ID A0A0E0KYD9_ORYPU Unreviewed; 891 AA.
AC A0A0E0KYD9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC05G02870.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC05G02870.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC05G02870.1}
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 ECO:0000256|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR036363};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR036363};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR036363}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC {ECO:0000256|ARBA:ARBA00005671, ECO:0000256|PIRNR:PIRNR036363}.
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DR AlphaFoldDB; A0A0E0KYD9; -.
DR STRING; 4537.A0A0E0KYD9; -.
DR EnsemblPlants; OPUNC05G02870.1; OPUNC05G02870.1; OPUNC05G02870.
DR Gramene; OPUNC05G02870.1; OPUNC05G02870.1; OPUNC05G02870.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR OMA; CKEGPAT; -.
DR Proteomes; UP000026962; Chromosome 5.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR CDD; cd07419; MPP_Bsu1_C; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041758; MPP_BSL_C.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR012391; Ser/Thr_prot_Pase_BSU1.
DR PANTHER; PTHR46422; SERINE/THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR PANTHER; PTHR46422:SF6; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL1-RELATED; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF13854; Kelch_5; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036363; PPP_BSU1; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036363};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR036363};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR036363};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036363};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR036363};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962}.
FT DOMAIN 657..662
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 374..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 97167 MW; 6BF70C1EE7FA9068 CRC64;
MGTAGKGAWV VPAPAYREVE GWEGAGDDSP GFRCGHSLTA VAPTKGHGPR LILFGGATAI
EAGASSGMPG IRLAGVTNSV HSYDVETRRW TRLHPAGEPP SPRAAHAAAA VGTMVVFQGG
IGPAGHSTDD LYVLDLTNDK FKWHRVVVQG AGPGPRYGHC MDLVAQRYLV TVSGNDGKRV
LSDAWALDTA QKPYRWQKLN PDGDRPSARM YATASARTDG MLLLCGGRDA SGMPLSDAYG
LLMHTSGQWE WTLAPGVSPS PRYQHAAVFV GARLHVTGGV LRGGRAIEGE GAIAVLDTAA
GVWLDRNGIV TSRTLKSSHD HDASSDLLRR CRHAAASVGT QIYIYGGLRG DILLDDFLVA
DNAPIQSEFT SSMYDRVPRA ENQNRNHNFN SDSPTTNNRH EIASGFSTDK KSIDMLTEAS
AAEAEAVSAV WRAAQEASHA SSEDSLSEGI GSESPLSETS PMPEDLDDGG SLEPDVKLHS
RAVVVSKEAV GDLGCLVRQL SLDQFENESR RMHPSSNDQS YPAKKALNRQ RSPQGLHKKV
ISFLLKPRNW RAPAERAFFL DSYEVGELCY AAEQIFMQEP TVLQLKAPIK VFGDLHGQFG
DLMRLFDEYG YPSTAGDITY IDYLFLGDYV DRGQHSLETI TLLLALKIEY PENVHLIRGN
HEAADINALF GFRLECIERM GESDGIWAWT RFNQLFNYLP LAAMIEKKII CMHGGIGRSI
NTIEQIEKLE RPITMDVGSI ILMDLLWSDP TENDSVEGLR PNARGPGLVT FGPDRVTEFC
KRNRLQLIIR AHECVMDGFE RFAHGQLITL FSATNYCGTA NNAGAILVVG RGLVIVPKLI
HPLPPPVNSP ESSPERAMDA TWMQELNIQR PPTPTRGRPQ SASDRNSLAY I
//
