ID A0A0K0E525_STRER Unreviewed; 994 AA.
AC A0A0K0E525;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
OS Strongyloides stercoralis (Threadworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC Strongyloides.
OX NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000460900.1};
RN [1] {ECO:0000313|WBParaSite:SSTP_0000460900.1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (AUG-2015) to UniProtKB.
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 AlphaFoldDB; A0A0K0E525; -.
DR STRING; 6248.A0A0K0E525; -.
DR WBParaSite; SSTP_0000460900.1; SSTP_0000460900.1; SSTP_0000460900.
DR Proteomes; UP000035681; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR Gene3D; 1.10.260.60; -; 1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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:UP000035681};
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 28..362
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 755..796
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 7..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 994 AA; 112431 MW; 43F29B64A270D8C4 CRC64;
MSSSKEASNE VHKKSGDELD RGPPKTEKKL KLSSPYGGES LYYFWNYEEK YKNKNKVIVV
EIVDLVRITK HKIKEINDVL KQHGHDIKSI EPYYNLENLR ILCRTFNKAV KQLGETYHNT
SKGDNSNKLG SSSNEQFQEI INRVYNKAVV DVNALNKHYG AFSSETYGET TWRRMATILE
ELKLTDKDVF VDLGSGVGQI VCQVAGSSKV GKAIGIEIAD LPAKYARRME FEFSRLMRWH
NKTFRQFKLY HGNFLDTKYR KLITEEATVI FINNYAFHEK LNMEIKRNLL HDLKDGVKVI
STKPFVIHKE ITERTLNDVS SIMNISEFKP VNCPASWTNK HVPYYLQIVN RERLLEYFNR
QKKARDLREM KETRASRGSS VSSTRIEASD DRKSSIDGKE PTKHKESKSN NKDKDKDSGH
ERSKNHKDDK DIKDVSVNSK ESGINESSTK DNNTTKEGSK KVVTDDDTEV VYGATTRKKW
KAIIGEMAEK EKPPHTSSCS NTTTTSTSTN DSQDVITTPS TTPLTSEIDM KRKGSVSEFS
KEKPKIKHGQ RGRPKKIVTI INGEQVTKND KVEVKITQED KEALELMEKL SEEAIEKVSH
EKSNNGTLVI DKPLQHIDDQ STIGVETDDE KDHSKDNNVV VVEVPEIDPP IEDVTNIPYI
PSKDPLIIKS VDIVLEEQRQ EILKFIDFMY SDDFRRQTEI KILKQRQLRE SKVQKINALK
TMIALQQEEG KQLLTTRIKE VGIDAKTAPE FIDAAKLIVE TNKIKQKRLA NLEREIAAAE
RTYEEYQARI NAKNAHDKSI TDVINSIANE NMIEDSIDSI INSVANNSLP SSTSESYCNT
PTPSIDYLTQ RRNVRGRSVV RSGGGKKVGG NKKGSTDKST PDITDVESQV ENILKKIQNQ
SKEQESLKSQ QRLKSDSKKR SNAVGISSTT QASLSSVNPI PTKKKRSNSS INSSLSRSKS
PQLNVNLENS SVNNVNSKQS LLSTTNVSSE EIPT
//
