SUVH4_ARATH
ID SUVH4_ARATH Reviewed; 624 AA.
AC Q8GZB6; Q9C5P3; Q9FFX9;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4;
DE EC=2.1.1.- {ECO:0000305|PubMed:15457214, ECO:0000305|PubMed:15598823};
DE EC=2.1.1.367 {ECO:0000305|PubMed:15457214, ECO:0000305|PubMed:15598823};
DE AltName: Full=Histone H3-K9 methyltransferase 4;
DE Short=H3-K9-HMTase 4;
DE AltName: Full=Protein KRYPTONITE;
DE AltName: Full=Protein SET DOMAIN GROUP 33;
DE AltName: Full=Suppressor of variegation 3-9 homolog protein 4;
DE Short=Su(var)3-9 homolog protein 4;
GN Name=SUVH4; Synonyms=KYP, SDG33, SET33; OrderedLocusNames=At5g13960;
GN ORFNames=MAC12.7;
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], NOMENCLATURE, AND TISSUE SPECIFICITY.
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 [GENOMIC DNA].
RC STRAIN=cv. Wassilewskija;
RX PubMed=12486005; DOI=10.1093/emboj/cdf687;
RA Malagnac F., Bartee L., Bender J.;
RT "An Arabidopsis SET domain protein required for maintenance but not
RT establishment of DNA methylation.";
RL EMBO J. 21:6842-6852(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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].
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 [6]
RP FUNCTION, AND MUTANTS KYP-1; KYP-2 AND KYP-3.
RX PubMed=11898023; DOI=10.1038/nature731;
RA Jackson J.P., Lindroth A.M., Cao X., Jacobsen S.E.;
RT "Control of CpNpG DNA methylation by the KRYPTONITE histone H3
RT methyltransferase.";
RL Nature 416:556-560(2002).
RN [7]
RP EPIGENETIC METHYLATION.
RX PubMed=12194816; DOI=10.1016/s0960-9822(02)00976-4;
RA Johnson L.M., Cao X., Jacobsen S.E.;
RT "Interplay between two epigenetic marks: DNA methylation and histone H3
RT lysine 9 methylation.";
RL Curr. Biol. 12:1360-1367(2002).
RN [8]
RP FUNCTION.
RX PubMed=15457214; DOI=10.1038/sj.emboj.7600430;
RA Lindroth A.M., Shultis D., Jasencakova Z., Fuchs J., Johnson L.,
RA Schubert D., Patnaik D., Pradhan S., Goodrich J., Schubert I., Jenuwein T.,
RA Khorasanizadeh S., Jacobsen S.E.;
RT "Dual histone H3 methylation marks at lysines 9 and 27 required for
RT interaction with CHROMOMETHYLASE3.";
RL EMBO J. 23:4286-4296(2004).
RN [9]
RP FUNCTION.
RX PubMed=15598823; DOI=10.1093/nar/gkh992;
RA Johnson L., Mollah S., Garcia B.A., Muratore T.L., Shabanowitz J.,
RA Hunt D.F., Jacobsen S.E.;
RT "Mass spectrometry analysis of Arabidopsis histone H3 reveals distinct
RT combinations of post-translational modifications.";
RL Nucleic Acids Res. 32:6511-6518(2004).
RN [10]
RP FUNCTION.
RX PubMed=16277745; DOI=10.1186/gb-2005-6-11-r90;
RA Tran R.K., Zilberman D., de Bustos C., Ditt R.F., Henikoff J.G.,
RA Lindroth A.M., Delrow J., Boyle T., Kwong S., Bryson T.D., Jacobsen S.E.,
RA Henikoff S.;
RT "Chromatin and siRNA pathways cooperate to maintain DNA methylation of
RT small transposable elements in Arabidopsis.";
RL Genome Biol. 6:R90.1-R90.11(2005).
RN [11]
RP FUNCTION.
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 [12]
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. The silencing mechanism via DNA CpNpG
CC methylation requires the targeting of chromomethylase CMT3 to
CC methylated histones, probably through an interaction with an HP1-like
CC adapter. By its function, KYP is directly required for the maintenance
CC of the DNA CpNpG and asymmetric methylation. Involved in the silencing
CC of transposable elements. {ECO:0000269|PubMed:11898023,
CC ECO:0000269|PubMed:15457214, ECO:0000269|PubMed:15598823,
CC ECO:0000269|PubMed:16277745, 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:15457214, ECO:0000305|PubMed:15598823};
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:15457214, ECO:0000305|PubMed:15598823};
CC -!- SUBUNIT: Interacts with H3 histone.
CC -!- INTERACTION:
CC Q8GZB6; P03562: AL2; Xeno; NbExp=4; IntAct=EBI-16175525, EBI-16175508;
CC Q8GZB6; Q96703: AL2; Xeno; NbExp=2; IntAct=EBI-16175525, EBI-16175606;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC Note=Associates with centromeric constitutive heterochromatin and at a
CC lower level with regions of euchromatin.
CC -!- TISSUE SPECIFICITY: Expressed in leaves stems and flowers.
CC {ECO:0000269|PubMed:11691919}.
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 -!- MISCELLANEOUS: Mutations in the KYP/SUVH4 gene decrease the level of
CC histone H3-K9 dimethylated, trimethylated or dimethylated in
CC association with H3-K14Ac by factors of 4,3 and 3, respectively. The
CC level of monomethylated H3-K9 is unchanged. Such mutations lead to a
CC drastic decrease of cytosine methylation at CpNpG sites, causing the
CC reactivation of endogenous retrotransposons. The KRYPTONYTE
CC methyltransferase name was given according to its involvement in
CC SUPERMAN gene silencing.
