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Database: UniProt
Entry: D7SK76_VITVI
LinkDB: D7SK76_VITVI
Original site: D7SK76_VITVI 
ID   D7SK76_VITVI            Unreviewed;       301 AA.
AC   D7SK76;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   OrderedLocusNames=VIT_06s0004g05530 {ECO:0000313|EMBL:CBI16052.3};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CBI16052.3, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
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   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273}.
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DR   EMBL; FN594951; CBI16052.3; -; Genomic_DNA.
DR   RefSeq; XP_010650977.1; XM_010652675.2.
DR   RefSeq; XP_010650978.1; XM_010652676.2.
DR   AlphaFoldDB; D7SK76; -.
DR   STRING; 29760.D7SK76; -.
DR   PaxDb; 29760-VIT_06s0004g05530-t01; -.
DR   EnsemblPlants; Vitvi06g00540_t001; Vitvi06g00540_P001; Vitvi06g00540.
DR   EnsemblPlants; Vitvi06g00540_t002; Vitvi06g00540_P002; Vitvi06g00540.
DR   EnsemblPlants; Vitvi06g00540_t003; Vitvi06g00540_P003; Vitvi06g00540.
DR   GeneID; 100250219; -.
DR   Gramene; Vitvi06g00540_t001; Vitvi06g00540_P001; Vitvi06g00540.
DR   Gramene; Vitvi06g00540_t002; Vitvi06g00540_P002; Vitvi06g00540.
DR   Gramene; Vitvi06g00540_t003; Vitvi06g00540_P003; Vitvi06g00540.
DR   KEGG; vvi:100250219; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   HOGENOM; CLU_004962_8_3_1; -.
DR   InParanoid; D7SK76; -.
DR   OMA; KQSVECI; -.
DR   OrthoDB; 5484004at2759; -.
DR   Proteomes; UP000009183; Chromosome 6.
DR   ExpressionAtlas; D7SK76; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   CDD; cd07414; MPP_PP1_PPKL; 1.
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   PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR11668:SF499; SERINE_THREONINE-PROTEIN PHOSPHATASE PP1 ISOZYME 1; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF16891; STPPase_N; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004273};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT   DOMAIN          121..126
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
SQ   SEQUENCE   301 AA;  34465 MW;  8981551B14E4C763 CRC64;
     MAQMESGVLD DIIDRLMEFR QGKSGKQVPL MESEIRQLCT VSREIFLQQP NLLELEAPIK
     ICGDIHGQYS DLLRLFDYGG YPPEANYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL
     LRGNHECASI NRIYGFYDEC KRRFNVRLWK TFTDCFNCLP VAALIDDKIL CMHGGLSPEL
     TNLDQIRKLS RPTDVPDSGL LCDLLWSDPG RDIKGWGMND RGVSFTFGPD KVSEFLSKHD
     MDLICRAHQV VEDGYEFFAD RQLVTIFSAP NYCGEFDNAG AMMSVDESLM CSFQILKPKF
     M
//
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