DIM5_NEUCR
ID DIM5_NEUCR Reviewed; 331 AA.
AC Q8X225; Q1K5Y7;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5;
DE EC=2.1.1.355 {ECO:0000269|PubMed:12372305, ECO:0000269|PubMed:12679815, ECO:0000269|PubMed:12887903};
DE AltName: Full=Histone H3-K9 methyltransferase dim-5;
DE Short=H3-K9-HMTase dim-5;
DE Short=HKMT;
GN Name=dim-5; ORFNames=29E8.110, NCU04402;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 18889 / 74-OR8-1a / 40-21 / DSM 1258 / FGSC 988;
RX PubMed=11713521; DOI=10.1038/35104508;
RA Tamaru H., Selker E.U.;
RT "A histone H3 methyltransferase controls DNA methylation in Neurospora
RT crassa.";
RL Nature 414:277-283(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND METHYLATION OF HISTONE H3.
RX PubMed=12679815; DOI=10.1038/ng1143;
RA Tamaru H., Zhang X., McMillen D., Singh P.B., Nakayama J., Grewal S.I.,
RA Allis C.D., Cheng X., Selker E.U.;
RT "Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in
RT Neurospora crassa.";
RL Nat. Genet. 34:75-79(2003).
RN [5]
RP SUBSTRATE SPECIFICITY, AND MUTAGENESIS OF PHE-281.
RX PubMed=15590646; DOI=10.1074/jbc.m410483200;
RA Collins R.E., Tachibana M., Tamaru H., Smith K.M., Jia D., Zhang X.,
RA Selker E.U., Shinkai Y., Cheng X.;
RT "In vitro and in vivo analyses of a Phe/Tyr switch controlling product
RT specificity of histone lysine methyltransferases.";
RL J. Biol. Chem. 280:5563-5570(2005).
RN [6]
RP SUBSTRATE SPECIFICITY.
RX PubMed=18215768; DOI=10.1016/j.chembiol.2007.11.013;
RA Rathert P., Zhang X., Freund C., Cheng X., Jeltsch A.;
RT "Analysis of the substrate specificity of the Dim-5 histone lysine
RT methyltransferase using peptide arrays.";
RL Chem. Biol. 15:5-11(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-331 IN COMPLEX WITH ZINC IONS,
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-251; ASN-254; HIS-255
RP AND TYR-296.
RX PubMed=12372305; DOI=10.1016/s0092-8674(02)00999-6;
RA Zhang X., Tamaru H., Khan S.I., Horton J.R., Keefe L.J., Selker E.U.,
RA Cheng X.;
RT "Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine
RT methyltransferase.";
RL Cell 111:117-127(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 30-331 IN COMPLEX WITH HISTONE
RP H3; S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY,
RP AND MUTAGENESIS OF TYR-191; ASP-222; PHE-294; LEU-330 AND TRP-331.
RX PubMed=12887903; DOI=10.1016/s1097-2765(03)00224-7;
RA Zhang X., Yang Z., Khan S.I., Horton J.R., Tamaru H., Selker E.U.,
RA Cheng X.;
RT "Structural basis for the product specificity of histone lysine
RT methyltransferases.";
RL Mol. Cell 12:177-185(2003).
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC histone H3 to form H3K9me3. H3K9me3 marks chromatin regions for DNA
CC methylation (PubMed:11713521, PubMed:12372305, PubMed:12679815,
CC PubMed:12887903). Dim-5 recognizes Arg-8 to Gly-12 of the H3 tail with
CC Thr-11 and Gly-12 being the most important specificity determinants,
CC the recognition of whcih is important to distinguish H3K9 from H3K27
CC and H4K20 (PubMed:18215768). {ECO:0000269|PubMed:11713521,
CC ECO:0000269|PubMed:12372305, ECO:0000269|PubMed:12679815,
CC ECO:0000269|PubMed:12887903, ECO:0000269|PubMed:18215768}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA-
CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355;
CC Evidence={ECO:0000269|PubMed:12372305, ECO:0000269|PubMed:12679815,
CC ECO:0000269|PubMed:12887903};
CC -!- INTERACTION:
CC Q8X225; P07041: hh3; NbExp=2; IntAct=EBI-1268994, EBI-1270655;
CC Q8X225; Q96UA9: 9G6.050; Xeno; NbExp=2; IntAct=EBI-1268994, EBI-15849296;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
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.
CC {ECO:0000269|PubMed:12372305}.
