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Database: UniProt/TrEMBL
Entry: Q23200_CAEEL
LinkDB: Q23200_CAEEL
Original site: Q23200_CAEEL 
ID   Q23200_CAEEL            Unreviewed;       313 AA.
AC   Q23200;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 3.
DT   24-JAN-2024, entry version 144.
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   Name=dot-1.3 {ECO:0000313|EMBL:CAA93538.3,
GN   ECO:0000313|WormBase:W06D11.4};
GN   ORFNames=CELE_W06D11.4 {ECO:0000313|EMBL:CAA93538.3}, W06D11.4
GN   {ECO:0000313|WormBase:W06D11.4};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA93538.3, ECO:0000313|Proteomes:UP000001940};
RN   [1] {ECO:0000313|EMBL:CAA93538.3, ECO:0000313|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA93538.3,
RC   ECO:0000313|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RA   Sulson J.E., Waterston R.;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
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}.
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DR   EMBL; BX284606; CAA93538.3; -; Genomic_DNA.
DR   PIR; T26226; T26226.
DR   RefSeq; NP_001333541.1; NM_001346618.1.
DR   AlphaFoldDB; Q23200; -.
DR   SMR; Q23200; -.
DR   STRING; 6239.W06D11.4.1; -.
DR   PaxDb; 6239-W06D11-4; -.
DR   EnsemblMetazoa; W06D11.4.1; W06D11.4.1; WBGene00012302.
DR   GeneID; 189244; -.
DR   UCSC; W06D11.4; c. elegans.
DR   AGR; WB:WBGene00012302; -.
DR   WormBase; W06D11.4; CE51782; WBGene00012302; dot-1.3.
DR   eggNOG; KOG3924; Eukaryota.
DR   GeneTree; ENSGT00390000013515; -.
DR   HOGENOM; CLU_046188_0_0_1; -.
DR   InParanoid; Q23200; -.
DR   OrthoDB; 2881295at2759; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00012302; Expressed in material anatomical entity and 3 other cell types or tissues.
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:UP000001940};
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          2..313
FT                   /note="DOT1"
FT                   /evidence="ECO:0000259|PROSITE:PS51569"
SQ   SEQUENCE   313 AA;  35283 MW;  021FAC02619E6CDA CRC64;
     MPVIHLSSAR KGNAEFKFPN TLHFRQTVKE MFEEIYKPIL DAVKVPLPSD AVVGNPDKFS
     QYIDALNLKL AHPDVLSRVP AKHHEITSTR LCSLTVAIKL AELAYRFSVP DANVLRHYAV
     GTSTVYGELH CSQMASFVDQ LNMGPSDYFM DLGSGIGHLV NFVAAYARTQ MSVGVELMDN
     LAEIAEKNKE FNERLLNHFG KKVYATRFIH GSFTSPAVIR EIQTKATVIL ANNVRFDPEL
     KLQLKEILMG CKDRTRIISS EPLVPSRARQ TNSRRADDFV KISDESLLNL VDNNVSWTSR
     KVPFYLTTIN RNK
//
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