ID   OCA1_USTMA              Reviewed;         158 AA.
AC   Q4P7L6; A0A0D1CM86;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Putative tyrosine-protein phosphatase OCA1;
DE            EC=3.1.3.48;
GN   Name=OCA1; ORFNames=UMAG_03897;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003150; KIS67838.1; -; Genomic_DNA.
DR   RefSeq; XP_011390380.1; XM_011392078.1.
DR   AlphaFoldDB; Q4P7L6; -.
DR   SMR; Q4P7L6; -.
DR   STRING; 237631.Q4P7L6; -.
DR   EnsemblFungi; KIS67838; KIS67838; UMAG_03897.
DR   GeneID; 23564228; -.
DR   KEGG; uma:UMAG_03897; -.
DR   VEuPathDB; FungiDB:UMAG_03897; -.
DR   eggNOG; KOG1572; Eukaryota.
DR   HOGENOM; CLU_047845_5_1_1; -.
DR   InParanoid; Q4P7L6; -.
DR   OMA; NAWDPIT; -.
DR   OrthoDB; 1539111at2759; -.
DR   Proteomes; UP000000561; Chromosome 11.
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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:EnsemblFungi.
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..158
FT                   /note="Putative tyrosine-protein phosphatase OCA1"
FT                   /id="PRO_0000333395"
FT   DOMAIN          7..158
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        99
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ   SEQUENCE   158 AA;  18274 MW;  30AC632977436C40 CRC64;
     MLVPPPNYGM VEENFYRSGQ PDQLNFPFLE KLGLKSVIWL APEEPEPGFL DFCVDQNIEL
     HHLGVLYSTN AWDPITEEVV LQALHLLVQP ATYPVLVMCN LGRHRTGTVV GCFRKLQRWN
     LSAILEEYRR FVGGQKYRIL NEQFIELFDE ELVFGASY