GenomeNet

Database: UniProt
Entry: Q294B9
LinkDB: Q294B9
Original site: Q294B9 
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   05-DEC-2018, entry version 95.
DE   RecName: Full=Histone-lysine N-methyltransferase Su(var)3-9;
DE            EC=2.1.1.43;
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.,
RA   Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J.,
RA   van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E.,
RA   Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D.,
RA   Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D.,
RA   Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R.,
RA   Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L.,
RA   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:
RT   chromosomal, gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-9' of histone H3 using monomethylated H3 'Lys-
CC       9' as substrate. H3 'Lys-9' trimethylation represents a specific
CC       tag for epigenetic transcriptional repression by recruiting
CC       Su(var)205/HP1 to methylated histones. Mainly functions in
CC       heterochromatin regions, thereby playing a central role in the
CC       establishment of constitutive heterochromatin at pericentric
CC       regions. Involved in heterochromatic gene silencing including the
CC       modification of position-effect-variegation (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBUNIT: Interacts with Su(var)205 and Su(var)3-7. Probably
CC       associates with Rpd3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome,
CC       centromere {ECO:0000250}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000250}.
CC   -!- DOMAIN: Although the SET domain contains the active site of
CC       enzymatic activity, both pre-SET and post-SET domains are required
CC       for methyltransferase activity. The SET domain also participates
CC       in stable binding to heterochromatin (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: In the pre-SET domain, Cys residues bind 3 zinc ions that
CC       are arranged in a triangular cluster; some of these Cys residues
CC       contribute to the binding of two zinc ions within the cluster.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar3-9 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; CM000070; EAL29045.3; -; Genomic_DNA.
DR   RefSeq; XP_001359893.3; XM_001359856.4.
DR   ProteinModelPortal; Q294B9; -.
DR   SMR; Q294B9; -.
DR   STRING; 7237.FBpp0301866; -.
DR   PRIDE; Q294B9; -.
DR   EnsemblMetazoa; FBtr0310181; FBpp0301866; FBgn0079618.
DR   GeneID; 4803095; -.
DR   KEGG; dpo:Dpse_GA19622; -.
DR   FlyBase; FBgn0079618; Dpse\GA19622.
DR   InParanoid; Q294B9; -.
DR   KO; K11419; -.
DR   PhylomeDB; Q294B9; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Proteomes; UP000001819; Unassembled WGS sequence.
DR   Bgee; FBgn0079618; Expressed in 5 organ(s), highest expression level in female reproductive system.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042054; F:histone methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; ISS:UniProtKB.
DR   GO; GO:0030702; P:chromatin silencing at centromere; ISS:UniProtKB.
DR   GO; GO:0006348; P:chromatin silencing at telomere; ISS:UniProtKB.
DR   GO; GO:0051567; P:histone H3-K9 methylation; ISS:UniProtKB.
DR   GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
DR   CDD; cd00024; CHROMO; 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   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   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; Complete proteome;
KW   Metal-binding; Methyltransferase; Nucleus; Reference proteome;
KW   Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc.
FT   CHAIN         1    633       Histone-lysine N-methyltransferase
FT                                Su(var)3-9.
FT                                /FTId=PRO_0000281817.
FT   DOMAIN      213    271       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      407    472       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      475    601       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      617    633       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      486    488       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      558    559       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       409    409       Zinc 1. {ECO:0000250}.
FT   METAL       409    409       Zinc 2. {ECO:0000250}.
FT   METAL       411    411       Zinc 1. {ECO:0000250}.
FT   METAL       419    419       Zinc 1. {ECO:0000250}.
FT   METAL       419    419       Zinc 3. {ECO:0000250}.
FT   METAL       425    425       Zinc 1. {ECO:0000250}.
FT   METAL       426    426       Zinc 1. {ECO:0000250}.
FT   METAL       426    426       Zinc 2. {ECO:0000250}.
FT   METAL       454    454       Zinc 2. {ECO:0000250}.
FT   METAL       454    454       Zinc 3. {ECO:0000250}.
FT   METAL       458    458       Zinc 2. {ECO:0000250}.
FT   METAL       460    460       Zinc 3. {ECO:0000250}.
FT   METAL       464    464       Zinc 3. {ECO:0000250}.
FT   METAL       561    561       Zinc 4. {ECO:0000250}.
FT   METAL       621    621       Zinc 4. {ECO:0000250}.
FT   METAL       623    623       Zinc 4. {ECO:0000250}.
FT   METAL       628    628       Zinc 4. {ECO:0000250}.
FT   BINDING     529    529       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
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
//
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