ID A0A3Q3FXT4_9LABR Unreviewed; 1459 AA.
AC A0A3Q3FXT4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=DOT1L {ECO:0000313|Ensembl:ENSLBEP00000024159.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000024159.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000024159.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 STRING; 56723.ENSLBEP00000024159; -.
DR Ensembl; ENSLBET00000025413.1; ENSLBEP00000024159.1; ENSLBEG00000018459.1.
DR GeneTree; ENSGT00390000013515; -.
DR InParanoid; A0A3Q3FXT4; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl.
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; 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:UP000261660};
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 1..239
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 246..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1267..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 462..537
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 246..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..323
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..753
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..808
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1430..1450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1459 AA; 157598 MW; E4F0167CC0B633B8 CRC64;
QWKGTTQPMK LNKRPSNGLL RHILQQVYNH SVTDPEKLNN YEPFSPEVYG ETSFDLVSQI
IDEMEMMEDD TFVDLGSVGQ VVLQVAAATN CKHYFGVEKA DTPSTYAETM DKEFKKWMKW
YGKKHGEYTL EKGDFLSEEW RERIATTIIF VNNFAFGPEV DHQLKERFAN MKEGKIVSSK
PFAPLNFRIN SRNLSIGTIM RVVELSPLRG SVSWTGKPVS YYLHTIDRTI FQLENYFASL
KNPKLREEQE AARRRLQKDT KDSKSNSTTP TKPKEQNQQD SCGEDERPSL VTVVKPPPKP
RRARLLTKGR KLNNKKRGRP KKAAPAAEKK NKKNQSALDL LHAKTLSAAP TQAYRPPLSP
FYQLPPKVQH YPSSQLLLSP TPPALQQLLN IKVQYLQFMT YMKTPQYYSN LQQLLDQEKQ
KHRDLSGQAE QLHSVCQTHK DKIKGLFQTK LDEQLGVKAL TVEDLLQAQK EISAHNRQLK
EQTKQLERDM ALLRDHSLLL LKSRCEELKL DWGSLCLESL LKEKQALRRQ ISEKQRHCLE
LQISIVELEK SQRQQELLQL KSSYSPCDGS PYRKSLESRS STDMDSSKIG LSSAQAFNGV
SPELSINGTS SPCFPSKGEL LSRYLPISPD HEIVPVSTDA RQRQQSFSHA LPDYTRFSPA
KIALRRHLNQ DSTQGKERSP SSQGDNSITS LPISIPLSTV HPSKLPVSIP LASVVLPNRA
ERLYSSGSGL MNGGSHPEDH NGASSSSPPH NHTLLTGPMG RGGHIQSPPL STGGVLQYAD
GPPRILSDDG QDHQGGESDM EPQDSEMRRR IFFSSSSSSS SSSSSSGSGG SAGGGSRLHH
HNCNSAKQGF HSNHGNHHHH QSPGTQHTHQ PTHTSSSQSS HSLGHQEGRK RGRRKRNSAV
SLTASGSPKR RSFPGLCSNN HSSGSPLNIN SMVNNINQPL EISAISSPEQ SSRSPSRLDL
DQPPILKRER PLELNGTCRY SSAPSSDDDD SGYPADSSSI ERKIATISLD GRDGPGRLGD
NSTGSEASSS SSSSMSSTSK WKSTFSPISD PKQPNSELRQ GGSPFGMGGS GRGTDSDSDH
KQQHQQLRRG SDGELSSYMN PNPFFSQEVG TRGGGSSGGG GSQGGSGSDQ RQALQKQKAP
RDWDVKTSAS QNLFISAAAS SGGGIMSGKV GESPVAVSST TGSSVGQYLA SQFPLGGTSV
LQSLFGAQTG GPTVSGAARL VNGHSALGSF SSAGLAGGAA GIFHHVVPTV PSHQFGATLP
NSGGLSSLLS LSSSSSTSSQ QHTTPQPAST RLAPVSSPLP LSMSQAQHSR IQSVLHSPSP
PTLSLPPLPP LHSAPSSSTS SSTTTHSDAA PSSRSDSLHS SRLSHSSLHH QRAQSSLSLS
ISSSTSASSA SVSAAAATAS HSSSSSLSTS SSRPFAVHYS PRLPPPPTAS SSGGGGSMWR
TQSMHGTHIA SQLPGSRPR
//
