ID K7MV85_SOYBN Unreviewed; 1257 AA.
AC K7MV85;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=100790196 {ECO:0000313|EnsemblPlants:KRH01516};
GN ORFNames=GLYMA_18G282300 {ECO:0000313|EMBL:KRH01515.1};
OS Glycine max (Soybean) (Glycine hispida).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH01516};
RN [1] {ECO:0000313|EMBL:KRH01515.1, ECO:0000313|EnsemblPlants:KRH01516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH01516};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH01515.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH01516}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH01516};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH01515.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH01515.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CM000851; KRH01515.1; -; Genomic_DNA.
DR EMBL; CM000851; KRH01516.1; -; Genomic_DNA.
DR RefSeq; XP_006603006.1; XM_006602943.2.
DR AlphaFoldDB; K7MV85; -.
DR PaxDb; 3847-GLYMA18G51840-2; -.
DR EnsemblPlants; KRH01515; KRH01515; GLYMA_18G282300.
DR EnsemblPlants; KRH01516; KRH01516; GLYMA_18G282300.
DR GeneID; 100790196; -.
DR Gramene; KRH01515; KRH01515; GLYMA_18G282300.
DR Gramene; KRH01516; KRH01516; GLYMA_18G282300.
DR KEGG; gmx:100790196; -.
DR eggNOG; KOG0323; Eukaryota.
DR HOGENOM; CLU_007943_0_0_1; -.
DR OrthoDB; 11699at2759; -.
DR Proteomes; UP000008827; Chromosome 18.
DR ExpressionAtlas; K7MV85; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR CDD; cd17729; BRCT_CTDP1; 1.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR011947; FCP1_euk.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02250; FCP1_euk; 1.
DR PANTHER; PTHR23081:SF2; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3; 1.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT DOMAIN 939..1119
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 1162..1255
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 568..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 137698 MW; 8FDC18E418B46D82 CRC64;
MIFGSLLDCE KLGKLEKMGK EVEDVEEGEI SDTASVEEIS AEDFNKQDVK VLNNNNKPNG
SDARVWAVHD LYSKYPTICR GYASGLYNLA WAQAVQNKPL NDIFVMEVDS DANANSNSNN
SNRLASVAVN PKDVVVVDVD KEEGELEEGE IDADAEPEGE AESVVAVPVV SDSEKLDDVK
RDVSNSEQLG VRGVLEGVTV ANVAESFAQT CSKLQNALPE VLSRPADSER DDLVRLSFNA
TEVVYSVFCS MDSLKKEQNK DSILRLLSFV KDQQQAQLFS PEHIKEIQGM MTAIDYFGAL
VNSEAIGKEK ELQTTVQTHE IKTQENQAVE AAELISYNKP LHSDIIGASH ALKFGQNSIK
GRGVLLPLLD LHKDHDADSL PSPTREAPSC FPVNKLLSVG EPMVSSGSAA AKPESGKMEL
DSEGSKFHLY ETDALKAVST YQQKFGRSSL FTNDKFPSPT PSGDCEDEIV DTNEEVSSAS
TGDFLTSTKP TLLDLPPVSA TSTDRSSLHG FISSRVDAAG PGSLPVKSSA KNRDPRLRFV
NSDASAVDNP STLIHNMPKV EYAGTTISRK QKAAEEPSLD VTVSKRQKSP LENTEHNMSE
VRTGIGGWLE EHTGPGAQFI ERNHLMDKFG PEPQKTLNTV SSSCTGSDNF NATSIRNEQA
PITSSNVLAS LPALLKGAAV NPTMLVNLLR IAEAQKKSAD SATNMLLHPT SSNSAMGTDS
TASIGSSMAT GLLQSSVGML PVSSQSTSMT QTLQDDSGKI RMKPRDPRRI LHTNNTIQKS
GNLGNEQFKA IVSPVSNNQG TGDNVNAQKL EGRVDSKLVP TQPSAQPDIA RQFARNLKNI
ADIMSVSQES STHTPVAQIF SSASVPLTSD RGEQKSVVSN SQNLEAGMVS AHETAASGTC
RSQNTWGDVE HLFEGYDEQQ KAAIQRERAR RIEEQNKMFA ARKLCLVLDL DHTLLNSAKF
VEVDPVHDEI LRKKEEQDRE KPHRHLFRFP HMGMWTKLRP GIWNFLEKAS KLYELHLYTM
GNKLYATEMA KVLDPKGLLF AGRVISRGDD TDSVDGEERA PKSKDLEGVL GMESSVVIID
DSVRVWPHNK LNLIVVERYT YFPCSRRQFG LPGPSLLEID HDERPEAGTL ASSLAVIEKI
HQIFFASRSL EEVDVRNILA SEQRKILAGC RIVFSRVFPV GEANPHLHPL WQTAEQFGAF
CTNQIDEQVT HVVANSPGTD KVNWALNNGR FVVHPGWVEA SALLYRRANE QDFAIKP
//
