ID F5HIR5_ANOGA Unreviewed; 2545 AA.
AC F5HIR5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 76.
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=1269184 {ECO:0000313|EnsemblMetazoa:AGAP003282-PA};
GN ORFNames=AgaP_AGAP003282 {ECO:0000313|EMBL:EGK96176.1};
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:EGK96176.1};
RN [1] {ECO:0000313|EMBL:EGK96176.1, ECO:0000313|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96176.1,
RC ECO:0000313|Proteomes:UP000007062};
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:EGK96176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96176.1};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EGK96176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96176.1};
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:EGK96176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96176.1};
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:EGK96176.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK96176.1};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EnsemblMetazoa:AGAP003282-PA}
RP IDENTIFICATION.
RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP003282-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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 EMBL; AAAB01008794; EGK96176.1; -; Genomic_DNA.
DR RefSeq; XP_003436434.1; XM_003436386.1.
DR STRING; 7165.F5HIR5; -.
DR PaxDb; 7165-AGAP003282-PB; -.
DR EnsemblMetazoa; AGAP003282-RA; AGAP003282-PA; AGAP003282.
DR GeneID; 1269184; -.
DR KEGG; aga:AgaP_AGAP003282; -.
DR VEuPathDB; VectorBase:AGAP003282; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_001460_1_0_1; -.
DR InParanoid; F5HIR5; -.
DR OMA; LNGTPHK; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031151; F:histone H3K79 methyltransferase activity; IBA:GO_Central.
DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 Reference proteome {ECO:0000313|Proteomes:UP000007062};
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..333
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 336..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1822..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1955..1987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2001..2044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2159..2258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2271..2307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2334..2545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 591..625
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 658..685
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 339..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1828..1874
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1966..1987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2001..2021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2168..2238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2390..2410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2434..2466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2521..2545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2545 AA; 268957 MW; F8BF3D8C7076E487 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 HHSRNDVDDD VVIGDDESSW HDRVSSGFDR LVAFASTELD
KTRRSNEDAP ASSASCTTSP DSGINQSDHS RTFLSSSSSS SQLDVPPGSA SVGSSSSSSI
SSSSSSNSST SSIGSVTGGH GGGSGGSHGV GGHAGVPGGL MMKHMVPIIK SSPAEPVDSP
PLSDVGLPRT PSPTSSPPLL FGHPTASSTA IAGGATTSAV STVMQPSLLH PPVVGGHAPV
AGSGNNNGVV PPAAGSAAPV NNSNSGNSSS SSSSLGIPLK YQRQSKSSSS SSEKHYKKKF
RERNWEEYEE SLSGGRNSAI SGSGDVPMDQ QDYHHTVASL NAPHSGSMDV GNASAPSSST
SMSAEPIGSA VGDKRNDDHA AQHHHQQQQQ QQQQQQQQHH HKHKSAKFRP KGKDWNWDDE
HLNASSGSAT STRGAGRSGT NTAST
//