ID   BSL1_ORYSJ              Reviewed;         883 AA.
AC   Q60EX6; Q0DKT4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 115.
DE   RecName: Full=Serine/threonine-protein phosphatase BSL1 homolog;
DE            EC=3.1.3.16;
DE   AltName: Full=BSU1-like protein 1 homolog;
GN   Name=BSL1; OrderedLocusNames=Os05g0144400, LOC_Os05g05240;
GN   ORFNames=OJ1607_F09.10;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA   Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA   Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA   Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT   "A fine physical map of the rice chromosome 5.";
RL   Mol. Genet. Genomics 274:337-345(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   INTERACTION WITH BSK3.
RX   PubMed=26697897; DOI=10.1104/pp.15.01668;
RA   Zhang B., Wang X., Zhao Z., Wang R., Huang X., Zhu Y., Yuan L., Wang Y.,
RA   Xu X., Burlingame A.L., Gao Y., Sun Y., Tang W.;
RT   "OsBRI1 activates BR signaling by preventing binding between the TPR and
RT   kinase domains of OsBSK3 via phosphorylation.";
RL   Plant Physiol. 170:1149-1161(2016).
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   -!- 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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with the phosphorylated form of BSK3.
CC       {ECO:0000305|PubMed:26697897}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AC104283; AAU90203.1; -; Genomic_DNA.
DR   EMBL; AP008211; BAF16539.1; -; Genomic_DNA.
DR   EMBL; AP014961; BAS92232.1; -; Genomic_DNA.
DR   EMBL; AK120211; BAG99920.1; -; mRNA.
DR   RefSeq; XP_015640150.1; XM_015784664.1.
DR   AlphaFoldDB; Q60EX6; -.
DR   SMR; Q60EX6; -.
DR   STRING; 39947.Q60EX6; -.
DR   PaxDb; 39947-Q60EX6; -.
DR   EnsemblPlants; Os05t0144400-01; Os05t0144400-01; Os05g0144400.
DR   GeneID; 4337785; -.
DR   Gramene; Os05t0144400-01; Os05t0144400-01; Os05g0144400.
DR   KEGG; osa:4337785; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   eggNOG; KOG0379; Eukaryota.
DR   HOGENOM; CLU_004962_7_1_1; -.
DR   InParanoid; Q60EX6; -.
DR   OMA; CKEGPAT; -.
DR   OrthoDB; 311640at2759; -.
DR   PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR   Proteomes; UP000000763; Chromosome 5.
DR   Proteomes; UP000059680; Chromosome 5.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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.
DR   Genevisible; Q60EX6; OS.
PE   1: Evidence at protein level;
KW   Hydrolase; Kelch repeat; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome; Repeat.
FT   CHAIN           1..883
FT                   /note="Serine/threonine-protein phosphatase BSL1 homolog"
FT                   /id="PRO_0000247484"
FT   REPEAT          64..113
FT                   /note="Kelch 1"
FT   REPEAT          221..271
FT                   /note="Kelch 2"
FT   REPEAT          273..323
FT                   /note="Kelch 3"
FT   REPEAT          341..387
FT                   /note="Kelch 4"
FT   REGION          381..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..451
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        653
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         586
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         588
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         620
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         620
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         652
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         705
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         784
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   883 AA;  96282 MW;  F75CF327E3815863 CRC64;
     MGTAGKGAWV VPAPAYREVE GWEGAGDDSP GFRCGHSLTV VAPTKGHGPR LILFGGATAI
     EAGASSGMPG IRLAGVTNSV HSYDVDTRRW 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 SDSPTTNNST DKKSIDMLTQ ASAAEAEAVS
     AVWRAAQEAS HASSEDSLSE GIGSESPLSE TSPMPEDLDD GGSLEPDVKL HSRAVVVSKE
     AVGDLGCLVR QLSLDQFENE SRRMHPSSND QSYPAKKALN RQRSPQGLHK KVISFLLKPR
     NWRAPAERAF FLDSYEVGEL CYAAEQIFMQ EPTVLQLKAP IKVFGDLHGQ FGDLMRLFDE
     YGYPSTAGDI TYIDYLFLGD YVDRGQHSLE TITLLLALKI EYPENVHLIR GNHEAADINA
     LFGFRLECIE RMGESDGIWA WTRFNQLFNY LPLAAMIEKK IICMHGGIGR SINTIEQIEK
     LERPITMDVG SIILMDLLWS DPTENDSVEG LRPNARGPGL VTFGPDRVTE FCKRNRLQLI
     IRAHECVMDG FERFAHGQLI TLFSATNYCG TANNAGAILV VGRGLVIVPK LIHPLPPPVN
     SPESSPERAM DATWMQELNI QRPPTPTRGR PQSASDRNSL AYI
//