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Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)

 DIM5_NEUCR              Reviewed;         331 AA.
Q8X225; Q1K5Y7;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 2.
08-MAY-2019, entry version 112.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5;
EC=2.1.1.43;
AltName: Full=Histone H3-K9 methyltransferase dim-5;
Short=H3-K9-HMTase dim-5;
Short=HKMT;
Name=dim-5; ORFNames=29E8.110, NCU04402;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=ATCC 18889 / 74-OR8-1a / 40-21 / DSM 1258 / FGSC 988;
PubMed=11713521; DOI=10.1038/35104508;
Tamaru H., Selker E.U.;
"A histone H3 methyltransferase controls DNA methylation in Neurospora
crassa.";
Nature 414:277-283(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[4]
FUNCTION, AND METHYLATION OF HISTONE H3.
PubMed=12679815; DOI=10.1038/ng1143;
Tamaru H., Zhang X., McMillen D., Singh P.B., Nakayama J.,
Grewal S.I., Allis C.D., Cheng X., Selker E.U.;
"Trimethylated lysine 9 of histone H3 is a mark for DNA methylation in
Neurospora crassa.";
Nat. Genet. 34:75-79(2003).
[5]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-331 IN COMPLEX WITH ZINC
IONS, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-251;
ASN-254; HIS-255 AND TYR-296.
PubMed=12372305; DOI=10.1016/S0092-8674(02)00999-6;
Zhang X., Tamaru H., Khan S.I., Horton J.R., Keefe L.J., Selker E.U.,
Cheng X.;
"Structure of the Neurospora SET domain protein DIM-5, a histone H3
lysine methyltransferase.";
Cell 111:117-127(2002).
[6]
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 30-331 IN COMPLEX WITH
HISTONE H3; S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS, FUNCTION,
CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-191; ASP-222; PHE-294;
LEU-330 AND TRP-331.
PubMed=12887903; DOI=10.1016/S1097-2765(03)00224-7;
Zhang X., Yang Z., Khan S.I., Horton J.R., Tamaru H., Selker E.U.,
Cheng X.;
"Structural basis for the product specificity of histone lysine
methyltransferases.";
Mol. Cell 12:177-185(2003).
-!- FUNCTION: Histone methyltransferase that specifically
trimethylates histone H3 to form H3K9me3. H3K9me3 marks chromatin
regions for DNA methylation. {ECO:0000269|PubMed:11713521,
ECO:0000269|PubMed:12372305, ECO:0000269|PubMed:12679815,
ECO:0000269|PubMed:12887903}.
-!- CATALYTIC ACTIVITY:
Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
Evidence={ECO:0000269|PubMed:12372305,
ECO:0000269|PubMed:12887903};
-!- INTERACTION:
Q96UA9:9G6.050 (xeno); NbExp=2; IntAct=EBI-1268994, EBI-15849296;
P07041:hh3; NbExp=2; IntAct=EBI-1268994, EBI-1270655;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
{ECO:0000250}.
-!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
are arranged in a triangular cluster; some of these Cys residues
contribute to the binding of two zinc ions within the cluster.
{ECO:0000269|PubMed:12372305}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAL35215.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAF06044.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF419248; AAL35215.1; ALT_SEQ; Genomic_DNA.
EMBL; BX908809; CAF06044.1; ALT_SEQ; Genomic_DNA.
EMBL; CM002239; EAA28243.2; -; Genomic_DNA.
RefSeq; XP_957479.2; XM_952386.3.
PDB; 1ML9; X-ray; 1.98 A; A=30-331.
PDB; 1PEG; X-ray; 2.59 A; A/B=30-331.
PDBsum; 1ML9; -.
PDBsum; 1PEG; -.
SMR; Q8X225; -.
DIP; DIP-39600N; -.
IntAct; Q8X225; 2.
ChEMBL; CHEMBL3309062; -.
PRIDE; Q8X225; -.
EnsemblFungi; EAA28243; EAA28243; NCU04402.
GeneID; 3873656; -.
KEGG; ncr:NCU04402; -.
