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Database: UniProt
Entry: D8QHK9_SCHCM
LinkDB: D8QHK9_SCHCM
Original site: D8QHK9_SCHCM 
ID   D8QHK9_SCHCM            Unreviewed;       331 AA.
AC   D8QHK9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   31-JUL-2019, entry version 50.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=SCHCODRAFT_12169 {ECO:0000313|EMBL:EFI92950.1};
OS   Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Schizophyllaceae;
OC   Schizophyllum.
OX   NCBI_TaxID=578458 {ECO:0000313|Proteomes:UP000007431};
RN   [1] {ECO:0000313|EMBL:EFI92950.1, ECO:0000313|Proteomes:UP000007431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H4-8 / FGSC 9210 {ECO:0000313|Proteomes:UP000007431};
RX   PubMed=20622885; DOI=10.1038/nbt.1643;
RA   Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E.,
RA   Stajich J.E., de Vries R.P., Record E., Levasseur A., Baker S.E.,
RA   Bartholomew K.A., Coutinho P.M., Erdmann S., Fowler T.J.,
RA   Gathman A.C., Lombard V., Henrissat B., Knabe N., Kuees U.,
RA   Lilly W.W., Lindquist E., Lucas S., Magnuson J.K., Piumi F.,
RA   Raudaskoski M., Salamov A., Schmutz J., Schwarze F.W.M.R.,
RA   vanKuyk P.A., Horton J.S., Grigoriev I.V., Woesten H.A.B.;
RT   "Genome sequence of the model mushroom Schizophyllum commune.";
RL   Nat. Biotechnol. 28:957-963(2010).
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|RuleBase:RU004273,
CC         ECO:0000256|SAAS:SAAS01116780};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
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DR   EMBL; GL377312; EFI92950.1; -; Genomic_DNA.
DR   RefSeq; XP_003027853.1; XM_003027807.1.
DR   STRING; 5334.XP_003027853.1; -.
DR   EnsemblFungi; EFI92950; EFI92950; SCHCODRAFT_12169.
DR   GeneID; 9596794; -.
DR   KEGG; scm:SCHCODRAFT_12169; -.
DR   eggNOG; ENOG410IN85; Eukaryota.
DR   eggNOG; ENOG410XPVF; LUCA.
DR   InParanoid; D8QHK9; -.
DR   KO; K06269; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000007431; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
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   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:UP000007431};
KW   Hydrolase {ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252};
KW   Manganese {ECO:0000256|SAAS:SAAS01017251};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01017255};
KW   Protein phosphatase {ECO:0000256|SAAS:SAAS01017274};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007431}.
FT   DOMAIN      122    127       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      308    331       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   331 AA;  38098 MW;  97B1FC1C38091609 CRC64;
     MADAQTEIDL DSVIDRLLEV RGNRPGKPVQ LQEYEIKYLC TKAREIFINQ PILLELEAPI
     KICGDIHGQY YDLLRLFEYG GFPPEANYLF LGDYVDRGKQ SLETICLLLA YKIKYPENFF
     ILRGNHECAS INRIYGFYDE CKRRYNIKLW KTFTDCFNCL PIAAIIDEKI FTMHGGLSPD
     LQSMEQIRRV MRPTDVPDTG LLCDLLWSDP DKDITGWSEN DRGVSFTFGP DVVSRFLQKH
     DMDLICRAHQ VVEDGYEFFA KRHLVTLFSA PNYCGEFDNA GAMMSVDETL LCSFQILKPA
     EKKAKYPYGG MNMGRPVTPP RKQKKKDSKM G
//
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