ID A0A1S3TJ82_VIGRR Unreviewed; 1008 AA.
AC A0A1S3TJ82;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
GN Name=LOC106756092 {ECO:0000313|RefSeq:XP_014493839.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014493839.1};
RN [1] {ECO:0000313|RefSeq:XP_014493839.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014493839.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|PIRNR:PIRNR036363, ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR036363};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR036363};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR036363}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC {ECO:0000256|ARBA:ARBA00005671, ECO:0000256|PIRNR:PIRNR036363}.
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DR RefSeq; XP_014493839.1; XM_014638353.2.
DR AlphaFoldDB; A0A1S3TJ82; -.
DR STRING; 3916.A0A1S3TJ82; -.
DR EnsemblPlants; Vradi02g07260.1; Vradi02g07260.1; Vradi02g07260.
DR GeneID; 106756092; -.
DR Gramene; Vradi02g07260.1; Vradi02g07260.1; Vradi02g07260.
DR KEGG; vra:106756092; -.
DR OrthoDB; 311640at2759; -.
DR Proteomes; UP000087766; Chromosome 2.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
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; 3.
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|PIRNR:PIRNR036363};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRNR:PIRNR036363};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR036363};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR036363};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR036363};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT DOMAIN 774..779
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
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"
SQ SEQUENCE 1008 AA; 107403 MW; 027DEDD40EDBA0DE CRC64;
MDVDSSMLPE ADHDSPVQNH AERDQLKESQ PPPSPPPLST AGGSQAQSPS QQQPSSPVAG
GQVQHSPVVG PRLAPTYSVV NAILEKKEDG PGPRCGHTLT AVAAVGEEGT PGYIGPRLIL
FGGATELEGN SAASGTPSSA GNAGIRLSGA TADVHCYDVI TNKWSRITPI GEPPTPRAAH
VATAVGTMVV IQGGIGPAGL FAEDLHVLDL TQQRPRWHRV GVPGPGPGPR YGHVMALVGQ
RYLMVIGGND GKRPLADVWA LDTAAKPYEW RKLEPEGEGP PPCMYATASA RSDGLLLLCG
GRDANSAPLA SAYGLAKHRD GRWEWAIAPG VSPSPRYQHA AVFVNARLHV FGGALGGGQM
VEDSSSVAVL DTAAGVWCDT KSVVTSPRTG RYSADAAGGD ASVELTRRCR HAAAAIGDLI
FIYGGLRGGV LLDDLLVAED LAAAETTAAA SHAAAAAASN VQAGRLPGRY GGFVDDRARQ
TMIEATPDGA VVLGNPVAPP VNGDIHTDIS TENALLPGSR RTSKGVEYLV EASAAEAEAI
SATLAAAKAR QVNGEVELPD RDRGAEATPS GKQIYSLIKP DSSASNSIPP GGVRLHHRAV
VVAAETGGAL GGMVRQLSID QFENEGRRVS YGTPESATAA RKLLDRQMSI NSVPKKVVAH
LLKPRGWKPP VRRQFFLDCN EIADLCDSAE RIFSSEPSVI QLRAPIKIFG DLHGQFGDLM
RLFDEYGSPS TAGDIAYIDY LFLGDYVDRG QHSLETISLL LALKVEYPNN VHLIRGNHEA
ADINALFGFR IECIERMGER DGIWAWHRIN RLFNWLPLAA LIEKKIICMH GGIGRSINHV
EQIENIQRPI TMEAGSIVLM DLLWSDPTEN DSVEGLRPNA RGPGLVTFGP DRVMEFCNNN
DLQLIVRAHE CVMDGFERFA QGHLITLFSA TNYCGTANNA GAILVLGRDL VVVPKLIHPL
PPAISSPETS PERHIEDTWM QELNANRPPT PTRGRPQVTN DRGSLAWI
//
