GenomeNet

Database: UniProt/TrEMBL
Entry: B4QYB7_DROSI
LinkDB: B4QYB7_DROSI
Original site: B4QYB7_DROSI 
ID   B4QYB7_DROSI            Unreviewed;      1838 AA.
AC   B4QYB7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-NOV-2023, entry version 83.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|PIRNR:PIRNR037123};
GN   Name=Dsim\GD19874 {ECO:0000313|EMBL:EDX11874.1};
GN   ORFNames=Dsim_GD19874 {ECO:0000313|EMBL:EDX11874.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX11874.1, ECO:0000313|Proteomes:UP000000304};
RN   [1] {ECO:0000313|EMBL:EDX11874.1, ECO:0000313|Proteomes:UP000000304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=mosaic {ECO:0000313|Proteomes:UP000000304};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
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   EMBL; CM000364; EDX11874.1; -; Genomic_DNA.
DR   SMR; B4QYB7; -.
DR   STRING; 7240.B4QYB7; -.
DR   HOGENOM; CLU_001460_1_0_1; -.
DR   OMA; LNGTPHK; -.
DR   PhylomeDB; B4QYB7; -.
DR   Proteomes; UP000000304; Chromosome 3r.
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; 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:UP000000304};
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          19..336
FT                   /note="DOT1"
FT                   /evidence="ECO:0000259|PROSITE:PS51569"
FT   REGION          338..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          555..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          971..996
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1033..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1223..1331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1343..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1430..1461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1479..1502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1523..1553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1567..1708
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1725..1751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          682..716
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        338..366
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        890..906
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1033..1050
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1239..1257
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1273..1287
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1295..1330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1680..1702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142..145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT   BINDING         165..174
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT   BINDING         192
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT   BINDING         228..229
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
SQ   SEQUENCE   1838 AA;  200337 MW;  B16E9E25ED3E505E CRC64;
     MATPQVKDLV LRSPAGSSDV ISFAWPLQIG HGQDKHDNGI DIIDTIKFVC DELPSMSSAF
     EETNLHQIDT ACYKTMTGLV DRFNKAVDSI VALEKGTSLP AERLNKFAHP SLLRHILQLV
     YNAAVLDPDK LNQYEPFSPE VYGETSYELV QQMLKHVTVS KEDTFIDLGS GVGQVVLQMA
     GSFPLKTCIG IEKADTPARY AERMDVIFRQ YMGWFGKRFC EYKLIKGDFL VDEHREKITS
     STLVFVNNFA FGPTVDHQLK ERFADLRDGA RVVSSKSFCP LNFRITDRNL SDIGTIMHVS
     EIPPLKGSVS WTCKPVSYYL HVIDRTILER YFQRLKTKGG NDHESVGTVR TTRDRAKREA
     NVGQHHHNNH HSNNHANSNN HQREREQSNG ATATAAHQQR HQSQSPANVS GAGIAVAASG
     QQAASKTRQQ LQHQHNQQQR SLDMESSTES DGEATNGNGG NTTTATNTTS ASNGPMTRKV
     WSDWCSSKGK SSQSDDEENN NSNSNGGSNG GSIGGGSVGR QARATTQKKR KKLTRKAAIA
     SKSAAAAQRE AEAAAAAASS VPSKESSSKE DPPRAASAGP GRKGRMKKGA RGRKSLKIVG
     LEALHKQTVL STSLDTMTKK LPAAPGTVDQ QLTALLTENM SHAELDIPTA PQDTPYALQI
     LLDVFRSQYT SMIEHMKSSA YVPQVQKQIA QEQERMARLK NRANQLDKQI KVLIDDSVAL
     LKVRMNELGI HVNSPNDLIA QAKEIVGRHK DLQHTASRMR NEVTFYEGEQ KLLLNKQLKN
     LPEYQKLCGT VNGKVKLEVP PELSETTAQE LVLKEIANTL SQRKKLYAQV STIEQETSVL
     QKTAEERSTA ATLLAQGTNM IVSTGSSSSS STTVCASAVT AQSNKLNSVK NSRRSREHRA
     RSQEWPEVPE VGKIQESNPE VLAQKIVETC RQIEAGKFQG AAAPSSQVNG KNKAIIEVPP
     PPPTVPVSIK SSPGHHYKDT TLMPAPKQQQ QQQMTLSQLP KCELPGLSAS RKQESPKVAN
     FEDRLKSIIT TALNEDQEQR SKAVESSPSP SPLHSPAPKR SKQHPAGAIN PAQSLPNNLH
     NIITVSTQGL MHLNANTTIS PITPPLPGPG AGATASTAPP PPANLPYGAY GGAVAKTTVS
     GKYQAAKEPK YSPVRQAPLP PPPPSHMASL YPAGQQTTPA DLGYQRRRSS VSATSYEHYM
     VQQQQQLQQQ QLMLAAAAHA AQRQQMRVEE QQQQQQHHQQ QQHHHHPQHR LPQHVQHQHP
     HHPNEFKAPP ADSHLQRSSS REQLIVEPPQ TQPLELLPRA SSANSDYSGY RIRPPSRPSS
     NSSQPDYTQV SPAKMALRRH LSQEKLSQHV TPQATPPLPG HGGAPTSGKT IGDLVNGEIE
     RTLEISHQSI INAAVNMSTS GASFMERAFL NERSNDRLLI NLNAQRPERV HVRPLSEESQ
     DPQPTSYAQE RGPGVGAAGG NSNLATLAHV AYAQKAQGGA RANAGTAPPA THSSSARSGR
     DYQPVALPRA ELKGSIEAYF HEEQQQKQSK GAGSAGASSL RGPRLNGANP PLEGLAASLQ
     DHVRARKYKE ETEERQRRAA AAASSSAGPP PGMELPTHYA HQAPPAHSYH HHGASINGTP
     HKVELGIKRS SPLAPHQQPP RPSKLAHYEP PTTQQQHAHA HLYANGQVLP PPPAHDATTP
     SPTPSSSSSS CGRRSNSNNG KLLVDPPLLM SPEINSLLGD ERPLQLSHHQ QQQQQMLHHH
     QSQQQQHLQL TQQQLRVAHL GHGHSTMPTL GVQRNGNGNA ADDVNDLATQ RTITNYDPRR
     RLRTTLSGPT KLSAAHSNQN LNGYVMADSS SSCPTVPQ
//
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