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Database: UniProt
Entry: A0A194V9C8_9PEZI
LinkDB: A0A194V9C8_9PEZI
Original site: A0A194V9C8_9PEZI 
ID   A0A194V9C8_9PEZI        Unreviewed;       532 AA.
AC   A0A194V9C8;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   31-JUL-2019, entry version 12.
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=VP1G_07684 {ECO:0000313|EMBL:KUI60489.1};
OS   Valsa mali var. pyri.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX   NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI60489.1, ECO:0000313|Proteomes:UP000078576};
RN   [1] {ECO:0000313|Proteomes:UP000078576}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA   Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA   Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT   "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific
RT   Adaption of Colonization on Woody Bark.";
RL   Submitted (DEC-2014) 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,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16;
CC         Evidence={ECO:0000256|SAAS:SAAS01116782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-
CC         [protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-
CC         COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977;
CC         EC=3.1.3.16; Evidence={ECO:0000256|PIRNR:PIRNR000909,
CC         ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01116780};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000909};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC       {ECO:0000256|PIRNR:PIRNR000909}.
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DR   EMBL; KN714752; KUI60489.1; -; Genomic_DNA.
DR   EnsemblFungi; KUI60489; KUI60489; VP1G_07684.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000078576; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0048037; F:cofactor binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PIRSF; PIRSF000909; PPPtase_PPZ; 2.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000078576};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000909,
KW   ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078576}.
FT   DOMAIN      322    327       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1    171       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      513    532       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     19       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     50     79       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     99    140       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   532 AA;  57906 MW;  52B60035306EA8C9 CRC64;
     MGNQPSKDGG SSSRPHSTTG GGDRIPDGLQ SYPSFSKSDT KDSTRSFKAL RSKIPGSSSK
     TESPRNSTLL SNGESGDKSD AGSVKSGKSG RFSRHRSSDP AITPASPSSV DTSGISSPTG
     DGELPPSPIQ SGSGMSGKHD VSAAQASGEV DHVSDAPPTG VANPNQEPQR PGQSILVKRE
     NTINPIHGGM SPSQETAGFA MSDIKDIDLD DYIKRLLDAA YAGKVTKGVC LKNAEIVAIC
     QRVREVFLSQ PALLELDAPV KIVGDVHGQY TDLIRMFEMC GFPPSANFLF LGDYVDRGKQ
     SLETILLLLC YKLKFPENFF LLRGNHECAN VTRVYGFYDE CKRRCNVKIW KTFIDTFNTL
     PIAAIVAGKI FCVHGGLSPA LSDMDDIRNI ARPTDVPDYG LLNDLLWSDP ADMDADWEAN
     ERGVSYCFGK KVITDFLTTH DFDLVCRAHM VVEDGYEFFT DRVLVTVFSA PNYCGEFDNW
     GAVMSVSSEL LCSFELLKPL DYNALKSHIK KGRNKRQHML NSPPASVYPQ SV
//
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