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
//