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Chromatin structure-remodeling complex protein SYD (EC 3.6.4.-) (ATP-dependent helicase SYD) (Protein CHROMATIN REMODELING 3) (Protein SPLAYED)

 SYD_ARATH               Reviewed;        3574 AA.
F4IHS2; F4IHS3; F4IHS4; Q5BN47; Q8L9D7; Q9AUB4; Q9SL27;
03-APR-2013, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 1.
23-MAY-2018, entry version 57.
RecName: Full=Chromatin structure-remodeling complex protein SYD;
EC=3.6.4.-;
AltName: Full=ATP-dependent helicase SYD;
AltName: Full=Protein CHROMATIN REMODELING 3;
AltName: Full=Protein SPLAYED;
Name=SYD; Synonyms=CHR3; OrderedLocusNames=At2g28290; ORFNames=T3B23;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISRUPTION
PHENOTYPE, MUTAGENESIS OF GLY-1153, AND TISSUE SPECIFICITY.
STRAIN=cv. Landsberg erecta;
PubMed=11818058; DOI=10.1016/S0960-9822(01)00651-0;
Wagner D., Meyerowitz E.M.;
"SPLAYED, a novel SWI/SNF ATPase homolog, controls reproductive
development in Arabidopsis.";
Curr. Biol. 12:85-94(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
PubMed=16640604; DOI=10.1111/j.1365-313X.2006.02734.x;
Su Y., Kwon C.S., Bezhani S., Huvermann B., Chen C., Peragine A.,
Kennedy J.F., Wagner D.;
"The N-terminal ATPase AT-hook-containing region of the Arabidopsis
chromatin-remodeling protein SPLAYED is sufficient for biological
activity.";
Plant J. 46:685-699(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3252-3574 (ISOFORM 3).
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=15833920; DOI=10.1101/gad.1276305;
Kwon C.S., Chen C., Wagner D.;
"WUSCHEL is a primary target for transcriptional regulation by SPLAYED
in dynamic control of stem cell fate in Arabidopsis.";
Genes Dev. 19:992-1003(2005).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=16854978; DOI=10.1242/dev.02508;
Kwon C.S., Hibara K., Pfluger J., Bezhani S., Metha H., Aida M.,
Tasaka M., Wagner D.;
"A role for chromatin remodeling in regulation of CUC gene expression
in the Arabidopsis cotyledon boundary.";
Development 133:3223-3230(2006).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Landsberg erecta;
PubMed=17293567; DOI=10.1105/tpc.106.048272;
Bezhani S., Winter C., Hershman S., Wagner J.D., Kennedy J.F.,
Kwon C.S., Pfluger J., Su Y., Wagner D.;
"Unique, shared, and redundant roles for the Arabidopsis SWI/SNF
chromatin remodeling ATPases BRAHMA and SPLAYED.";
Plant Cell 19:403-416(2007).
[9]
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[10]
INTERACTION WITH BARD1/ROW1.
PubMed=18591352; DOI=10.1105/tpc.108.058867;
Han P., Li Q., Zhu Y.-X.;
"Mutation of Arabidopsis BARD1 causes meristem defects by failing to
confine WUSCHEL expression to the organizing center.";
Plant Cell 20:1482-1493(2008).
[11]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY WOUNDING.
STRAIN=cv. Landsberg erecta;
PubMed=19079584; DOI=10.1371/journal.ppat.1000237;
Walley J.W., Rowe H.C., Xiao Y., Chehab E.W., Kliebenstein D.J.,
Wagner D., Dehesh K.;
"The chromatin remodeler SPLAYED regulates specific stress signaling
pathways.";
PLoS Pathog. 4:E1000237-E1000237(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[13]
FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH LFY.
PubMed=22323601; DOI=10.1073/pnas.1113409109;
Wu M.F., Sang Y., Bezhani S., Yamaguchi N., Han S.K., Li Z., Su Y.,
Slewinski T.L., Wagner D.;
"SWI2/SNF2 chromatin remodeling ATPases overcome polycomb repression
and control floral organ identity with the LEAFY and SEPALLATA3
transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 109:3576-3581(2012).
[14]
GENE FAMILY.
