ID B0W3M5_CULQU Unreviewed; 1684 AA.
AC B0W3M5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=6032769 {ECO:0000313|EnsemblMetazoa:CPIJ001411-PA};
GN ORFNames=CpipJ_CPIJ001411 {ECO:0000313|EMBL:EDS31811.1};
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000313|EMBL:EDS31811.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000313|EMBL:EDS31811.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:CPIJ001411-PA}
RP IDENTIFICATION.
RC STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ001411-PA};
RG EnsemblMetazoa;
RL Submitted (FEB-2021) 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; DS231832; EDS31811.1; -; Genomic_DNA.
DR RefSeq; XP_001843309.1; XM_001843257.1.
DR STRING; 7176.B0W3M5; -.
DR EnsemblMetazoa; CPIJ001411-RA; CPIJ001411-PA; CPIJ001411.
DR KEGG; cqu:CpipJ_CPIJ001411; -.
DR VEuPathDB; VectorBase:CPIJ001411; -.
DR VEuPathDB; VectorBase:CQUJHB010026; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_001460_1_0_1; -.
DR InParanoid; B0W3M5; -.
DR OMA; TENMAHT; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000002320; 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 Reference proteome {ECO:0000313|Proteomes:UP000002320};
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..331
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 331..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1252..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1291..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1356..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1610..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 561..595
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 335..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..974
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1134..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1684 AA; 186697 MW; C868722916BB9E93 CRC64;
MATPNYKELK LQSPAGAEPF LYNWPFSIGG GHDNGIELIE NVRWVCEDMP EIKSAIEEIN
LNELDTGDFD AMKNLCDRFN KAIDSVAALE KGTSLSSQRF TYPSRGLLRH IIQQVYNQAV
VEPEKLNQYE PFSPEVYGET SFDLICQMID QIKITSDDVF VDLGSGVGQV VLQMAASTPV
KVCYGIEKAD VPSRYAEGMN ATFKMWMHWF GKKYSDYELI KGDFLADEHR EKITAATIVF
VNNFAFGPNV DHQLKERFAD LRDGARIVSS KSFCPLNFRI TDRNLSDIGT IMHVSEMSPL
RGSVSWTGKP VSYYLHIIDR TKLERYFQRL KTKGGDNEGP TSSTTTRASR SKKDTVPKQP
VNNDESTSDS DADDPGPTQA PPPPPRKPWS GWCSGKEKSS QSEEENNNSP VLRNGRIPVA
TKKRRKITRT KTAKKEPVAP KDMVDIIIPQ MPIDAQGVGA KKRGRGVKKG RQRRALKING
LDLLHSETLL STSDQAIGKR LPPAPGCVDQ LLTSLAGDMQ HTELDIPEAP SETPYALQIL
LDLFKTQFMK AIESFRKPSY KDNVQQQIER EKERNQRLLN RAGQLEKQIK VLIDDSVALL
KARMNELGIS TTSQNDLLCK AKEIVGRHKE LQVMAAKLQS QVTTIEQEQK RIVMQHMHRI
ADKYIKTEEV ELTPKTSQEM VLKEIANTLS QRKKLCAQVS SLENELNIID KLAEERKANP
VLTVTTQHHH AREHPATHSS GSSRSQRKSR ENRTRSQEWP EIPDIGKIEE NNPEILAQKI
LETGRQIEAG KLRNQKERET KNHHMQQQQH ASIPPQQSQI HHPGDAALMP APPTLNKSHH
RNKMSSVKAE PRAKLQDSHK VVNFEDRLKS IITSVLQGPP KTISASQQQP PPTQQVQMVQ
QQQQQHPQMM LAHGTEHISP GKGSSSYGKT VYLQSGPPTS SMHSGGTIHD MSSRSSGQHQ
LPHPSSSQPP HHLNASTTIA TAPYYQKGMS ASLNHHSPGA GAANNNTSTH QQILQQQERE
AREREMRQNP VVMQQHYGGQ PHPAIDPHHL LHRGGVTMDG KLEFKAPEQS YRYDPRNPVE
APIYQSHSRS SSATSLDGDY PPGPGGNVRY IGVPTAQQQQ QQQQRDRDQR DQQLGGNNSR
PGSSSSQPDY TQVSPAKMAL RRHLSQEKLT HPGMPASGGG GSTVKTIGDL VNGEIERTLE
ISNQSIINAA VNMSTTASQA AAAIHTVINT NVQRPERVSI RVLEELGLNG GVQTTFSPVS
RPNSNETSKS PVHLHGQSNL ATLAQVATYN NKKPPAPAAS SSQQQYSTYQ TGRGPQDKPP
STSYPAPGER VEAPPYMALP RADMKPYLES YFIDEHKRQQ HQQQQTQQQL HRQGSPAMAA
QAHHHPTAAH HPPPQASARG NDHHHRSHPA PVDRREAPMA PHLMDDRMDR LNGSPPLEGL
AASLQARVIA QLKSKEEDEE RHRRADLMAM HNSGPVGSNS IQLVQTPHLK VDKYPSGLKR
TSPIIENPPR PPKMLYTDCS DVMITPELLH AASRGVSGPS RNMALMSPEI NSLTTVGDDR
HHLLRHGRND VDGKFAAWRN HAGIETSKKK THTAFLSVIN LPYGGGSMSS ATTGCSNPTT
TTSSASSRNY GQHQQYRIQK PMAAAAGNHR PPPQHHHRSH GGGSGGSGSA NKYHNHPNNS
YPSK
//
