ID   BSL2_ORYSJ              Reviewed;        1009 AA.
AC   Q2QM47;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   16-JUN-2009, entry version 32.
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; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
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
RT   resistance genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   MEDLINE=22752273; 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: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC   -!- SIMILARITY: Contains 5 Kelch repeats.
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DR   EMBL; DP000011; ABA99873.2; -; Genomic_DNA.
DR   EMBL; AK065064; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001067290.1; -.
DR   UniGene; Os.81458; -.
DR   GeneID; 4352808; -.
DR   KEGG; osa:4352808; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011498; Kelch_2.
DR   InterPro; IPR004843; M-pesterase.
DR   InterPro; IPR012391; PPP_BSU1.
DR   InterPro; IPR006186; T_phtase_apaH.
DR   Gene3D; G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
DR   PANTHER; PTHR11668; T_phtase_apaH; 1.
DR   Pfam; PF01344; Kelch_1; 1.
DR   Pfam; PF07646; Kelch_2; 2.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF036363; PPP_BSU1; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   ProDom; PD000252; T_phtase_apaH; 1.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Iron; Kelch repeat; Manganese; Metal-binding; Nucleus;
KW   Protein phosphatase; Repeat.
FT   CHAIN         1   1009       Serine/threonine-protein phosphatase BSL2
FT                                homolog.
FT                                /FTId=PRO_0000247274.
FT   REPEAT      136    182       Kelch 1.
FT   REPEAT      240    288       Kelch 2.
FT   REPEAT      293    344       Kelch 3.
FT   REPEAT      349    396       Kelch 4.
FT   REPEAT      417    463       Kelch 5.
FT   COMPBIAS     21     28       Poly-Gly.
FT   COMPBIAS     44     83       Ala-rich.
FT   ACT_SITE    778    778       Proton donor (By similarity).
FT   METAL       711    711       Iron (By similarity).
FT   METAL       713    713       Iron (By similarity).
FT   METAL       745    745       Iron (By similarity).
FT   METAL       745    745       Manganese (By similarity).
FT   METAL       777    777       Manganese (By similarity).
FT   METAL       830    830       Manganese (By similarity).
FT   METAL       909    909       Manganese (By similarity).
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
//