PubMed=24265739; DOI=10.1371/journal.pone.0078982;
Xu R., Zhang S., Huang J., Zheng C.;
"Genome-wide comparative in silico analysis of the RNA helicase gene
family in Zea mays and Glycine max: a comparison with Arabidopsis and
Oryza sativa.";
PLoS ONE 8:E78982-E78982(2013).
-!- FUNCTION: Catalytic component of the chromatin structure-
remodeling complex (RSC), which is involved in transcription
regulation and nucleosome positioning. Controls stem cell fate via
the transcription regulation of WUS in the shoot apical meristem,
by modulating its promoter. LFY-dependent repressor of the
meristem identity switch from vegetative to reproductive
development probably by modulating chromatin state. Involved in
the regulation of floral homeotic gene expression in response to
environmental stimuli. Required for carpel and ovule development,
and for cotyledon separation via the regulation of CUC2
transcription. Regulates the promoters of several genes downstream
of the jasmonate (JA) and ethylene (ET) signaling pathways.
Required for resistance against the necrotrophic pathogen
B.cinerea but not the biotrophic pathogen P.syringae.
{ECO:0000269|PubMed:11818058, ECO:0000269|PubMed:15833920,
ECO:0000269|PubMed:16640604, ECO:0000269|PubMed:16854978,
ECO:0000269|PubMed:17293567, ECO:0000269|PubMed:19079584,
ECO:0000269|PubMed:22323601}.
-!- SUBUNIT: Interacts with LFY (PubMed:22323601). Binds to BARD1/ROW1
(PubMed:18591352). {ECO:0000269|PubMed:18591352,
ECO:0000269|PubMed:22323601}.
-!- INTERACTION:
Q00958:LFY; NbExp=4; IntAct=EBI-15967899, EBI-1644366;
O22456:SEP3; NbExp=2; IntAct=EBI-15967899, EBI-592020;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=F4IHS2-1; Sequence=Displayed;
Name=2;
IsoId=F4IHS2-2; Sequence=VSP_046250;
Name=3;
IsoId=F4IHS2-3; Sequence=VSP_046249;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Mostly expressed in rapidly dividing cells in
the vegetative, inflorescence, and root meristems, as well as in
young leaf and flower primordia. Isoform 1 is predominantly found
in seedlings whereas isoform 2 is present in both seedlings and
inflorescences (at protein level). {ECO:0000269|PubMed:11818058,
ECO:0000269|PubMed:16640604}.
-!- INDUCTION: By wounding. {ECO:0000269|PubMed:19079584}.
-!- PTM: Phosphorylated.
-!- DISRUPTION PHENOTYPE: Precocious transition from inflorescence to
flower formation and impaired maintenance of the shoot apical
meristem (SAM) during the reproductive phase. Abnormal flowers
with splayed open first-whorl sepals due to outward bending of the
pointy sepal tips. Reduced male fertility and reduced anther
dehiscence. Partially unfused at the tip fourth-whorl carpels,
with stigmatic tissue missing or placed internal to the carpel
tip, leading to funnel shaped carpels. Female sterility ovule
growth arrest at megagametogenesis. Fused cotyledons. Impaired
expression of PDF1.2a, leading to reduced ethylene (ET) and
jasmonic acid (JA) signaling. Reduced resistance toward B.
cinerea. {ECO:0000269|PubMed:11818058,
ECO:0000269|PubMed:15833920, ECO:0000269|PubMed:16854978,
ECO:0000269|PubMed:17293567, ECO:0000269|PubMed:19079584,
ECO:0000269|PubMed:22323601}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD29835.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAM66026.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF247809; AAK31908.1; -; mRNA.
EMBL; AY927849; AAX22009.1; -; mRNA.
EMBL; AC006202; AAD29835.2; ALT_SEQ; Genomic_DNA.
EMBL; CP002685; AEC08099.1; -; Genomic_DNA.
EMBL; CP002685; AEC08100.1; -; Genomic_DNA.
EMBL; CP002685; AEC08101.1; -; Genomic_DNA.
EMBL; CP002685; ANM63245.1; -; Genomic_DNA.
EMBL; AY088490; AAM66026.1; ALT_INIT; mRNA.
PIR; A84683; A84683.