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:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL35215.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAF06044.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF419248; AAL35215.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX908809; CAF06044.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002239; EAA28243.2; -; Genomic_DNA.
DR RefSeq; XP_957479.2; XM_952386.3.
DR PDB; 1ML9; X-ray; 1.98 A; A=30-331.
DR PDB; 1PEG; X-ray; 2.59 A; A/B=30-331.
DR PDBsum; 1ML9; -.
DR PDBsum; 1PEG; -.
DR AlphaFoldDB; Q8X225; -.
DR SMR; Q8X225; -.
DR DIP; DIP-39600N; -.
DR IntAct; Q8X225; 2.
DR STRING; 5141.EFNCRP00000005137; -.
DR BindingDB; Q8X225; -.
DR ChEMBL; CHEMBL3309062; -.
DR PRIDE; Q8X225; -.
DR EnsemblFungi; EAA28243; EAA28243; NCU04402.
DR GeneID; 3873656; -.
DR KEGG; ncr:NCU04402; -.
DR VEuPathDB; FungiDB:NCU04402; -.
DR HOGENOM; CLU_020840_11_0_1; -.
DR InParanoid; Q8X225; -.
DR OMA; DKFTDPD; -.
DR EvolutionaryTrace; Q8X225; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0005694; C:chromosome; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0016571; P:histone methylation; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR007728; Pre-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc.
FT CHAIN 1..331
FT /note="Histone-lysine N-methyltransferase, H3 lysine-9
FT specific dim-5"
FT /id="PRO_0000186062"
FT DOMAIN 77..159
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 162..297
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 315..331
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12372305,
FT ECO:0000269|PubMed:12887903, ECO:0007744|PDB:1ML9,
FT ECO:0007744|PDB:1PEG"
FT BINDING 172..174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT BINDING 251
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT BINDING 254..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:12887903,
FT ECO:0007744|PDB:1PEG"
FT SITE 209
FT /note="Interacts with H3S10"
FT /evidence="ECO:0000269|PubMed:18215768"
FT SITE 227
FT /note="Interacts with H3R8"
FT /evidence="ECO:0000269|PubMed:18215768"
FT MUTAGEN 191
FT /note="Y->F: Reduces enzyme activity by 97%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT MUTAGEN 191
FT /note="Y->V: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT MUTAGEN 222
FT /note="D->E: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT MUTAGEN 222
FT /note="D->K: Reduces enzyme activity by 97%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT MUTAGEN 222
FT /note="D->Q: Reduces enzyme activity by 97%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT MUTAGEN 251
FT /note="R->H: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:12372305"
FT MUTAGEN 254
FT /note="N->Q: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:12372305"
FT MUTAGEN 255
FT /note="H->K: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:12372305"
FT MUTAGEN 281
FT /note="F->Y: Converts the product-specificity of the HKMT
FT from H3K9me3 to H3K9me1/2."
FT /evidence="ECO:0000269|PubMed:15590646"
FT MUTAGEN 294
FT /note="F->W: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT MUTAGEN 294
FT /note="F->Y: Reduces enzyme activity by 20%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT MUTAGEN 296
FT /note="Y->F: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:12372305"
FT MUTAGEN 330
FT /note="L->A: Reduces enzyme activity by over 99%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT MUTAGEN 331
FT /note="W->A: Reduces enzyme activity by 97%."
FT /evidence="ECO:0000269|PubMed:12887903"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1PEG"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1PEG"
FT TURN 122..125
FT /evidence="ECO:0007829|PDB:1PEG"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:1ML9"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:1ML9"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:1ML9"
SQ SEQUENCE 331 AA; 37572 MW; 2C97AB4B5E582D88 CRC64;
MEKAFRPHFF NHGKPDANPK EKKNCHWCQI RSFATHAQLP ISIVNREDDA FLNPNFRFID
HSIIGKNVPV ADQSFRVGCS CASDEECMYS TCQCLDEMAP DSDEEADPYT RKKRFAYYSQ
GAKKGLLRDR VLQSQEPIYE CHQGCACSKD CPNRVVERGR TVPLQIFRTK DRGWGVKCPV
NIKRGQFVDR YLGEIITSEE ADRRRAESTI ARRKDVYLFA LDKFSDPDSL DPLLAGQPLE
VDGEYMSGPT RFINHSCDPN MAIFARVGDH ADKHIHDLAL FAIKDIPKGT ELTFDYVNGL
TGLESDAHDP SKISEMTKCL CGTAKCRGYL W
