ID SUV91_XENLA Reviewed; 421 AA. AC Q6NRE8; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Histone-lysine N-methyltransferase SUV39H1; DE EC=2.1.1.355 {ECO:0000250|UniProtKB:O43463}; DE AltName: Full=Suppressor of variegation 3-9 homolog 1; DE Short=Su(var)3-9 homolog 1; GN Name=suv39h1; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Oocyte; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(9)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + CC N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + 3 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:60276, Rhea:RHEA-COMP:15538, Rhea:RHEA- CC COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.355; CC Evidence={ECO:0000250|UniProtKB:O43463, ECO:0000255|PROSITE- CC ProRule:PRU00912}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere CC {ECO:0000250}. Note=Associates with centromeric constitutive CC heterochromatin. {ECO:0000250}. 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; BC070805; AAH70805.1; -; mRNA. DR RefSeq; NP_001084892.1; NM_001091423.1. DR AlphaFoldDB; Q6NRE8; -. DR SMR; Q6NRE8; -. DR BioGRID; 101309; 1. DR DNASU; 431943; -. DR GeneID; 431943; -. DR KEGG; xla:431943; -. DR AGR; Xenbase:XB-GENE-6049313; -. DR CTD; 431943; -. DR Xenbase; XB-GENE-6049313; suv39h1.L. DR OrthoDB; 5481936at2759; -. DR Proteomes; UP000186698; Chromosome 8L. DR Bgee; 431943; Expressed in egg cell and 14 other cell types or tissues. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0140949; F:histone H3K9 trimethyltransferase 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:0032259; P:methylation; IEA:UniProtKB-KW. DR CDD; cd18639; CD_SUV39H1_like; 1. DR CDD; cd10525; SET_SUV39H1; 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; 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:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SUV39H1; 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; 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..421 FT /note="Histone-lysine N-methyltransferase SUV39H1" FT /id="PRO_0000281812" FT DOMAIN 46..104 FT /note="Chromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053" FT DOMAIN 189..249 FT /note="Pre-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00157" FT DOMAIN 252..375 FT /note="SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT DOMAIN 405..421 FT /note="Post-SET" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 191 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" 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 196 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 196 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 203 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 204 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 204 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" 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 235 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 237 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 241 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000250" FT BINDING 263..265 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 306 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190" FT BINDING 332..333 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000250" FT BINDING 335 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 409 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 411 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250" FT BINDING 416 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0000250" SQ SEQUENCE 421 AA; 48581 MW; 776BD7633D03C069 CRC64; MAENSNGALG CVVRCLSSES ELQELCREEQ LCCAELGVTR KNLSDFEVEY LWNYKKVQDQ ELYLVKWKYY PDSESTWEPR HHLKCNNLLK QFHLDLEREL LRRAKAAGTK KTAVRCPRRL DQSLSHYLVL KAKQRKRLRQ WAQQLNAKRS HLGLILVENE VDLEGPPRDF VYINEYRVGE GVTINRISAG CKCRDCFSDE GGCCPGAFQH KKAYNNEGQV KVKPGFPIYE CNSCCRCGPS CPNRVVQKGI QYKFCIFRTS DGRGWGVRTL EKIRKNSFVM EYVGEIITSE EAERRGQIYD RQGTTYLFDL DYVEDVYTVD AARYGNISHF VNHSCKPNLQ VYNVFIDNLD ERLPRIAFFA TRTIRTGEEL TFDYNMQVDP VDVESSKMDS NFGIAGLPAS PKKRVRVECK CGVSSCRKYL F //