ID A0A1I8M6Q1_MUSDO Unreviewed; 2607 AA.
AC A0A1I8M6Q1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 45.
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 Name=101896384 {ECO:0000313|EnsemblMetazoa:MDOA001796-PB};
GN Synonyms=LOC101896384 {ECO:0000313|RefSeq:XP_011290411.1,
GN ECO:0000313|RefSeq:XP_019890544.1};
OS Musca domestica (House fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Musca.
OX NCBI_TaxID=7370 {ECO:0000313|EnsemblMetazoa:MDOA001796-PB};
RN [1] {ECO:0000313|EnsemblMetazoa:MDOA001796-PB}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|EnsemblMetazoa:MDOA001796-PB};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_011290411.1, ECO:0000313|RefSeq:XP_019890544.1}
RP IDENTIFICATION.
RC STRAIN=Aabys {ECO:0000313|RefSeq:XP_011290411.1,
RC ECO:0000313|RefSeq:XP_019890544.1};
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 -!- 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 RefSeq; XP_011290411.1; XM_011292109.2.
DR RefSeq; XP_019890544.1; XM_020034985.1.
DR STRING; 7370.A0A1I8M6Q1; -.
DR EnsemblMetazoa; MDOA001796-RB; MDOA001796-PB; MDOA001796.
DR GeneID; 101896384; -.
DR KEGG; mde:101896384; -.
DR VEuPathDB; VectorBase:MDOA001796; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000095301; Unassembled WGS sequence.
DR Proteomes; UP000694905; 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: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:UP000694905};
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 19..336
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 339..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1225..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1430..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1599..1685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1804..2182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2241..2352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2453..2482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2511..2607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 689..716
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 820..854
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 362..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1518
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1636
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2019..2037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2055..2075
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2090
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2131..2161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2246..2308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2315..2352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2538..2607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2607 AA; 283210 MW; 8472EB72F79156E4 CRC64;
