GenomeNet

Database: UniProt
Entry: Q6DGD3
LinkDB: Q6DGD3
Original site: Q6DGD3 
ID   SV91A_DANRE             Reviewed;         411 AA.
AC   Q6DGD3; A5XBP4; B0S580;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   16-JAN-2019, entry version 110.
DE   RecName: Full=Histone-lysine N-methyltransferase SUV39H1-A;
DE            EC=2.1.1.43;
DE   AltName: Full=Suppressor of variegation 3-9 homolog 1-A;
DE            Short=Su(var)3-9 homolog 1-A;
GN   Name=suv39h1a; Synonyms=suv39h1; ORFNames=si:dkey-16n15.2, zgc:101027;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 214-409, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=18231586; DOI=10.1371/journal.pone.0001499;
RA   Sun X.-J., Xu P.-F., Zhou T., Hu M., Fu C.-T., Zhang Y., Jin Y.,
RA   Chen Y., Chen S.-J., Huang Q.-H., Liu T.X., Chen Z.;
RT   "Genome-wide survey and developmental expression mapping of zebrafish
RT   SET domain-containing genes.";
RL   PLoS ONE 3:E1499-E1499(2008).
RN   [4]
RP   FUNCTION.
RX   PubMed=16980612; DOI=10.1128/MCB.00312-06;
RA   Rai K., Nadauld L.D., Chidester S., Manos E.J., James S.R.,
RA   Karpf A.R., Cairns B.R., Jones D.A.;
RT   "Zebra fish Dnmt1 and Suv39h1 regulate organ-specific terminal
RT   differentiation during development.";
RL   Mol. Cell. Biol. 26:7077-7085(2006).
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 HP1
CC       (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly
CC       functions in heterochromatin regions, thereby playing a central
CC       role in the establishment of constitutive heterochromatin at
CC       pericentric and telomere regions. H3 'Lys-9' trimethylation is
CC       also required to direct DNA methylation at pericentric repeats.
CC       SUV39H1 is targeted to histone H3 via its interaction with RB1 and
CC       is involved in many processes, such as regulation of organ-
CC       specific terminal differentiation during development.
CC       {ECO:0000269|PubMed:16980612}.
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU00912};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome,
CC       centromere {ECO:0000250}. Note=Associates with centromeric
CC       constitutive heterochromatin. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed ubuitiously.
CC       {ECO:0000269|PubMed:18231586}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       {ECO:0000269|PubMed:18231586}.
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:PRU00912}.
DR   EMBL; BX005340; CAQ14784.1; -; Genomic_DNA.
DR   EMBL; BC076417; AAH76417.1; -; mRNA.
DR   EMBL; DQ840140; ABI34869.1; -; mRNA.
DR   RefSeq; NP_001003592.1; NM_001003592.1.
DR   UniGene; Dr.80633; -.
DR   ProteinModelPortal; Q6DGD3; -.
DR   SMR; Q6DGD3; -.
DR   STRING; 7955.ENSDARP00000034818; -.
DR   PaxDb; Q6DGD3; -.
DR   Ensembl; ENSDART00000038955; ENSDARP00000034818; ENSDARG00000026799.
DR   GeneID; 445198; -.
DR   KEGG; dre:445198; -.
DR   CTD; 445198; -.
DR   ZFIN; ZDB-GENE-040801-111; suv39h1a.
DR   eggNOG; KOG1082; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000160063; -.
DR   HOGENOM; HOG000231244; -.
DR   HOVERGEN; HBG055621; -.
DR   InParanoid; Q6DGD3; -.
DR   KO; K11419; -.
DR   OMA; EARGAWC; -.
DR   OrthoDB; 753093at2759; -.
DR   PhylomeDB; Q6DGD3; -.
DR   TreeFam; TF106452; -.
DR   Reactome; R-DRE-427359; SIRT1 negatively regulates rRNA expression.
DR   PRO; PR:Q6DGD3; -.
