ID A0A1R3JKT5_COCAP Unreviewed; 1194 AA.
AC A0A1R3JKT5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=CCACVL1_05415 {ECO:0000313|EMBL:OMO95414.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO95414.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO95414.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO95414.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:OMO95414.1}.
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DR EMBL; AWWV01007660; OMO95414.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JKT5; -.
DR STRING; 210143.A0A1R3JKT5; -.
DR EnsemblPlants; OMO95414; OMO95414; CCACVL1_05415.
DR Gramene; OMO95414; OMO95414; CCACVL1_05415.
DR OMA; MAPEEND; -.
DR OrthoDB; 311640at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
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; IPR011043; Gal_Oxase/kelch_b-propeller.
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; 2.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF50965; Galactose oxidase, central domain; 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:UP000188268}.
FT DOMAIN 840..845
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 127871 MW; 5E994FC0B2E8FE0E CRC64;
MDVDSSMVPE TDHDQNHGGA SQSPAPMERE QQQQQPPPQQ QNQQLEDQTS PPGPGGSPPP
PAQQQAAAVA AAAQVQPQTP VVGPRCAPTY SVVNAIIEKK EDGPGPRCGH TLTAVAAVGE
EGTPGYIGPR LILFGGATAL EGNSAASGTP SSAGSAGIRL AGATADVHCY DVLTNKWSRI
TPFGEPPTPR AAHVATAVGT MVVIQGGIGP AGLSAEDLHV LDLTQQRPRW HRVVVQGPGP
GPRYGHVMAL VGQRYLMAIG GNDGKRPLAD VWALDTAAKP YEWRKLEPEG EGPPPCMYAT
ASARSDGLLL LCGGRDANSV GRLAYISVNG GTDLNHNFIC VVREERHSNE NQRFSQPVLS
SWFLWCAVFQ PLASAYGLAK HRDGRWEWAI APGVSPSPRY QHAAVFVNAR LHVSGGALGG
GRMVEDSSSV AVLDTAAGVW CDTKSVVTSP RTGRYSADAA GGDASVELTR RCRHAAAAVG
DLIFIYGGLR GGVLLDDLLV AEDLAAAETT TAASHAAAAA AASNTGRLPA TGRYGFVDER
TRQTMPEAVS DGSVVLGNPV APPVNGDMYT DISTENAMLQ GSRRMSKGVE YLVEASAAEA
EAISATLAAA KARQGQVNGE VELPDRDRGA EATPSGKQMS TLIKMPDSAG ANNVAPAGVR
LHHRAVVVAA ETGGALGGMV RQLSIDQFEN EGRRVSYGTP ESATAARKLL DRQMSINSVP
KKVIAHLLKP RGWKPPVRRQ FFLDCNEIAD LCDSAERIFC TEPSVLQLKA PIKIFGDLHG
QFGDLMRLFD EYGAPSTAGD IAYIDYLFLG DYVDRGQHSL ETITLLLALK VEYPNNVHLI
RGNHEAADIN ALFGFRIECI ERMGERDGIW AWHRINRLFN WLPLAALIEK KIICMHGGIG
RSINHVEQIE NLQRPITMEA GSIVLMDLLW SDPTENDSVE GLRPNARGPG LVTFGPDRVM
EFCNNNDLQL IVRAHECVMD GFERFAQGHL ITLFSATNYC GTANNAGAIL VLGRDLVVVP
KLIHPLPPAM SSPEASPERH IEDTWMQGLG VGKDWVIREY RLEEGGIVHD YVLCVVWKKE
SLGDYQFAAP FIDDDEIEVE NLVWTGTNSC SGSGSNSAPV LSSGLASMDD MVVPVPESME
ASQVADQVTA QVQSNSIDNY SMEFPCGYDV PESMEAPQVA DQVPAQVQSI PLWI
//
