ID SYD_ARATH Reviewed; 3574 AA.
AC F4IHS2; F4IHS3; F4IHS4; Q5BN47; Q8L9D7; Q9AUB4; Q9SL27;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Chromatin structure-remodeling complex protein SYD;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase SYD;
DE AltName: Full=Protein CHROMATIN REMODELING 3;
DE AltName: Full=Protein SPLAYED;
GN Name=SYD; Synonyms=CHR3; OrderedLocusNames=At2g28290; ORFNames=T3B23;
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), FUNCTION, DISRUPTION PHENOTYPE,
RP MUTAGENESIS OF GLY-1153, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11818058; DOI=10.1016/s0960-9822(01)00651-0;
RA Wagner D., Meyerowitz E.M.;
RT "SPLAYED, a novel SWI/SNF ATPase homolog, controls reproductive development
RT in Arabidopsis.";
RL Curr. Biol. 12:85-94(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=16640604; DOI=10.1111/j.1365-313x.2006.02734.x;
RA Su Y., Kwon C.S., Bezhani S., Huvermann B., Chen C., Peragine A.,
RA Kennedy J.F., Wagner D.;
RT "The N-terminal ATPase AT-hook-containing region of the Arabidopsis
RT chromatin-remodeling protein SPLAYED is sufficient for biological
RT activity.";
RL Plant J. 46:685-699(2006).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3252-3574 (ISOFORM 3).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15833920; DOI=10.1101/gad.1276305;
RA Kwon C.S., Chen C., Wagner D.;
RT "WUSCHEL is a primary target for transcriptional regulation by SPLAYED in
RT dynamic control of stem cell fate in Arabidopsis.";
RL Genes Dev. 19:992-1003(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=16854978; DOI=10.1242/dev.02508;
RA Kwon C.S., Hibara K., Pfluger J., Bezhani S., Metha H., Aida M., Tasaka M.,
RA Wagner D.;
RT "A role for chromatin remodeling in regulation of CUC gene expression in
RT the Arabidopsis cotyledon boundary.";
RL Development 133:3223-3230(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
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 [9]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP INTERACTION WITH BARD1/ROW1.
RX PubMed=18591352; DOI=10.1105/tpc.108.058867;
RA Han P., Li Q., Zhu Y.-X.;
RT "Mutation of Arabidopsis BARD1 causes meristem defects by failing to
RT confine WUSCHEL expression to the organizing center.";
RL Plant Cell 20:1482-1493(2008).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY WOUNDING.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=19079584; DOI=10.1371/journal.ppat.1000237;
RA Walley J.W., Rowe H.C., Xiao Y., Chehab E.W., Kliebenstein D.J., Wagner D.,
RA Dehesh K.;
RT "The chromatin remodeler SPLAYED regulates specific stress signaling
RT pathways.";
RL PLoS Pathog. 4:E1000237-E1000237(2008).
RN [12]
RP IDENTIFICATION BY 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 [13]
RP FUNCTION, DISRUPTION PHENOTYPE, AND 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).
CC -!- FUNCTION: Catalytic component of the chromatin structure-remodeling
CC complex (RSC), which is involved in transcription regulation and
CC nucleosome positioning. Controls stem cell fate via the transcription
CC regulation of WUS in the shoot apical meristem, by modulating its
CC promoter. LFY-dependent repressor of the meristem identity switch from
CC vegetative to reproductive development probably by modulating chromatin
CC state. Involved in the regulation of floral homeotic gene expression in
CC response to environmental stimuli. Required for carpel and ovule
CC development, and for cotyledon separation via the regulation of CUC2
CC transcription. Regulates the promoters of several genes downstream of
CC the jasmonate (JA) and ethylene (ET) signaling pathways. Required for
CC resistance against the necrotrophic pathogen B.cinerea but not the
CC biotrophic pathogen P.syringae. {ECO:0000269|PubMed:11818058,
CC ECO:0000269|PubMed:15833920, ECO:0000269|PubMed:16640604,
CC ECO:0000269|PubMed:16854978, ECO:0000269|PubMed:17293567,
CC ECO:0000269|PubMed:19079584, ECO:0000269|PubMed:22323601}.
