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
//
