ID A0A1U7R0T1_MESAU Unreviewed; 1740 AA.
AC A0A1U7R0T1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|PIRNR:PIRNR037123};
GN Name=Dot1l {ECO:0000313|RefSeq:XP_005083345.1,
GN ECO:0000313|RefSeq:XP_012978459.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005083345.1};
RN [1] {ECO:0000313|RefSeq:XP_005083345.1, ECO:0000313|RefSeq:XP_012978459.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-79' of histone H3.
CC {ECO:0000256|PIRNR:PIRNR037123}.
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|PIRNR:PIRNR037123, 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|PIRNR:PIRNR037123,
CC ECO:0000256|RuleBase:RU271113}.
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DR RefSeq; XP_005083345.1; XM_005083288.3.
DR RefSeq; XP_012978459.1; XM_013123005.2.
DR GeneID; 101827360; -.
DR KEGG; maua:101827360; -.
DR CTD; 84444; -.
DR eggNOG; KOG3924; Eukaryota.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0031507; P:heterochromatin formation; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd20902; CC_DOT1L; 1.
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; IPR021169; DOT1L/grappa.
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 PIRSF; PIRSF037123; Histone_H3-K79_MeTrfase_met; 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|PIRNR:PIRNR037123}; Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR037123};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037123};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR037123};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037123}.
FT DOMAIN 16..330
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 336..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1150..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1591..1627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 565..637
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 392..417
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1029
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1354..1374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 159..168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 222..223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
SQ SEQUENCE 1740 AA; 185373 MW; 1E23FAA1AF0A0542 CRC64;
MGEKLELRLK SPVGAEPAVY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD LKLAMENYVL
IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNT RPSNGLLRHI LQQVYNHSVT
DPEKLNNYEP FSPEVYGETS FDLVAQMIDE IKMTEDDLFV DLGSGVGQVV LQVAAATSCK
HHYGVEKADI PAKYAETMDR EFRKWMKWYG KKHAEYTLER GDFLSEEWRE RIANTSVIFV
NNFAFGPEVD HQLKERFANM KEGGRIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLK
GSVSWTGKPV SYYLHTIDRT ILENYFSSLK NPKLREEQEA ARRRQQRESK SSATTPTKVS
ESKAAAAAAA EAPVDSGAEE EKSGVATVKK PSPSKARKKK LNKKGRKMAG RKRGRPKKMS
AANAERKSKK SQSSLDLLCS PPADPPSASP QDAYRAPHSP FYQLPPSTQL HSPNPLLVAP
TPPALQKLLE SFKIQYLQFL AYTKTPQYKA NLQQLLDQEK EKNTRLLGTA QQLFGHCQAQ
KEEIRRLFQQ KLDELGVKAL TYNDLIQAQK EISAHNQQLR EQSEQLEKDN SELRSQSLRL
LRARCEELRL DWSTLSLENL RKEKQALRSQ ISEKQRHCLE LQISIVELEK SQRQQELLQL
KSCVPPDDAL SLHLRGKGTL ARELEADAGR LRLELDCAKI SLPHLSSMSP ELSMNGHVAA
GYELCSAASR PSSKQNTPQY LASPLDQEVV PCTPSHSGRP RLEKLSGLAL PDYTRLSPAK
IVLRRHLSQD HTGASKAAAS EPHPRAEHTK ESTLPYQSPG LSNSMKLSPQ DPLPASPASS
PLTSEKGSEK GVKERAYSSH GETITSLPVS IPLSTVQPNK LPVSIPLASV VLPSRAERAR
STPSPVPQPR DASSTLEKQT GASAHGAGGS AAGGRSLALA PTGFYAGSVA ISGALANSPA
PLASGMEPAV FDEPSGPGSL FAIMASRSTP PQLPPLLPQP RNSGPASPAH QLSASPRLSV
TTQGPLLDTS KGELPSEPAF SDPESEAKRR IAFSITASSS SKQSPSTRHS PLASSTRGDC
VQSHGQDSRK RSRRKRAAAG TPSLSTGVSP KRRALPTVAG LFTQSSGSPL NLNSMVSNIN
QPLEITAISS PESSLKSSPT PYQDHDQPPV LRKERPLGPT NGAHYSPLTS DEEPGSEDEP
SSARIERKIA TISLESKSPP KTLENGGGLV GRKSAPSSEP VNSSKWKSTF SPISDLSLAK
AVDSPLQAGS ALSHSPLFSF RPALEEPAAE AKLPTHPRKS FAGSLAAAEG PSPGANPPNG
LAFSGSLAAD LGLHSFNDGA SLAHKGPEVA SLSASVSFPS QRGKDSTTEA NPFLSRRQPE
GLGGLKGEGS AGKESGETLS LCGPADKVAL PHGSGRGSKG RDRELDFKGG HNLFISAAAV
PPGGLLGGPG LVTVASSVGS VTPAAQAPRP FLSTFTPGPQ FTLGPVSLQA NLGSVAGSSV
LQSLFSTVPA AAGLVHVSST ATRLTNSHTM GSFSSGVAGG TVGGVFTHAV PSASAHPFGA
GVGSGAVCSS ATLGLSPLQA AASTSASSFQ AAASVETRPP PPPPLLPPQH LGRPPAGPPV
LHAPPPNVAL PPPPALLASN SEPVLLQSLA SLPANKAFLP PSSAASLQPA NASLSVKLAS
LPHKVSRPSF TVHHQPLPRL ALAQAAPAAP QASSSGPSAV WVSLGMPPPY AAHLSGVKPR
//
