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Database: UniProt
Entry: A0A1Y2F2F6_9BASI
LinkDB: A0A1Y2F2F6_9BASI
Original site: A0A1Y2F2F6_9BASI 
ID   A0A1Y2F2F6_9BASI        Unreviewed;       489 AA.
AC   A0A1Y2F2F6;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   31-JUL-2019, entry version 9.
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=BCR35DRAFT_305182 {ECO:0000313|EMBL:ORY78023.1};
OS   Leucosporidium creatinivorum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Leucosporidiales; Leucosporidium.
OX   NCBI_TaxID=106004 {ECO:0000313|EMBL:ORY78023.1, ECO:0000313|Proteomes:UP000193467};
RN   [1] {ECO:0000313|EMBL:ORY78023.1, ECO:0000313|Proteomes:UP000193467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=62-1032 {ECO:0000313|EMBL:ORY78023.1,
RC   ECO:0000313|Proteomes:UP000193467};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A.,
RA   Culley D., Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E.,
RA   Spatafora J.W., Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORY78023.1}.
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DR   EMBL; MCGR01000030; ORY78023.1; -; Genomic_DNA.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000193467; 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:UP000193467};
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:UP000193467}.
FT   DOMAIN      285    290       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1    167       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     37     74       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     80    167       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   489 AA;  52036 MW;  86DA2AA1C7E49985 CRC64;
     MGNTGSKEKK LKSSRGSISN GAGAGAAAAG GAGQDTDTPQ RGDSGSSTTG TGADGTALGS
     STSSSTTAPS PGATTAGDLT PARSRPQSGS ANSLSTPSAS APTDIPTTQT ILANPISTAN
     GPSSLVPSIS SQQQQPQPST SSSSAGASGG QPTTYLSTSP TSPSKQTQQF DIDDMIARLL
     DAGYSGKVTK SVCLKNAEIT AICQAAREVF LSQPTLIELS PPVKIVGDVH GQYSDLIRLF
     EMCGFPPAAN YLFLGDYVDR GKQSLETILL LLCYKIKYPE NFFLLRGNHE CANVTRVYGF
     YDECKRRCNI KIWKTFIDVF NCLPIAAVVA SKIFCVHGGL SPSLSSMDDI RRISRPTDVP
     DYGLLNDLLW SDPSDTALDW EDNERGVSYC FGKTVIGAFL ARYDFDLICR AHMVVEDGYE
     FWNERTLVTI FSAPNYCGEF DNFAAVMSVS EDLLCAFELL KPLDSAQLKK EMAKNRRRLS
     SGVAAAAPT
//
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