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OCA1_DEBHA
ID   OCA1_DEBHA              Reviewed;         196 AA.
AC   Q6BLZ8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Putative tyrosine-protein phosphatase OCA1;
DE            EC=3.1.3.48;
GN   Name=OCA1; OrderedLocusNames=DEHA2F09482g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Putative tyrosine-protein phosphatase required for protection
CC       against superoxide stress. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; CR382138; CAG89114.1; -; Genomic_DNA.
DR   RefSeq; XP_460773.1; XM_460773.1.
DR   AlphaFoldDB; Q6BLZ8; -.
DR   SMR; Q6BLZ8; -.
DR   STRING; 4959.XP_460773.1; -.
DR   EnsemblFungi; CAG89114; CAG89114; DEHA2F09482g.
DR   GeneID; 2903615; -.
DR   KEGG; dha:DEHA2F09482g; -.
DR   VEuPathDB; FungiDB:DEHA2F09482g; -.
DR   eggNOG; KOG1572; Eukaryota.
DR   HOGENOM; CLU_047845_2_2_1; -.
DR   InParanoid; Q6BLZ8; -.
DR   OMA; NAWDPIT; -.
DR   OrthoDB; 1539111at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; -; 1.
DR   InterPro; IPR020428; PFA-DSPs.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR004861; Siw14-like.
DR   InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR   Pfam; PF03162; Y_phosphatase2; 1.
DR   PRINTS; PR01911; PFDSPHPHTASE.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Protein phosphatase; Reference proteome;
KW   Stress response.
FT   CHAIN           1..196
FT                   /note="Putative tyrosine-protein phosphatase OCA1"
FT                   /id="PRO_0000333391"
FT   DOMAIN          33..192
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        130
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   196 AA;  22378 MW;  A1DD3F03B7601FEF CRC64;
     MSESQSEIEH NNNNSKLTKI SQPPTVRIIP PLNFCPVEKQ LYRSGQPSII NQSFLQDLNL
     KTILWLASEE PQEDFLDYCS MNNIAVEFVG LMNEYSYQNV NPWDALSEDT IKKALELICN
     KENYPLLVCC GMGRHRTGTV IGCLRRLQGW NLASVSEEYR RFTGSRGGRI MVELLIESFD
     INSVQIDPTK MPGWLT
 
 
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