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Database: UniProt
Entry: A0A1Q9EPG8_SYMMI
LinkDB: A0A1Q9EPG8_SYMMI
Original site: A0A1Q9EPG8_SYMMI 
ID   A0A1Q9EPG8_SYMMI        Unreviewed;       727 AA.
AC   A0A1Q9EPG8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   31-JUL-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   Name=gsp-2 {ECO:0000313|EMBL:OLQ09335.1};
GN   ORFNames=AK812_SmicGene7041 {ECO:0000313|EMBL:OLQ09335.1};
OS   Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS   microadriatica).
OC   Eukaryota; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC   Symbiodinium.
OX   NCBI_TaxID=2951 {ECO:0000313|EMBL:OLQ09335.1};
RN   [1] {ECO:0000313|EMBL:OLQ09335.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP2467 {ECO:0000313|EMBL:OLQ09335.1};
RA   Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M.,
RA   Piel J., Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T.,
RA   Bayer T., Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT   "Genome analysis of coral dinoflagellate symbionts highlights
RT   evolutionary adaptations to a symbiotic lifestyle.";
RL   Submitted (FEB-2016) 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:OLQ09335.1}.
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DR   EMBL; LSRX01000098; OLQ09335.1; -; Genomic_DNA.
DR   OrthoDB; 766640at2759; -.
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,
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}.
FT   DOMAIN      165    170       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION      360    381       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   727 AA;  78773 MW;  3BBA96C27AB7984D CRC64;
     MSKGSANCRA VLSWACKILS YEKIGPGNLV APIRRQSRSR SAPEMKKTED LANDEIIEKC
     LEVKGGKPGK LVQIPEGQVK SLCTSARGVF LEQSPLLELE APLKICGDVH GQYHDLLRLF
     EYGGFPPESN YLFLGDYVDR GKQSLETITL LFAYKVKFPE NFFLLRGNHE CASITRIYGF
     YDECKRRYNI KLWKQFCDVF NCMPVCAIID EKIICMHGGL SPEITSFDQV KRIVRPTDVP
     DTGLICDLLW ADPDKDISGW AENDRGVSFI FGPDVVTTFL HKHDMDLVCR AHQVVEDGYE
     FFAKRQLITL FSAPNYCGEF DNAGAMMSID DTLMNHMHVR GVAELSVQLQ SLEAREEEVS
     FEAAEATGRG GPSGRRPPRL RDLGAGFARP TEEFLSNRPS WSAMNRIFLK GTSYVAISPE
     PDRGGCIGKG RQEEAVELSM LNWSLGGVAA ISSEEDFPQM YAAEIEKHAG PVGQATITFR
     QELMKPLEVL PRSEFFRCGR PWDSDVFQLM VDEVAAASVR TLGTGLLARR GQLPSKAAAA
     PVCSLATSAA LVALGLQQGL LLASRAVPMT MKIVAAAAGA MAFQALGGLF ASPARAAWGW
     FMDVPTGLGF TCSEGTSLGC ASPAGCEDSN FTCTVVPDAG MSCDVTSTFV VCSIKGTAAQ
     NFVPDSANPM CAQDNTSSHY NNASLSWSTV PTCGTTTSTT TGAMSTSDAS MEVVGFAAAA
     LATAQLL
//
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