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}.
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DR EMBL; AF344447; AAK28969.1; -; mRNA.
DR EMBL; AF538715; AAO17392.1; -; Genomic_DNA.
DR EMBL; AB005230; BAB11124.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91966.1; -; Genomic_DNA.
DR EMBL; BT002313; AAN86146.1; -; mRNA.
DR RefSeq; NP_196900.1; NM_121399.3.
DR PDB; 4QEN; X-ray; 2.00 A; A=93-624.
DR PDB; 4QEO; X-ray; 2.00 A; A=93-624.
DR PDB; 4QEP; X-ray; 3.10 A; A=93-624.
DR PDBsum; 4QEN; -.
DR PDBsum; 4QEO; -.
DR PDBsum; 4QEP; -.
DR AlphaFoldDB; Q8GZB6; -.
DR SMR; Q8GZB6; -.
DR BioGRID; 16522; 1.
DR DIP; DIP-62058N; -.
DR IntAct; Q8GZB6; 3.
DR STRING; 3702.AT5G13960.1; -.
DR iPTMnet; Q8GZB6; -.
DR PaxDb; Q8GZB6; -.
DR PRIDE; Q8GZB6; -.
DR ProteomicsDB; 226520; -.
DR EnsemblPlants; AT5G13960.1; AT5G13960.1; AT5G13960.
DR GeneID; 831244; -.
DR Gramene; AT5G13960.1; AT5G13960.1; AT5G13960.
DR KEGG; ath:AT5G13960; -.
DR Araport; AT5G13960; -.
DR TAIR; locus:2159133; AT5G13960.
DR eggNOG; KOG1082; Eukaryota.
DR HOGENOM; CLU_004556_3_1_1; -.
DR InParanoid; Q8GZB6; -.
DR OrthoDB; 265171at2759; -.
DR PhylomeDB; Q8GZB6; -.
DR PRO; PR:Q8GZB6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GZB6; baseline and differential.
DR Genevisible; Q8GZB6; 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:0010385; F:double-stranded methylated DNA binding; IDA:TAIR.
DR GO; GO:0042054; F:histone methyltransferase activity; IBA:GO_Central.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:TAIR.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051567; P:histone H3-K9 methylation; IMP:TAIR.
DR GO; GO:0016571; P:histone methylation; IDA:TAIR.
DR GO; GO:0010216; P:maintenance of DNA methylation; IDA:TAIR.
DR GO; GO:0018022; P:peptidyl-lysine 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; 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..624
FT /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT specific SUVH4"
FT /id="PRO_0000186075"
FT DOMAIN 149..302
FT /note="YDG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00358"
FT DOMAIN 381..443
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 446..594
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 608..624
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 429
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 456..458
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 548
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 551..552
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 612
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 614
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT CONFLICT 189
FT /note="E -> D (in Ref. 2; AAO17392)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="R -> T (in Ref. 1; AAK28969)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="V -> A (in Ref. 1; AAK28969)"
FT /evidence="ECO:0000305"
FT HELIX 101..121
FT /evidence="ECO:0007829|PDB:4QEO"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4QEO"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4QEN"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:4QEO"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:4QEO"
FT TURN 187..192
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:4QEN"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4QEP"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 271..288
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 292..302
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:4QEN"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:4QEO"
FT TURN 358..361
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:4QEO"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:4QEO"
FT HELIX 396..400
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:4QEP"
FT HELIX 436..441
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 471..474
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:4QEO"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 541..544
FT /evidence="ECO:0007829|PDB:4QEO"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 557..567
FT /evidence="ECO:0007829|PDB:4QEO"
FT HELIX 570..572
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 574..581
FT /evidence="ECO:0007829|PDB:4QEO"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:4QEO"
SQ SEQUENCE 624 AA; 70056 MW; 67B5CF6606F16B07 CRC64;
MAGKRKRANA PDQTERRSSV RVQKVRQKAL DEKARLVQER VKLLSDRKSE ICVDDTELHE
KEEENVDGSP KRRSPPKLTA MQKGKQKLSV SLNGKDVNLE PHLKVTKCLR LFNKQYLLCV
QAKLSRPDLK GVTEMIKAKA ILYPRKIIGD LPGIDVGHRF FSRAEMCAVG FHNHWLNGID
YMSMEYEKEY SNYKLPLAVS IVMSGQYEDD LDNADTVTYT GQGGHNLTGN KRQIKDQLLE
RGNLALKHCC EYNVPVRVTR GHNCKSSYTK RVYTYDGLYK VEKFWAQKGV SGFTVYKYRL
KRLEGQPELT TDQVNFVAGR IPTSTSEIEG LVCEDISGGL EFKGIPATNR VDDSPVSPTS
GFTYIKSLII EPNVIIPKSS TGCNCRGSCT DSKKCACAKL NGGNFPYVDL NDGRLIESRD
VVFECGPHCG CGPKCVNRTS QKRLRFNLEV FRSAKKGWAV RSWEYIPAGS PVCEYIGVVR
RTADVDTISD NEYIFEIDCQ QTMQGLGGRQ RRLRDVAVPM NNGVSQSSED ENAPEFCIDA
GSTGNFARFI NHSCEPNLFV QCVLSSHQDI RLARVVLFAA DNISPMQELT YDYGYALDSV
HGPDGKVKQL ACYCGALNCR KRLY
