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Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: SUV39_DROME I0DHL3_DROME
LinkDB: SUV39_DROME I0DHL3_DROME
Original site: SUV39_DROME I0DHL3_DROME 
ID   SUV39_DROME             Reviewed;         635 AA.
AC   P45975; Q9VFA6;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   21-NOV-2003, sequence version 2.
DT   27-SEP-2017, entry version 177.
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=Lysine N-methyltransferase 1;
DE   AltName: Full=Protein suppressor of variegation 3-9;
GN   Name=Su(var)3-9; Synonyms=KMT1; ORFNames=CG6476;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=Oregon-R;
RX   PubMed=7915232;
RA   Tschiersch B., Hofmann A., Krauss V., Dorn R., Korge G., Reuter G.;
RT   "The protein encoded by the Drosophila position-effect variegation
RT   suppressor gene Su(var)3-9 combines domains of antagonistic regulators
RT   of homeotic gene complexes.";
RL   EMBO J. 13:3822-3831(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Karsnas;
RX   PubMed=11063691;
RA   Krauss V., Reuter G.;
RT   "Two genes become one: the genes encoding heterochromatin protein
RT   Su(var)3-9 and translation initiation factor subunit eIF-2gamma are
RT   joined to a dicistronic unit in holometabolic insects.";
RL   Genetics 156:1157-1167(2000).
RN   [3]
RP   SEQUENCE REVISION TO 509.
RA   Schotta G., Ebert A., Lein S., Kubicek S., Krauss V., Jenuwein T.,
RA   Reuter F.;
RT   "Histone H3-K9 methylation potential of Drosophila Su(var)3-9 mutants
RT   correlates with extent of gene silencing.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [6]
RP   INTERACTION WITH RPD3.
RX   PubMed=11571273; DOI=10.1093/embo-reports/kve210;
RA   Czermin B., Schotta G., Huelsmann B.B., Brehm A., Becker P.B.,
RA   Reuter G., Imhof A.;
RT   "Physical and functional association of SU(VAR)3-9 and HDAC1 in
RT   Drosophila.";
RL   EMBO Rep. 2:915-919(2001).
RN   [7]
RP   ENZYME ACTIVITY, AND INTERACTION WITH SU(VAR)205 AND SU(VAR)3-7.
RX   PubMed=11867540; DOI=10.1093/emboj/21.5.1121;
RA   Schotta G., Ebert A., Krauss V., Fischer A., Hoffmann J., Rea S.,
RA   Jenuwein T., Dorn R., Reuter G.;
RT   "Central role of Drosophila SU(VAR)3-9 in histone H3-K9 methylation
RT   and heterochromatic gene silencing.";
RL   EMBO J. 21:1121-1131(2002).
RN   [8]
RP   FUNCTION.
RX   PubMed=14630943; DOI=10.1101/gad.281503;
RA   Greil F., van der Kraan I., Delrow J., Smothers J.F., de Wit E.,
RA   Bussemaker H.J., van Driel R., Henikoff S., van Steensel B.;
RT   "Distinct HP1 and Su(var)3-9 complexes bind to sets of developmentally
RT   coexpressed genes depending on chromosomal location.";
RL   Genes Dev. 17:2825-2838(2003).
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.
CC       {ECO:0000269|PubMed:14630943}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000269|PubMed:11867540}.
CC   -!- SUBUNIT: Interacts with Su(var)205 and Su(var)3-7. Probably
CC       associates with Rpd3. {ECO:0000269|PubMed:11571273,
CC       ECO:0000269|PubMed:11867540}.
CC   -!- INTERACTION:
CC       Q94517:Rpd3; NbExp=2; IntAct=EBI-110378, EBI-302197;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere.
CC       Note=Associates with centromeric constitutive heterochromatin.
CC   -!- DEVELOPMENTAL STAGE: Expressed maternally and zygotically.
CC       Expressed throughout development with a peak of expression during
CC       early embryogenesis (0-9 hours old embryos). Weak expression in
CC       larvae, pupae and adult flies. {ECO:0000269|PubMed:7915232}.
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; X80070; CAA56376.1; -; mRNA.
DR   EMBL; AJ290956; CAB93768.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAF55154.1; -; Genomic_DNA.
DR   PIR; S47004; S47004.
DR   RefSeq; NP_524357.2; NM_079633.3.
DR   UniGene; Dm.3299; -.
DR   ProteinModelPortal; P45975; -.
DR   SMR; P45975; -.
DR   BioGrid; 66596; 38.
DR   DIP; DIP-23970N; -.
DR   IntAct; P45975; 4.
DR   MINT; MINT-748988; -.
DR   STRING; 7227.FBpp0302536; -.
DR   BindingDB; P45975; -.
DR   ChEMBL; CHEMBL2169720; -.
DR   PaxDb; P45975; -.
DR   PRIDE; P45975; -.
DR   GeneID; 41483; -.
DR   KEGG; dme:Dmel_CG43664; -.
DR   CTD; 41483; -.
DR   FlyBase; FBgn0263755; Su(var)3-9.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   eggNOG; COG5257; LUCA.
DR   InParanoid; P45975; -.
