OCA1_PICST
ID OCA1_PICST Reviewed; 212 AA.
AC A3LW52;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Putative tyrosine-protein phosphatase OCA1;
DE EC=3.1.3.48;
GN Name=OCA1; ORFNames=PICST_46361;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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; CP000499; ABN66907.1; -; Genomic_DNA.
DR RefSeq; XP_001384936.1; XM_001384899.1.
DR AlphaFoldDB; A3LW52; -.
DR SMR; A3LW52; -.
DR STRING; 4924.XP_001384936.1; -.
DR EnsemblFungi; ABN66907; ABN66907; PICST_46361.
DR GeneID; 4839644; -.
DR KEGG; pic:PICST_46361; -.
DR eggNOG; KOG1572; Eukaryota.
DR HOGENOM; CLU_047845_2_2_1; -.
DR InParanoid; A3LW52; -.
DR OMA; NAWDPIT; -.
DR OrthoDB; 1539111at2759; -.
DR Proteomes; UP000002258; Chromosome 5.
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..212
FT /note="Putative tyrosine-protein phosphatase OCA1"
FT /id="PRO_0000333394"
FT DOMAIN 40..208
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 146
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
SQ SEQUENCE 212 AA; 24185 MW; 4CBBA80963E04A6D CRC64;
MSNKDTSILK GNVDHEEADS NPKLRKIGRP PALRIIPPLN FCPVERQLYR SGQPSAINQS
FLEQLNLKTI LWLASEEPQD DFLEFSNDHN INIEFVGIIN EFSNYQNYNT NQTLTVNPWD
ALNEQTIKRA LELIVNRENY PLLVCCGMGR HRTGTVIGCL RRLQGWNLAS VSEEYRRFTG
ARGGRILVEL LIESFDIGSV EIDPSKVPDW LT