RefSeq; NP_001077971.1; NM_001084502.2. [F4IHS2-2]
RefSeq; NP_001325347.1; NM_001336158.1. [F4IHS2-2]
RefSeq; NP_850116.1; NM_179785.3. [F4IHS2-1]
RefSeq; NP_850117.1; NM_179786.2. [F4IHS2-3]
UniGene; At.22414; -.
ProteinModelPortal; F4IHS2; -.
SMR; F4IHS2; -.
BioGrid; 2725; 33.
DIP; DIP-60019N; -.
IntAct; F4IHS2; 2.
STRING; 3702.AT2G28290.1; -.
iPTMnet; F4IHS2; -.
PaxDb; F4IHS2; -.
PRIDE; F4IHS2; -.
EnsemblPlants; AT2G28290.1; AT2G28290.1; AT2G28290. [F4IHS2-1]
EnsemblPlants; AT2G28290.2; AT2G28290.2; AT2G28290. [F4IHS2-3]
EnsemblPlants; AT2G28290.3; AT2G28290.3; AT2G28290. [F4IHS2-2]
EnsemblPlants; AT2G28290.4; AT2G28290.4; AT2G28290. [F4IHS2-2]
GeneID; 817375; -.
Gramene; AT2G28290.1; AT2G28290.1; AT2G28290. [F4IHS2-1]
Gramene; AT2G28290.2; AT2G28290.2; AT2G28290. [F4IHS2-3]
Gramene; AT2G28290.3; AT2G28290.3; AT2G28290. [F4IHS2-2]
Gramene; AT2G28290.4; AT2G28290.4; AT2G28290. [F4IHS2-2]
KEGG; ath:AT2G28290; -.
Araport; AT2G28290; -.
TAIR; locus:2062840; AT2G28290.
eggNOG; KOG0386; Eukaryota.
eggNOG; KOG1181; Eukaryota.
eggNOG; COG0553; LUCA.
HOGENOM; HOG000176878; -.
InParanoid; F4IHS2; -.
OMA; NTFQEAF; -.
OrthoDB; EOG0936002W; -.
PRO; PR:F4IHS2; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; F4IHS2; baseline and differential.
Genevisible; F4IHS2; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:TAIR.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0042393; F:histone binding; IEA:InterPro.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; NAS:TAIR.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009908; P:flower development; IMP:TAIR.
GO; GO:0010199; P:organ boundary specification between lateral organs and the meristem; IGI:TAIR.
GO; GO:1900150; P:regulation of defense response to fungus; IMP:UniProtKB.
GO; GO:0010104; P:regulation of ethylene-activated signaling pathway; IMP:UniProtKB.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:TAIR.
GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0009611; P:response to wounding; IEP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00079; HELICc; 1.
Gene3D; 3.40.50.10810; -; 1.
InterPro; IPR014978; Gln-Leu-Gln_QLQ.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014012; HSA_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR029295; SnAC.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF14619; SnAC; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00951; QLQ; 1.
SMART; SM01314; SnAC; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51204; HSA; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
DNA-binding; Ethylene signaling pathway; Helicase; Hydrolase;
Jasmonic acid signaling pathway; Nucleotide-binding; Nucleus;
Phosphoprotein; Plant defense; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 3574 Chromatin structure-remodeling complex
protein SYD.
/FTId=PRO_0000421936.
DOMAIN 573 647 HSA. {ECO:0000255|PROSITE-
ProRule:PRU00549}.
DOMAIN 766 933 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1077 1223 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 779 786 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 884 887 DEAH box.
MOTIF 1266 1273 Nuclear localization signal.
{ECO:0000250}.
VAR_SEQ 3339 3383 Missing (in isoform 3).
{ECO:0000303|Ref.5}.
/FTId=VSP_046249.
VAR_SEQ 3339 3369 Missing (in isoform 2).
{ECO:0000303|PubMed:16640604}.
/FTId=VSP_046250.
MUTAGEN 1153 1153 G->E: In syd-1; precocious transition
from inflorescence to flower formation,
abnormal flowers exhibiting variable
petals and stamens number and position as
well as some mosaic organs (stamenoid
petals). {ECO:0000269|PubMed:11818058}.
CONFLICT 757 757 Y -> E (in Ref. 1; AAK31908 and 2;
AAX22009). {ECO:0000305}.
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


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