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
//
