ID I1R7X4_ORYGL Unreviewed; 1007 AA.
AC I1R7X4;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 glaberrima (African rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA12G0163000.1, ECO:0000313|Proteomes:UP000007306};
RN [1] {ECO:0000313|Proteomes:UP000007306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA Zuccolo A.;
RT "The complete genome of Oryza glaberrima.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORGLA12G0163000.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-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; I1R7X4; -.
DR STRING; 4538.I1R7X4; -.
DR EnsemblPlants; ORGLA12G0163000.1; ORGLA12G0163000.1; ORGLA12G0163000.
DR Gramene; ORGLA12G0163000.1; ORGLA12G0163000.1; ORGLA12G0163000.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_004962_7_0_1; -.
DR OMA; HDEAQSP; -.
DR Proteomes; UP000007306; Unassembled WGS sequence.
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; 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:SF13; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL2 HOMOLOG; 1.
DR Pfam; PF01344; Kelch_1; 1.
DR Pfam; PF07646; Kelch_2; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF13418; Kelch_4; 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}.
FT DOMAIN 772..777
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1007 AA; 106261 MW; 74079307486AF27F CRC64;
RRSRTPTRTP RRRGGGGGGG GGFGSETSSA SPSAPGTPTA MGAGGGAAPI AAAAAAVAAA
ASAAVVAGPR PAPGYTVVNA AMEKKEDGPG CRCGHTLTAV PAVGEEGAPG YVGPRLILFG
GATALEGNSA TPPSSAGSAG IRLAGATADV HCYDVSSNKW SRLTPVGEPP SPRAAHVATA
VGTMVVIQGG IGPAGLSAED LHVLDLTQQR PRWHRVVVQG PGPGPRYGHV MALVGQRFLL
TIGGNDGKRP LADVWALDTA AKPYEWRKLE PEGEGPPPCM YATASARSDG LLLLCGGRDA
NSVPLASAYG LAKHRDGRWE WAIAPGVSPS PRYQHAAVFV NARLHVSGGA LGGGRMVEDS
SSVAVLDTAA GVWCDTKSVV TTPRTGRYSA DAAGGDASVE LTRRCRHAAA AVGDMIYVYG
GLRGGVLLDD LLVAEDLAAA ETTNAANQAA AIAAASDIQA GREPGRYAYN DEQTGQPATV
TSPDGAVVLG TPVAAPVNGD MYTDISPENA VIQGQRRMSK GVDYLVEASA AEAEAISATL
AAVKARQVNG DAEHSPDREQ SPDATPSVKQ NASLIKPDYA LSNNSTPPPG VRLHHRAVVV
AAETGGALGG MVRQLSIDQF ENEGRRVIYG TPESATAARK LLDRQMSINS VPKKVIASLL
KPRGWKPPVR RQFFLDCNEI ADLCDSAERI FSSEPSVLQL KAPIKIFGDL HGQFGDLMRL
FDEYGAPSTA GDIAYIDYLF LGDYVDRGQH SLETITLLLA LKVEYPLNVH LIRGNHEAAD
INALFGFRIE CIERMGERDG IWTWHRMNRL FNWLPLAALI EKKIICMHGG IGRSINHVEQ
IENLQRPITM EAGSVVLMDL LWSDPTENDS VEGLRPNARG PGLVTFGPDR VMEFCNNNDL
QLIVRAHECV MDGFERFAQG HLITLFSATN YCGTANNAGA ILVLGRDLVV VPKLIHPLPP
AITSPETSPE HHLEDTWMQE LNANRPPTPT RGRPQAANND RGSLAWI
//
