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Database: UniProt
Entry: A0A0C2T4L3_AMAMU
LinkDB: A0A0C2T4L3_AMAMU
Original site: A0A0C2T4L3_AMAMU 
ID   A0A0C2T4L3_AMAMU        Unreviewed;       445 AA.
AC   A0A0C2T4L3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   31-JUL-2019, entry version 25.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=M378DRAFT_155784 {ECO:0000313|EMBL:KIL70850.1};
OS   Amanita muscaria Koide BX008.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Amanitaceae; Amanita.
OX   NCBI_TaxID=946122 {ECO:0000313|EMBL:KIL70850.1, ECO:0000313|Proteomes:UP000054549};
RN   [1] {ECO:0000313|EMBL:KIL70850.1, ECO:0000313|Proteomes:UP000054549}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Koide BX008 {ECO:0000313|EMBL:KIL70850.1,
RC   ECO:0000313|Proteomes:UP000054549};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (APR-2014) 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|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; KN818223; KIL70850.1; -; Genomic_DNA.
DR   EnsemblFungi; KIL70850; KIL70850; M378DRAFT_155784.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000054549; Unassembled WGS sequence.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; 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; 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:UP000054549};
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:UP000054549}.
FT   DOMAIN      245    250       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1    119       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS      8     26       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     30     73       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     74     88       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS     89    119       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   445 AA;  49153 MW;  DBC52E679D1BEB6B CRC64;
     MGQQSSKKSR KTGKDKDKDK DAADATSLPT PEDSAESVPQ SASSRISDAP TSTLPNGSEP
     SPNGNLPSTS TTLQPSPQPS PQPSPPIEIP TQTILSNSSR APLLGDSPNN KFTQGESVGN
     GGSNALLKQF DIDDMIQRLL DVGYTGKVSK SLCLKNNEVT AICLAARDVF LGQPTLVELS
     PPVKIVGDVH GQYSDLIRLF EMCGFPPTSN YLFLGDYVDR GKQSLETILL LLCYKIKYPE
     NFFLLRGNHE CANVTRVYGF YDECKRRCNI KIWKTFIDVF NCLPIAAIVA SKIFCVHGGL
     SPSLNSMEDI KRIQRPTDVP DYGLLNDLLW SDPSDTALDW EENERGVSFC FGKAIINEFL
     VRYDMDLICR AHMVVEDGYE FWNDRTLVTV FSAPNYCGEF DNYGACMSVS EDLLCAFELL
     KPLDGAALRK EMTKAKRKSL MQTAT
//
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