SWISSPROT: C5DD09_LACTC

ID   C5DD09_LACTC            Unreviewed;       150 AA.
AC   C5DD09;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|RuleBase:RU003470};
DE            EC=3.1.1.- {ECO:0000256|RuleBase:RU003470};
DE            EC=3.1.1.96 {ECO:0000256|RuleBase:RU003470};
GN   OrderedLocusNames=KLTH0B07370g {ECO:0000313|EMBL:CAR21670.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21670.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21670.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + H(+) +
CC         tRNA; Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59871, ChEBI:CHEBI:78442, ChEBI:CHEBI:79333;
CC         EC=3.1.1.96; Evidence={ECO:0000256|RuleBase:RU003470};
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|RuleBase:RU003470};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003470}.
CC   -!- SIMILARITY: Belongs to the DTD family.
CC       {ECO:0000256|RuleBase:RU003470}.
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DR   EMBL; CU928166; CAR21670.1; -; Genomic_DNA.
DR   RefSeq; XP_002552108.1; XM_002552062.1.
DR   STRING; 381046.XP_002552108.1; -.
DR   EnsemblFungi; CAR21670; CAR21670; KLTH0B07370g.
DR   GeneID; 8290948; -.
DR   KEGG; lth:KLTH0B07370g; -.
DR   HOGENOM; HOG000113981; -.
DR   InParanoid; C5DD09; -.
DR   KO; K07560; -.
DR   OMA; MDVSLTN; -.
DR   OrthoDB; 1411453at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   CDD; cd00563; Dtyr_deacylase; 1.
DR   Gene3D; 3.50.80.10; -; 1.
DR   HAMAP; MF_00518; Deacylase_Dtd; 1.
DR   InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR   InterPro; IPR023509; DTD-like_sf.
DR   PANTHER; PTHR10472; PTHR10472; 1.
DR   Pfam; PF02580; Tyr_Deacylase; 1.
DR   SUPFAM; SSF69500; SSF69500; 1.
DR   TIGRFAMs; TIGR00256; TIGR00256; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DD09.
DR   SWISS-2DPAGE; C5DD09.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Cytoplasm {ECO:0000256|RuleBase:RU003470};
KW   Hydrolase {ECO:0000256|RuleBase:RU003470};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   RNA-binding {ECO:0000256|RuleBase:RU003470};
KW   tRNA-binding {ECO:0000256|RuleBase:RU003470}.
SQ   SEQUENCE   150 AA;  16470 MW;  945B151160D24F44 CRC64;
     MRVVLQKVSK AAVTVDSEVV SAIKEGYMLL VGISVHDTIE DAEKISRKVL NLRIFEDENG
     AFWKKNVKEA GGQILSISQF TLQAVTKKGT KPDFHLAQKG PIAKGLYDEF LGLLRKDMGD
     ENVKDGVFGA MMSCELVNEG PVTIVLDTKE
//