ID A8XAU4_CAEBR Unreviewed; 400 AA. AC A8XAU4; DT 15-JAN-2008, integrated into UniProtKB/TrEMBL. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|RuleBase:RU271113}; DE EC=2.1.1.360 {ECO:0000256|ARBA:ARBA00012190, ECO:0000256|RuleBase:RU271113}; DE AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|ARBA:ARBA00029821, ECO:0000256|RuleBase:RU271113}; GN ORFNames=CBG10214 {ECO:0000313|EMBL:CAP29759.1, GN ECO:0000313|WormBase:CBG10214}, CBG_10214 GN {ECO:0000313|EMBL:CAP29759.1}; OS Caenorhabditis briggsae. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP29759.1, ECO:0000313|Proteomes:UP000008549}; RN [1] {ECO:0000313|EMBL:CAP29759.1, ECO:0000313|Proteomes:UP000008549} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AF16 {ECO:0000313|EMBL:CAP29759.1, RC ECO:0000313|Proteomes:UP000008549}; RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045; RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., RA Durbin R., Waterston R.H.; RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative RT genomics."; RL PLoS Biol. 1:166-192(2003). CC -!- FUNCTION: Histone methyltransferase that specifically trimethylates CC histone H3 to form H3K79me3. This methylation is required for telomere CC silencing and for the pachytene checkpoint during the meiotic cell CC cycle by allowing the recruitment of RAD9 to double strand breaks. CC Nucleosomes are preferred as substrate compared to free histone. CC {ECO:0000256|RuleBase:RU271113}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) CC + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:60328, Rhea:RHEA-COMP:15549, Rhea:RHEA- CC COMP:15552, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.360; CC Evidence={ECO:0000256|ARBA:ARBA00001569, CC ECO:0000256|RuleBase:RU271113}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123, CC ECO:0000256|RuleBase:RU271113}. CC -!- MISCELLANEOUS: In contrast to other lysine histone methyltransferases, CC it does not contain a SET domain, suggesting the existence of another CC mechanism for methylation of lysine residues of histones. CC {ECO:0000256|RuleBase:RU271113}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. DOT1 family. {ECO:0000256|RuleBase:RU271113}. 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; HE600905; CAP29759.1; -; Genomic_DNA. DR RefSeq; XP_002631953.1; XM_002631907.1. DR AlphaFoldDB; A8XAU4; -. DR STRING; 6238.A8XAU4; -. DR EnsemblMetazoa; CBG10214.1; CBG10214.1; WBGene00031651. DR GeneID; 8573952; -. DR KEGG; cbr:CBG_10214; -. DR CTD; 8573952; -. DR WormBase; CBG10214; CBP08493; WBGene00031651; -. DR eggNOG; KOG3924; Eukaryota. DR HOGENOM; CLU_778993_0_0_1; -. DR InParanoid; A8XAU4; -. DR OMA; IVMESNI; -. DR OrthoDB; 2881295at2759; -. DR Proteomes; UP000008549; Unassembled WGS sequence. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0031151; F:histone H3K79 methyltransferase activity; IBA:GO_Central. DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR025789; DOT1_dom. DR InterPro; IPR030445; H3-K79_meTrfase. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR21451; HISTONE H3 METHYLTRANSFERASE; 1. DR PANTHER; PTHR21451:SF0; HISTONE-LYSINE N-METHYLTRANSFERASE, H3 LYSINE-79 SPECIFIC; 1. DR Pfam; PF08123; DOT1; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51569; DOT1; 1. PE 3: Inferred from homology; KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853, KW ECO:0000256|RuleBase:RU271113}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, KW ECO:0000256|RuleBase:RU271113}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU271113}; KW Reference proteome {ECO:0000313|Proteomes:UP000008549}; KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, KW ECO:0000256|RuleBase:RU271113}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU271113}. FT DOMAIN 63..375 FT /note="DOT1" FT /evidence="ECO:0000259|PROSITE:PS51569" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 25..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 400 AA; 44793 MW; 4788AB38C62D9B31 CRC64; MSKVQQNFSV VSDDADKPGP LQPASVRSLR STTKRNASSE VAGPAPKIAV KVEKWTIESV CKNGRRLDLS SNEPNAASVI KTLFKEIHGS VLSKLNIHPL HWDECADSEL GPFLKTFNNS VKAFRKKNPR DVLLSKENWR QKEASEFRVI CDLACQLAIP NPRVLNTHYA GFSSGTYGET NIETLQKILD LLGVKEDDVF MDLGSGIGQL VTFAAAYTNI AHVRGIELQQ VPAGFADENV RQFKKLMRHF GEKPRPFELK LGDFNTEEIE TFLKEKATII FCNNLAFDPD LMIKLRAILQ FCNNGTKIVV TQKLETTKKG RTPRDCFFTA SADTILLFET DGSEKGNVSW TNNIVPYYLT TVDNYKPFRE AATRAKQEEA NRLAKLMCSK KNGAKHGEKE //