DR   Proteomes; UP000000437; Chromosome 8.
DR   Bgee; ENSDARG00000026799; Expressed in 21 organ(s), highest expression level in mature ovarian follicle.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0031017; P:exocrine pancreas development; IMP:ZFIN.
DR   GO; GO:0051567; P:histone H3-K9 methylation; IMP:ZFIN.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ZFIN.
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; 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; 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; PS51579; SAM_MT43_SUVAR39_3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Centromere; Chromatin regulator; Chromosome;
KW   Complete proteome; Differentiation; Metal-binding; Methyltransferase;
KW   Nucleus; Reference proteome; Repressor; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase; Zinc.
FT   CHAIN         1    411       Histone-lysine N-methyltransferase
FT                                SUV39H1-A.
FT                                /FTId=PRO_0000281811.
FT   DOMAIN       43    101       Chromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      178    239       Pre-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00157}.
FT   DOMAIN      242    365       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      395    411       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION      253    255       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      322    323       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   METAL       180    180       Zinc 1. {ECO:0000250}.
FT   METAL       180    180       Zinc 2. {ECO:0000250}.
FT   METAL       182    182       Zinc 1. {ECO:0000250}.
FT   METAL       185    185       Zinc 1. {ECO:0000250}.
FT   METAL       185    185       Zinc 3. {ECO:0000250}.
FT   METAL       193    193       Zinc 1. {ECO:0000250}.
FT   METAL       194    194       Zinc 1. {ECO:0000250}.
FT   METAL       194    194       Zinc 2. {ECO:0000250}.
FT   METAL       221    221       Zinc 2. {ECO:0000250}.
FT   METAL       221    221       Zinc 3. {ECO:0000250}.
FT   METAL       225    225       Zinc 2. {ECO:0000250}.
FT   METAL       227    227       Zinc 3. {ECO:0000250}.
FT   METAL       231    231       Zinc 3. {ECO:0000250}.
FT   METAL       325    325       Zinc 4. {ECO:0000250}.
FT   METAL       399    399       Zinc 4. {ECO:0000250}.
FT   METAL       401    401       Zinc 4. {ECO:0000250}.
FT   METAL       406    406       Zinc 4. {ECO:0000250}.
FT   BINDING     296    296       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   CONFLICT    139    139       W -> R (in Ref. 2; AAH76417).
FT                                {ECO:0000305}.
FT   CONFLICT    152    152       M -> L (in Ref. 2; AAH76417).
FT                                {ECO:0000305}.
FT   CONFLICT    183    183       E -> A (in Ref. 2; AAH76417).
FT                                {ECO:0000305}.
FT   CONFLICT    284    284       Q -> R (in Ref. 2; AAH76417).
FT                                {ECO:0000305}.
SQ   SEQUENCE   411 AA;  47471 MW;  3C86D47CEC18C150 CRC64;
     MARDLKDCRV PCKLLLEDLQ ALCRRKKLVC KQLSVTKNNF NDYEVEYLCN YKKHKGREFF
     LVKWKGYEES ENTWEPLKNL KCPILLHQFR KDMKAALLQA NEPLDSASLS GPIISFLRQK
     ATQRIRLKKW EDLMNQTCWH KGRIFVSNEV DMDGPPKNFT YINENKLGKG VDMNAVIVGC
     ECEDCVSQPV DGCCPGLLKF RRAYNESRRV KVMPGVPIYE CNSKCRCGPD CANRVVQRGI
     QYDLCIFKTD NGRGWGVRTL QRINKNSFVM EYLGEIITTD EAEQRGVLYD KQGVTYLFDL
     DYVDDVYTID AAHYGNISHF VNHSCDPNLQ VYNVFIDNLD ERLPRIALFA KRGIKAGEEL
     TFDYKMTVDP VDAESTKMDL DFSRAGIEGS PIKRVHMECK CGVRNCRKYL F
//
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