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Entry: A0A1V1TEC1_9FUNG
LinkDB: A0A1V1TEC1_9FUNG
Original site: A0A1V1TEC1_9FUNG 
ID   A0A1V1TEC1_9FUNG        Unreviewed;       309 AA.
AC   A0A1V1TEC1;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   11-DEC-2019, entry version 10.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=ANO14919_086340 {ECO:0000313|EMBL:GAW19150.1};
OS   fungal sp. No.14919.
OC   Eukaryota; Fungi.
OX   NCBI_TaxID=1813822 {ECO:0000313|EMBL:GAW19150.1, ECO:0000313|Proteomes:UP000189293};
RN   [1] {ECO:0000313|EMBL:GAW19150.1, ECO:0000313|Proteomes:UP000189293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.14919 {ECO:0000313|EMBL:GAW19150.1,
RC   ECO:0000313|Proteomes:UP000189293};
RG   Technology Reseach Association of Highly Efficient Gene Design;
RA   Itoh H., Matsui M., Shibata T.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAW19150.1, ECO:0000313|Proteomes:UP000189293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No.14919 {ECO:0000313|EMBL:GAW19150.1,
RC   ECO:0000313|Proteomes:UP000189293};
RA   Itoh H., Matsui M., Kumagai T., Arita M., Machida M., Shibata T.;
RT   "Genome Sequence of Fungus Strain No.14919 Producing HMG-CoA Reductase
RT   Inhibitor FR901512.";
RL   Submitted (MAR-2017) 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|RuleBase:RU004273,
CC         ECO:0000256|SAAS:SAAS01116780};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273, ECO:0000256|SAAS:SAAS01017257}.
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:GAW19150.1}.
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DR   EMBL; BDMC01000028; GAW19150.1; -; Genomic_DNA.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000189293; Unassembled WGS sequence.
DR   GO; GO:0000164; C:protein phosphatase type 1 complex; IEA:InterPro.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR037979; PPP1CA.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668:SF377; PTHR11668:SF377; 1.
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   Hydrolase {ECO:0000256|RuleBase:RU004273, 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:UP000189293}.
FT   DOMAIN          121..126
FT                   /note="SER_THR_PHOSPHATASE"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   309 AA;  35712 MW;  2900A340388D34B4 CRC64;
     MADQHDVDLD SIIDRLLEVR GSRPGKQVQL LETEIRYLCT KAREIFISQP ILLELEAPIK
     ICGDIHGQYY DLLRLFEYGG FPPEANYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFI
     LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIIDEKIF TMHGGLSPDL
     NSMEQIRRVM RPTDIPDCGL LCDLLWSDPD KDITGWSEND RGVSFTFGPD VVSRFLQKHD
     MDLICRAHQV VEDGYEFFSK RQLVTLFSAP NYCGEFDNAG AMMSVDESLL CSFQILKPAE
     KKQKFGRTR
//
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