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Database: UniProt
Entry: A0A2N0WXL4_9GAMM
LinkDB: A0A2N0WXL4_9GAMM
Original site: A0A2N0WXL4_9GAMM 
ID   A0A2N0WXL4_9GAMM        Unreviewed;       145 AA.
AC   A0A2N0WXL4;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|HAMAP-Rule:MF_00518};
DE            Short=DTD {ECO:0000256|HAMAP-Rule:MF_00518};
DE            EC=3.1.1.96 {ECO:0000256|HAMAP-Rule:MF_00518};
DE   AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000256|HAMAP-Rule:MF_00518};
DE            EC=3.1.1.- {ECO:0000256|HAMAP-Rule:MF_00518};
GN   Name=dtd {ECO:0000256|HAMAP-Rule:MF_00518,
GN   ECO:0000313|EMBL:PKF60888.1};
GN   ORFNames=CW745_13520 {ECO:0000313|EMBL:PKF60888.1};
OS   Psychromonas sp. psych-6C06.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=2058089 {ECO:0000313|EMBL:PKF60888.1, ECO:0000313|Proteomes:UP000233619};
RN   [1] {ECO:0000313|EMBL:PKF60888.1, ECO:0000313|Proteomes:UP000233619}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psych-6C06 {ECO:0000313|Proteomes:UP000233619};
RX   PubMed=27311813; DOI=.1038/ncomms11965;
RA   Datta M.S., Sliwerska E., Gore J., Polz M.F., Cordero O.X.;
RT   "Microbial interactions lead to rapid micro-scale successions on model
RT   marine particles.";
RL   Nat. Commun. 7:11965-11965(2016).
CC   -!- FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC       D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala),
CC       protecting cells against glycine mischarging by AlaRS. Acts via tRNA-
CC       based rather than protein-based catalysis; rejects L-amino acids rather
CC       than detecting D-amino acids in the active site. By recycling D-
CC       aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme
CC       counteracts the toxicity associated with the formation of D-aminoacyl-
CC       tRNA entities in vivo and helps enforce protein L-homochirality.
CC       {ECO:0000256|HAMAP-Rule:MF_00518}.
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|HAMAP-Rule:MF_00518};
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00518};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00518}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00518}.
CC   -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active site
CC       of the other monomer to allow specific chiral rejection of L-amino
CC       acids. {ECO:0000256|HAMAP-Rule:MF_00518}.
CC   -!- SIMILARITY: Belongs to the DTD family. {ECO:0000256|ARBA:ARBA00009673,
CC       ECO:0000256|HAMAP-Rule:MF_00518}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PKF60888.1}.
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DR   EMBL; PIZM01000009; PKF60888.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0WXL4; -.
DR   OrthoDB; 9801395at2; -.
DR   Proteomes; UP000233619; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0106026; F:Gly-tRNA(Ala) hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043908; F:Ser(Gly)-tRNA(Ala) hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00563; Dtyr_deacylase; 1.
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|HAMAP-Rule:MF_00518};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00518};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233619};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00518};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00518}.
FT   MOTIF           137..138
FT                   /note="Gly-cisPro motif, important for rejection of L-amino
FT                   acids"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00518"
SQ   SEQUENCE   145 AA;  15912 MW;  89CECB6E86F8C82D CRC64;
     MIALIQRVTN ANVQVSGKVV GEIKAGLLIL LAVEKGDDEK HCQRLAEKVM AYRIFADEND
     KMNLNVQQAG GDLLVISQFT LAADTKKGNR PGFSNGALPS EAERLYESFN QYCRDKGMLV
     ENGIFAADMQ VSSTNDGPTT FWLQV
//
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