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QTRT2_ANOGA
ID   QTRT2_ANOGA             Reviewed;         432 AA.
AC   Q7Q727;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 3.
DT   03-AUG-2022, entry version 112.
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=AGAP005542;
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
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; AAAB01008960; EAA11801.3; -; Genomic_DNA.
DR   RefSeq; XP_315542.3; XM_315542.4.
DR   AlphaFoldDB; Q7Q727; -.
DR   SMR; Q7Q727; -.
DR   STRING; 7165.AGAP005542-PA; -.
DR   PaxDb; Q7Q727; -.
DR   GeneID; 1276225; -.
DR   KEGG; aga:AgaP_AGAP005542; -.
DR   CTD; 1276225; -.
DR   VEuPathDB; VectorBase:AGAP005542; -.
DR   eggNOG; KOG3909; Eukaryota.
DR   HOGENOM; CLU_037350_2_0_1; -.
DR   InParanoid; Q7Q727; -.
DR   OMA; AKEMTAW; -.
DR   OrthoDB; 883398at2759; -.
DR   PhylomeDB; Q7Q727; -.
DR   Proteomes; UP000007062; Chromosome 2L.
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; IBA:GO_Central.
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..432
FT                   /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT                   /id="PRO_0000383931"
FT   REGION          390..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..432
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         329
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         334
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   432 AA;  48326 MW;  9C85B13E0442CEBC CRC64;
     MKFTLSTVTK CSGRLGVLGG LDRLPNLSLQ TPAFIFHTKG GSIPHLSKEA MQHVSGDPSC
     FLHLSISNTL HMQEAIKASR ITIAEFIAQS NCATLLFVRD PSEPPIPGLP EKDSLPIYTR
     NGRRNITLEQ YMTLVETFRP DAYVPLYDGD TDASSSKKRD QKSLDRTEKF VEQCLEWHRK
     SDALQSSCLI GPVVGGYNEK LREQSVAFLR QSDDAFAGYL IEGLHMHGPS VARMDGSAAL
     GIVANVCKQL PEAKVRLCFG SYDPALVLEM VAAGVDVFDT SYVYLKAAQE HRALVFSFDV
     TSTEQEHVTE LDTTDARWAE DFGPLLPGCK CYTCQKHSRA YVHHLHNTRE MLGPILLMMH
     NLHHYVEFFK AIRHHVANDS LPELRNHLAG QKSLPPYEPP KEEKLPMPAA QKAELMEPME
     DLGEKQNKKQ RA
 
 
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