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Database: UniProt
Entry: S3DQ04_GLAL2
LinkDB: S3DQ04_GLAL2
Original site: S3DQ04_GLAL2 
ID   S3DQ04_GLAL2            Unreviewed;       158 AA.
AC   S3DQ04;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|ARBA:ARBA00020007, ECO:0000256|RuleBase:RU003470};
DE            EC=3.1.1.96 {ECO:0000256|ARBA:ARBA00013056, ECO:0000256|RuleBase:RU003470};
GN   ORFNames=GLAREA_09684 {ECO:0000313|EMBL:EPE28563.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE28563.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE28563.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC         H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC         Evidence={ECO:0000256|ARBA:ARBA00033671};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC         Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC         Evidence={ECO:0000256|ARBA:ARBA00000741};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003470}.
CC   -!- SIMILARITY: Belongs to the DTD family. {ECO:0000256|ARBA:ARBA00009673,
CC       ECO:0000256|RuleBase:RU003470}.
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DR   EMBL; KE145368; EPE28563.1; -; Genomic_DNA.
DR   RefSeq; XP_008084471.1; XM_008086280.1.
DR   AlphaFoldDB; S3DQ04; -.
DR   STRING; 1116229.S3DQ04; -.
DR   GeneID; 19468731; -.
DR   KEGG; glz:GLAREA_09684; -.
DR   eggNOG; KOG3323; Eukaryota.
DR   HOGENOM; CLU_076901_0_4_1; -.
DR   OMA; VFGADMK; -.
DR   OrthoDB; 2872788at2759; -.
DR   Proteomes; UP000016922; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.80.10; D-tyrosyl-tRNA(Tyr) deacylase; 1.
DR   HAMAP; MF_00518; Deacylase_Dtd; 1.
DR   InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR   InterPro; IPR023509; DTD-like_sf.
DR   NCBIfam; TIGR00256; D-aminoacyl-tRNA deacylase; 1.
DR   PANTHER; PTHR10472:SF5; D-AMINOACYL-TRNA DEACYLASE 1; 1.
DR   PANTHER; PTHR10472; D-TYROSYL-TRNA TYR DEACYLASE; 1.
DR   Pfam; PF02580; Tyr_Deacylase; 1.
DR   SUPFAM; SSF69500; DTD-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU003470};
KW   Hydrolase {ECO:0000256|RuleBase:RU003470};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   RNA-binding {ECO:0000256|RuleBase:RU003470};
KW   tRNA-binding {ECO:0000256|RuleBase:RU003470}.
SQ   SEQUENCE   158 AA;  16988 MW;  489EF60E166458D2 CRC64;
     MKAILQRVLS ASVTVDQQLI SSIGKGILVF AAVAPGDTEK DVETLATKVL KMRLWDDESG
     GRWKKSVQDI DGEVLCVSQF TLLAVTKKGT KPDFHGALGG DKAKELYQLF VKKVEQGYAA
     ERVKDGVFQA MMEVALVNDG PVTLEMSVGP SGEKASSN
//
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