EuPathDB; FungiDB:NCU04402; -.
InParanoid; Q8X225; -.
KO; K11419; -.
OMA; KRIRVEC; -.
EvolutionaryTrace; Q8X225; -.
Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR007728; Pre-SET_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF05033; Pre-SET; 1.
Pfam; PF00856; SET; 1.
SMART; SM00468; PreSET; 1.
SMART; SM00317; SET; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50867; PRE_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
3D-structure; Chromosome; Complete proteome; Metal-binding;
Methyltransferase; Nucleus; Reference proteome;
S-adenosyl-L-methionine; Transferase; Zinc.
CHAIN 1 331 Histone-lysine N-methyltransferase, H3
lysine-9 specific dim-5.
/FTId=PRO_0000186062.
DOMAIN 77 159 Pre-SET. {ECO:0000255|PROSITE-
ProRule:PRU00157}.
DOMAIN 162 297 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 315 331 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
REGION 172 174 S-adenosyl-L-methionine binding.
REGION 254 255 S-adenosyl-L-methionine binding.
METAL 79 79 Zinc 1.
METAL 79 79 Zinc 2.
METAL 81 81 Zinc 1.
METAL 87 87 Zinc 1.
METAL 87 87 Zinc 3.
METAL 92 92 Zinc 1.
METAL 94 94 Zinc 2.
METAL 141 141 Zinc 2.
METAL 141 141 Zinc 3.
METAL 145 145 Zinc 2.
METAL 147 147 Zinc 3.
METAL 151 151 Zinc 3.
METAL 257 257 Zinc 4.
METAL 319 319 Zinc 4.
METAL 321 321 Zinc 4.
METAL 326 326 Zinc 4.
BINDING 215 215 S-adenosyl-L-methionine.
BINDING 217 217 S-adenosyl-L-methionine.
BINDING 251 251 S-adenosyl-L-methionine.
MUTAGEN 191 191 Y->F: Reduces enzyme activity by 97%.
{ECO:0000269|PubMed:12887903}.
MUTAGEN 191 191 Y->V: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:12887903}.
MUTAGEN 222 222 D->E: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:12887903}.
MUTAGEN 222 222 D->K: Reduces enzyme activity by 97%.
{ECO:0000269|PubMed:12887903}.
MUTAGEN 222 222 D->Q: Reduces enzyme activity by 97%.
{ECO:0000269|PubMed:12887903}.
MUTAGEN 251 251 R->H: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:12372305}.
MUTAGEN 254 254 N->Q: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:12372305}.
MUTAGEN 255 255 H->K: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:12372305}.
MUTAGEN 294 294 F->W: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:12887903}.
MUTAGEN 294 294 F->Y: Reduces enzyme activity by 20%.
{ECO:0000269|PubMed:12887903}.
MUTAGEN 296 296 Y->F: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:12372305}.
MUTAGEN 330 330 L->A: Reduces enzyme activity by over
99%. {ECO:0000269|PubMed:12887903}.
MUTAGEN 331 331 W->A: Reduces enzyme activity by 97%.
{ECO:0000269|PubMed:12887903}.
STRAND 41 44 {ECO:0000244|PDB:1ML9}.
STRAND 46 49 {ECO:0000244|PDB:1ML9}.
HELIX 73 75 {ECO:0000244|PDB:1ML9}.
HELIX 86 88 {ECO:0000244|PDB:1ML9}.
HELIX 93 95 {ECO:0000244|PDB:1ML9}.
STRAND 96 98 {ECO:0000244|PDB:1PEG}.
STRAND 115 118 {ECO:0000244|PDB:1ML9}.
STRAND 119 121 {ECO:0000244|PDB:1PEG}.
TURN 122 125 {ECO:0000244|PDB:1PEG}.
HELIX 129 134 {ECO:0000244|PDB:1ML9}.
HELIX 155 158 {ECO:0000244|PDB:1ML9}.
STRAND 164 168 {ECO:0000244|PDB:1ML9}.
STRAND 170 172 {ECO:0000244|PDB:1ML9}.
