BRM_ARATH
ID BRM_ARATH Reviewed; 2193 AA.
AC Q6EVK6; O82366; O82780;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=ATP-dependent helicase BRM {ECO:0000303|PubMed:15371304};
DE EC=3.6.4.12;
DE AltName: Full=Protein BRAHMA {ECO:0000303|PubMed:15371304};
DE Short=AtBRM {ECO:0000303|PubMed:15371304};
DE AltName: Full=Protein CHROMATIN REMODELING 2 {ECO:0000303|PubMed:16547115};
DE Short=AtCHR2 {ECO:0000303|PubMed:16547115};
GN Name=BRM {ECO:0000303|PubMed:15371304};
GN Synonyms=CHR2 {ECO:0000303|PubMed:16547115};
GN OrderedLocusNames=At2g46020 {ECO:0000312|Araport:AT2G46020};
GN ORFNames=F4I18, T3F17.33 {ECO:0000312|EMBL:AAC62901.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SWI3C AND BSH,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15371304; DOI=10.1242/dev.01363;
RA Farrona S., Hurtado L., Bowman J.L., Reyes J.C.;
RT "The Arabidopsis thaliana SNF2 homolog AtBRM controls shoot development and
RT flowering.";
RL Development 131:4965-4975(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16547115; DOI=10.1534/genetics.105.051664;
RA Shaked H., Avivi-Ragolsky N., Levy A.A.;
RT "Involvement of the Arabidopsis SWI2/SNF2 chromatin remodeling gene family
RT in DNA damage response and recombination.";
RL Genetics 173:985-994(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH SWI3A; SWI3B AND SWI3D.
RX PubMed=16845477; DOI=10.1007/s11103-006-9021-2;
RA Hurtado L., Farrona S., Reyes J.C.;
RT "The putative SWI/SNF complex subunit BRAHMA activates flower homeotic
RT genes in Arabidopsis thaliana.";
RL Plant Mol. Biol. 62:291-304(2006).
RN [6]
RP INTERACTION WITH HISTONES H3 AND H4.
RX PubMed=17825834; DOI=10.1016/j.jmb.2007.07.012;
RA Farrona S., Hurtado L., Reyes J.C.;
RT "A nucleosome interaction module is required for normal function of
RT Arabidopsis thaliana BRAHMA.";
RL J. Mol. Biol. 373:240-250(2007).
RN [7]
RP FUNCTION.
RX PubMed=17293567; DOI=10.1105/tpc.106.048272;
RA Bezhani S., Winter C., Hershman S., Wagner J.D., Kennedy J.F., Kwon C.S.,
RA Pfluger J., Su Y., Wagner D.;
RT "Unique, shared, and redundant roles for the Arabidopsis SWI/SNF chromatin
RT remodeling ATPases BRAHMA and SPLAYED.";
RL Plant Cell 19:403-416(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF GLY-1138.
RX PubMed=18508955; DOI=10.1104/pp.108.121996;
RA Tang X., Hou A., Babu M., Nguyen V., Hurtado L., Lu Q., Reyes J.C.,
RA Wang A., Keller W.A., Harada J.J., Tsang E.W.T., Cui Y.;
RT "The Arabidopsis BRAHMA chromatin-remodeling ATPase is involved in
RT repression of seed maturation genes in leaves.";
RL Plant Physiol. 147:1143-1157(2008).
RN [10]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2137,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1641, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP INTERACTION WITH LFY.
RX PubMed=22323601; DOI=10.1073/pnas.1113409109;
RA Wu M.F., Sang Y., Bezhani S., Yamaguchi N., Han S.K., Li Z., Su Y.,
RA Slewinski T.L., Wagner D.;
RT "SWI2/SNF2 chromatin remodeling ATPases overcome polycomb repression and
RT control floral organ identity with the LEAFY and SEPALLATA3 transcription
RT factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3576-3581(2012).
RN [14]
RP GENE FAMILY.
RX PubMed=24265739; DOI=10.1371/journal.pone.0078982;
RA Xu R., Zhang S., Huang J., Zheng C.;
RT "Genome-wide comparative in silico analysis of the RNA helicase gene family
RT in Zea mays and Glycine max: a comparison with Arabidopsis and Oryza
RT sativa.";
RL PLoS ONE 8:E78982-E78982(2013).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH FGT1.
RC STRAIN=cv. Columbia;
RX PubMed=27680998; DOI=10.7554/elife.17061;
RA Brzezinka K., Altmann S., Czesnick H., Nicolas P., Gorka M., Benke E.,
RA Kabelitz T., Jaehne F., Graf A., Kappel C., Baeurle I.;
RT "Arabidopsis FORGETTER1 mediates stress-induced chromatin memory through
RT nucleosome remodeling.";
RL Elife 5:0-0(2016).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH REF6.
