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Database: UniProt/TrEMBL
Entry: E0VWC8_PEDHC
LinkDB: E0VWC8_PEDHC
Original site: E0VWC8_PEDHC 
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
//
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