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Database: UniProt
Entry: A0A0K3CNK3_RHOTO
LinkDB: A0A0K3CNK3_RHOTO
Original site: A0A0K3CNK3_RHOTO 
ID   A0A0K3CNK3_RHOTO        Unreviewed;       319 AA.
AC   A0A0K3CNK3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   31-JUL-2019, entry version 21.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   Name=FGENESH: predicted gene_16.96 {ECO:0000313|EMBL:CTR11209.1};
GN   ORFNames=BN2166_0070700 {ECO:0000313|EMBL:CTR11209.1};
OS   Rhodosporidium toruloides (Yeast) (Rhodotorula gracilis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR11209.1, ECO:0000313|Proteomes:UP000199069};
RN   [1] {ECO:0000313|EMBL:CTR11209.1, ECO:0000313|Proteomes:UP000199069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Single colony {ECO:0000313|EMBL:CTR11209.1};
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-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,
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; CWKI01000016; CTR11209.1; -; Genomic_DNA.
DR   EnsemblFungi; CTR11209; CTR11209; BN2166_0070700.
DR   Proteomes; UP000199069; 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:UP000199069};
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:UP000199069}.
FT   DOMAIN      122    127       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      298    319       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   319 AA;  36452 MW;  DD26F585A180DD54 CRC64;
     MAAEGQDIDL DSVIDRLLEV RGNRPGKQVQ LQEYEIKFLC TKAREIFINQ PILLELEAPI
     KICGDIHGQY YDLLRLFEYG GFPPEANYLF LGDYVDRGKQ SLETICLLLA YKIKYPENFF
     ILRGNHECAS INRIYGFYDE CKRRYNIKLW KTFTDCFNCL PIAAIIDEKI FTMHGGLSPD
     LQSMEQIRRV MRPTDVPDTG LLCDLLWSDP DKDITGWSEN DRGVSFTFGP DVVSRFLQKH
     DMDLICRAHQ VVEDGYEFFA KRQLVTLFSA PGAMMSVDET LLCSFQILKP AEKKKTFAYG
     GAGQGRPVTP PRKAKGGKK
//
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