RX PubMed=27111034; DOI=10.1038/ng.3555;
RA Li C., Gu L., Gao L., Chen C., Wei C.Q., Qiu Q., Chien C.W., Wang S.,
RA Jiang L., Ai L.F., Chen C.Y., Yang S., Nguyen V., Qi Y., Snyder M.P.,
RA Burlingame A.L., Kohalmi S.E., Huang S., Cao X., Wang Z.Y., Wu K., Chen X.,
RA Cui Y.;
RT "Concerted genomic targeting of H3K27 demethylase REF6 and chromatin-
RT remodeling ATPase BRM in Arabidopsis.";
RL Nat. Genet. 48:687-693(2016).
CC -!- FUNCTION: ATPase subunit of a multiprotein complex equivalent of the
CC SWI/SNF complex that acts by remodeling the chromatin by catalyzing an
CC ATP-dependent alteration in the structure of nucleosomal DNA. Represses
CC embryonic genes in leaves and controls shoot development and flowering.
CC Activates flower homeotic genes. The association of BRM with its target
CC genes requires REF6 (PubMed:27111034). Necessary to acquire heat stress
CC (HS) memory, by globally binding to HS memory genes (PubMed:27680998).
CC {ECO:0000269|PubMed:16845477, ECO:0000269|PubMed:17293567,
CC ECO:0000269|PubMed:18508955, ECO:0000269|PubMed:27111034,
CC ECO:0000269|PubMed:27680998}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts with SWI3B, SWI3C, H3 and H4, but not with SWI3A,
CC SWI3D or BSH (PubMed:15371304, PubMed:16845477, PubMed:17825834).
CC Interacts with LFY (PubMed:22323601). Interacts with REF6
CC (PubMed:27111034). Binds to FGT1 (PubMed:27680998).
CC {ECO:0000269|PubMed:15371304, ECO:0000269|PubMed:16845477,
CC ECO:0000269|PubMed:17825834, ECO:0000269|PubMed:22323601,
CC ECO:0000269|PubMed:27111034, ECO:0000269|PubMed:27680998}.
CC -!- INTERACTION:
CC Q6EVK6; Q00958: LFY; NbExp=3; IntAct=EBI-2025535, EBI-1644366;
CC Q6EVK6; Q9ZVD0: SE; NbExp=6; IntAct=EBI-2025535, EBI-6553299;
CC Q6EVK6; O22456: SEP3; NbExp=2; IntAct=EBI-2025535, EBI-592020;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:15371304, ECO:0000269|PubMed:19245862,
CC ECO:0000269|PubMed:27111034}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6EVK6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6EVK6-2; Sequence=VSP_034709;
CC -!- TISSUE SPECIFICITY: Highly expressed in inflorescences and leaves. Low
CC expression in siliques, roots and seedlings. Detected in shoot apical
CC meristem, root meristem, vascular tissue of developing leaves, petals,
CC stamens filaments, anthers and carpels. {ECO:0000269|PubMed:15371304}.
CC -!- DOMAIN: The bromodomain binds histones.
CC -!- DOMAIN: The AT-hook region (1568-1919) contains at least 3 DNA-binding
CC sites with different characteristics.
CC -!- DISRUPTION PHENOTYPE: Sterility. Reduced heat stress (HS) memory
CC associated with a premature decline of expression of HSA32, HSP18.2,
CC HSP21, HSP22 and HSP101 after HS. The double mutant brm-1 fgt1-1
CC exhibits retarted seedling development resulting in reduced development
CC and delayed leaf initiation, as well as delayed flowering time.
CC {ECO:0000269|PubMed:27680998}.
CC -!- MISCELLANEOUS: Was previously split between At2g46010 and At2g46020.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62900.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC62901.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM14971.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ703891; CAG28313.1; -; mRNA.
DR EMBL; AC004665; AAM14971.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005397; AAC62900.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005397; AAC62901.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10632.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10633.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61549.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61550.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61551.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61552.1; -; Genomic_DNA.
DR PIR; G84897; G84897.
DR RefSeq; NP_001318432.1; NM_001337166.1. [Q6EVK6-2]
DR RefSeq; NP_001323760.1; NM_001337168.1. [Q6EVK6-1]
DR RefSeq; NP_001323761.1; NM_001337169.1. [Q6EVK6-2]
DR RefSeq; NP_001323762.1; NM_001337167.1. [Q6EVK6-1]
DR RefSeq; NP_182126.2; NM_130165.3. [Q6EVK6-2]
DR RefSeq; NP_973695.1; NM_201966.2. [Q6EVK6-1]
DR AlphaFoldDB; Q6EVK6; -.
DR SMR; Q6EVK6; -.
