ID A0A3B0KDD1_DROGU Unreviewed; 2289 AA.
AC A0A3B0KDD1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=DGUA_6G016780 {ECO:0000313|EMBL:SPP84239.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP84239.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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; OUUW01000008; SPP84239.1; -; Genomic_DNA.
DR STRING; 7266.A0A3B0KDD1; -.
DR OMA; TENMAHT; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000268350; 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 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 366..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1091..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1297..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1566..1591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1841..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1948..1977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1989..2128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2210..2289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 692..726
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 375..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1032
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1343
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1671..1687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1716..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1788..1810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1841..1860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1868..1890
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1955..1977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1989..2100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2258..2289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2289 AA; 247604 MW; 751BF906BE53B051 CRC64;
MATPQVKDLV LRSPSGSSET IAYAWPLQIG HGQDKHDNGI DIIDTIKFVC DDLPSIQSAF
EEINLNQIDT ACYKTMTNLV DRFNKAVDSI VALEKGTSLP AERLNKFAHP SLLRHILQLV
YNAAVLDPDK LNQYEPFSPE VYGETSYELV QQMLKHVTVG REDTFIDLGS GVGQVVLQMA
GSFPLKTCIG IEKADTPARY AERMDLFFRQ HMGWFGKRYC EYKLIKGDFL VDEHRENITS
STLVFVNNFA FGPTVDHQLK ERFADLRDGA RVVSSKSFCP LNFRITDRNL SDIGTIMHVS
EIPPLKGSVS WTCKPVSYYL HVIDRTILER YFQRLKTKGG NDHHEHVGTV RTTRDRAKRE
ANIGQQHNNH HHHNNNHNNN QNNNNNQQRE REQSSGPTGA TNNQRHQSQS PANVSGGGVG
GGAAATAAAS KTRQQLQQQQ QQQQQQQRSL DMESSTESDG EATNGNGGNT TTATTATSVS
NGGGGGSSGP MTRRPWYDFS SSKGKSSQSD DEENNNSNSN GGNTSVTGVR QARAATQKKR
KKLTRKAAIA SKSAAAAQRE AEAAAAAALA SKESSSKEDA PRAASAGPGR KGRMKKGAGG
RGRKSLKIVG LDALHNQTVL STTQDTAAKK LPAAPGTVDQ QLTSLLTETM SHRELDIPAA
PQDTPYGLQI LLECLRSQYM SFMDVMKSSA YLPQIQKNIA QEQERMSRLK NRASQLDKQI
KVLIDDSVAL LKVRMNELGI NVNSPNDLIA QAKEIVGRHK DLQHTVSKMR NEVTFYEGEQ
KMLLSKQLKN LPEYQKLCGN GPINGKVKLE LPSEFSETTA HELVLKEIAN TLSQRKKLYA
QVSTIEQETT VLQKSAEDRS TAASLLAQGT NISLATSSSS NSSSNGSSAV SASSTASNSA
LNPTPPKANS AKSSRRSREH RVRSQEWPEV PEVGKIQEEN PEVLALKIVE TCRQIEAGTF
QAKTSVPPYQ LNGKNKEPHM PQMPVGAASA SNKSAPGGAA GGHHYKDSTL MPAPKQQQQQ
QQQQQLQVQQ LQGAPSMLPK CELPGMGMGM GLGLGMGGLS SAAISAACRK QESPKVANFE
DRLKSIITTA LNEDQEQRSK AIPAEMPSQP SPSPLQSPVS KRSKQHHQQQ QQQQQLPPSN
LHNVITVSTQ GLMHLNANTT ISPITPPLPG PGAGATASTA PPPPPNLPYG AYGGKSTPSG
KYQASKEQFN KYSPARQHTP SSGAASVPPP PPPQVPVSSH MAALYAAGQP TAPTPADLGY
QRRRSSMSAS SYEHFIVQQQ QQQQQHALML AAAAHVAQRQ RVEEHHQQQQ QQQQQQHRLQ
QQHQQQQQHL HLHHHHHQHH PHSHPQEFKA PPSDNLLQRS SSRDQLVEPP PQQQHMELLP
RASSANSDYG AYRVRPPSRP SSNSSQPDYT QVSPAKMALR RHLSQEKLNQ HVTPQPTPPP
QGPLPQPPPT GKTIGDLVNG EIERTLEISH QTIINAAVNM STSGTQFMDR AFNERATSNE
RLLINLNAQR PERVHVRPLS EESQEAHPTN YVSSGGAAAA QAAAAGQGSN NSNLATLAHV
AYVQKSAPQS GGRTAAPATP TPARSGRDSY QTVALPRAEM KGCIEAYFHE EQKTKNVGGG
GAGATAGGAA ALRGPRLNGA NPPLEGLAAS LQDHVRARKY KEETEERQRR AAAAASSSSS
SSTATPSAVV ADLQQHYGQA PPAHSYLHHP IHHGAANLNG SNNSSSSTPH KLELGVKRTS
PLAPHQQPPR PSKIPHYEQP PHVHAHSHLY ANGGQVLPPP PSHDATTPSP TPSSSSSSCG
RRSNNNNGKM HVEPPLLMSP EINSLMGDER PLQLSTNPHH LMQQQQHHHQ QQQQHHIHQQ
QHLRVAAHLG HSHGHGHGHN PSHGHSHSHS HSHSTTPTLG VMQRNANANN AADDDDVIAA
DDESHWQHRV SSGFDRLVAF ASTELDKTRR SIDGDTVPAS ISCNTSPDSG ITHSSSNSDA
VRTFLSTSSS SSQLELPIGS GGSGSSSHSL YGSNQVHNLS NHLQQHNSSG SGSSSSGGSN
SSANNMVHHH QQQQQPLQQL QSQQHQHQHQ QQQHHQMTDH LSDSSMKSTA GSSLKTVSPV
DPSAIDSPPL SDVGLPRTPS PSAASVATPP LANAPLGLGN ELGIPLKYQR KSKSGSEKHY
KKKFCERNWE YDCDELLAYS NSSAPPTAAD AAGNGPPALL ETPSVVGGVV ANMMGGKSGK
SPKEKSSPHH SANHNAGYHH KSSKFRPKGK DWDWSLDSRS QTGDGLLPPT CPPNGANNNN
NNNTTTSSN
//
