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Database: UniProt
Entry: A0A2P6R1C2_ROSCH
LinkDB: A0A2P6R1C2_ROSCH
Original site: A0A2P6R1C2_ROSCH 
ID   A0A2P6R1C2_ROSCH        Unreviewed;       546 AA.
AC   A0A2P6R1C2;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=RchiOBHm_Chr4g0433171 {ECO:0000313|EMBL:PRQ40169.1};
OS   Rosa chinensis (China rose).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC   Rosa.
OX   NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ40169.1, ECO:0000313|Proteomes:UP000238479};
RN   [1] {ECO:0000313|EMBL:PRQ40169.1, ECO:0000313|Proteomes:UP000238479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA   Bendahmane M.;
RT   "The Rosa genome provides new insights in the design of modern roses.";
RL   Nat. Genet. 0:0-0(2018).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PRQ40169.1}.
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DR   EMBL; PDCK01000042; PRQ40169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6R1C2; -.
DR   STRING; 74649.A0A2P6R1C2; -.
DR   EnsemblPlants; PRQ40169; PRQ40169; RchiOBHm_Chr4g0433171.
DR   Gramene; PRQ40169; PRQ40169; RchiOBHm_Chr4g0433171.
DR   OMA; LTPDMEF; -.
DR   Proteomes; UP000238479; Chromosome 4.
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; 3.60.40.10; PPM-type phosphatase domain; 1.
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:SF86; PROTEIN-SERINE_THREONINE PHOSPHATASE; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
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:UP000238479}.
FT   DOMAIN          69..538
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          317..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   546 AA;  59397 MW;  CDF85A2A05218A88 CRC64;
     MTTTTENAAV SHSDASSIPA ALDPITAFSS LKRKRPPKIE IPNVLQEIKT EKQRDLAPRN
     GVVCFSGIGV GVSSAKGKKK FMEDAHKIVS CLQGNSKRGF FGVYDGHGGS KAAEFAAENL
     HTNVLEMMEA CAEKEEAFRA GYLKTDHEFL KQGVGSGTCC VTALVDEQEV VISNVGDCRA
     VLSRGGVAEA LTRDHTAAQE GERQRIQDKG GYVEFHRGAW RVHGVLSVSR SIGDAHLKSW
     VLGEPETNVL QLTPDMDFVV LASDGLWEKV GNQEAIDMVT RTCSVQKKMA PPGNGLKDND
     EDHLCVSVSP SSKLRRTLLV KEPKVTQSPG ELQKDNNDES GCVSASPSSN PSSKLQRISL
     VKQPKGTRSP GELLIDNNED YGYVNVSPSS KLRRISLVKQ PKGMQSPGYK KALFGSKDAD
     NDFSSENESP PSKSRRLSML KRVNMKTESP IKEKCGCKIR PTCGENEFAS ENESPPSKSR
     RISLVKRVNM KSESPIKENS GYKMRPASGG LVTACKELVN LTLSRGSLDD ITVMIIDLNH
     FRCNSG
//
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