ID A0A0D9WQU0_9ORYZ Unreviewed; 739 AA.
AC A0A0D9WQU0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR06G13980.1, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR06G13980.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR06G13980.1, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR06G13980.1}
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}.
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DR AlphaFoldDB; A0A0D9WQU0; -.
DR STRING; 77586.A0A0D9WQU0; -.
DR EnsemblPlants; LPERR06G13980.1; LPERR06G13980.1; LPERR06G13980.
DR Gramene; LPERR06G13980.1; LPERR06G13980.1; LPERR06G13980.
DR eggNOG; KOG0698; Eukaryota.
DR HOGENOM; CLU_022688_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 6.
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; 2.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2.
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; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR47992:SF45; PROTEIN-SERINE_THREONINE PHOSPHATASE; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 2.
DR SUPFAM; SSF81606; PP2C-like; 2.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
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:UP000032180}.
FT DOMAIN 113..360
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 482..730
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 83..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 739 AA; 79968 MW; C74A4DCED249F5DE CRC64;
MSSRRAPSPA AAGGGLAGAL LRRMARAAGL RALVGIEAAG RGGRVAVAAG HRGGFPGWPG
VGCGSSSSSS AASFSLTRAQ ARRAAGSAAR TRPPSESNGW ITGGSASEDG RLSWGFSSFK
GRRPSMEDRF SIKIETIDRQ TVGLFGVFDG HGGPLAAEYL KEHLFENLVQ HPEFLKDTKL
AISQTFLKTD ADFLESVSSN PFRDDGSTAV TAILVGNQLY VANVGDSRAV ALEAGKAVPL
SEDHKPNRKD EQKRIEDAGG IIVLDDTWRV NGLLAMSRAF GNCALKQYVK AEPDIQEKTI
DESLEYLILA TDGLWDVMRN EDVISQLKAQ DGPEAAAMKL TEVAHSRLSL DNITCLVLEF
HHEKSASSSL HSFPLLRNGA AAPRFFSSRG RGRAGALAKS LIEDEEIDDD DEDEAGLNDW
IREAFFLSIS SDEEGEAPST RESAAPSGGG GCRRGRKNSE RPPLRLRFDG GEDGCSNDGE
FSWGYSSFKG KRPSMEDRFS IKLTTIDGQT IGLFGVFDGH CGPRAAEYLK QHLFENLVKH
PKFLKDTKLA IKQTFLKIDA DFLHSTSSDR LIRDDGSTAV TAILIGNRLY VANVGDSRAV
ALKAGKAVPL SKDHKPNRKD ERKRIEAAGG IVSVDDTWRV NRNLAVSRAF GNHAMKRYVI
ANPDIQEKVV GEGFEYLVLA SDGLWDVIRN EDVVSLLKGQ DGPKVAAMKL TEVAHSRFTL
DNVTCIVLQF HHGKSTNSK
//
