ID E2A766_CAMFO Unreviewed; 1330 AA.
AC E2A766;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 57.
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=EAG_06605 {ECO:0000313|EMBL:EFN70722.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN70722.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL437267; EFN70722.1; -; Genomic_DNA.
DR RefSeq; XP_011252754.1; XM_011254452.2.
DR STRING; 104421.E2A766; -.
DR EnsemblMetazoa; XM_011254452.3; XP_011252754.1; LOC105249170.
DR GeneID; 105249170; -.
DR InParanoid; E2A766; -.
DR OMA; LTQDYIL; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000000311; 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 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; 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:UP000000311};
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 12..329
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 331..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 536..563
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 589..616
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 335..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..919
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1063
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1330 AA; 147363 MW; 68FDB2123F74B822 CRC64;
MELRLHSPAG AEPIVYQWPL TSGSGSDRHD GALDVIETMR WVCEDLPDLK LPLENNILCN
YDPRDYESMK SLCDRFNRAI DSLVQLEKGT SLPSQRLNKR PSRGLLRHIL QQTYNQAVVE
PDKLNQYEPF SPEVYGETSY ELVCQMIDQI DVTDDDVFVD LGSGVGQVVL QMAAATLCKI
CIGVERADVP STYAQSMEVN FRKWLNWYGK RCGDYRLVKG DFLADEHRES ITGATIVFVN
NFAFGPTVDH QLKERFADLR DGARIVSSKS FCPLNFRITD RNLSDIGTIM HVSEMSPLKG
SVSWTGKPVS YYLHVIDRTK LERYFHRLKN NKQGGLDENS DSVISNTASN SSKVSNRNER
GDRAKRDLSR QLDSPNNSEQ QGTNSDSELD ENAIKNRRQP NKIRRKFNRK TSNGITRAPA
RGRQRGRGVK RAKPKKTINI SGLDLLHSQT LLSTSPQALG KKPPPAPGCV DQQLSSLTLS
LQSHSTSVHE ELSIPSAPSA TPYALQILLD LYRDQFMLML ESMRTPTYKV SVNTDIAKER
ERNSKLQSRA AQLEKQIKVL IDDSVALLKA RMTELGINAT SPGDLLAKAK EIVLRHKQLQ
AKASKLQAQV ASIETEQSRL VALRHQELQE KYNGNVNGIT NPPQSLTQDY ILKEISATLS
QRKRLHSQVS KLEHELNLLE RTSNEKQVAA IAQQQRDMIG SKHSQSLHHH QQGNKNGTTR
KSREGRSRSQ EWPDVPDIGK IQENNPEILA QKILETGRQI EAGRIPHRQS TNGNNNSRTR
LPQASLSFSN ASSANSSTPS PQTVNKDANR TQEPPRVANF EDRLKSIITS VLNEDQQNRT
KQQQMQLQVQ LQSQSEPDRK RAPLPQSVST PDYTQVSPAK LALRRHLSQE RISSSHSTSS
DRSTVDSRQS SSHDNRLVTS GSGLLVSTVG ELMNGEIERT LEISNQSIIN ATVDMSSIIR
PETVYSPISR PASAEGDAGL STLAHVASYV PTSGTSTSTP TTSSRSSVLF TPVTQPQRYT
PVQLPRADIK PYHESYFSDN PAQSLNQSHS APLPLHSSQT TSNGELLPVE GLAASLHARI
LNNHNNSGKT ESTLSNNTRF QPYPRYATNS NSGNANTTNA NAVTAICQSQ TSMSIKTEAV
VSSVSTSGAP LSPLVEPHSN TSTPLVDEPQ MTTQRQRNVV GDDDGEADWQ DRISSGFDRL
VAFASTELDK RRRSTEGVNT SPDSGLGSDS AVTGPPPVVP SPDEALGPPR TPSPTSPRPA
NLSSGNPPSS ASSSVPLKYQ RQPDPERHHF KKKFFHRDWN NSASTSKFRP KGKDWDWNHS
GQWPSNDEQS
//