SUVH6_ARATH
ID SUVH6_ARATH Reviewed; 790 AA.
AC Q8VZ17; Q9C5P2; Q9ZQ40;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH6;
DE EC=2.1.1.- {ECO:0000305|PubMed:15014946, ECO:0000305|PubMed:16287862};
DE EC=2.1.1.367 {ECO:0000305|PubMed:15014946, ECO:0000305|PubMed:16287862};
DE AltName: Full=Histone H3-K9 methyltransferase 6;
DE Short=H3-K9-HMTase 6;
DE AltName: Full=Protein SET DOMAIN GROUP 23;
DE AltName: Full=Suppressor of variegation 3-9 homolog protein 6;
DE Short=Su(var)3-9 homolog protein 6;
GN Name=SUVH6; Synonyms=SDG23, SET23; OrderedLocusNames=At2g22740;
GN ORFNames=T9I22.18;
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 [GENOMIC DNA], AND NOMENCLATURE.
RX PubMed=11691919; DOI=10.1093/nar/29.21.4319;
RA Baumbusch L.O., Thorstensen T., Krauss V., Fischer A., Naumann K.,
RA Assalkhou R., Schulz I., Reuter G., Aalen R.B.;
RT "The Arabidopsis thaliana genome contains at least 29 active genes encoding
RT SET domain proteins that can be assigned to four evolutionarily conserved
RT classes.";
RL Nucleic Acids Res. 29:4319-4333(2001).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15014946; DOI=10.1007/s00412-004-0275-7;
RA Jackson J.P., Johnson L., Jasencakova Z., Zhang X., PerezBurgos L.,
RA Singh P.B., Cheng X., Schubert I., Jenuwein T., Jacobsen S.E.;
RT "Dimethylation of histone H3 lysine 9 is a critical mark for DNA
RT methylation and gene silencing in Arabidopsis thaliana.";
RL Chromosoma 112:308-315(2004).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16287862; DOI=10.1128/mcb.25.23.10507-10515.2005;
RA Ebbs M.L., Bartee L., Bender J.;
RT "H3 lysine 9 methylation is maintained on a transcribed inverted repeat by
RT combined action of SUVH6 and SUVH4 methyltransferases.";
RL Mol. Cell. Biol. 25:10507-10515(2005).
RN [7]
RP GENE FAMILY.
RX PubMed=16384625; DOI=10.1016/j.jplph.2005.10.015;
RA Fischer A., Hofmann I., Naumann K., Reuter G.;
RT "Heterochromatin proteins and the control of heterochromatic gene silencing
RT in Arabidopsis.";
RL J. Plant Physiol. 163:358-368(2006).
CC -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-9' of histone H3.
CC H3 'Lys-9' methylation represents a specific tag for epigenetic
CC transcriptional repression. Seems to act preferentially on dsMRNA.
CC {ECO:0000269|PubMed:15014946, ECO:0000269|PubMed:16287862}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000305|PubMed:15014946, ECO:0000305|PubMed:16287862};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC Evidence={ECO:0000305|PubMed:15014946, ECO:0000305|PubMed:16287862};
CC -!- INTERACTION:
CC Q8VZ17; C0SUW7: ARID6; NbExp=3; IntAct=EBI-15193239, EBI-15192335;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358}.
CC Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric
CC constitutive heterochromatin. {ECO:0000250}.
CC -!- DOMAIN: Although the SET domain contains the active site of enzymatic
CC activity, both pre-SET and post-SET domains are required for
CC methyltransferase activity.
CC -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that are
CC arranged in a triangular cluster; some of these Cys residues contribute
CC to the binding of two zinc ions within the cluster. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. Suvar3-9
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00908}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15582.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF344449; AAK28971.1; -; Genomic_DNA.
DR EMBL; AC006340; AAD15582.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC07347.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07348.1; -; Genomic_DNA.
DR EMBL; AY065374; AAL38815.1; -; mRNA.
DR EMBL; BT002751; AAO22580.1; -; mRNA.
DR PIR; C84616; C84616.
DR RefSeq; NP_850030.1; NM_179699.3.
DR RefSeq; NP_973514.1; NM_201785.1.
DR PDB; 6A5K; X-ray; 1.90 A; A=264-790.
DR PDB; 6A5M; X-ray; 2.30 A; A=264-790.
DR PDB; 6A5N; X-ray; 2.40 A; A=264-790.
DR PDBsum; 6A5K; -.
DR PDBsum; 6A5M; -.
DR PDBsum; 6A5N; -.
DR AlphaFoldDB; Q8VZ17; -.
DR SMR; Q8VZ17; -.
DR BioGRID; 2157; 2.
DR DIP; DIP-62061N; -.
DR IntAct; Q8VZ17; 4.
DR STRING; 3702.AT2G22740.1; -.
DR PaxDb; Q8VZ17; -.
DR PRIDE; Q8VZ17; -.
DR ProteomicsDB; 226522; -.
DR EnsemblPlants; AT2G22740.1; AT2G22740.1; AT2G22740.