DR   KO; K11419; -.
DR   OrthoDB; EOG091G0624; -.
DR   PhylomeDB; P45975; -.
DR   Reactome; R-DME-427359; SIRT1 negatively regulates rRNA Expression.
DR   SABIO-RK; P45975; -.
DR   GenomeRNAi; 41483; -.
DR   PRO; PR:P45975; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0263755; -.
DR   ExpressionAtlas; P45975; differential.
DR   Genevisible; P45975; DM.
DR   GO; GO:0000775; C:chromosome, centromeric region; TAS:FlyBase.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0000792; C:heterochromatin; IDA:FlyBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005701; C:polytene chromosome chromocenter; IDA:FlyBase.
DR   GO; GO:0042054; F:histone methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:FlyBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
DR   GO; GO:0006342; P:chromatin silencing; IMP:FlyBase.
DR   GO; GO:0030702; P:chromatin silencing at centromere; IMP:FlyBase.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IMP:FlyBase.
DR   GO; GO:0051276; P:chromosome organization; IMP:FlyBase.
DR   GO; GO:0006306; P:DNA methylation; IMP:FlyBase.
DR   GO; GO:0048132; P:female germ-line stem cell asymmetric division; IDA:FlyBase.
DR   GO; GO:0016458; P:gene silencing; IMP:FlyBase.
DR   GO; GO:0031507; P:heterochromatin assembly; IMP:FlyBase.
DR   GO; GO:0070868; P:heterochromatin organization involved in chromatin silencing; IMP:FlyBase.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IDA:FlyBase.
DR   GO; GO:0016571; P:histone methylation; IDA:FlyBase.
DR   GO; GO:0016570; P:histone modification; IMP:FlyBase.
DR   GO; GO:2001229; P:negative regulation of response to gamma radiation; IMP:FlyBase.
DR   GO; GO:0048477; P:oogenesis; IDA:FlyBase.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
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; 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   1: Evidence at protein level;
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    635       Histone-lysine N-methyltransferase
FT                                Su(var)3-9.
FT                                /FTId=PRO_0000186061.
FT   DOMAIN      219    278       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      410    474       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      477    603       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      619    635       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION       81    188       Binds to Su(var)205 and Suvar(3)7.
FT   REGION      488    490       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      560    561       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       412    412       Zinc 1. {ECO:0000250}.
FT   METAL       412    412       Zinc 2. {ECO:0000250}.
FT   METAL       414    414       Zinc 1. {ECO:0000250}.
FT   METAL       421    421       Zinc 1. {ECO:0000250}.
FT   METAL       421    421       Zinc 3. {ECO:0000250}.
FT   METAL       427    427       Zinc 1. {ECO:0000250}.
FT   METAL       428    428       Zinc 1. {ECO:0000250}.
FT   METAL       428    428       Zinc 2. {ECO:0000250}.
FT   METAL       456    456       Zinc 2. {ECO:0000250}.
FT   METAL       456    456       Zinc 3. {ECO:0000250}.
FT   METAL       460    460       Zinc 2. {ECO:0000250}.
FT   METAL       462    462       Zinc 3. {ECO:0000250}.
FT   METAL       466    466       Zinc 3. {ECO:0000250}.
FT   METAL       563    563       Zinc 4. {ECO:0000250}.
FT   METAL       623    623       Zinc 4. {ECO:0000250}.
FT   METAL       625    625       Zinc 4. {ECO:0000250}.
FT   METAL       630    630       Zinc 4. {ECO:0000250}.
FT   BINDING     531    531       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    275    275       T -> I (in Ref. 4; AAF55154).
FT                                {ECO:0000305}.
FT   CONFLICT    509    509       G -> E (in Ref. 1; CAA56376).
FT                                {ECO:0000305}.
FT   CONFLICT    627    627       R -> A (in Ref. 4; AAF55154).
FT                                {ECO:0000305}.
SQ   SEQUENCE   635 AA;  71904 MW;  4154A49F54B60E14 CRC64;
     MATAEAQIGV NRNLQKQDLS NLDVSKLTPL SPEVISRQAT INIGTIGHVA HGKSTVVKAI
     SGVQTVRFKN ELERNITIKL ERLSEKKIKN LLTSKQQRQQ YEIKQRSMLR HLAELRRHSR
     FRRLCTKPAS SSMPASTSSV DRRTTRRSTS QTSLSPSNSS GYGSVFGCEE HDVDKIPSLN
     GFAKLKRRRS SCVGAPTPNS KRSKNNMGVI AKRPPKGEYV VERIECVEMD QYQPVFFVKW
     LGYHDSENTW ESLANVADCA EMEKFVERHQ QLYETYIAKI TTELEKQLEA LPLMENITVA
     EVDAYEPLNL QIDLILLAQY RAAGSRSQRE PQKIGERALK SMQIKRAQFV RRKQLADLAL
     FEKRMNHVEK PSPPIRVENN IDLDTIDSNF MYIHDNIIGK DVPKPEAGIV GCKCTEDTEE
     CTASTKCCAR FAGELFAYER STRRLRLRPG SAIYECNSRC SCDSSCSNRL VQHGRQVPLV
     LFKTANGSGW GVRAATALRK GEFVCEYIGE IITSDEANER GKAYDDNGRT YLFDLDYNTA
     QDSEYTIDAA NYGNISHFIN HSCDPNLAVF PCWIEHLNVA LPHLVFFTLR PIKAGEELSF
     DYIRADNEDV PYENLSTAVR VECRCGRDNC RKVLF
//
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Ontology (24)   
   GO (24)   
Drug (1)   
   CHEMBL-UP (1)   
Chemical reaction (2)   
   KEGG ENZYME (1)   
   SABIO-RK-UP (1)   
Gene (5)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   FLYBASE (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (20)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (5)   
   SMART (3)   
Literature (7)   
   PubMed (7)   
All databases (63)   

Download RDF
ID   I0DHL3_DROME            Unreviewed;       635 AA.
