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Database: UniProt
Entry: A0A151ZI51_9MYCE
LinkDB: A0A151ZI51_9MYCE
Original site: A0A151ZI51_9MYCE 
ID   A0A151ZI51_9MYCE        Unreviewed;       321 AA.
AC   A0A151ZI51;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   16-OCT-2019, entry version 15.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=DLAC_05047 {ECO:0000313|EMBL:KYQ93662.1};
OS   Tieghemostelium lacteum.
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelids;
OC   Dictyosteliales; Raperosteliaceae; Tieghemostelium.
OX   NCBI_TaxID=361077 {ECO:0000313|EMBL:KYQ93662.1, ECO:0000313|Proteomes:UP000076078};
RN   [1] {ECO:0000313|EMBL:KYQ93662.1, ECO:0000313|Proteomes:UP000076078}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TK {ECO:0000313|EMBL:KYQ93662.1,
RC   ECO:0000313|Proteomes:UP000076078};
RA   Gloeckner G., Schaap P.;
RT   "Dictyostelia acquired genes for synthesis and detection of signals
RT   that induce cell-type specialization by lateral gene transfer from
RT   prokaryotes.";
RL   Submitted (DEC-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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KYQ93662.1}.
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DR   EMBL; LODT01000025; KYQ93662.1; -; Genomic_DNA.
DR   EnsemblProtists; KYQ93662; KYQ93662; DLAC_05047.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000076078; Unassembled WGS sequence.
DR   GO; GO:0000164; C:protein phosphatase type 1 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; IPR037981; PPP1CC.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   InterPro; IPR031675; STPPase_N.
DR   PANTHER; PTHR11668:SF204; PTHR11668:SF204; 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   Complete proteome {ECO:0000313|Proteomes:UP000076078};
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:UP000076078}.
FT   DOMAIN      117    122       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      300    321       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   321 AA;  37122 MW;  8C7A9C1CA442D55C CRC64;
     MEIDLDSIIT RLLEPRTTKP GKFVDLLEEE IRYLTIQATE IFINQPILLE LEAPIKICGD
     IHGQYYDLLR LFEYGGFPPQ SNYLFLGDYV DRGKQSLETI CLLLAYKIKY PENFFILRGN
     HECASINRIY GFYDECKRRY NTKLWKAFTD CFNCLPVAAI IDEKIFCMHG GLSPDLKNMD
     QIRRIVRPTV VPDNGLLCDL LWADPDKTVQ GWDDNDRGVS YIFGPDIVET FLKKHDLDLI
     CRAHQVVEDG YEFFAKRQLV TLFSAPNYFG EFDNAGAMMG VDETLMCSFQ ILKPADKKKI
     TNDNNGRLLT PPRNKQQKQK K
//
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