CC -!- SUBUNIT: Interacts with LFY (PubMed:22323601). Binds to BARD1/ROW1
CC (PubMed:18591352). {ECO:0000269|PubMed:18591352,
CC ECO:0000269|PubMed:22323601}.
CC -!- INTERACTION:
CC F4IHS2; Q00958: LFY; NbExp=4; IntAct=EBI-15967899, EBI-1644366;
CC F4IHS2; O22456: SEP3; NbExp=2; IntAct=EBI-15967899, EBI-592020;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=F4IHS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IHS2-2; Sequence=VSP_046250;
CC Name=3;
CC IsoId=F4IHS2-3; Sequence=VSP_046249;
CC -!- TISSUE SPECIFICITY: Mostly expressed in rapidly dividing cells in the
CC vegetative, inflorescence, and root meristems, as well as in young leaf
CC and flower primordia. Isoform 1 is predominantly found in seedlings
CC whereas isoform 2 is present in both seedlings and inflorescences (at
CC protein level). {ECO:0000269|PubMed:11818058,
CC ECO:0000269|PubMed:16640604}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:19079584}.
CC -!- PTM: Phosphorylated.
CC -!- DISRUPTION PHENOTYPE: Precocious transition from inflorescence to
CC flower formation and impaired maintenance of the shoot apical meristem
CC (SAM) during the reproductive phase. Abnormal flowers with splayed open
CC first-whorl sepals due to outward bending of the pointy sepal tips.
CC Reduced male fertility and reduced anther dehiscence. Partially unfused
CC at the tip fourth-whorl carpels, with stigmatic tissue missing or
CC placed internal to the carpel tip, leading to funnel shaped carpels.
CC Female sterility ovule growth arrest at megagametogenesis. Fused
CC cotyledons. Impaired expression of PDF1.2a, leading to reduced ethylene
CC (ET) and jasmonic acid (JA) signaling. Reduced resistance toward B.
CC cinerea. {ECO:0000269|PubMed:11818058, ECO:0000269|PubMed:15833920,
CC ECO:0000269|PubMed:16854978, ECO:0000269|PubMed:17293567,
CC ECO:0000269|PubMed:19079584, ECO:0000269|PubMed:22323601}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD29835.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM66026.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF247809; AAK31908.1; -; mRNA.
DR EMBL; AY927849; AAX22009.1; -; mRNA.
DR EMBL; AC006202; AAD29835.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08099.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08100.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08101.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63245.1; -; Genomic_DNA.
DR EMBL; AY088490; AAM66026.1; ALT_INIT; mRNA.
DR PIR; A84683; A84683.
DR RefSeq; NP_001077971.1; NM_001084502.2. [F4IHS2-2]
DR RefSeq; NP_001325347.1; NM_001336158.1. [F4IHS2-2]
DR RefSeq; NP_850116.1; NM_179785.3. [F4IHS2-1]
DR RefSeq; NP_850117.1; NM_179786.2. [F4IHS2-3]
DR SMR; F4IHS2; -.
DR BioGRID; 2725; 34.
DR ComplexPortal; CPX-7726; SYD-associated SWI/SNF ATP-dependent chromatin remodeling complex.
DR DIP; DIP-60019N; -.
DR IntAct; F4IHS2; 2.
DR STRING; 3702.F4IHS2; -.
DR iPTMnet; F4IHS2; -.
DR PaxDb; 3702-AT2G28290-1; -.
