P2C76_ORYSJ
ID P2C76_ORYSJ Reviewed; 499 AA.
AC A3CCP9; A0A0N7KT50;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Putative protein phosphatase 2C 76;
DE Short=OsPP2C76;
DE EC=3.1.3.16;
DE Flags: Precursor;
GN OrderedLocusNames=Os11g0586001, LOC_Os11g37540;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(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, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AC104847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP014967; BAT14634.1; -; Genomic_DNA.
DR AlphaFoldDB; A3CCP9; -.
DR SMR; A3CCP9; -.
DR STRING; 4530.OS11T0586001-00; -.
DR PRIDE; A3CCP9; -.
DR EnsemblPlants; Os11t0586001-00; Os11t0586001-00; Os11g0586001.
DR Gramene; Os11t0586001-00; Os11t0586001-00; Os11g0586001.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_013173_0_2_1; -.
DR InParanoid; A3CCP9; -.
DR OMA; CASESTT; -.
DR Proteomes; UP000000763; Chromosome 11.
DR Proteomes; UP000059680; Chromosome 11.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..499
FT /note="Putative protein phosphatase 2C 76"
FT /id="PRO_0000363323"
FT DOMAIN 92..457
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 67..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 499 AA; 55114 MW; EE34F0D5EBA2094D CRC64;
MRLGCSGRRR RLLRAALLRL VVLVLVAPPR RCAGESATCL AVYREGGAPA VFQSAHCPRW
TLLAPSAGSG GEGDGDRRSS SSSPPPPPHP RGCHVAVDRG RRRSQEDRAV CALGIRIPFI
GIYHKIKEVD VGVVAVFDGH NGAEASEMAS KLLLEYFLLH VYFLLDGIYS IMFRKSTGKL
TYKEVTILNN VINLYKEDQS SHSKGSCWAL PAILDRSFHM EVLKESLLRA VHDVDLTFSK
EALRNNFESG STAAVILIVD GQIIAANVGD SKAFLCSESH DSSIDKKTSV VSGKRRRKRN
SNNRDDFALA NYDGPFYNVK ELTKDHHPDR EDERSRVEAA GGYVLEWAGV HRVNGELALS
RAIGDVPYKR YGVIPTPELT EWQSLSANDT FLIASSDGVF EKMTMQDVCD LMLRVKLGVN
QELGSFAVTQ RNLADYVVDL ALEKGTTDNV AAVIVPLGSH YSSKVTLEDW YMLEENSKTS
ISPLQTIPYQ QKSGRFNVQ