DR BioGRID; 4545; 170.
DR DIP; DIP-46526N; -.
DR IntAct; Q6EVK6; 7.
DR STRING; 3702.AT2G46020.2; -.
DR iPTMnet; Q6EVK6; -.
DR PaxDb; Q6EVK6; -.
DR PRIDE; Q6EVK6; -.
DR ProteomicsDB; 240409; -. [Q6EVK6-1]
DR EnsemblPlants; AT2G46020.1; AT2G46020.1; AT2G46020. [Q6EVK6-2]
DR EnsemblPlants; AT2G46020.2; AT2G46020.2; AT2G46020. [Q6EVK6-1]
DR EnsemblPlants; AT2G46020.3; AT2G46020.3; AT2G46020. [Q6EVK6-1]
DR EnsemblPlants; AT2G46020.4; AT2G46020.4; AT2G46020. [Q6EVK6-1]
DR EnsemblPlants; AT2G46020.5; AT2G46020.5; AT2G46020. [Q6EVK6-2]
DR EnsemblPlants; AT2G46020.6; AT2G46020.6; AT2G46020. [Q6EVK6-2]
DR GeneID; 819210; -.
DR Gramene; AT2G46020.1; AT2G46020.1; AT2G46020. [Q6EVK6-2]
DR Gramene; AT2G46020.2; AT2G46020.2; AT2G46020. [Q6EVK6-1]
DR Gramene; AT2G46020.3; AT2G46020.3; AT2G46020. [Q6EVK6-1]
DR Gramene; AT2G46020.4; AT2G46020.4; AT2G46020. [Q6EVK6-1]
DR Gramene; AT2G46020.5; AT2G46020.5; AT2G46020. [Q6EVK6-2]
DR Gramene; AT2G46020.6; AT2G46020.6; AT2G46020. [Q6EVK6-2]
DR KEGG; ath:AT2G46020; -.
DR Araport; AT2G46020; -.
DR TAIR; locus:2062999; AT2G46020.
DR eggNOG; KOG0386; Eukaryota.
DR HOGENOM; CLU_000942_0_1_1; -.
DR InParanoid; Q6EVK6; -.
DR OMA; KPLRNMA; -.
DR OrthoDB; 685477at2759; -.
DR PhylomeDB; Q6EVK6; -.
DR PRO; PR:Q6EVK6; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q6EVK6; baseline and differential.
DR Genevisible; Q6EVK6; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0090691; P:formation of plant organ boundary; IMP:TAIR.
DR GO; GO:0010199; P:organ boundary specification between lateral organs and the meristem; IGI:TAIR.
DR GO; GO:1900036; P:positive regulation of cellular response to heat; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
DR GO; GO:1903798; P:regulation of miRNA maturation; IDA:TAIR.
DR GO; GO:0010449; P:root meristem growth; IGI:TAIR.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031056; BRM.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF978; PTHR10799:SF978; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00951; QLQ; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; ATP-binding; Bromodomain;
KW Chromatin regulator; Coiled coil; Developmental protein; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..2193
FT /note="ATP-dependent helicase BRM"
FT /id="PRO_0000343902"
FT DOMAIN 463..499
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 993..1158
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1312..1489
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1918..1988
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2022..2193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..58
FT /evidence="ECO:0000255"
FT COILED 726..795
FT /evidence="ECO:0000255"
FT COILED 1109..1129
FT /evidence="ECO:0000255"
FT COILED 1618..1638
FT /evidence="ECO:0000255"
FT MOTIF 705..712
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 1901..1908
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 19..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1616..1637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1652
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1817..1833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1834..1894
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2022..2037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2050..2068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2098..2114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2146..2170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1006..1013
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 1641
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 2137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT VAR_SEQ 1075..1079
FT /note="EVCAM -> VKFE (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034709"
FT MUTAGEN 1138
FT /note="G->R: In brm-5/essp3; ectopic expression of seed
FT storage proteins in leaves."
