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Database: UniProt
Entry: W2L4M7_PHYPR
LinkDB: W2L4M7_PHYPR
Original site: W2L4M7_PHYPR 
ID   W2L4M7_PHYPR            Unreviewed;       464 AA.
AC   W2L4M7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=L917_09293 {ECO:0000313|EMBL:ETL92356.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL92356.1};
RN   [1] {ECO:0000313|EMBL:ETL92356.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL92356.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KI679893; ETL92356.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2L4M7; -.
DR   EnsemblProtists; ETL92356; ETL92356; L917_09293.
DR   VEuPathDB; FungiDB:PPTG_12127; -.
DR   Proteomes; UP000054423; 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   tRNA processing {ECO:0000256|HAMAP-Rule:MF_03043};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_03043}.
FT   DOMAIN          34..412
FT                   /note="tRNA-guanine(15) transglycosylase-like"
FT                   /evidence="ECO:0000259|Pfam:PF01702"
FT   REGION          432..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        432..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT   BINDING         351
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT   BINDING         354
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
FT   BINDING         380
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03043"
SQ   SEQUENCE   464 AA;  51181 MW;  952973AD938284A1 CRC64;
     MSKLNDSPKR SPTSGDMLNR VAKTTFARVN ALFSKTQTPC YLPPSIAGNV PHLTPDNCSK
     VEDLTAQMVD FADMCVCSHL SWHLAFVSDI GCSLGLVKLA TDKKKPFREL LNVTDYELVL
     SARDYISESN PPSSKGTGFM VETSSGRRIV SIEEFMTATK LLQPELVVPL ADEIPSDKGR
     NRHRAAVQTS LDWLDACQSL NTSLTPICGV VVGGNDHTLR RMSAGETCKR DIQAILLSGL
     GSCTDRAKRL ELIDAIVSEI TPASLPRVVT GIGHPLDVLD TVNRGIDVFV SPYPASITKA
     GSALIFWISD DEDGGSASER NAERECSGGV LHLREKRFAT DFGPLMAGCD CFACQKYTRA
     YIHHLLNVRE MLGDILLYLH NLQHYYRFFR EIRTAINTDR FPTYHAEFAT RFEERASTAA
     PLIIPPAIEE RKRKVDTEKA ATKETKAKAA AAKHEAAILK RPRP
//
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