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Database: UniProt
Entry: A0A2G2WMR6_CAPBA
LinkDB: A0A2G2WMR6_CAPBA
Original site: A0A2G2WMR6_CAPBA 
ID   A0A2G2WMR6_CAPBA        Unreviewed;       986 AA.
AC   A0A2G2WMR6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
DE   Flags: Fragment;
GN   ORFNames=CQW23_15608 {ECO:0000313|EMBL:PHT46450.1};
OS   Capsicum baccatum (Peruvian pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=33114 {ECO:0000313|EMBL:PHT46450.1, ECO:0000313|Proteomes:UP000224567};
RN   [1] {ECO:0000313|EMBL:PHT46450.1, ECO:0000313|Proteomes:UP000224567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RC   TISSUE=Leaf {ECO:0000313|EMBL:PHT46450.1};
RX   PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA   Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA   Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA   Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA   Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA   Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA   Bennetzen J.L., Choi D.;
RT   "New reference genome sequences of hot pepper reveal the massive evolution
RT   of plant disease-resistance genes by retroduplication.";
RL   Genome Biol. 18:R210.1-R210.11(2017).
RN   [2] {ECO:0000313|Proteomes:UP000224567}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. PBC81 {ECO:0000313|Proteomes:UP000224567};
RA   Kim S., Park J., Yeom S.-I., Kim Y.-M., Seo E., Kim K.-T., Kim M.-S.,
RA   Lee J.M., Cheong K., Shin H.-S., Kim S.-B., Han K., Lee J., Park M.,
RA   Lee H.-A., Lee H.-Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E.,
RA   Jeon J., Kim H., Choi G., Song H., Lee J., Lee S.-C., Kwon J.-K.,
RA   Lee H.-Y., Koo N., Hong Y., Kim R.W., Kang W.-H., Huh J.H., Kang B.-C.,
RA   Yang T.-J., Lee Y.-H., Bennetzen J.L., Choi D.;
RT   "Multiple reference genome sequences of hot pepper reveal the massive
RT   evolution of plant disease resistance genes by retroduplication.";
RL   J. Anim. Genet. bioRxivorg:115410-115410(2017).
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|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC       {ECO:0000256|ARBA:ARBA00005671}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PHT46450.1}.
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DR   EMBL; MLFT02000006; PHT46450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G2WMR6; -.
DR   STRING; 33114.A0A2G2WMR6; -.
DR   Proteomes; UP000224567; Chromosome 6.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; PF13415; Kelch_3; 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|RuleBase:RU004273};
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000224567}.
FT   DOMAIN          758..763
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..559
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          965..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         986
FT                   /evidence="ECO:0000313|EMBL:PHT46450.1"
SQ   SEQUENCE   986 AA;  105325 MW;  403732DF46D265BF CRC64;
     MDVDSTMSPE SDHDQNKGAS SEQLNGQSSA GGSPAETPKD EQQQQQQQGS TPVAGPRCAP
     PYSVVHAVME KKEDGPGPRC GHTLTAVPAI GEEGSSNYVG PRLILFGGAT ALEGNSAAPG
     TPSSAGSAGI RLAGATADVH SYDVLTNKWS RMTPIGEPPT PRAAHVATAV GTMVVIQGGI
     GPAGLSSEDL HVLDLTQQRP RWHRVVVQGP GPGPRYGHVM ALVGQRYLMA IGGNDGKRPL
     ADVWALDTAA KPYEWRKLEP EGEGPPPCMY ATASARSDGL LLLCGGRDAN SVPLASAYGL
     AKHRDGRWEW AIAPGVSPSP RYQHAAVFVN ARLHVSGGAL GGGRMVEDSS SIAVLDTAAG
     VWCDTKSVVT SPRTGRYSAD AAGGDAAVEL TRRCRHAAVA VGDLIFIYGG LRGGVLLDDL
     LVAEDLAAAE TTSAASHAAA AAVNVQSGRL TGRYGFGDER TRQRGPEAVN DGSVVLGPPV
     APPVNGDMYS DISTENATLQ GPRRLIQGVE YLVEASAAEA EAISATLAAA KARQQGNGEV
     EVPDRDRGAE ATPSGKQAST LIKPDSALSS NSVPAGVRLH HRAVVIAAET GGALGGMVRQ
     LSIDQFENEG RRVSYGTPEN ATAARKLLDR QMSINSVPKK VISHLLKPRG WKPPVRRQFF
     LDCNEIADLC DCAERIFASE PSVLQLRAPI KIFGDLHGQF GDLMRLFDEY GSPSTAGDIS
     YIDYLFLGDY VDRGQHSLET MTLLLALKVE YPLNVHLIRG NHEAADINAL FGFRIECIER
     MGERDGIWAW HRFNRLFNWL PLAALIEKKI ICMHGGIGRS INHVEQIKNI QRPITMDAGS
     IVLMDLLWSD PTENDSVEGL RPNARGPGLV TFGPDRVMEF CNNNDLQLIV RAHECVMDGF
     ERFAQGHLIT LFSATNYCGT ANNAGAILVL GRDLVVVPKL IHPLPPAISS PETSPERHIE
     DTWMQELNAN RPPTPTRGRP QVANDR
//
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