SV91A_DANRE
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 03-AUG-2022, entry version 124.
DE RecName: Full=Histone-lysine N-methyltransferase SUV39H1-A;
DE EC=2.1.1.- {ECO:0000305|PubMed:16980612};
DE EC=2.1.1.366 {ECO:0000305|PubMed:16980612};
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 Danionidae; Danioninae; 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., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., 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., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., 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., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT 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., Chen Y.,
RA Chen S.-J., Huang Q.-H., Liu T.X., Chen Z.;
RT "Genome-wide survey and developmental expression mapping of zebrafish SET
RT 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., Karpf A.R.,
RA 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 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 HP1 (CBX1, CBX3 and/or CBX5)
CC proteins to methylated histones. Mainly functions in heterochromatin
CC regions, thereby playing a central role in the establishment of
CC constitutive heterochromatin at pericentric and telomere regions. H3
CC 'Lys-9' trimethylation is also required to direct DNA methylation at
CC pericentric repeats. SUV39H1 is targeted to histone H3 via its
CC interaction with RB1 and is involved in many processes, such as
CC regulation of organ-specific terminal differentiation during
CC development. {ECO:0000269|PubMed:16980612}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00913, ECO:0000305|PubMed:16980612};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60288, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15541, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; EC=2.1.1.366; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00913, ECO:0000305|PubMed:16980612};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Note=Associates with centromeric constitutive
CC 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 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:PRU00912}.
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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 AlphaFoldDB; Q6DGD3; -.
DR SMR; Q6DGD3; -.
DR STRING; 7955.ENSDARP00000034818; -.
DR PaxDb; Q6DGD3; -.
DR PRIDE; 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 GeneTree; ENSGT00940000160063; -.
DR HOGENOM; CLU_020840_8_0_1; -.
DR InParanoid; Q6DGD3; -.
DR OMA; CCRGYLN; -.
DR OrthoDB; 753093at2759; -.
DR PhylomeDB; Q6DGD3; -.
DR TreeFam; TF106452; -.
DR Reactome; R-DRE-3214841; PKMTs methylate histone lysines.
DR PRO; PR:Q6DGD3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000026799; Expressed in mature ovarian follicle and 18 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IBA:GO_Central.
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:0006325; P:chromatin organization; 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:0034968; P:histone lysine methylation; IBA:GO_Central.
DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ZFIN.
DR Gene3D; 2.170.270.10; -; 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 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; SM00468; PreSET; 1.
DR SMART; SM00317; SET; 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; PS51579; SAM_MT43_SUVAR39_3; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Centromere; Chromatin regulator; Chromosome; Differentiation;
KW Metal-binding; Methyltransferase; Nucleus; Reference proteome; Repressor;
KW S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW Transferase; Zinc.
FT CHAIN 1..411
FT /note="Histone-lysine N-methyltransferase SUV39H1-A"
FT /id="PRO_0000281811"
FT DOMAIN 43..101
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 178..239
FT /note="Pre-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157"
FT DOMAIN 242..365
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 395..411
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 253..255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 322..323
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT CONFLICT 139
FT /note="W -> R (in Ref. 2; AAH76417)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="M -> L (in Ref. 2; AAH76417)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="E -> A (in Ref. 2; AAH76417)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="Q -> R (in Ref. 2; AAH76417)"
FT /evidence="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
