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Database: UniProt
Entry: A0A0L1IWJ0_ASPNO
LinkDB: A0A0L1IWJ0_ASPNO
Original site: A0A0L1IWJ0_ASPNO 
ID   A0A0L1IWJ0_ASPNO        Unreviewed;       512 AA.
AC   A0A0L1IWJ0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   31-JUL-2019, entry version 21.
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=ANOM_010561 {ECO:0000313|EMBL:KNG83533.1};
OS   Aspergillus nomius NRRL 13137.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG83533.1, ECO:0000313|Proteomes:UP000037505};
RN   [1] {ECO:0000313|EMBL:KNG83533.1, ECO:0000313|Proteomes:UP000037505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG83533.1,
RC   ECO:0000313|Proteomes:UP000037505};
RA   Moore M.G., Shannon B.M., Brian M.M.;
RT   "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus
RT   nomius.";
RL   Submitted (JUN-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KNG83533.1}.
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DR   EMBL; JNOM01000262; KNG83533.1; -; Genomic_DNA.
DR   RefSeq; XP_015404456.1; XM_015555817.1.
DR   EnsemblFungi; KNG83533; KNG83533; ANOM_010561.
DR   GeneID; 26812365; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000037505; Unassembled WGS sequence.
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; 1.
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:UP000037505};
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:UP000037505}.
FT   DOMAIN      302    307       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1    146       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     27       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     37     91       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   512 AA;  56140 MW;  8AAC314EF18E439B CRC64;
     MGQSHSKGNS GPGDSLQSYP SFSRSDTKES LRSIRGSIRS KIRSSDSPRA STSALSTGSQ
     TDKSDAGSIK STGSRRSSTN LTAQSPGADD SASQLDAPDP PPSPTLSSSL KRGHKDVDAM
     QQSGEVDHVS DAPPTGAAPT GSSQKVGESI LIKRQDQLNP ILDFIMNTPL NDTSSSPGMG
     MGALKSIDLD DMITRLLDAG YSTKVTKTVC LKNAEITAIC SAARELFLSQ PALLELSAPV
     KIVGDVHGQY TDLIRLFEMC GFPPSSNYLF LGDYVDRGKQ SLETILLLLC YKLKYPENFF
     LLRGNHECAN VTRVYGFYDE CKRRCNIKIW KTFIDTFNCL PIASIVAGKI FCVHGGLSPS
     LSHMDDIRGI ARPTDVPDYG LLNDLLWSDP ADMEEDWEPN ERGVSYCFGK KVIMNFLQRH
     DFDLVCRAHM VVEDGYEFYQ DRILVTVFSA PNYCGEFDNW GAIMSVSDEL LCSFELLKPL
     DSTALKNHIK KGRNKRNSML NSPPAIVSAQ SY
//
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