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Database: UniProt
Entry: M2XVK4_GALSU
LinkDB: M2XVK4_GALSU
Original site: M2XVK4_GALSU 
ID   M2XVK4_GALSU            Unreviewed;       357 AA.
AC   M2XVK4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   31-JUL-2019, entry version 38.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=Gasu_50270 {ECO:0000313|EMBL:EME27434.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME27434.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M.,
RA   Carr K., Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E.,
RA   Oesterhelt C., Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
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; KB454532; EME27434.1; -; Genomic_DNA.
DR   RefSeq; XP_005703954.1; XM_005703897.1.
DR   STRING; 130081.XP_005703954.1; -.
DR   EnsemblPlants; EME27434; EME27434; Gasu_50270.
DR   GeneID; 17086343; -.
DR   Gramene; EME27434; EME27434; Gasu_50270.
DR   KEGG; gsl:Gasu_50270; -.
DR   KO; K06269; -.
DR   OMA; EEHEIRY; -.
DR   OrthoDB; 766640at2759; -.
DR   Proteomes; UP000030680; 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   Complete proteome {ECO:0000313|Proteomes:UP000030680};
KW   Hydrolase {ECO:0000256|RuleBase:RU004273,
KW   ECO:0000256|SAAS:SAAS01017252, ECO:0000313|EMBL:EME27434.1};
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:UP000030680}.
FT   DOMAIN      140    145       SER_THR_PHOSPHATASE.
FT                                {ECO:0000259|PROSITE:PS00125}.
FT   REGION        1     24       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      335    357       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    335    350       Polar. {ECO:0000256|SAM:MobiDB-lite}.
SQ   SEQUENCE   357 AA;  40691 MW;  E054471071EBBAA7 CRC64;
     MGACVDGIPL SDKDDGTKSE PSSNQFNADL IIERLLEVRG QRPGKQVNLK EEEIRELCLR
     SREIFLSQKP LLELEAPIRI CGDIHGQYHD LLRLFEYGGF PPESNYLFLG DYVDRGKQSI
     ETICLLLAYK VKYPENFFIL RGNHECANIN RIYGFYDECR RRYNVKLWKT FCDVFNCLPI
     AAIIDEKIFC THGGLSPELT SMDQIRRITR PTDVPDQGLL CDLLWSDPEK DIKGWGENDR
     GVSFTFGEDV VERFLQRFDL DLVCRAHQVV EDGYEFFGDR KLVTIFSAPN YCGEFDNAGA
     MMSVDETLMC SFQILKPAEK SQKLQLSGLC YPMSPQSSSI ANSSVSPVTP PKTKKKK
//
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