ID A0A0E0KGU1_ORYPU Unreviewed; 1003 AA.
AC A0A0E0KGU1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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:OPUNC03G25160.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC03G25160.1}
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:OPUNC03G25160.1}
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; A0A0E0KGU1; -.
DR STRING; 4537.A0A0E0KGU1; -.
DR EnsemblPlants; OPUNC03G25160.1; OPUNC03G25160.1; OPUNC03G25160.
DR Gramene; OPUNC03G25160.1; OPUNC03G25160.1; OPUNC03G25160.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR OMA; WDWVLAP; -.
DR Proteomes; UP000026962; Chromosome 3.
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; IPR011498; Kelch_2.
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:SF4; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF13415; Kelch_3; 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 763..768
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1003 AA; 106152 MW; 7D512A0399B364CF CRC64;
MDVDSRMTTE SDSDSDAAAA SVAAQGGGCG GGLASETSCS SSSSVSAPST PGTPTVAPAP
AAVGATGPRP APGYTAVTAV IEKKEDGPGC RCGHTLTAVP AVGEEGTPGY IGPRLVLFGG
ATALEGNSAT PPSSAGSAGI RLAGATADVH CYDVLSNKWS RLTPQGEPPS PRAAHVATAV
GTMVVIQGGI GPAGLSAEDL HVLDLTQQRP RWHRVVVQGP GPGPRYGHVM ALVGQRFLLT
IGGNDGKRPL ADVWALDTAA KPYEWRKLEP EGEGPPPCMY ATASARSDGL LLLCGGRDAN
SVPLASAYGL AKHRDGRWEW AIAPGVSPSP RYQHAAVFVN ARLHVSGGAL GGGRMVEDSS
SVAVLDTAAG VWCDTKSVVT TPRIGRYSAD AAGGDAAVEL TRRCRHAAAA VGDQIFIYGG
LRGGVLLDDL LVAEDLAAAE TTTAANHAAA SAAATNVQSG RTPGRYAYND ERARQTAPES
AQDGSVVLGT PVAPPVNGDM YTDISPENAV LQGQRRLSKG VDYLVEASAA EAEAISATLA
AVKARQVNGE MEQLPDKEQS PDSTSTSKHS SLIKPDTALS NNMTPPPGVV VAAETGGALG
GMVRQLSIDQ FENEGRRVSY GTPENATAAR KLLDRQMSIN SVPKKVIASL LKPRGWKPPV
RRQFFLDCNE IADLCDSAER IFSSEPSVLQ LKAPVKIFGD LHGQFGDLMR LFDEYGAPST
AGDIAYIDYL FLGDYVDRGQ HSLETMALLL ALKVEYPQNV HLIRGNHEAA DINALFGFRI
ECIERMGERD GIWTWHRMNR LFNWLPLAAL IEKKIICMHG GIGRSINHVE QIENLQRPIT
MEAGSVVLMD LLWSDPTEND SVEGLRPNAR GPGLVTFGPD RVMEFCNNND LQLIVRAHEC
VMDGFERFAQ GHLITLFSAT NYCGTANNAG AILVLGRDLV VVPKLIHPLP PAITSPETSP
EHHIEDTWMQ ELNANRPPTP TRGRPQSKVI CVCETVAHSH AKR
//