ID   OCA1_EREGS              Reviewed;         225 AA.
AC   Q75B37;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=Putative tyrosine-protein phosphatase OCA1;
DE            EC=3.1.3.48;
GN   Name=OCA1; OrderedLocusNames=ADL260W;
OS   Eremothecium gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL
OS   Y-1056) (Yeast) (Ashbya gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51660.1; -; Genomic_DNA.
DR   RefSeq; NP_983836.1; NM_209189.1.
DR   AlphaFoldDB; Q75B37; -.
DR   SMR; Q75B37; -.
DR   STRING; 284811.Q75B37; -.
DR   EnsemblFungi; AAS51660; AAS51660; AGOS_ADL260W.
DR   GeneID; 4619971; -.
DR   KEGG; ago:AGOS_ADL260W; -.
DR   eggNOG; KOG1572; Eukaryota.
DR   HOGENOM; CLU_047845_2_2_1; -.
DR   InParanoid; Q75B37; -.
DR   OMA; STNAWDP; -.
DR   OrthoDB; 131574at2759; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
DR   CDD; cd14531; PFA-DSP_Oca1; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR31126; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR31126:SF8; TYROSINE-PROTEIN PHOSPHATASE OCA1-RELATED; 1.
DR   Pfam; PF03162; Y_phosphatase2; 1.
DR   PRINTS; PR01911; PFDSPHPHTASE.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 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..225
FT                   /note="Putative tyrosine-protein phosphatase OCA1"
FT                   /id="PRO_0000333388"
FT   DOMAIN          42..196
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        138
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   225 AA;  24960 MW;  7093A43D07072C75 CRC64;
     MTDNCREDDD NLGTSGDNAL SAPTQLLVTP PAPHQTIVPP LNFCPVERYL YRSGQPSTVN
     FPFLLNLNLR TIIWLANEEP QDALLAFCDM HDIRLRFAAI NPEGGEDDNP WDGLTEHSIV
     SALQTIVHRD NYPLLVCCGM GRHRTGTVIG CLRRIMGWNL ASVSEEYRRF TGSRGGRILV
     ELLIEAFDTK SVTIDKANAP EWLATAVSAS EASYVPATTY SIHEM
//