ID A0A3Q3MP48_9TELE Unreviewed; 1378 AA.
AC A0A3Q3MP48;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
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:ENSMAMP00000029368.2};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000029368.2, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000029368.2}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSMAMT00000030127.2; ENSMAMP00000029368.2; ENSMAMG00000019781.2.
DR GeneTree; ENSGT00390000013515; -.
DR Proteomes; UP000261640; 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: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:UP000261640};
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 16..330
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 335..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..1078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 498..525
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 551..626
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 335..351
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..411
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..881
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..957
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1078
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1223..1242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 149842 MW; 456DD9CBC332DD05 CRC64;
MGEKLELKLK SPVGAEPAGY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD LKLAMENYVL
IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNK RPSNGLLRHI LQQVYNHSVT
DPEKLNNYEP FSPEVYGETS FDLVAQIIDE MEMMEDDTFV DLGSGVGQVV LQVAAATNCK
HYYGVEKADI PATYAETMDK EFKKWMKWYG KKHGEYTLER GDFLSEEWKE RIANTSIIFV
NNFAFGPEVD HQLKERFANM KEGGKIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLR
GSVSWTGKPV SYYLHTIDRT ILENYFASLK NPKLREEQEA ARRRQQKDTK DSKSNSTTPT
KTKEQSKDSC GEEERPSLVT VVKPTAKPRR TRLLSKGRKL SNKKRGRPKK ATVAAEKKNK
KNQSALDLLH AKTISAAPSQ DAYRPPQSPF YQLPPKVQHY PATQLLLSPT PPGLQQLLDN
MKVQYLQFMA YMKTPQYRSN LQQLLEQEKQ KHQDLSGQVE QLHSVCQSHK DRIKGLFQTK
LDELGVKALT VEDLLQAQKE ISAHNRQLKE QTKQLERDMA LLRDHSLLLL KSRCEELKLD
WGSLCMESLL KEKQALRRQI SEKQKHCLEL QISIVELEKF QRQQELVQLK VYSPCEGSPF
RKSLESRSST DIDSSKLGLS SGPALNGISP ELSINGTSSP CFDRANIKGE LLSRYLPISP
DHDIMSATPD ARQRQQNSSH TLPDYTRLSP AKIALRRHLN QDPTASAHLR CPGLTTQREL
CGVNSPLGGK LNCPSPNASD AQNTSKISER GGKERSPSVQ GDNSITSLPI SIPLSTVHPS
KLPVSIPLAS VVLTSRVRST PSPVSQAGQT NGYSSSSGLM NGGPHPEDHN GASSSPPPHS
NTPLTGPSGR GVPIQSPAPS TGGVLQYADG PPRILPEDGQ DRQGGESDTE PQDNELRRRI
FFSSSSSSSS SSSSGSGGSA SGGSRLHHHT GNSAKQGYHS IHGNHHHQSP GTQHSHTPTH
TSSSHSSHGL STLEGRKRGR RKRGAAGPVT ATGSPKRRPF PGLSTSNHSS GSPLNINTMV
NNINQPLEIS AISSPEQSSR SPSGPDLDQP PILKRERPLE LNGTGRYSSA PSSDDDDSGY
PADSSSSRIE RKIATISLES RDGPGRLGDS ERGRKSGSSS GNSTDPKQPN SDLRQGGSPF
GMGGSNRGTD SDSDHKQQQV RKGSDAESSS YMTPNPFLSQ ETAARGGGSG AGGAQGGSCS
DQRQALQKQK APRDWELKTS SSLASQNLFI SAAASGGGGI LSGKVGGSPV AVSSTTGSSI
GQYLGSQFPL GGTSVLQSLF GAQTGNSTVS GTPRLVNGHS ALGSFSSAGL AGGAAGGN
//
