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Database: UniProt
Entry: A0A0D9YUQ5_9ORYZ
LinkDB: A0A0D9YUQ5_9ORYZ
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ID   A0A0D9YUQ5_9ORYZ        Unreviewed;       876 AA.
AC   A0A0D9YUQ5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G23840.4};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM02G23840.4}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM02G23840.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000256|ARBA:ARBA00006702,
CC       ECO:0000256|RuleBase:RU003465}.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC       {ECO:0000256|RuleBase:RU000383}.
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DR   AlphaFoldDB; A0A0D9YUQ5; -.
DR   EnsemblPlants; OGLUM02G23840.4; OGLUM02G23840.4; OGLUM02G23840.
DR   Gramene; OGLUM02G23840.4; OGLUM02G23840.4; OGLUM02G23840.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 2.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR013763; Cyclin-like_dom.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR004367; Cyclin_C-dom.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR048258; Cyclins_cyclin-box.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   PANTHER; PTHR13832:SF285; PROTEIN PHOSPHATASE 2C 22-RELATED; 1.
DR   Pfam; PF02984; Cyclin_C; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SMART; SM01332; Cyclin_C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS00292; CYCLINS; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cyclin {ECO:0000256|ARBA:ARBA00023127, ECO:0000256|RuleBase:RU000383};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026961}.
FT   DOMAIN          560..841
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          135..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..876
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   876 AA;  95416 MW;  794834214010EF83 CRC64;
     MDSIMEPYVA DLLADDITAS MVELLSGDGG AAQMDVGVLD AYLRAIGALP AHPAAPGADL
     AAAAEVESMA SNDDTNGNWD TKVDAKVPSA FLPPPPGFPP LPVPALADEP VYAAPVDEGD
     AIRAFMQQLE WSEQYNGDDD APAPDDSMAS RPQLCAPYDD DIDANLRAME KDAAERPSPD
     YLDTVHSGQI SAASRASLVA WMGRLTHRYE LAAGTLHRAV SYFDRFLSAR ALPSYTEHQL
     SLVGATAVYT AAKYEDQGTV FKLDAREIAS YGEFASAQEV LAMEREMMAA LGYRLGGPNA
     ETFVEHFTRY SKGKEELRVQ RLARHIADRS LESYGCLGYL PSVVAAAVIS IARWTLNPPG
     ALPWSSELHG LTGGEAVVVR RPEQKTKGVE LSGRRRRARR RVGLNAAPRG SSACTPERLG
     GADQYPGYGG GGGGGGGIPP RRPQGSARVG PGARAARGAH LGRRIRRSSH VGPIQRTRCA
     RSGRRRKLWV GFTTFCAPPP LACKALAPLT HFCFAITTIF TSHKRSGIAE RKEASAMGAS
     PSRPLEQSPS SSEGENHRVK YASYTTQGFR PHMEDALAVE LDLDATTSFF GVYDGHGGAE
     VAMYCAKRFH TMLLEDVDYI NNLPNAITSV CFRLDDDLQR SNEWRESLNP CANRNCLTNI
     CANLHHFTED YVPPSYEGST ACVVIIRGNQ IIVGNVGDSR CVLSKNGQAI SLSFDHKPHH
     EAERERIQRA GGHVFLRRIL GMLATSRAIG DFAYKQNRNM PPSQQMVTCV PDIRVENITD
     DTEFLVIASD GVWDGMRNNN VVQFVRQELR PGEENLRETC EKLVGHCLHS NDNATAILVK
     FKPIEEDPDE VASARDEHQH NPEGGDEKLD INNDNV
//
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