ID E0VWC8_PEDHC Unreviewed; 1674 AA.
AC E0VWC8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 71.
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=8239419 {ECO:0000313|EnsemblMetazoa:PHUM478060-PA};
GN ORFNames=Phum_PHUM478060 {ECO:0000313|EMBL:EEB17684.1};
OS Pediculus humanus subsp. corporis (Body louse).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Psocodea; Phthiraptera; Anoplura; Pediculidae;
OC Pediculus.
OX NCBI_TaxID=121224;
RN [1] {ECO:0000313|EMBL:EEB17684.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB17684.1};
RA Kirkness E., Hannick L., Hass B., Bruggner R., Lawson D., Bidwell S.,
RA Joardar V., Caler E., Walenz B., Inman J., Schobel S., Galinsky K.,
RA Amedeo P., Strausberg R.;
RT "Annotation of Pediculus humanus corporis strain USDA.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEB17684.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=USDA {ECO:0000313|EMBL:EEB17684.1};
RG The Human Body Louse Genome Consortium;
RA Kirkness E., Walenz B., Hass B., Bruggner R., Strausberg R.;
RT "The genome of the human body louse.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:PHUM478060-PA}
RP IDENTIFICATION.
RC STRAIN=USDA {ECO:0000313|EnsemblMetazoa:PHUM478060-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; AAZO01005790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAZO01005791; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DS235818; EEB17684.1; -; Genomic_DNA.
DR RefSeq; XP_002430422.1; XM_002430377.1.
DR STRING; 121224.E0VWC8; -.
DR EnsemblMetazoa; PHUM478060-RA; PHUM478060-PA; PHUM478060.
DR GeneID; 8239419; -.
DR KEGG; phu:Phum_PHUM478060; -.
DR CTD; 8239419; -.
DR VEuPathDB; VectorBase:PHUM478060; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_001460_0_0_1; -.
DR InParanoid; E0VWC8; -.
DR OMA; LTQDYIL; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000009046; 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:UP000009046};
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 26..341
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 340..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 928..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1412..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1472..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1653..1674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 597..631
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 734..764
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 342..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..440
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..800
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..999
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1481..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1547
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1674 AA; 187601 MW; F12C5CD934DA1E09 CRC64;
MPFNAIKLVD YLSKMELRLH SPAGAEPVVY TWPLSGGSGS HDGALEIVET IRWVCEDIPE
LKLPLENNIL ADYDTKSYDS MRSLCDRFNR AIDSIVQLEK GTSLPAARLN KYPSRGLLRH
ILQQVYNQAV TDPEKLNQYE PFSPEVYGET SYDLICQMID QIEITSDDIF VDLGSGVGQV
VLQMAAATPC KVCFGVEKAE VPSRYAEDMN KNFKKWMGWY GKKYGEYHLI KGDFLKAEHR
EKIVSATIVF VNNFAFGPNV DHSLKERFAD LKDGARIVSS KSFCPLNFRI TDRNLSDIGT
IMHVSEMSPL KGSVSWTGKP VSYYLHIIDR TKLERYFQRT KNPRARGNNN SSSSNSNNNN
SNNNHNNGGL QDSISNNMLR NSRARRDSSK QTMNSVSSES RDSDEDSNCP LSTVSKNARN
KSTVRRYGPE TNRRKSSISE EENNNIQNTS NNNGKFKKGT NKTVQNKKLR KNVKANDKNL
NPPPRAPPAP KRTKTKLRRG KAKKTLKITG LDLLHSQTLL STSPQAIGKK LPPAPGCVDQ
QLTALRVMPS VELSDVHNEL DIPPAPADTP YALQLLLEMY RAQYLQLLEL IKTPQHKLDV
KAQIETEKEK NEKLKSRAAQ LEKQINVLVS DSVALLKARM SELGINATST ADLLKEAKDI
VWRHRELQAR AVQLQNQVST IEEDQAKLVS QRQKEIIEKY KKIGYANGVN ESIDISTLTL
EYILKEISVT LSHRKRLQNH VTRLENELNA MEKAEEDKKI LSNVPKQIVV PEKSLSQLNQ
SKSPRKSREH RSRSQEWPEV PNIEKIEENN PEILAQKILE TGRQIEAGKF PSSNIKYNNS
LSNGYVANES KFSSDANIRQ HNYYPPTSTN GRNVGMTKTD STTKTKWKSQ HVKEKQSYNA
NRTQEPPRLD NFEDRLKSII TSVLNEDQNN RDRQQSHQHH QNHSKPPSAT VTLSQLQTQE
SYQNNNSCFY SSNGLVKQEQ KSFKKAETVN REKERSQPRP DYTQVSPAKL ALRRHLSQEK
LAAASAQQIQ QLDEKGGLGY VATRSIGDLV SGEIERTLEI SNQHIINVAI DMSPILNSSS
ASSVANNMPP KTERSGSRLS RVEDTFKKEE ERVASSPSPL LRTVYSPISR PSSAEVGNPP
TPTNIIHPTT ILEGLAYPHR PKSPISHNNL ATLAQVAYNQ QSYSANTYPH RNNNPYSNMP
YHNLPTQRQN NACRYTPVQL PRADIKPYQE SYFTDMKDFK PNSTKAYTCP QPNFAPVEGL
AATLHARLLN DGSSISPAND VKEESDTAVL DCMHYDSKYN SIGRTVDKRP EIPKIEVCPP
YVEVQDKKHM AMYRSSVLST SIVHNATIKN EIPDRNFTGR NADYKDRKSI PQKRASPVIH
GPIRSAKKSH LAESVADISS VVNNASQPLA ISAISSPENN SGKSTPYNEE DRRPHEEALD
SVLDDEDKGD KWQDKISSGF DRLVAFASTE LDKRRRSTEG ESNASCNTSP DSGIGHGDPP
STNLMLPPGK KRFSIADIEG LCPGPKMPRL FKTPPAKPSP GRDSPPVLDP PLVIDMVNVP
RTPSPSSPPP LTINTFSPAP LDGPYSPIST TAEDLSAPHV SPSPPSLPPS VPVKYPATSD
NAVKKTPHHF KKKFFHRENW EVYDTSSNVQ CRPKEKFRPK GKDWNWGGSS EFQK
//