STRAND 174 177 {ECO:0000244|PDB:1ML9}.
STRAND 187 190 {ECO:0000244|PDB:1ML9}.
STRAND 194 196 {ECO:0000244|PDB:1ML9}.
HELIX 198 207 {ECO:0000244|PDB:1ML9}.
HELIX 210 212 {ECO:0000244|PDB:1ML9}.
HELIX 214 217 {ECO:0000244|PDB:1ML9}.
STRAND 218 220 {ECO:0000244|PDB:1ML9}.
STRAND 227 230 {ECO:0000244|PDB:1ML9}.
HELIX 232 235 {ECO:0000244|PDB:1ML9}.
STRAND 240 242 {ECO:0000244|PDB:1ML9}.
STRAND 244 247 {ECO:0000244|PDB:1ML9}.
HELIX 249 252 {ECO:0000244|PDB:1ML9}.
STRAND 260 269 {ECO:0000244|PDB:1ML9}.
HELIX 270 275 {ECO:0000244|PDB:1ML9}.
STRAND 277 284 {ECO:0000244|PDB:1ML9}.
STRAND 291 294 {ECO:0000244|PDB:1ML9}.
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


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Related Genes :
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.43) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[EHMT1 EUHMTASE1 GLP KIAA1876 KMT1D] Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Histone H3-K9 methyltransferase 5) (H3-K9-HMTase 5) (Lysine N-methyltransferase 1D)
[SUVH4 KYP SDG33 SET33 At5g13960 MAC12.7] Histone-lysine N-methyltransferase, H3 lysine-9 specific SUVH4 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 4) (H3-K9-HMTase 4) (Protein KRYPTONITE) (Protein SET DOMAIN GROUP 33) (Suppressor of variegation 3-9 homolog protein 4) (Su(var)3-9 homolog protein 4)
[EHMT2 BAT8 C6orf30 G9A KMT1C NG36] Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Lysine N-methyltransferase 1C) (Protein G9a)
[Suv39h1 Suv39h] Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1)
[SUV39H1 KMT1A SUV39H] Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Lysine N-methyltransferase 1A) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1)
[SETDB1 ESET KIAA0067 KMT1E] Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.43) (ERG-associated protein with SET domain) (ESET) (Histone H3-K9 methyltransferase 4) (H3-K9-HMTase 4) (Lysine N-methyltransferase 1E) (SET domain bifurcated 1)
[Ehmt2 Bat8 G9a Ng36] Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Protein G9a)
[SUV39H2 KMT1B] Histone-lysine N-methyltransferase SUV39H2 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 2) (H3-K9-HMTase 2) (Lysine N-methyltransferase 1B) (Suppressor of variegation 3-9 homolog 2) (Su(var)3-9 homolog 2)
[Suv39h2] Histone-lysine N-methyltransferase SUV39H2 (EC 2.1.1.43) (Histone H3-K9 methyltransferase 2) (H3-K9-HMTase 2) (Suppressor of variegation 3-9 homolog 2) (Su(var)3-9 homolog 2)
[SETD7 KIAA1717 KMT7 SET7 SET9] Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.43) (Histone H3-K4 methyltransferase SETD7) (H3-K4-HMTase SETD7) (Lysine N-methyltransferase 7) (SET domain-containing protein 7) (SET7/9)
[Setd7 Kiaa1717 Set7 Set9] Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.43) (Histone H3-K4 methyltransferase SETD7) (H3-K4-HMTase SETD7) (SET domain-containing protein 7) (SET7/9)
