ID   BSL2_ORYSJ              Reviewed;        1009 AA.
AC   Q2QM47; Q0ILV6;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Serine/threonine-protein phosphatase BSL2 homolog;
DE            EC=3.1.3.16;
DE   AltName: Full=BSU1-like protein 2 homolog;
GN   Name=BSL2; OrderedLocusNames=Os12g0617900, LOC_Os12g42310;
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=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(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).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC       {ECO:0000305}.
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DR   EMBL; DP000011; ABA99873.2; -; Genomic_DNA.
DR   EMBL; AP008218; BAF30309.1; -; Genomic_DNA.
DR   EMBL; AP014968; BAT18111.1; -; Genomic_DNA.
DR   EMBL; AK065064; BAG89347.1; -; mRNA.
DR   RefSeq; XP_015620177.1; XM_015764691.1.
DR   AlphaFoldDB; Q2QM47; -.
DR   SMR; Q2QM47; -.
DR   STRING; 4530.OS12T0617900-02; -.
DR   PaxDb; Q2QM47; -.
DR   PRIDE; Q2QM47; -.
DR   EnsemblPlants; Os12t0617900-02; Os12t0617900-02; Os12g0617900.
DR   GeneID; 4352808; -.
DR   Gramene; Os12t0617900-02; Os12t0617900-02; Os12g0617900.
DR   KEGG; osa:4352808; -.
DR   eggNOG; KOG0374; Eukaryota.
DR   eggNOG; KOG0379; Eukaryota.
DR   InParanoid; Q2QM47; -.
DR   OMA; MAPEEND; -.
DR   OrthoDB; 124339at2759; -.
DR   PlantReactome; R-OSA-5632095; Brassinosteroid signaling.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   ExpressionAtlas; Q2QM47; baseline and differential.
DR   Genevisible; Q2QM47; OS.
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; 2.120.10.80; -; 2.
DR   Gene3D; 3.60.21.10; -; 1.
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   Pfam; PF01344; Kelch_1; 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; SSF117281; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Kelch repeat; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome; Repeat.
FT   CHAIN           1..1009
FT                   /note="Serine/threonine-protein phosphatase BSL2 homolog"
FT                   /id="PRO_0000247274"
FT   REPEAT          136..182
FT                   /note="Kelch 1"
FT   REPEAT          240..288
FT                   /note="Kelch 2"
FT   REPEAT          293..344
FT                   /note="Kelch 3"
FT   REPEAT          349..396
FT                   /note="Kelch 4"
FT   REPEAT          417..463
FT                   /note="Kelch 5"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          549..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..999
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        778
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         711
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         713
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         745
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         745
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         777
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         830
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         909
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1009 AA;  106426 MW;  9BDD845DC706A3A3 CRC64;
     MDVDSRMTTE SDSDSDAAAQ GGGGGGFGSE TSSASPSAPG TPTAMGAGGG AAPIAAAAIA
     AAASAAVVAG PRPAPGYTVV NAAMEKKEDG PGCRCGHTLT AVPAVGEEGA PGYVGPRLIL
     FGGATALEGN SATPPSSAGS AGIRLAGATA DVHCYDVSSN KWSRLTPVGE PPSPRAAHVA
     TAVGTMVVIQ GGIGPAGLSA EDLHVLDLTQ QRPRWHRVVV QGPGPGPRYG HVMALVGQRF
     LLTIGGNDGK RPLADVWALD TAAKPYEWRK LEPEGEGPPP CMYATASARS DGLLLLCGGR
     DANSVPLASA YGLAKHRDGR WEWAIAPGVS PSPRYQHAAV FVNARLHVSG GALGGGRMVE
     DSSSVAVLDT AAGVWCDTKS VVTTPRTGRY SADAAGGDAS VELTRRCRHA AAAVGDMIYV
     YGGLRGGVLL DDLLVAEDLA AAETTNAANQ AAAIAAASDI QAGREPGRYA YNDEQTGQPA
     TITSPDGAVV LGTPVAAPVN GDMYTDISPE NAVIQGQRRM SKGVDYLVEA SAAEAEAISA
     TLAAVKARQV NGEAEHSPDR EQSPDATPSV KQNASLIKPD YALSNNSTPP PGVRLHHRAV
     VVAAETGGAL GGMVRQLSID QFENEGRRVI YGTPESATAA RKLLDRQMSI NSVPKKVIAS
     LLKPRGWKPP VRRQFFLDCN EIADLCDSAE RIFSSEPSVL QLKAPIKIFG DLHGQFGDLM
     RLFDEYGAPS TAGDIAYIDY LFLGDYVDRG QHSLETITLL LALKVEYPLN VHLIRGNHEA
     ADINALFGFR IECIERMGER DGIWTWHRMN RLFNWLPLAA LIEKKIICMH GGIGRSINHV
     EQIENLQRPI TMEAGSVVLM DLLWSDPTEN DSVEGLRPNA RGPGLVTFGP DRVMEFCNNN
     DLQLIVRAHE CVMDGFERFA QGHLITLFSA TNYCGTANNA GAILVLGRDL VVVPKLIHPL
     PPAITSPETS PEHHLEDTWM QELNANRPPT PTRGRPQAAN NDRGSLAWI