SUV39_DROPS
ID SUV39_DROPS Reviewed; 633 AA.
AC Q294B9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Histone-lysine N-methyltransferase Su(var)3-9;
DE EC=2.1.1.355 {ECO:0000250|UniProtKB:P45975};
DE AltName: Full=Histone H3-K9 methyltransferase;
DE Short=H3-K9-HMTase;
DE AltName: Full=Protein suppressor of variegation 3-9;
GN Name=Su(var)3-9; ORFNames=GA19622;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates
CC 'Lys-9' of histone H3 using monomethylated H3 'Lys-9' as substrate. H3
CC 'Lys-9' trimethylation represents a specific tag for epigenetic
CC transcriptional repression by recruiting Su(var)205/HP1 to methylated
CC histones. Mainly functions in heterochromatin regions, thereby playing
CC a central role in the establishment of constitutive heterochromatin at
CC pericentric regions. Involved in heterochromatic gene silencing
CC including the modification of position-effect-variegation (By
CC similarity). {ECO:0000250}.
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:0000250|UniProtKB:P45975};
CC -!- SUBUNIT: Interacts with Su(var)205 and Su(var)3-7. Probably associates
CC with HDAC1/Rpd3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Note=Associates with centromeric constitutive
CC 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. The SET domain also participates in stable
CC binding to heterochromatin (By similarity). {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. {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:PRU00190}.
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DR EMBL; CM000070; EAL29045.3; -; Genomic_DNA.
DR RefSeq; XP_001359893.3; XM_001359856.4.
DR AlphaFoldDB; Q294B9; -.
DR SMR; Q294B9; -.
DR STRING; 7237.FBpp0301866; -.
DR EnsemblMetazoa; FBtr0310181; FBpp0301866; FBgn0079618.
DR GeneID; 4803095; -.
DR KEGG; dpo:Dpse_GA19622; -.
DR eggNOG; KOG1082; Eukaryota.
DR HOGENOM; CLU_020840_8_1_1; -.
DR InParanoid; Q294B9; -.
DR PhylomeDB; Q294B9; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0079618; Expressed in female reproductive system and 3 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblMetazoa.
DR GO; GO:0005701; C:polytene chromosome chromocenter; IEA:EnsemblMetazoa.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblMetazoa.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IEA:EnsemblMetazoa.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR GO; GO:0006306; P:DNA methylation; IEA:EnsemblMetazoa.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IEA:EnsemblMetazoa.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IEA:EnsemblMetazoa.
DR GO; GO:0051567; P:histone H3-K9 methylation; ISS:UniProtKB.
DR GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR GO; GO:2001229; P:negative regulation of response to gamma radiation; IEA:EnsemblMetazoa.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; ISS:UniProtKB.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR011381; Histone_H3-K9_MeTrfase.
DR InterPro; IPR027417; P-loop_NTPase.
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; PF00385; Chromo; 1.
DR Pfam; PF05033; Pre-SET; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF009343; SUV39_SET; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50867; PRE_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Centromere; Chromatin regulator; Chromosome; Metal-binding;
KW Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc.
FT CHAIN 1..633
FT /note="Histone-lysine N-methyltransferase Su(var)3-9"
FT /id="PRO_0000281817"
FT DOMAIN 213..271
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 407..472
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 475..601
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 617..633
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 486..488
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 558..559
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 561
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 621
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 623
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 628
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
SQ SEQUENCE 633 AA; 71612 MW; 094CDAAA9499BD32 CRC64;
MATAEAQVNV NRNLQKQDLR NLEVSNLTPL SPEVISRQAT INIGTIGHVA HGKSTVVKAI
SGVQTVRFKN ELERNITIKL ERLSEKKIKL LLKSKHQRHK YDIQQQKLLR ILAERRKARA
MTPLAPASVL APSMETARPR LRSTSLNSLS PSNSSGYGSI LGCDDSDQSS QLVLKPNVLK
RRRSNCVQIP TPAAKRSRKN DGTTVKRRPK GEYIVEKIES VEVVQFQPVF FVKWLGYDVS
ANTWESYVNL SDCAEMEKFV ERHLQLHQHY IAQITGELDT QLSDIPQTED LKTISIAEID
AYDPLELQID FILLAQYRAA ASRSQREPER IGARALHRMQ VRRSHFARRK QLIDLLLFEH
RMNRVELPSP PIRVENNWDL DTIDSGFKYI QKNIIGEGVP KPQAGLVGCM CRHQSGEQCT
ASSMCCGRMA GEIFAYDRTT GRLRLRPGSA IYECNSRCSC DESCTNRVVQ NGRKHPLVLF
KTSNGSGWGV RTPQPLKKGV FVCEYIGEII TCEEANERGK AYDDNGRTYL FDLDYNTSRD
SEYTVDAANF GNISHFINHS CDPNLAVFPC WIEHLNTALP HLVFFTIRPI KAGEELSFDY
IRADNEEVPY ENLSTAARVQ CRCGAANCRK VLF
