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Database: UniProt
Entry: A0A0F4YU84_TALEM
LinkDB: A0A0F4YU84_TALEM
Original site: A0A0F4YU84_TALEM 
ID   A0A0F4YU84_TALEM        Unreviewed;       513 AA.
AC   A0A0F4YU84;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   11-DEC-2019, entry version 24.
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=T310_4312 {ECO:0000313|EMBL:KKA21655.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA21655.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA21655.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA21655.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) 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, ChEBI:CHEBI:43474,
CC         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-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKA21655.1}.
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DR   EMBL; LASV01000175; KKA21655.1; -; Genomic_DNA.
DR   RefSeq; XP_013328267.1; XM_013472813.1.
DR   EnsemblFungi; KKA21655; KKA21655; T310_4312.
DR   GeneID; 25316660; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000053958; 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   Hydrolase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252, ECO:0000313|EMBL:KKA21655.1};
KW   Manganese {ECO:0000256|PIRNR:PIRNR000909, 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:UP000053958}.
FT   DOMAIN          303..308
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..76
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  55797 MW;  16F4D16D9BBD08E4 CRC64;
     MGQSQSKGGD SRSGDPLQSY PSFSKSDTKE SIRSLRGSIR SKIPGRSSDK NNDSPRGSTV
     GLSDDKSETA SVRSAGSARG APSPAPSALS DDATASRAGT PDPPPSPSQS TSLNRGHKDV
     NAAQQSGEVD LVSDAPPSVP PATPQAPGES ILVKHENQIN PVLLDILASQ PTETSGSPGM
     GMGALKSIDL DDMISRLLDA GYSTKVTKSV CLKNAEIVAI CTAARELLLS QPALLELSAP
     VKIVGDVHGQ YTDLIRLFEM CGFPPAANYL FLGDYVDRGK QSLETILLLL CYKLKYPENF
     FLLRGNHECA NVTRVYGFYD ECKRRCNIKI WKTFIDTFNC LPIASIVAGK IFCVHGGLSP
     SLSHMDDIRG IARPTDVPDY GLLNDLLWSD PADMEEDWEP NERGVSYCFG KKVIMDFLQR
     HDFDLVCRAH MVVEDGYEFF QDRILVTVFS APNYCGEFDN WGAIMSVSAE LLCSFELLKP
     LDSSALKNHI KKGRNRRNSM LNSPPAVVSA QSY
//
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