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Database: UniProt
Entry: A0A0W4ZK49_PNEJ7
LinkDB: A0A0W4ZK49_PNEJ7
Original site: A0A0W4ZK49_PNEJ7 
ID   A0A0W4ZK49_PNEJ7        Unreviewed;       149 AA.
AC   A0A0W4ZK49;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=T551_02596 {ECO:0000313|EMBL:KTW28746.1};
OS   Pneumocystis jirovecii (strain RU7) (Human pneumocystis pneumonia agent).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX   NCBI_TaxID=1408657 {ECO:0000313|EMBL:KTW28746.1, ECO:0000313|Proteomes:UP000053447};
RN   [1] {ECO:0000313|Proteomes:UP000053447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RU7 {ECO:0000313|Proteomes:UP000053447};
RX   PubMed=26899007; DOI=10.1038/ncomms10740;
RA   Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA   Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA   Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA   Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA   Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA   Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA   Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT   "Genome analysis of three Pneumocystis species reveals adaptation
RT   mechanisms to life exclusively in mammalian hosts.";
RL   Nat. Commun. 7:10740-10740(2016).
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}.
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:KTW28746.1}.
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DR   EMBL; LFWA01000011; KTW28746.1; -; Genomic_DNA.
DR   RefSeq; XP_018229081.1; XM_018374859.1.
DR   AlphaFoldDB; A0A0W4ZK49; -.
DR   STRING; 1408657.A0A0W4ZK49; -.
DR   GeneID; 28941114; -.
DR   VEuPathDB; FungiDB:T551_02596; -.
DR   eggNOG; KOG3323; Eukaryota.
DR   OrthoDB; 2872788at2759; -.
DR   Proteomes; UP000053447; 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   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:UP000053447};
KW   RNA-binding {ECO:0000256|RuleBase:RU003470};
KW   tRNA-binding {ECO:0000256|RuleBase:RU003470}.
SQ   SEQUENCE   149 AA;  16866 MW;  E1F3B02E22FA9635 CRC64;
     MHAVIQRVIS ANVKVNHQKI SSISQGLVVF VGINDTISDV ENLTQTILKL RLFDSIKDGE
     RKKWNQNIKD IGGEILLSQF TLQARIKKSK PDFHMAAKSE EAKELYIRIL EKLRQNLGDD
     KIKEGIFGAM MEVQLINDGP VTIDYDTQS
//
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