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Database: UniProt
Entry: G1WY13_ARTOA
LinkDB: G1WY13_ARTOA
Original site: G1WY13_ARTOA 
ID   G1WY13_ARTOA            Unreviewed;       556 AA.
AC   G1WY13;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   16-OCT-2019, entry version 41.
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=AOL_s00004g173 {ECO:0000313|EMBL:EGX54140.1};
OS   Arthrobotrys oligospora (strain ATCC 24927 / CBS 115.81 / DSM 1491)
OS   (Nematode-trapping fungus) (Didymozoophaga oligospora).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=756982 {ECO:0000313|EMBL:EGX54140.1, ECO:0000313|Proteomes:UP000008784};
RN   [1] {ECO:0000313|EMBL:EGX54140.1, ECO:0000313|Proteomes:UP000008784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24927 / CBS 115.81 / DSM 1491
RC   {ECO:0000313|Proteomes:UP000008784};
RX   PubMed=21909256; DOI=10.1371/journal.ppat.1002179;
RA   Yang J., Wang L., Ji X., Feng Y., Li X., Zou C., Xu J., Ren Y., Mi Q.,
RA   Wu J., Liu S., Liu Y., Huang X., Wang H., Niu X., Li J., Liang L.,
RA   Luo Y., Ji K., Zhou W., Yu Z., Li G., Liu Y., Li L., Qiao M., Feng L.,
RA   Zhang K.-Q.;
RT   "Genomic and proteomic analyses of the fungus Arthrobotrys oligospora
RT   provide insights into nematode-trap formation.";
RL   PLoS Pathog. 7:E1002179-E1002179(2011).
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:EGX54140.1}.
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DR   EMBL; ADOT01000005; EGX54140.1; -; Genomic_DNA.
DR   RefSeq; XP_011117125.1; XM_011118823.1.
DR   STRING; 13349.G1WY13; -.
DR   EnsemblFungi; EGX54140; EGX54140; AOL_s00004g173.
DR   GeneID; 22888020; -.
DR   InParanoid; G1WY13; -.
DR   OMA; AEIMAIC; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000008784; 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; 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:UP000008784};
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:UP000008784}.
FT   DOMAIN      345    350       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1    197       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      537    556       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     10     48       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     83    133       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    539    556       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   556 AA;  59980 MW;  1E0805F843654A5D CRC64;
     MGNAPSKKAG SNGILGNSSS ASLGKDANDQ DNAESTSTSK SLRGSLRSKI AGSSKDKDRD
     NSNTLSPSTA GPGLPLDKGD SASIRSAKSQ RSTSVQQNHG TPVSPVAATP TGEKSSTPPT
     SPTDDSTLGP TSPVSEGGKV PSPPPSPSQS RSLGKGHHAL DEPTGEVGKV SDKPAGQAGP
     HTATDTTHQT PKEPILIRPA GSLPVTLGTD IAEESPGGHS QFGMSALNPL DLDEMITRLL
     DAGYAGKVTK TVCLKNAEIT AICSAARQVF LSQPSLIELK APVKIVGDVH GQYTDLLRMF
     EMCGFPPNSN FLFLGDYVDR GKQSLETILL LLCYKLKYPE NFFLLRGNHE CANVTRVYGF
     YDECKRRCNV KIWKTFVDTF NTLPIAAVVA GKIFCVHGGL SPSLSHMDDI RNISRPTDVP
     DYGLLNDLLW SDPADMQNDW EENERGVSYC FGKKVILEFL QRHDFDLVCR AHMVVEDGYE
     FFNDRTLVTV FSAPNYCGEF DNWGAVMSVS PELLCSFELI KPLDSAALKS HIKKGRNKRN
     SLYPQSPPVT RGPQSF
//
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