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Database: UniProt/TrEMBL
Entry: E2A766_CAMFO
LinkDB: E2A766_CAMFO
Original site: E2A766_CAMFO 
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
//
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