ID A0A0D3C2B6_BRAOL Unreviewed; 997 AA.
AC A0A0D3C2B6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
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};
GN Name=106342265 {ECO:0000313|EnsemblPlants:Bo4g161490.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo4g161490.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo4g161490.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo4g161490.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-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 RefSeq; XP_013636596.1; XM_013781142.1.
DR AlphaFoldDB; A0A0D3C2B6; -.
DR STRING; 109376.A0A0D3C2B6; -.
DR EnsemblPlants; Bo4g161490.1; Bo4g161490.1; Bo4g161490.
DR GeneID; 106342265; -.
DR Gramene; Bo4g161490.1; Bo4g161490.1; Bo4g161490.
DR KEGG; boe:106342265; -.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_004962_7_0_1; -.
DR OMA; PRMYATA; -.
DR OrthoDB; 311640at2759; -.
DR Proteomes; UP000032141; Chromosome C4.
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; 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:UP000032141}.
FT DOMAIN 763..768
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 106024 MW; 1BE3D2B6D1EC9643 CRC64;
MDSDSSMLHE ENDQDPASPN HQPPPQDSPS ESPAQTGSES ASAFTPTPAT SAQQQPPAVA
GPRCAPPYSV VNAILEKKED GPGPRCGHTL TAVPAVGEEG SANYIGPRLI LFGGATALEG
NSGGTGTPTS AGSAGGIRLA GATADVHCYD VLTNKWSRLS PHGEPPSPRA AHVATAVGTM
VVIQGGIGPA GLSAEDLHVL DLTQQRPRWH RVVVQGPGPG PRYGHVMALV GQRYLMAIGG
NDGKRPLADV WALDTAAKPY EWRKLEPEGE GPPTCMYATA SARSDGLLLL CGGRDANSVP
LASAYGLAKH RDGRWEWAIA PGVSPSARYQ HAAVFVNARL HVSGGALGGG RMVEDSSSIA
VLDTAAGVWC DTKSVVTSPR TGRYSADAAG GDASGELTRR CRHAAAAVGD LIFIYGGLRG
GVLLDDLLVA EDLAAAETTS AASHAAAAAA TNSPPGRSPG RYGFSDERTG ELSESAPDAV
VLGSPVAPPL NGDMYTDIST ENAMLPGTRR TSKGVEYLVE ASAAEAEAIS ATLAAAKARQ
VNGEVEQPDR DRGAEATPSG KPSSSLIKPD SAVSTSVIPA GVRLHHRAVV VAAETGGALG
GMVRQLSIDQ FENEGRRVGY GTPESATAAR KLLDRQQSIN SVPKKVVAHL LKPRGWKPPV
RRQFFLDCNE IADLCDSAER IFSSEPTVLQ LRAPIKIFGD LHGQFGDLMR LFDEYGSPST
AGDISYIDYL FLGDYVDRGQ HSLETITLLL ALKVEYQHNV HLIRGNHEAA DINALFGFRI
ECIERMGERD GIWVWHRINR LFNWLPLAAL IEKKIICMHG GIGRSINHVE QIENIQRPIT
MEAGSIVLMD LLWSDPTEND SVEGLRPNAR GPGLVTFGPD RVMEFCKNND LQLIVRAHEC
VMDGFERFAQ GHLITLFSAT NYCGTANNAG AILVLGRDLV VVPKLIHPLP PAITSPETSP
ERHVDDTWMQ ELNANRPPTP TRGRPQTPDD RGSLAWI
//