DR ProteomicsDB; 232978; -. [F4IHS2-1]
DR EnsemblPlants; AT2G28290.1; AT2G28290.1; AT2G28290. [F4IHS2-1]
DR EnsemblPlants; AT2G28290.2; AT2G28290.2; AT2G28290. [F4IHS2-3]
DR EnsemblPlants; AT2G28290.3; AT2G28290.3; AT2G28290. [F4IHS2-2]
DR EnsemblPlants; AT2G28290.4; AT2G28290.4; AT2G28290. [F4IHS2-2]
DR GeneID; 817375; -.
DR Gramene; AT2G28290.1; AT2G28290.1; AT2G28290. [F4IHS2-1]
DR Gramene; AT2G28290.2; AT2G28290.2; AT2G28290. [F4IHS2-3]
DR Gramene; AT2G28290.3; AT2G28290.3; AT2G28290. [F4IHS2-2]
DR Gramene; AT2G28290.4; AT2G28290.4; AT2G28290. [F4IHS2-2]
DR KEGG; ath:AT2G28290; -.
DR Araport; AT2G28290; -.
DR TAIR; AT2G28290; SYD.
DR eggNOG; KOG0386; Eukaryota.
DR eggNOG; KOG1181; Eukaryota.
DR InParanoid; F4IHS2; -.
DR PRO; PR:F4IHS2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IHS2; baseline and differential.
DR Genevisible; F4IHS2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; ISS:TAIR.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0010199; P:organ boundary specification between lateral organs and the meristem; IGI:TAIR.
DR GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0010104; P:regulation of ethylene-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; DNA-binding;
KW Ethylene signaling pathway; Helicase; Hydrolase;
KW Jasmonic acid signaling pathway; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Plant defense; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..3574
FT /note="Chromatin structure-remodeling complex protein SYD"
FT /id="PRO_0000421936"
FT DOMAIN 573..647
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 766..933
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1077..1223
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 76..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1342..1472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1690..1811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1830..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2040..2068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2089..2115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2143..2162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2179..2220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2235..2338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2350..2451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2517..2538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2684..2703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2718..2759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2865..2884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3017..3045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3189..3208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3316..3337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3512..3574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 884..887
FT /note="DEAH box"
FT MOTIF 1266..1273