MAAPQVKDLV LRSPAGSSEV ITFSWPLQVG TGSDRHDNGI DIIDTIKFVC DELPSISSAF
EEINLNHIDT ACYKTMTNLV DRFNKAVDSI VALEKGTSLP AERLNKFAHP SLLRHILQLV
YNFAVLDPDK LNNYEPFSPE VYGETSYELV LQMIKHVNVT NDDTFIDLGS GVGQVVLQMA
GSFPLKSCIG IEKADTPARY AERMDMFFRQ FMAWFGKRFC EYKLLKGDFL VDEHREKITS
SSLVFVNNFA FGPNVDHQLK ERFADLRDGA RIVSSKSFCP LNFRITDRNL SDIGTIMHVS
EIPPLKGSVS WTCKPVSYYL HVIDRTILER YFQRLKTQKG AENDHVGGST RTTRDRAKRE
ANNQANSQNS NSSLTARTNS PAAHAKDNNS NSNSNNSGGN NNNNNSNTGT TTSNTTTTTS
STKTRQQQQQ QQQQQQQRSA EMETSTESDG DAATTNGGNS NGSGGPVTRK NWSDWASSKG
KSSQSDEEEN NNQTTTTSST RTVRTTTQKK RKKLTRKAAI ASKSAAAAAQ REAAAKERAE
AAAAAAKDNS SNQDGGGNNS AGGSSSAKGT SAGSAGTAAG RKGRLKKGAV RGKRCANIAG
LEILHKQTLL STSIEAMSKK LPPAPGCVDQ QLTSLLTDNM AHRELDIPTQ PNDTPYALQI
LLDVFRSQYM AMIEQMKSKS FVPSIKRQIQ LEQERKQRIK NRASQLDKQI KVLIDDSVAL
LKVRMNELGI NVSSPNDLIA KAKEIVGRHK ELQGVAKKIQ SQVTACEMEQ RRLLKKHLQH
LPEYQLLYGA NGKTKLHDVP GGGGGELSEA AAHELVLKEI ANTLAQRKKL VAQVSSIEKE
AKSLEKAAEE RRATAALLAQ GTNIIVANNN SSACSSSSRS SSAMDVSPAN QPLQLTTHNH
VNTTTISINH VANTNCSSAS SSSSSSLSAA TASVVGSAGP SSTPSTSLVP NNATIQPSIT
VTKTTSNTGK SGRKARDHRS RSQEWPDVPD VGKIEESNPE VLAQKILETG RKIEAGKLAK
QQQLQQQQQH HQQQQPLALN NHHHYQMQAQ HHLPHAAAAA HQQHQQQHHH HPQHHPEDKP
YRKKHERSAS NEHLPSIGGA YAAQYSGQQH PDAATLMPAP KQRNSGGLEQ PMNLNNSNNN
AMRALNGPGT VGSSSSILPK CEMPGMRKNH ASPAAVVSIQ ESPKVANFED RLKSIITSAL
NEDQEQRKAQ QVNQVQVDIT PIQQSTTTAA KRQKHAAPPP SLPQSNHNSL SNIINVATHS
MTHLNATTTI SPINTTLPPP PQSGSHNKYA SGGVGSASSK AMLHPLNTTS SGVMNSTASK
SNSSSTAKYG HHPNHIGGPP HLNSSSSSSA NNHPYGHPAE HNMLRRRSSI SAASYEQYMA
QQQQHQHHHM NQNLHHHHQQ QHQQQQPLMM NANTHNNMAL EFKQPPLENH LAHQQRSSSR
EMLIDETQPV RSSSANSDSA LSYYPPTRDR LMSMERSNSR ESATAGQHLG GGAQQQQQSQ
QPPSRPSSNS SQPDYTQVSP AKMALRRHLS QEKLNQHMPP GSAGAGGGGM ASKTIGDLVN
GEIERTLEIT HQSIINAAVN MSTVGNASGE RNPYLLERSI YGSSHDLQRE RDRSNERERE
RERERERERE RMIINSNAQR PERVHVKLMD EAGQHGGPGA APPQQPPNAS AGNYAEISPR
NAGEPKSAYA HNLATLANVA YQHKSMVGSN NNAVAGGAAA AAASSTAASS SSSSSSSRHY
NNREREASSY HSAASNAKMP ANMTNSSNTS TASSSGAAPN NRDYQPVALP RAEMKPCIEA
YFQEEQHQHH SSSSSHSHKS NNKEKHSNRG NRMNGTNPPL EGLAASLMAS RKFREEHEER
QKRAAAASST SGGATNGNNN NNSGHNAEHN VNHNQMHHYA SNNNNAYGGG GSGHHQQPTS
TNHNSHHHQH NGTPMKVELG VKRTSPMTNH HPRPSKIPHY EQQSHMGNHH NQQQQQLQAG
NTTSSVNPYA NTNGGGLNHH HHPHHSQHAA GGHQVAGGYP QHSPSSSSAQ QHRRGNKQTV
EPLLMSPEIN SIMGGDDGRS SSSSSSANHG GRPTVNNSHH QHHHQHNKQQ QQQHGHGQSH
YHQQQQQHQS QQQQQHQNNN NNHHIHQHSQ HHQQQQQQLL HHHNSLTNST PMTNNNSHHQ
QQQQHHNHHH HQQHLSHNST SNTSAAAVLT NTNTNPTVVG GRAADDDDVI AADDETHWQH
RVSSGFDRLV AFASTELDKT RRSIDNDTVP SSISCNTSPD SGITHSSSNS EAARTFLSTS
STSSQLDLPI SSGSSTSSGN SSFMGGHLSA GHHNSLHHHS SSSSSLHPDH LSDSSMKSSH
SGDMMSSSLP ITLKNCSSPA DVSVSAIDSP PLSDMGLPRT PSPTVTVNTP PPGGLMMHGH
NLDASGGLKI PLKYQRKSKS SSEKHYKKKF CERNWEYDCD EILAYSNSSS TAAADAAGTT
TPGAATNSNS THNGPSLLEN NSSSAVDQID GLAAAMAHHN NNKDLDNISL QQQQQQQNAV
QQHHKSSKFR PKGKDWDWSM DSNSSNISAS GHKSKSSSSM DMSNNNNNNS NNMMASSSSS
TGNINSNNNT NNNNNLSLHS QKTSIIN
//
