ID V7B453_PHAVU Unreviewed; 802 AA.
AC V7B453;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=PHAVU_008G105400g {ECO:0000313|EMBL:ESW12355.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW12355.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM002295; ESW12355.1; -; Genomic_DNA.
DR RefSeq; XP_007140361.1; XM_007140299.1.
DR AlphaFoldDB; V7B453; -.
DR EnsemblPlants; ESW12355; ESW12355; PHAVU_008G105400g.
DR GeneID; 18622470; -.
DR Gramene; ESW12355; ESW12355; PHAVU_008G105400g.
DR OMA; RSEELCV; -.
DR OrthoDB; 1200617at2759; -.
DR Proteomes; UP000000226; Chromosome 8.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR CDD; cd10845; DSRM_RNAse_III_family; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081:SF24; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 2; 1.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR Pfam; PF00035; dsrm; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00358; DSRM; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 134..382
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 678..744
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 539..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 802 AA; 89800 MW; 04C6C4BBFCA53C12 CRC64;
MNRLGFKHEV YDGDKHVGEL DVSPTTPFHN FRFPNNEIRI HHFSAKSERC PPLSILQTIA
AFNVRCKLDS SVVAEQKELT SIHASCFYEM KTAVVLVNDE EIHLVSMPSK RKKFPCFWCF
AVPVGLYHAC LGMLNLRCLA IVFDLDETLI VANTMKSFED RIEALRVWLS REIDPLRVQG
MSAELKRYLE DRLLLKQFAE SDCVMDNGKV YKVQMEEVLP HSGSHEKLIR PVVRLQDKNI
VLTRINPEIR DTSVLVRLRP AWEDLRCYLT AKGRKRFEVY VCTMAERDYA LEMWRLLDPE
AHLIGPKQIL ERVICVKSGS RKSLPNVFQD GMCHPKMAMV IDDRSKVWED KDQPRVHVVP
AFTPYYAPQA ETANAVPVLC VARNVACNVR GCFFKEFDES LLQRIAEIFF EDDIGILPHP
PDVSNYLMSE DVPNGNTNAP LSEGINGAEV ERRLSQPGDK FPVDMVTQPM ANSVEFRHEA
SQPTAGIISS VTGPGSSRIL IPSLKPGLLG PPVKHEASSV DRDYDMRKGV LGMRHGPDIR
GQISAEPPLI SRPPNQASAS LMPQSFGGGL VEDDITSRTQ TNNWSIASGK ESSLVKSDKH
QAQLKPFSHS VIGSPSNVVH QQASQLKTEE ATSVSDLPRQ NAPSKSLLSE DGISQNHASS
NSKDLQNEAG KLNLLPPLSI QVLQEIGRRC NSKVEFKSIL STSKDLQFSV EVLFTGEKIG
VGMGRTRKDA QQQAAENALR SLAEKYVAHV EPQCRVVDRE FDKLSLGRDN GFLWDVVNPE
SNELRREDGV PRENASEHQC EG
//