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 79..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1593..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1795..1811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1836..1865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2040..2061
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2089..2105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2179..2196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2285..2312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2322..2336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2371..2394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2403..2420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2432..2451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2517..2531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2718..2740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2741..2758
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3316..3330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3519..3537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3538..3562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 779..786
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT VAR_SEQ 3339..3383
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_046249"
FT VAR_SEQ 3339..3369
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16640604"
FT /id="VSP_046250"
FT MUTAGEN 1153
FT /note="G->E: In syd-1; precocious transition from
FT inflorescence to flower formation, abnormal flowers
FT exhibiting variable petals and stamens number and position
FT as well as some mosaic organs (stamenoid petals)."
FT /evidence="ECO:0000269|PubMed:11818058"
FT CONFLICT 757
FT /note="Y -> E (in Ref. 1; AAK31908 and 2; AAX22009)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3574 AA; 389864 MW; 14209D18F717A69B CRC64;
MTSSSHNIEL EAAKFLHKLI QDSKDEPAKL ATKLYVILQH MKTSGKENTM PYQVISRAMD
TVVNQHGLDI EALKSSCLPH PGGTQTEDSG SAHLAGSSQA VGVSNEGKAT LVENEMTKYD
AFTSGRQLGG SNSASQTFYQ GSGTQSNRSF DRESPSNLDS TSGISQPHNR SETMNQRDVK
SSGKRKRGES SLSWDQNMDN SQIFDSHKID DQTGEVSKIE MPGNSGDIRN LHVGLSSDAF
TTPQCGWQSS EATAIRPAIH KEPGNNVAGE GFLPSGSPFR EQQLKQLRAQ CLVFLALRNG
LVPKKLHVEI ALRNTFREED GFRGELFDPK GRTHTSSDLG GIPDVSALLS RTDNPTGRLD
EMDFSSKETE RSRLGEKSFA NTVFSDGQKL LASRIPSSQA QTQVAVSHSQ LTFSPGLTKN
TPSEMVGWTG VIKTNDLSTS AVQLDEFHSS DEEEGNLQPS PKYTMSQKWI MGRQNKRLLV
DRSWSLKQQK ADQAIGSRFN ELKESVSLSD DISAKTKSVI ELKKLQLLNL QRRLRSEFVY
NFFKPIATDV EHLKSYKKHK HGRRIKQLEK YEQKMKEERQ RRIRERQKEF FGGLEVHKEK
LEDLFKVRRE RLKGFNRYAK EFHKRKERLH REKIDKIQRE KINLLKINDV EGYLRMVQDA
KSDRVKQLLK ETEKYLQKLG SKLKEAKLLT SRFENEADET RTSNATDDET LIENEDESDQ
AKHYLESNEK YYLMAHSIKE NINEQPSSLV GGKLREYQMN GLRWLVSLYN NHLNGILADE
MGLGKTVQVI SLICYLMETK NDRGPFLVVV PSSVLPGWQS EINFWAPSIH KIVYCGTPDE
RRKLFKEQIV HQKFNVLLTT YEYLMNKHDR PKLSKIHWHY IIIDEGHRIK NASCKLNADL
KHYVSSHRLL LTGTPLQNNL EELWALLNFL LPNIFNSSED FSQWFNKPFQ SNGESSAEEA
