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 27-MAR-2024, entry version 133. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 7955-ENSDARP00000034818; -. DR GeneID; 445198; -. DR KEGG; dre:445198; -. DR AGR; ZFIN:ZDB-GENE-040801-111; -. DR CTD; 445198; -. DR ZFIN; ZDB-GENE-040801-111; suv39h1a. DR eggNOG; KOG1082; Eukaryota. DR HOGENOM; CLU_020840_8_0_1; -. DR InParanoid; Q6DGD3; -. DR OMA; CECADCP; -. DR OrthoDB; 5481936at2759; -. DR PhylomeDB; Q6DGD3; -. DR TreeFam; TF106452; -. DR Reactome; R-DRE-3214841; PKMTs methylate histone lysines. DR PRO; PR:Q6DGD3; -. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000026799; Expressed in mature ovarian follicle and 18 other cell types or 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 H3K9 methyltransferase activity; IMP:ZFIN. DR GO; GO:0140948; F:histone H3K9 monomethyltransferase activity; IEA:RHEA. 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:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:ZFIN. DR CDD; cd18639; CD_SUV39H1_like; 1. DR Gene3D; 2.40.50.40; -; 1. DR Gene3D; 2.170.270.10; SET domain; 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; H3-K9_MeTrfase_SUV39H1/2-like. DR InterPro; IPR003616; Post-SET_dom. DR InterPro; IPR007728; Pre-SET_dom. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR046341; SET_dom_sf. DR PANTHER; PTHR46223; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H; 1. DR PANTHER; PTHR46223:SF4; HISTONE-LYSINE N-METHYLTRANSFERASE-RELATED; 1. 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; Chromo domain-like; 1. DR SUPFAM; SSF82199; SET domain; 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 //