FT /evidence="ECO:0000269|PubMed:18508955"
SQ SEQUENCE 2193 AA; 245469 MW; ECC557B079A91301 CRC64;
MQSGGSGGGP ARNPAMGPAG RTASTSSAAS PSSSSSSVQQ QQQQQQQQQQ QQQLASRQQQ
QQHRNSDTNE NMFAYQPGGV QGMMGGGNFA SSPGSMQMPQ QSRNFFESPQ QQQQQQQQGS
STQEGQQNFN PMQQAYIQFA MQAQHQKAQQ QARMGMVGSS SVGKDQDARM GMLNMQDLNP
SSQPQASSSK PSGDQFARGE RQTESSSQQR NETKSHPQQQ VGTGQLMPGN MIRPMQAPQA
QQLVNNMGNN QLAFAQQWQA MQAWARERNI DLSHPANASQ MAHILQARMA AQQKAGEGNV
ASQSPSIPIS SQPASSSVVP GENSPHANSA SDISGQSGSA KARHALSTGS FASTSSPRMV
NPAMNPFSGQ GRENPMYPRH LVQPTNGMPS GNPLQTSANE TPVLDQNAST KKSLGPAEHL
QMQQPRQLNT PTPNLVAPSD TGPLSNSSLQ SGQGTQQAQQ RSGFTKQQLH VLKAQILAFR
RLKKGEGSLP PELLQAISPP PLELQTQRQI SPAIGKVQDR SSDKTGEDQA RSLECGKESQ
AAASSNGPIF SKEEDNVGDT EVALTTGHSQ LFQNLGKEAT STDVATKEEQ QTDVFPVKSD
QGADSSTQKN PRSDSTADKG KAVASDGSQS KVPPQANSPQ PPKDTASARK YYGPLFDFPF
FTRKLDSYGS ATANANNNLT LAYDIKDLIC EEGAEFLSKK RTDSLKKING LLAKNLERKR
IRPDLVLRLQ IEEKKLRLSD LQSRVREEVD RQQQEIMSMP DRPYRKFVRL CERQRLEMNR
QVLANQKAVR EKQLKTIFQW RKKLLEAHWA IRDARTARNR GVAKYHEKML REFSKRKDDG
RNKRMEALKN NDVERYREML LEQQTNMPGD AAERYAVLSS FLTQTEDYLH KLGGKITATK
NQQEVEEAAN AAAVAARLQG LSEEEVRAAA TCAREEVVIR NRFTEMNAPK ENSSVNKYYT
LAHAVNEVVV RQPSMLQAGT LRDYQLVGLQ WMLSLYNNKL NGILADEMGL GKTVQVMALI
AYLMEFKGNY GPHLIIVPNA VLVNWKSELH TWLPSVSCIY YVGTKDQRSK LFSQEVCAMK
FNVLVTTYEF IMYDRSKLSK VDWKYIIIDE AQRMKDRESV LARDLDRYRC QRRLLLTGTP
LQNDLKELWS LLNLLLPDVF DNRKAFHDWF AQPFQKEGPA HNIEDDWLET EKKVIVIHRL
HQILEPFMLR RRVEDVEGSL PAKVSVVLRC RMSAIQSAVY DWIKATGTLR VDPDDEKLRA
QKNPIYQAKI YRTLNNRCME LRKACNHPLL NYPYFNDFSK DFLVRSCGKL WILDRILIKL
QRTGHRVLLF STMTKLLDIL EEYLQWRRLV YRRIDGTTSL EDRESAIVDF NDPDTDCFIF
LLSIRAAGRG LNLQTADTVV IYDPDPNPKN EEQAVARAHR IGQTREVKVI YMEAVVEKLS
SHQKEDELRS GGSVDLEDDM AGKDRYIGSI EGLIRNNIQQ YKIDMADEVI NAGRFDQRTT
HEERRMTLET LLHDEERYQE TVHDVPSLHE VNRMIARSEE EVELFDQMDE EFDWTEEMTN
HEQVPKWLRA STREVNATVA DLSKKPSKNM LSSSNLIVQP GGPGGERKRG RPKSKKINYK
EIEDDIAGYS EESSEERNID SGNEEEGDIR QFDDDELTGA LGDHQTNKGE FDGENPVCGY
DYPPGSGSYK KNPPRDDAGS SGSSPESHRS KEMASPVSSQ KFGSLSALDT RPGSVSKRLL
DDLEEGEIAA SGDSHIDLQR SGSWAHDRDE GDEEQVLQPT IKRKRSIRLR PRQTAERVDG
SEMPAAQPLQ VDRSYRSKLR TVVDSHSSRQ DQSDSSSRLR SVPAKKVAST SKLHVSSPKS
GRLNATQLTV EDNAEASRET WDGTSPISSS NAGARMSHII QKRCKIVISK LQRRIDKEGQ
QIVPMLTNLW KRIQNGYAAG GVNNLLELRE IDHRVERLEY AGVMELASDV QLMLRGAMQF
YGFSHEVRSE AKKVHNLFFD LLKMSFPDTD FREARNALSF SGSAPTLVST PTPRGAGISQ
GKRQKLVNEP ETEPSSPQRS QQRENSRIRV QIPQKETKLG GTTSHTDESP ILAHPGELVI
CKKKRKDREK SGPKTRTGGS SSPVSPPPAM IGRGLRSPVS GGVPRETRLA QQQRWPNQPT
HPNNSGAAGD SVGWANPVKR LRTDSGKRRP SHL