DR EnsemblPlants; AT2G22740.2; AT2G22740.2; AT2G22740.
DR GeneID; 816804; -.
DR Gramene; AT2G22740.1; AT2G22740.1; AT2G22740.
DR Gramene; AT2G22740.2; AT2G22740.2; AT2G22740.
DR KEGG; ath:AT2G22740; -.
DR Araport; AT2G22740; -.
DR TAIR; locus:2065988; AT2G22740.
DR eggNOG; KOG1082; Eukaryota.
DR HOGENOM; CLU_004556_0_0_1; -.
DR InParanoid; Q8VZ17; -.
DR OMA; HQNTSCQ; -.
DR OrthoDB; 75825at2759; -.
DR PhylomeDB; Q8VZ17; -.
DR PRO; PR:Q8VZ17; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VZ17; baseline and differential.
DR Genevisible; Q8VZ17; AT.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0042054; F:histone methyltransferase activity; IBA:GO_Central.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:TAIR.
DR GO; GO:0010428; F:methyl-CpNpG binding; IDA:TAIR.
DR GO; GO:0010429; F:methyl-CpNpN binding; IDA:TAIR.
DR GO; GO:0008168; F:methyltransferase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0016571; P:histone methylation; IDA:TAIR.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 2.30.280.10; -; 1.
DR InterPro; IPR025794; H3-K9-MeTrfase_plant.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00466; SRA; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS51575; SAM_MT43_SUVAR39_2; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS51015; YDG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromatin regulator; Chromosome; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Zinc.
FT CHAIN 1..790
FT /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT specific SUVH6"
FT /id="PRO_0000186077"
FT DOMAIN 330..482
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT DOMAIN 551..613
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 616..760
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 774..790
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 251..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 553
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 559
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 601
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 605
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 626..628
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 662
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 664
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 714
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 717..718
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 720
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 778
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 780
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 785
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT CONFLICT 386
FT /note="N -> D (in Ref. 4; AAL38815)"
FT /evidence="ECO:0000305"
FT HELIX 268..292
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:6A5M"
FT TURN 301..304
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 359..365
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 368..376
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:6A5N"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:6A5M"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 453..468
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 474..482
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:6A5K"
FT TURN 510..513
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 514..517
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:6A5M"
FT HELIX 568..572
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 590..593
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 618..622
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 624..626
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 628..634
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 647..651
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 652..657
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 658..660
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 665..669
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 675..683
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 699..705
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 707..710
FT /evidence="ECO:0007829|PDB:6A5K"
FT HELIX 712..715
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 723..732
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 740..747
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 754..757
FT /evidence="ECO:0007829|PDB:6A5K"
FT STRAND 763..767
FT /evidence="ECO:0007829|PDB:6A5N"
FT STRAND 769..773
FT /evidence="ECO:0007829|PDB:6A5M"
FT STRAND 787..790
FT /evidence="ECO:0007829|PDB:6A5K"
SQ SEQUENCE 790 AA; 87477 MW; AEA7AC629AD23E6B CRC64;
MEMGVMENLM VHTEISKVKS QSNGEVEKRG VSVLENGGVC KLDRMSGLKF KRRKVFAVRD
FPPGCGSRAM EVKIACENGN VVEDVKVVES LVKEEESLGQ RDASENVSDI RMAEPVEVQP
LRICLPGGDV VRDLSVTAGD ECSNSEQIVA GSGVSSSSGT ENIVRDIVVY ADESSLGMDN
LDQTQPLEIE MSDVAVAKPR LVAGRKKAKK GIACHSSLKV VSREFGEGSR KKKSKKNLYW
RDRESLDSPE QLRILGVGTS SGSSSGDSSR NKVKETLRLF HGVCRKILQE DEAKPEDQRR
KGKGLRIDFE ASTILKRNGK FLNSGVHILG EVPGVEVGDE FQYRMELNIL GIHKPSQAGI
DYMKYGKAKV ATSIVASGGY DDHLDNSDVL TYTGQGGNVM QVKKKGEELK EPEDQKLITG
NLALATSIEK QTPVRVIRGK HKSTHDKSKG GNYVYDGLYL VEKYWQQVGS HGMNVFKFQL
RRIPGQPELS WVEVKKSKSK YREGLCKLDI SEGKEQSPIS AVNEIDDEKP PLFTYTVKLI
YPDWCRPVPP KSCCCTTRCT EAEARVCACV EKNGGEIPYN FDGAIVGAKP TIYECGPLCK
CPSSCYLRVT QHGIKLPLEI FKTKSRGWGV RCLKSIPIGS FICEYVGELL EDSEAERRIG
NDEYLFDIGN RYDNSLAQGM SELMLGTQAG RSMAEGDESS GFTIDAASKG NVGRFINHSC
SPNLYAQNVL YDHEDSRIPH VMFFAQDNIP PLQELCYDYN YALDQVRDSK GNIKQKPCFC
GAAVCRRRLY
