GenomeNet

Database: UniProt/TrEMBL
Entry: F5HIR5_ANOGA
LinkDB: F5HIR5_ANOGA
Original site: F5HIR5_ANOGA 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system