LLSEEENLLI INRLHQVLRP FVLRRLKHKV ENELPEKIER LIRCEASAYQ KLLMKRVEDN
LGSIGNAKSR AVHNSVMELR NICNHPYLSQ LHSEEVNNII PKHFLPPIVR LCGKLEMLDR
MLPKLKATDH RVLFFSTMTR LLDVMEDYLT LKGYKYLRLD GQTSGGDRGA LIDGFNKSGS
PFFIFLLSIR AGGVGVNLQA ADTVILFDTD WNPQVDLQAQ ARAHRIGQKK DVLVLRFETV
NSVEEQVRAS AEHKLGVANQ SITAGFFDNN TSAEDRKEYL ESLLRESKKE EDAPVLDDDA
LNDLIARRES EIDIFESIDK QRKENEMETW NTLVHGPGSD SFAHIPSIPS RLVTEDDLKL
LYETMKLNDV PMVAKESTVG MKRKDGSMGG LDTHQYGRGK RAREVRSYEE KLTEEEFEKL
CQTESPDSPQ GKGEGSERSL ANDTSNIPVE NSSDTLLPTS PTQAITVQPM EPVRPQSHTL
KEETQPIKRG RGRPKRTDKA LTPVSLSAVS RTQATGNAIS SAATGLDFVS SDKRLEAASH
PTSSLALTSP DLSGPPGFQS LPASPAPTPI RGRGRGRSRG RGAGRGRRVE GVLHGSNSSI
TQRTETATSL ASDAEATKFA LPRSASEIVS RVPKANEGST SNPDQVSPVH SATTALRSDK
AADKDLDAPP GFDSGSHVQT LNVLENSSER KAFAVKKRPL IQGVSSQHPG PNKQPLDLPV
STSSTLLGGG PVQNQNAVSS VCDGSKSPSE GRTYTALQGV TTAPSDATLP MSSQPSDATL
PMSSQPVGST VEAQEANVPS LPAALPAKRR VRNLPSRGET PKRQGKRRGQ PLPATDASSA
RSTGLTPQIE VKVGNLSGTK AKFDAVAKEQ PHFSQSVAPD IHSSGSLSQE IRRDTSGTGG
SARKQTADVT DVARVMKEIF SETSLLKHKV GEPSATTRTN VPDAQSPGEM NLHTVETHKA
EDSSGLKNQE ALYNLSKADK LVSDIPHPVP GDLTTSGSVA NKDVDIGSSK VAAENELVKI
PGGDVDSSVI QLSLGNTLTA KSSLEKCTAD QLLGEKLSQE GETTPASDGE TCHLAEETAS
SLSYVRSEPT ASASTTAEPL PTDKLEKNIS FQDEVKTLNG DKREAILLSS EEQTNVNSKI
ETNSEELQAS RTDEVPHVDG KSVDVANQTV KEDEAKHSVE IQSSMLEPDE LPNAGQKGHS
SIDLQPLVLV TSNENAMSLD DKDYDPISKS ADIEQDPEES VFVQGVGRPK VGTADTQMED
TNDAKLLVGC SVESEEKEKT LQSLIPGDDA DTEQDPEESV SDQRPKVGSA YTQMEDTDEA
KLLMGCSVES EEKEKTLQSH IPGDDADTEK NPEESVSVQG VDRPKVGTTD TQMEDTNDAK
LLVGCSVASE EKEKTLQSHI PGDDADTEQN PEESVSVQGV NRPKVGNANT QMEDTDEAKV
LVGCSVESEE KEKTLQSHIP GDDADTEQNP EESVSNFDRP KDGTADTHME DIDDAKLLVG
CSVESEEKEK SLQSHMPSDD AVLHAPFENT KDSKGDDLHG ESLVSCPTME VMEQKGFESE
THARTDSGGI DRGNEVSENM SDGVKMNISS VQVPDASHDL NVSQDQTDIP LVGGIDPEHV
QENVDVPASP HGAAPNIVIF QSEGHLSPSI LPDDVAGQLE SMSNDEKTNI SSEQVPDVSH
DLKVSQDQTD IPPVGGIVPE NLQEIVDVPA SPHGVVPDVV VSQSEEIQSP SILPDDVPGQ
PDDGNCEKMD TMQNNTSIDI GITSGKTCQP SSSTQPEDEN RNSLSHCEPS EVVEQRDSRD
QVCIGSVESQ VEISSAILEN RSADIQPPQS ILVDQKDIEE SKEPGIESAD VSLHQLADIQ
AEPSNLVDQM DIEESKEPGT ESADVSLHQL ADIQPGPSIL VDQMDTEKSK EPGTESADVS
LHQLADIQPG PSILVDQMDT EKSKEPGTES ADVSLHQLAD IQPGPSILVD QMDTEEFKNP
DVSLHQLADI EPSLSISAVQ KNIEDKDQSH VETAGSELVD VSAECSTEPQ VQLPPSSEPV
GDMHVHLGAS KSEIVAEGTD FSSSLPKTEE ENAKSQLADT EPSSSLTAVQ KNIEDQVETA
GCEFVVVSTG CSTEPQVQLP PSAEPVVAEG TEFPSSLLMT GVDNSSHLMT GVDNAKTHLA
DVVPSSSPTT MEKNIEAQDQ DQVTTGGCGL VDVLTECSSE PQLQLPPSAE PVISEGTELA
TLPLTEEENA DSQLANIEPS SSPSVVEKNI EAQDQDQVKT AGCELVSTGC SSEPQVHLPP
SAEPDGDIHV HLKETEKSES MVVVGEGTAF PSSLPVTEEG NAESQLADTE PFTSPTVVEK
NIKDQEQVET TGCGLVDDST GCSSEPQVQL PPSAEPMEGT HMHLEETKKS ETVVTEIQLA
DIDPSFSLIV VQTNIEDQDQ IETGGCDLIN VPSGCSTEPQ IQLSSSAEPE EGMHIHLEAA
MNSETVVTEG SELPSSLPMT EDENADGQLA EVEPSVSLTV EQTNIEEKDH IETAECELVD
VSPGCSSQPE VKFPPSPDAV GGMDVHLETV VTEDTDSNSS LPKTEEKDAE NPSDRLDGES
DGTTVATVEG TCVESNSLVA EESNIEVPKD NEDV
//
