDDLGGY LIAGLHSNGS SAGDLKESNL
LEVVSHACQL LPADKARFMF GAFSPGTVLK LVSNGIDVLD TSYAYLKTQQ NRALTFSFDV
HEKDVESRET ELDVRDPKWT EDFNGFIESC SCLACTKHTK AYAHHLYNTR EMLGPIILMI
HNLHHYLEFF KVIRKHVKED TLNLLIEHLQ KQKDAPLFEE TSTDKAKSDL LEPSDNVTKK
LKV
//
