ID F6HPS0_VITVI Unreviewed; 398 AA.
AC F6HPS0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN OrderedLocusNames=VIT_13s0156g00060 {ECO:0000313|EMBL:CCB56676.1};
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:CCB56676.1, 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-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, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000256|ARBA:ARBA00001512};
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|ARBA:ARBA00001482,
CC ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; FN596003; CCB56676.1; -; Genomic_DNA.
DR AlphaFoldDB; F6HPS0; -.
DR PaxDb; 29760-VIT_13s0156g00060-t01; -.
DR EnsemblPlants; Vitvi06g00085_t002; Vitvi06g00085_P002; Vitvi06g00085.
DR Gramene; Vitvi06g00085_t002; Vitvi06g00085_P002; Vitvi06g00085.
DR eggNOG; KOG0017; Eukaryota.
DR eggNOG; KOG0371; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; F6HPS0; -.
DR Proteomes; UP000009183; Chromosome 13.
DR ExpressionAtlas; F6HPS0; baseline and differential.
DR GO; GO:0005829; C:cytosol; 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 GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR CDD; cd09272; RNase_HI_RT_Ty1; 1.
DR Gene3D; 3.60.21.10; -; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR047129; PPA2-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR PANTHER; PTHR45619:SF12; SERINE_THREONINE-PROTEIN PHOSPHATASE PP2A; 1.
DR Pfam; PF00149; Metallophos; 2.
DR PIRSF; PIRSF033096; PPPtase_5; 2.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000009183}.
FT DOMAIN 203..208
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
SQ SEQUENCE 398 AA; 45531 MW; C8652990B818419E CRC64;
MDLISSDSHG NLDAQISQLM QCKPLSEQEV RTLCEKAKEI LMEESNVQPV KSPVTICGDI
HGQFHDLAEL FRIGGKCPDT NYLFMGDYVD RGYYSVETVT MFVKSNKQDR VSKSPTKFEY
RTMSLACSKI IWLRGLLAEL DFSETDPTPL HADNTSANQI TTNPVYHERT KHIEVDCHSI
RAAFEARLLV ALKVRYPQRI TILRGNHESR QITQVYGFYD ECLRKYGNAN VWKIFTDLFD
YFPLTALVES EIFCLHGGLS PSIETLDNIR NFDRVQEVPH EGPMCDLLWS DPDDRCGWGI
SPRGAGYTFG QDISEQFNHT NNLKLIARAH QLVMEGFNWG HEQKVVTIFS APNYCYRCGN
MASILEVDDC KGHTFIQFEP APRRGEPDVT RRTPDYFL
//
