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Database: UniProt
Entry: A0A2P8A1F2_9PEZI
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ID   A0A2P8A1F2_9PEZI        Unreviewed;       532 AA.
AC   A0A2P8A1F2;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   08-NOV-2023, entry version 24.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
GN   ORFNames=B9Z65_3421 {ECO:0000313|EMBL:PSK54302.1};
OS   Elsinoe australis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Elsinoe.
OX   NCBI_TaxID=40998 {ECO:0000313|EMBL:PSK54302.1, ECO:0000313|Proteomes:UP000243723};
RN   [1] {ECO:0000313|EMBL:PSK54302.1, ECO:0000313|Proteomes:UP000243723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NL1 {ECO:0000313|EMBL:PSK54302.1,
RC   ECO:0000313|Proteomes:UP000243723};
RA   Cheng Q.;
RT   "Draft genome sequence of Elsinoe australis.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000909};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000909,
CC         ECO:0000256|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|PIRNR:PIRNR000909};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000909}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC       {ECO:0000256|ARBA:ARBA00029458, ECO:0000256|PIRNR:PIRNR000909}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PSK54302.1}.
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DR   EMBL; NHZQ01000083; PSK54302.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P8A1F2; -.
DR   STRING; 40998.A0A2P8A1F2; -.
DR   Proteomes; UP000243723; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR011159; PPPtase_PPZ/Ppq1.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF484; SERINE/THREONINE-PROTEIN PHOSPHATASE PP-Z1-RELATED; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PIRSF; PIRSF000909; PPPtase_PPZ; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR000909};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000909};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000909};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|PIRNR:PIRNR000909};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243723}.
FT   DOMAIN          322..327
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   532 AA;  58430 MW;  7D70C2F7FDD54DAC CRC64;
     MGNQPSKDGE SIGRSRSNTP TSGGLGPKLE SLPSFSKSDT QGSSRSIRNS LKSKIPGTII
     KNDGSKGSSS NISSPVEEKD SAVSDVASTK SGQSNHRRQL SETTSPTSPS DASRRGSVVS
     ESEPQPPPSP TMSASLGHGH SDIKKAQKSG EVEHVSDAPP SGVLHPASNA EPGESILMKK
     GSGEKTDEAT KLAEGVDAMN IGALKPADLD EFIKRLIDAA YNNKVTKTVC LKNAEITAIC
     QAARECFLSQ PALLELAAPV KIVGDVHGQY MDLIRMFEMC GFPPNANFLF LGDYVDRGKQ
     SLETILLLLC YKLRFPENFF LLRGNHECAN VTRVYGFYDE CKRRCNVKIW KTFVDTFNCL
     PIASIVAGKI FCVHGGLSPS LSHMDDIRQI ARPTDVPDYG LLNDLLWSDP ADMESDWEAN
     ERGVSYCFSK KVIMEFLQKH DFDLVCRAHM VVEDGYEFFN DRVLVTVFSA PNYCGEFDNW
     GAVMSVSQEL LCSFELLKPL ESSQLKTHMK KGRNERQRML NSPPASQYPQ SY
//
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