ID D0NHT2_PHYIT Unreviewed; 409 AA.
AC D0NHT2;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000256|HAMAP-Rule:MF_03218};
DE EC=2.4.2.64 {ECO:0000256|HAMAP-Rule:MF_03218};
DE AltName: Full=Guanine insertion enzyme {ECO:0000256|HAMAP-Rule:MF_03218};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000256|HAMAP-Rule:MF_03218};
GN ORFNames=PITG_12050 {ECO:0000313|EMBL:EEY59007.1};
OS Phytophthora infestans (strain T30-4) (Potato late blight agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=403677 {ECO:0000313|EMBL:EEY59007.1, ECO:0000313|Proteomes:UP000006643};
RN [1] {ECO:0000313|Proteomes:UP000006643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T30-4 {ECO:0000313|Proteomes:UP000006643};
RX PubMed=19741609; DOI=10.1038/nature08358;
RG The Broad Institute Genome Sequencing Platform;
RA Haas B.J., Kamoun S., Zody M.C., Jiang R.H., Handsaker R.E., Cano L.M.,
RA Grabherr M., Kodira C.D., Raffaele S., Torto-Alalibo T., Bozkurt T.O.,
RA Ah-Fong A.M., Alvarado L., Anderson V.L., Armstrong M.R., Avrova A.,
RA Baxter L., Beynon J., Boevink P.C., Bollmann S.R., Bos J.I., Bulone V.,
RA Cai G., Cakir C., Carrington J.C., Chawner M., Conti L., Costanzo S.,
RA Ewan R., Fahlgren N., Fischbach M.A., Fugelstad J., Gilroy E.M., Gnerre S.,
RA Green P.J., Grenville-Briggs L.J., Griffith J., Grunwald N.J., Horn K.,
RA Horner N.R., Hu C.H., Huitema E., Jeong D.H., Jones A.M., Jones J.D.,
RA Jones R.W., Karlsson E.K., Kunjeti S.G., Lamour K., Liu Z., Ma L.,
RA Maclean D., Chibucos M.C., McDonald H., McWalters J., Meijer H.J.,
RA Morgan W., Morris P.F., Munro C.A., O'Neill K., Ospina-Giraldo M.,
RA Pinzon A., Pritchard L., Ramsahoye B., Ren Q., Restrepo S., Roy S.,
RA Sadanandom A., Savidor A., Schornack S., Schwartz D.C., Schumann U.D.,
RA Schwessinger B., Seyer L., Sharpe T., Silvar C., Song J., Studholme D.J.,
RA Sykes S., Thines M., van de Vondervoort P.J., Phuntumart V., Wawra S.,
RA Weide R., Win J., Young C., Zhou S., Fry W., Meyers B.C., van West P.,
RA Ristaino J., Govers F., Birch P.R., Whisson S.C., Judelson H.S.,
RA Nusbaum C.;
RT "Genome sequence and analysis of the Irish potato famine pathogen
RT Phytophthora infestans.";
RL Nature 461:393-398(2009).
CC -!- FUNCTION: 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). Catalysis occurs
CC through a double-displacement mechanism. The nucleophile active site
CC attacks the C1' of nucleotide 34 to detach the guanine base from the
CC RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor
CC active site deprotonates the incoming queuine, allowing a nucleophilic
CC attack on the C1' of the ribose to form the product.
CC {ECO:0000256|HAMAP-Rule:MF_03218}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(34) in tRNA + queuine = guanine + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:16633, Rhea:RHEA-COMP:10341, Rhea:RHEA-
CC COMP:18571, ChEBI:CHEBI:16235, ChEBI:CHEBI:17433, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:194431; EC=2.4.2.64; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_03218};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03218};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit and an accessory subunit.
CC {ECO:0000256|HAMAP-Rule:MF_03218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03218}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000256|HAMAP-Rule:MF_03218}.
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; DS028138; EEY59007.1; -; Genomic_DNA.
DR RefSeq; XP_002901480.1; XM_002901434.1.
DR AlphaFoldDB; D0NHT2; -.
DR STRING; 403677.D0NHT2; -.
DR EnsemblProtists; PITG_12050T0; PITG_12050T0; PITG_12050.
DR GeneID; 9471018; -.
DR KEGG; pif:PITG_12050; -.
DR VEuPathDB; FungiDB:PITG_12050; -.
DR eggNOG; KOG3908; Eukaryota.
DR HOGENOM; CLU_022060_0_1_1; -.
DR InParanoid; D0NHT2; -.
DR OMA; IDLFDCV; -.
DR OrthoDB; 167782at2759; -.
DR Proteomes; UP000006643; Partially assembled 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_00168; Q_tRNA_Tgt; 1.
DR InterPro; IPR004803; TGT.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR NCBIfam; TIGR00430; Q_tRNA_tgt; 1.
DR NCBIfam; TIGR00449; tgt_general; 1.
DR PANTHER; PTHR43530; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1.
DR PANTHER; PTHR43530:SF1; QUEUINE TRNA-RIBOSYLTRANSFERASE CATALYTIC SUBUNIT 1; 1.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; tRNA-guanine transglycosylase; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03218};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_03218};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03218}; Reference proteome {ECO:0000313|Proteomes:UP000006643};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03218};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_03218}; Zinc {ECO:0000256|HAMAP-Rule:MF_03218}.
FT DOMAIN 17..386
FT /note="tRNA-guanine(15) transglycosylase-like"
FT /evidence="ECO:0000259|Pfam:PF01702"
FT REGION 257..263
FT /note="RNA binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT REGION 281..285
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 98..102
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03218"
SQ SEQUENCE 409 AA; 45609 MW; 6CD06BD25B360349 CRC64;
MKMPSALSFE VLGRHHRARA ATLTLPHGEV RTPVYMAVGT QGAIKGLTTQ QMQEQPVDCQ
IFLANTYHLA LRPGTEVLAQ LPGKLHEFMQ WPRNLLTDSG GFQMVSLSRL CQVSEHGVQF
ESFVDGSTML LTPEASIAHQ NRIGADIIMA LDDVVSSLTD DDERFKEACG RTVRWLDRCI
QAHAHPDKQN LFGIVQGGLD VSEGGLRDQC LTELIKRDLP GYAIGGLAGG ESKEAFWKVV
AKCTAQLPEN KPRYLMGVGY PLDLVVCSAL GVDMFDCVYP TRTARFGTAI VPSGLLKLKS
AKCELDSRPI DDTCECFVCK KYTRAYLRVL LKKEETFGDA EATTGSIGAH LVTYHNVTYM
LNLMRRLRQS IIDRKFEQFV QNFMLQQFPE RNYPQWAVDA LTEAKISLN
//
