ID V7CMD9_PHAVU Unreviewed; 964 AA.
AC V7CMD9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=PHAVU_002G226900g {ECO:0000313|EMBL:ESW31299.1};
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:ESW31299.1, 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; CM002289; ESW31299.1; -; Genomic_DNA.
DR RefSeq; XP_007159305.1; XM_007159243.1.
DR AlphaFoldDB; V7CMD9; -.
DR STRING; 3885.V7CMD9; -.
DR EnsemblPlants; ESW31299; ESW31299; PHAVU_002G226900g.
DR GeneID; 18638810; -.
DR Gramene; ESW31299; ESW31299; PHAVU_002G226900g.
DR KEGG; pvu:PHAVU_002G226900g; -.
DR eggNOG; KOG0323; Eukaryota.
DR OMA; GWFPAEE; -.
DR OrthoDB; 1200617at2759; -.
DR PhylomeDB; V7CMD9; -.
DR Proteomes; UP000000226; Chromosome 2.
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; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.30.160.20; -; 2.
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:SF0; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 1; 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; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50137; DS_RBD; 2.
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 128..376
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 708..774
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 844..915
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 520..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 107636 MW; 96A8AD9ED3342C5F CRC64;
MYKSVVYQGE VVLGEVEVYP EENNYKNFHV KEIRISHFSQ PSERCPPLAV LHTVTSCGVC
FKMESKTQQQ DGLFHLHSLC IRENKTAVIP LGGEEIHLVA MHSRNDDRPR FWGFIVALGL
YDSCLVMLNL RCLGIVFDLD ETLIVANTMR SFEDRIDALQ RKINSEVDPQ RISGMQAEVK
RYQEDKNILK QYAENDQVVD NGRVVKVQSE IVPALSDNHQ PIVRPLIRLQ DKNIILTRIN
PQIRDTSVLV RLRPAWEDLR SYLTARGRKR FEVYVCTMAE RDYALEMWRL LDPDSNLINS
KELLGRIVCV KSGLKKSLFN VFQDGLCHPK MALVIDDRLK VWDEKDQPRV HVVPAFAPYY
APQAEASNSI PVLCVARNVA CNVRGGFFKE FDDGLLQKIP QVAYEDDIKD IPIPPDVSNY
LVSEDDGSSA ISNGNRDPFL FDSMGDAEVE RKSKVPTRAP NEHDALSAAS TIPVTTANLD
PRLTSLQYAM VSSGSAPPPT AQASMMPFTH VQFPQPAALV KPMGQAAPSE SSLHSSPARE
EGEVPESELD PDTRRRLLIL QHGQDTRDHT SNEPTYAIRH PVPVSAPRVS SRGGWFPAEE
DIGSQPLNRV VPKEFSVDSG SLVIEKHRPH HPSFFSKVES SISSDRILHD SHQRLPKEMY
HRDDRPRSNH MLSSYRSLSV DEIPFSRSSS SHRDLDSESS HSVFHADTPV VVLQEIALKC
GTKVEFMSSL VASTELQFSI EAWFSGKKIG HGFGRTRKEA QHKAAEDSIK HLADIYLSSA
KDEPGSTYGD VGGFPNANDN GYMVIASSLS NQPLPKEDSA SFSTASDPSR VLDPRLEVSK
RPMGSISALK ELCMMEGLGV NFLSAPAPVS TNSLQKDEVH AQVEIDGKVF GKGIGLTWDE
AKMQAAEKAL GSLRSKLGQS IQKRQSSPRS HQGFSNKRLK QEYPRAMQRI PSSTRYPRNA
PPIP
//
