ID Q7PTQ0_ANOGA Unreviewed; 2137 AA.
AC Q7PTQ0;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 5.
DT 08-NOV-2023, entry version 119.
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=AgaP_AGAP003282 {ECO:0000313|EMBL:EAA03558.6};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA03558.6};
RN [1] {ECO:0000313|EMBL:EAA03558.6}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EAA03558.6};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EAA03558.6}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA03558.6};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA03558.6}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA03558.6};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EAA03558.6}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA03558.6};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EAA03558.6}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EAA03558.6};
RG VectorBase;
RL Submitted (MAY-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAA03558.6}.
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DR EMBL; AAAB01008794; EAA03558.6; -; Genomic_DNA.
DR RefSeq; XP_307790.5; XM_307790.5.
DR GeneID; 1269184; -.
DR VEuPathDB; VectorBase:AGAP003282; -.
DR HOGENOM; CLU_001460_1_0_1; -.
DR OrthoDB; 146338at2759; -.
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};
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}.
SQ SEQUENCE 2137 AA; 227396 MW; 4B060F516452B213 CRC64;
MATPNYKELK LQSPAGAEPF LYNFPFSTVM GTGHDSGAEL IENVRWVCED MPEIKSAIEE
IDLNNLDTNN YDAMKNLCDR FNRAIDSVAA LEKGTSLSNQ RFTYPSRGLL KHILQQVYNQ
AVVEPEKLNQ YEPFSPEVYG ETSFDLICQM IDQVKITADD VFVDLGSGVG QVVLQMAAST
PVKVCFGIEK ADVPSKYAEG MNTTFKLWMR WFGKKYGDYE LIKGDFLADE YREKITSATI
VFVNNFAFGP NVDHQLKERF ADLRDGARIV SSKSFCPLNF RITDRNLSDI GTIMHVSEMS
PLRGSVSWTG KPVSYYLHII DRTKLERYFQ RLKTKGTENH TDGTSGGGSG SHSTRSSRSR
KDNNTNHHHH HPKVITNDDS TSESDTDVVG PTTRKAWSDW NSGKEGKTSP SEEENNNSPV
LRNGRIPVAT KKRRKITRTK AAGKKAELAA ASAAAAAAAA AAAAAANRDM GVGTSAASAA
AAAAAAMAGG KKRGRVKGKG RQRRPLNIAG LDLLHNETLL STSEQMIGKR LPPAPGCVDQ
QLTSLAGDMQ HNELDIPEAP SETPYALQIL LDLYKTQFMK TIEAMRKPSY KDNVQQQFDR
EKERNQRLMN RAGQLEKQIK VLIDDSVALL KARMNELGIS TTSQNDLLCK AKEIVGRHKE
LQVMAAKLQN QVNVIEQEQK RLVMQHLTKL TVEQQQQHQQ QQQHQQLHPH QPYIKQEDAE
LTSSSSNELV LKAIASTLSQ RKKLYAQVSN LETELNLIEK LTEERKSMVV GLSAAAPNSN
HNSASSTAAA AAAAATSTII SVARATEVRD REQYGHAGQL HPATIGGGRE REHIHPDGTT
TSKHTSDPVR TLPAGAAAGP VGVAGSAAPL PPPPMAGVGS ASVTVPSTPT KQGSGGGSSR
SAQRKSRENR TRSQEWPEIP DIGKIEENNP EILAQKILET GRQIEAGKLF AAGKHASKER
SSEGKLAPVV TAGHGSSAAA GTAAPQHIAH PPTVGAPAPQ QQPYPHHHQQ PHSQPSQPPV
HPHLHHPDTA LMPAPASTIN KAHHHHRSNS GGPSGAVPPP VPTGGGSLPK CFVPGTASNE
HHSGGGRNAP EGASGTGRGG GSGGGGGGGK LQDSHKVVNF EDRLKSIITS VLQGSPKTGN
TASSASAPVS LTVTGPPPAG PSPGAGHRDA HHRSGSGGHQ PLTMEPAGSP LKATSASGAG
YGSAAGPGKT TVYLQSSPGA GSHHPHQMVV AQDMSARSST GGRGPSPSAH NPAHQQQIHP
HQVSQSQYQQ QQQLLHHPHH PHAQQSLHHQ QQQHQHYQMQ QQQQHQHQQQ QQGMLNVITS
GAHHLNASTS ISTSPVPTSP YKMHPTGPPA SSIAGSASTK ISPSSKYPYP KGGPVAGMSH
HSPGSSALST HQQIIQQQER ERAMLYAAAA HGGGLPIDHP HHPLHQHHHR GMPPSLVDGK
MLEFKAPENF RYDPRASGPS GAAGNGPPML DTSAVSLQSH SRSSSTNSLD SIPAADYGPA
SAGASAVGGG GARYGGQQQP IPLVTHSPGV GSQGSGQQHG GNNSRPGSTS SQPDYTQVSP
AKMALRRHLS QEKLTHPSAG GPAAGGPVSG GTGAGGSGGG LGTVKTIGDL VNGEIERTLE
ISNQSIINAA INMSSHQQQQ QSSAASGNSS APSASGNNTV INTHVQRPER VSIRLLEEAG
HAAAGGPPPP GSSGGTYSPI SRPGSVGDSG SKSPVHHLHG QSNLASLVQV SAYNSKNHKG
AGTTAVPSTI VSPRGGGSSQ QQQHQQYSTA QGSGAAGGPG AVYQQSTSRG HDRHHSGEPM
PYMALPRADM KPYLESYFTD EHNKRQQQLH QQQQQHQQHP QHQQQHQQQH LQHPVQSPSP
SAMSASAMGL HHHQQQQMHH QHAPLAMHRA SHPVDLHRGS VVMNEPGMLS RSRGEMIPMD
DNRMDRLNGG PPLEGLAASL QARVIATLKI KEEDEERHRR DLSIHHSTSG TINSSSNSIN
STNSNIHGGS LQIVQTAHIK SEKYTSSSSS SSTSSTSSTS SHHHHALKRT SPIVEHPAGT
RPPKMLYTTS ASAGGMDCGP DADMLHVPRG TVPGSSVVGH SAVRGGLLVA PPLVMSPEIN
SLSSVVDDGR HHHQLHVRHN HHSRNDVDEG TTATYYH
//
