GenomeNet

Database: UniProt
Entry: W9XGL2_9EURO
LinkDB: W9XGL2_9EURO
Original site: W9XGL2_9EURO 
ID   W9XGL2_9EURO            Unreviewed;       551 AA.
AC   W9XGL2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   31-JUL-2019, entry version 26.
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=A1O5_00599 {ECO:0000313|EMBL:EXJ76091.1};
OS   Cladophialophora psammophila CBS 110553.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ76091.1, ECO:0000313|Proteomes:UP000019471};
RN   [1] {ECO:0000313|EMBL:EXJ76091.1, ECO:0000313|Proteomes:UP000019471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ76091.1,
RC   ECO:0000313|Proteomes:UP000019471};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W.,
RA   Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S.,
RA   Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL   Submitted (MAR-2013) 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:EXJ76091.1}.
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DR   EMBL; AMGX01000001; EXJ76091.1; -; Genomic_DNA.
DR   RefSeq; XP_007739408.1; XM_007741218.1.
DR   STRING; 1182553.XP_007739408.1; -.
DR   EnsemblFungi; EXJ76091; EXJ76091; A1O5_00599.
DR   GeneID; 19185335; -.
DR   Proteomes; UP000019471; 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:UP000019471};
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:UP000019471}.
FT   DOMAIN      341    346       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1    183       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      1     40       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     64    114       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    169    183       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   551 AA;  60218 MW;  FCEF6F1675658467 CRC64;
     MGQQQSKSSD GTRTPLKSGS SSNLPETLQQ YPSISKSDTR ESASRSIRSS IRSKIKSSGD
     DKTNDSPRAS GSTLAGSDGP NNDRADASSI ASGRSASSRP PREKITNNPL VESPTSPPDE
     DEAPSPGANT PARPPSPTQS KSVGKGHKSV DRAQRTGEVG AVSEEAPHQA HVHSSTQKAG
     DSILVKRENQ INPRAPETKA SLRAKLAELP GASPGGGMGM SEVNDMDLDD MISRLLDAGY
     TTKVTKAVCL KNAEITAICT AVREVLLSQP ALLELTAPVK IVGDIHGQYN DLIRLFEMCG
     FPPNANYLFL GDYVDRGKQS LETILLLFCY KLKYPENFFI LRGNHECANV TRVYGFYDEC
     KRRCNIKIWK TFIDTFNCLP IAAIVADKIF CVHGGLSPSL SHMDDIRQIA RPTDVPDYGL
     LNDLLWSDPA DMDQDWESNE RGVSYCFGKK VIVDFLARHD FDLVCRAHMV VEDGYEFFND
     RLLVTVFSAP NYCGEFDNWG AVMSVSSNLL CSFELLKPLD SSALKSHIKK GRNARQNMLN
     SPPAQVSAQS F
//
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