ID L5L6H9_PTEAL Unreviewed; 1413 AA.
AC L5L6H9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ORFNames=PAL_GLEAN10005977 {ECO:0000313|EMBL:ELK19334.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK19334.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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 Izumo family.
CC {ECO:0000256|ARBA:ARBA00009633}.
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; KB030265; ELK19334.1; -; Genomic_DNA.
DR STRING; 9402.L5L6H9; -.
DR eggNOG; KOG3924; Eukaryota.
DR InParanoid; L5L6H9; -.
DR Proteomes; UP000010552; 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; 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; IPR029389; IZUMO.
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 Pfam; PF15005; IZUMO; 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:UP000010552};
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 145..509
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 466..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 940..992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 692..781
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 466..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..547
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1048
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1413 AA; 154506 MW; AFFA045FFADA7E89 CRC64;
MKELHLAIPA EITREKLDQV ANAVYEKMDQ LYQGKMYFPG YFPNELRAIF REQVHLIQNA
IIESIFQYET ISCSNCTDSH VICFGYNCES SAQWETAVQG LLHYINNWHK WHPSATAGRG
SSVGRRCSAC CLWSPGPAVA NLDCSVRSKP CPSVFQDKHH DAAHEIIETI RWVCEEIPDL
KLAMENYVLI DYDTKSLLPM CCLPVAFSEL GSEQHRPFAF FSFESMQRLC DKYNRAIDSI
HQLWKGTTQP MKLNTRPSNG LLRHILQQVY NHSVTDPEKL NNYEPFSPEV YGETSFDLVA
QMIDEIKMTE DDLFVDLGSG VGQVVLQVAA ATNCKHHYGV EKADIPAKYA ETMDREFRKW
MKWYGKKHAE YTLERGDFLS EEWRERIANT SVIFVNNFAF GPEVDHQLKE RFANMKEDIG
TIMRVVELSP LKGSVSWTGK PVSYYLHTID RTILENYFSS LKNPKLREEQ EAARRRQQRE
NKSNTTTPTK VPESKVAVTA DTPVDSGAEE EKTGTATIKK PSPSKARKKK LNKKGRKLAG
RKRGRPKKMS TANPERKPRK SPTALDLLHA QTVSQAAASP QDAYKSPHSP FHQLPPSVQR
HPPDQLLLAP TPPALQKLLE SFRIQYLQFL AYTKTPQYKA GLQQLLDQEK EKNARLLGAA
QQLFGHCQAQ KEEIKRLFQQ KLDELGVKAL TYDDLIQAQK EISAHNQQLR EQTEQLETDN
RALRGQSLQL LKARCEELRL DWPTLSLEKL LKEKQALKSQ ISEKQRRCLE LQISIVELEK
SQRQQELLQL KSCVPPDEAV AMHLRGKGGL GRELEVEPSR LHLELDCSKF SLPPFSSLSP
ELSVNGHAAG YELCGTLSRP PSKQNTPQDL ASVLDQEVVP CTPSHGSRPR LDKLSGLASP
DYTRLSPAKL VLRRHLSQDH AAGSKAATSE LHPRAEHVKE NGLPYHSPGL ANGIKLSPQE
PRPSSPVALQ MTGEKGSEKG LKERGHASSG EAITSLPVSI PLSTVQPSKL PVSIPLASVV
LPSRAEKVRS TPSPVPQARE SSSTLEKQVG AHAHGAGSKG LTLAPTAGFS YAGSVAITGA
LTGSPAPLAP GAEPPAFDES SSSGSLFAPM GSRSSTPQHP PLLAQPRNSG PASPAHQLCA
SPRLGATQGP LPDASKGDLP SEAGFSDPES EAKRRAVFTV SASAGSAKQS PSSKHSPLPA
GTQNHGQDSR KRGRRKRASA GTPSLSTGVS PKRRALPSVA GLFTQSSGSP LNLNSMVNNI
NQPLEITAIS SPESSLKSSP IPYQDNDQPP VLKKEKPLSQ TNGAHYSPLT SDEEPGSEDE
PGSASTAPSA QTHRPFLGTF APGPQFSLGP MSLQANLGPS VLQSLFNSVP AAAGLVHVSS
AATRLTNSHA MGSFSSGVAG GAVGGRQTCV SPV
//