[ASHH2 EFS LAZ2 SDG8 SET8 At1g77300 T14N5.15] Histone-lysine N-methyltransferase ASHH2 (EC 2.1.1.43) (ASH1 homolog 2) (H3-K4-HMTase) (Histone H3-K36 methyltransferase 8) (H3-K36-HMTase 8) (Protein EARLY FLOWERING IN SHORT DAYS) (Protein LAZARUS 2) (Protein SET DOMAIN GROUP 8)
[NSD1 ARA267 KMT3B] Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific (EC 2.1.1.43) (Androgen receptor coactivator 267 kDa protein) (Androgen receptor-associated protein of 267 kDa) (H3-K36-HMTase) (H4-K20-HMTase) (Lysine N-methyltransferase 3B) (Nuclear receptor-binding SET domain-containing protein 1) (NR-binding SET domain-containing protein)
[HTR2 At1g09200 T12M4.9; HTR3 At3g27360 K1G2.8; HTR13 At5g10390 F12B17_260; HTR9 At5g10400 F12B17_250; HTR1 At5g65360 MNA5.9] Histone H3.2 (Histone H3.1)
[Hist1h3b H3-53 H3.2 H3b; Hist1h3c H3-143; Hist1h3d H3-B; Hist1h3e H3-F; Hist1h3f H3.2-221 H3f; Hist2h3b H3.2-616; Hist2h3c1 H3.2-615 Hist2h3ca1; Hist2h3c2 H3.2-614 Hist2h3ca2] Histone H3.2
[HIST1H3A H3FA; HIST1H3B H3FL; HIST1H3C H3FC; HIST1H3D H3FB; HIST1H3E H3FD; HIST1H3F H3FI; HIST1H3G H3FH; HIST1H3H H3FK; HIST1H3I H3FF; HIST1H3J H3FJ] Histone H3.1 (Histone H3/a) (Histone H3/b) (Histone H3/c) (Histone H3/d) (Histone H3/f) (Histone H3/h) (Histone H3/i) (Histone H3/j) (Histone H3/k) (Histone H3/l)
[HHT1 YBR010W YBR0201; HHT2 SIN2 YNL031C N2749] Histone H3
[HTR4 At4g40030 T5J17.200; HTR5 At4g40040 T5J17.210; HTR8 At5g10980 T30N20_250 T5K6.6] Histone H3.3 (Histone H3.2)
[Hist1h3a H3a; Hist1h3g H3.1-221 H3g; Hist1h3h H3.1-291 H3h; Hist1h3i H3.1-I H3i] Histone H3.1
[Ehmt1 Euhmtase1 Glp Kmt1d] Histone-lysine N-methyltransferase EHMT1 (EC 2.1.1.-) (EC 2.1.1.43) (Euchromatic histone-lysine N-methyltransferase 1) (Eu-HMTase1) (G9a-like protein 1) (GLP) (GLP1) (Lysine N-methyltransferase 1D)
[H3f3a H3.3a; H3f3b H3.3b] Histone H3.3
[HIST2H3A; HIST2H3C H3F2 H3FM; HIST2H3D] Histone H3.2 (Histone H3/m) (Histone H3/o)
[H3F3C] Histone H3.3C (Histone H3.5)
[H3-I; H3-II; H3-III; H3-IV; H3-V; H3-VI; H3-VII; H3-VIII] Histone H3.2 (Histone H3 class I)
[H3F3A H3.3A H3F3 PP781; H3F3B H3.3B] Histone H3.3
[HHT1 TTHERM_00570560; HHT2 TTHERM_00189180] Histone H3 (H3S) (Histone H3-I/H3-II) (Major histone H3) [Cleaved into: H3F]
[KDM2B CXXC2 FBL10 FBXL10 JHDM1B PCCX2] Lysine-specific demethylase 2B (EC 1.14.11.27) (CXXC-type zinc finger protein 2) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) (Jumonji domain-containing EMSY-interactor methyltransferase motif protein) (Protein JEMMA) (Protein-containing CXXC domain 2) ([Histone-H3]-lysine-36 demethylase 1B)
[SUVR5 CZS SDG6 SET6 At2g23740/At2g23730/At2g23750 F27L4.8/F27L4.9/F27L4.7] Histone-lysine N-methyltransferase SUVR5 (EC 2.1.1.43) (C2H2 zinc finger-SET histone methyltransferase) (Protein C2H2 SET) (Protein SET DOMAIN GROUP 6) (Suppressor of variegation 3-9-related protein 5) (Su(var)3-9-related protein 5)
[HIST3H3 H3FT] Histone H3.1t (H3/t) (H3t) (H3/g)

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