ID Q174S1_AEDAE Unreviewed; 1707 AA.
AC Q174S1;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 24-JAN-2024, entry version 101.
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=AAEL006783 {ECO:0000313|EMBL:EAT41580.1};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EMBL:EAT41580.1, ECO:0000313|Proteomes:UP000682892};
RN [1] {ECO:0000313|EMBL:EAT41580.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT41580.1};
RA Loftus B.J., Nene V.M., Hannick L.I., Bidwell S., Haas B., Amedeo P.,
RA Orvis J., Wortman J.R., White O.R., Salzberg S., Shumway M., Koo H.,
RA Zhao Y., Holmes M., Miller J., Schatz M., Pop M., Pai G., Utterback T.,
RA Rogers Y.-H., Kravitz S., Fraser C.M.;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EAT41580.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT41580.1};
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
RN [3] {ECO:0000313|EMBL:EAT41580.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:EAT41580.1};
RG VectorBase;
RL Submitted (SEP-2012) 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; CH477406; EAT41580.1; -; Genomic_DNA.
DR RefSeq; XP_001652229.1; XM_001652179.1.
DR STRING; 7159.Q174S1; -.
DR PaxDb; 7159-AAEL006783-PA; -.
DR VEuPathDB; VectorBase:AAEL019732; -.
DR eggNOG; KOG3924; Eukaryota.
DR OMA; LNGTPHK; -.
DR PhylomeDB; Q174S1; -.
DR Proteomes; UP000682892; 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; cd02440; AdoMet_MTases; 1.
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 18..332
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 335..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1559..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 551..585
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 618..645
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 675..702
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 335..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 835..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1707 AA; 189355 MW; 49BD9987B3EDC97E CRC64;
MATPNYKELK LQSPAGAEPF LYNWPFSIGG GNDNGGMELI ENVRWVCEDM PEIKSAIEEI
NLNDIDTGDY DAMKNLCDRF NKAIDSVTAL EKGTSLSNQR FTYPSRGLLR HIVQQVYNQA
VVEPEKLNQY EPFSPEVYGE TSFDLICQMI DEIKITADDV FVDLGSGVGQ VVLQMAASTP
VKICYGIEKA DVPSRYAEGM NATFKMWMRW FGKKYGDYEL IKGDFLADEH REKIMSATIV
FVNNFAFGPN VDHQLKERFA DLRDGARIVS SKSFCPLNFR ITDRNLSDIG TIMHVSEMTP
LKGSVSWTGK PVSYYLHIID RTKLERYFQR LKTKGNENDN QASGSTNTRA SRSRKDKCEK
AVTNDESTSD SDAEPAGPPN RKQPWSDWCS GKEKESSQSE EENNNSPVLR NGRIPVATKK
RKKITRPKTV KKDPVAQAAQ QAAKEAQAAV TKRRGRVKKG RQRRALKING LDLLHSETLL
STSDQAIGKR LPPAPGCVDQ LLTSLAGDMQ HTELDIPEAP SETPYGLQIL LDLYKTQFMK
AIESMRKSSY KDNVQQQIER EKERNQRLLN RAGQLEKQIK VLIDDSVALL KARMNELGIS
TTSQNDLLCK AKEIVGRHKE LQVMAAKLQN QVTSIEQEQK RLVMQHVQRI ADKYIKTEDV
EMTPKTSHEL VLKEIANTLS QRKKLYAQVS SMENELNVIE KLAEERKAAA VLQTTIVTHQ
RGEQPLQQPS GSSRSQRKSR ENRTRSQEWP EIPDIGKIEE NNPEILAQKI LETGRQIEAG
KLLANSASKH QKERESKNHH LQQQYQQSQQ THQLPHHTHP ADAALMPAPA TLSKSHHRGG
STTNIKSESR SKLQDSHKVV NFEDRLKSII TSVLQAPPKS IGSGGGLQQQ QQPPPHQGSS
QHHMREVSQP MLLGHGEHAS PTKSSSSYGK TVYLTSGPPP PPSSMHNSLH DMGPRNSGNQ
HHLPHPSSGG QTSQPPSQFS SLMNPVTTAH HLNATTTITS SPISPYKGHG SSQRANSTHQ
QILQQQERDR ELRQTQMAMH YGSHSGQPHP NVVDPHLLHR SALEGKMEFK APEQFRYDHR
NPIEPPMGGQ SHSRSSSATS LEGDYSSAGS NLRYVNVPTN PQQQPQQVPL QQQQLSGGNN
SRPGSSSSQP DYTQVSPAKM ALRRHLSQEK LTHPMPPSSN TVKTIGDLVN GEIERTLEIS
NQSIINAAVN MSTAGPSGHT VINTNVQRPE RVSIRVLEEA GLNGSVQASS YSPVSRPSSR
EMTKSPVHLH GQSNLATLAQ VATYNHKKAS SSSSSSSSSA AVISPRGGPV QQPVDNRGHS
TSTQQYPQTA PHASVVYQPS RGGEKPSYSS SSDRHGAEPT YMALPRADIK PHLDSYFIDE
HKRQQQQQQQ QQQQQHQLHR QDSAAVGSHL PPTSHHQTGS SGMRVTMGDM YHRGHAVSAM
EQSHPRREPM ASQAIDDRMN GSPPLEGLAA SLRARVIAQL NSKDEDVERH RRPDLGAPMH
TGPVNSNNTI QLVQAPHVKT EKYSAGIKRT SPIIENPPRP PKMLYTDCSD AMVNSDLLHV
GRSGSGSSRG MGPLMSPEIN SLSAVDDRQH LMRHGRNDVD GSSSSSSNVA GLHQQQPTSS
SSVTVINLPY GSGGMSSANT GCSNPPSQRN YNHHQQQRPM QPQHQQQQQQ QSHQQYRVQS
RNDGQIPPAQ RHHHYAPNKY PPNSYSK
//