AC   I0DHL3;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   05-JUL-2017, entry version 42.
DE   SubName: Full=FI20106p1 {ECO:0000313|EMBL:AFH89831.1};
GN   Name=Su(var)3-9-RA {ECO:0000313|EMBL:AFH89831.1};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AFH89831.1};
RN   [1] {ECO:0000313|EMBL:AFH89831.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000256|SAAS:SAAS00591578}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|SAAS:SAAS00563877}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00574581}.
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DR   EMBL; BT133458; AFH89831.1; -; mRNA.
DR   RefSeq; NP_524357.2; NM_079633.3.
DR   UniGene; Dm.3299; -.
DR   ProteinModelPortal; I0DHL3; -.
DR   IntAct; I0DHL3; 3.
DR   PaxDb; I0DHL3; -.
DR   PRIDE; I0DHL3; -.
DR   EnsemblMetazoa; FBtr0310385; FBpp0302536; FBgn0263755.
DR   GeneID; 41483; -.
DR   KEGG; dme:Dmel_CG43664; -.
DR   CTD; 41483; -.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   eggNOG; COG5257; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   KO; K11419; -.
DR   OMA; THERYKI; -.
DR   GenomeRNAi; 41483; -.
DR   Bgee; FBgn0263755; -.
DR   ExpressionAtlas; I0DHL3; differential.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR016197; Chromodomain-like.
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   2: Evidence at transcript level;
KW   Chromosome {ECO:0000256|SAAS:SAAS00508265};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009343-2};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS00590675};
KW   Nucleus {ECO:0000256|SAAS:SAAS00574642};
KW   S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00591079};
KW   Transferase {ECO:0000256|SAAS:SAAS00591533};
KW   Zinc {ECO:0000256|PIRSR:PIRSR009343-2}.
FT   DOMAIN      219    278       Chromo. {ECO:0000259|PROSITE:PS50013}.
FT   DOMAIN      410    474       Pre-SET. {ECO:0000259|PROSITE:PS50867}.
FT   DOMAIN      477    603       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN      619    635       Post-SET. {ECO:0000259|PROSITE:PS50868}.
FT   METAL       412    412       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       412    412       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       414    414       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       427    427       Zinc 1. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       428    428       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       456    456       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       456    456       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       460    460       Zinc 2. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       462    462       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       466    466       Zinc 3. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       563    563       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       623    623       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       625    625       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
FT   METAL       630    630       Zinc 4. {ECO:0000256|PIRSR:PIRSR009343-
FT                                2}.
SQ   SEQUENCE   635 AA;  71831 MW;  DAC7A45C5E177D91 CRC64;
     MATAEAQIGV NRNLQKQDLS NLDVSKLTPL SPEVISRQAT INIGTIGHVA HGKSTVVKAI
     SGVQTVRFKN ELERNITIKL ERLSEKKIKN LLTSKQQRQQ YEIKQRSMLR HLAELRRHSR
     FRRLCTKPAS SSMPASTSSV DRRTTRRSTS QTSLSPSNSS GYGSVFGCEE HDVDKIPSLN
     GFAKLKRRRS SCVGAPTPNS KRSKNNMGVI AKRPPKGEYV VERIECVEMD QYQPVFFVKW
     LGYHDSENTW ESLANVADCA EMEKFVERHQ QLYEIYIAKI TTELEKQLEA LPLMENITVA
     EVDAYEPLNL QIDLILLAQY RAAGSRSQRE PQKIGERALK SMQIKRAQFV RRKQLADLAL
     FEKRMNHVEK PSPPIRVENN IDLDTIDSNF MYIHDNIIGK DVPKPEAGIV GCKCTEDTEE
     CTASTKCCAR FAGELFAYER STRRLRLRPG SAIYECNSRC SCDSSCSNRL VQHGRQVPLV
     LFKTANGSGW GVRAATALRK GEFVCEYIGE IITSDEANER GKAYDDNGRT YLFDLDYNTA
     QDSEYTIDAA NYGNISHFIN HSCDPNLAVF PCWIEHLNVA LPHLVFFTLR PIKAGEELSF
     DYIRADNEDV PYENLSTAVR VECRCGADNC RKVLF
//
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Ontology (4)   
   GO (4)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (5)   
   SMART (4)   
All databases (31)   

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