ID A0A3B5QGA4_XIPMA Unreviewed; 1583 AA.
AC A0A3B5QGA4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:ENSXMAP00000029948.1};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000029948.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000029948.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000029948.1};
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; 8083.ENSXMAP00000029948; -.
DR Ensembl; ENSXMAT00000029003.1; ENSXMAP00000029948.1; ENSXMAG00000012854.2.
DR GeneTree; ENSGT00390000013515; -.
DR InParanoid; A0A3B5QGA4; -.
DR OMA; SEKQRRC; -.
DR Proteomes; UP000002852; 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: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; 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:UP000002852};
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..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 552..627
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 352..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..410
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..922
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..997
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1458
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1583 AA; 171365 MW; 0243CB9B64188D1E CRC64;
MGEKLELKLK SPVGAEPAGY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD LKLAMENYVL
IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNK RPSNGLLRHI LQQVYNHSVT
DPEKLNNYEP FSPEVYGETS FDLVAQIIDE MEMMEEDTFV DLGSGVGQVV LQVAAATNCK
HYYGVEKADI PASYAETMDK EFKKWMRWYG KKHGEYTLER GDFLSEEWKE RIATTSIIFV
NNFAFGPEVD HQLKERFANM KEGGKIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLR
GSVSWTGKPV SYYLHTIDRT ILENYFASLK NPKLREEQEA ARRRQQKDTK DSKSNNTTPT
KLKEQNKQQD SGGEEERPRL VTVVKPPPKP RRTRLLAKGR KLNNKKRGRP KKATPAAEKN
KKNQSALDLL HAKTLSAAPP QDAYRPPQTP FYQLPPKVQH YNPSQLLMSP TPPGLQQLLD
NIKVQYLQFM AHMKTPQYRS NLQQLLELEK EKHRDLSGQA EQLHLVCQSH KDKIKGLFQT
KLDELGVKAL TVEDLIQAQK EISAHNRQLK EQTKQLEREM VLLRDHSLLL LKSRCEELKL
DWGSLCLESL LKEKQALRRQ ISEKQKHCLE LQISIVELEK SQRQQELLQL KSYSPRDSSP
YRKSLDSRGS TDMDSSRLGL SSAPALNGIS PDLSVNGTGS PCFDRANAKA ELSRYLPISP
DHDAVAAASE ARQRQQSSSQ PDYTRFSPAK IALRRHLNQD PTASAHLRGS GLMTHRELGG
VNSPHGAKQN CPSPNSSDSQ CNVKISDRVG KERSPSVQGD SITSLPISIP LSTVHPSKLP
VSIPLASVVL PSRAERLRNT PSPVSQSGQT NGYSCSSGLM NGGPHPEDHN GASLSPLPHS
NSPLTGPMSR GGPIQSPSLS TGGVLHYADG PPRILPEDGA ERQGNGNCVA GGSRLHHHAG
STKQGYHSNH GNHHHQSPST QHAHTPTHTS SSHSFGSQEG RRRGRRKRGS TGAAASGSPK
RRSFPGVSSN GHSTGSPLNI NSMVNNINQP LEISAISSPE QSSRSPHGPD LDQPPVLKRE
RPLELNGTGR YSTAPSSDDE DSGYPPDSSS SRIERKIATI SLESREGHGR LGDGERGRKS
GSSSGNSTGS EASSSSFCSN SKWKSTFSPI SDPKQPNSDL RQGGSPFSTG GSSRSTDSDS
DYKQQNGRKA GDGDSSSYMT PNPFLSQETG TWAVASSSVQ GGTASDQRQV LQKQKGPRDW
ELKTTSSMAS QNLFIAAAAA TSGGGILNGK VGGSPVAVSS TTGSAMGQYL GSQFPLGGAS
VLQSLFGAQT GVTVNGTSRL VNGHSALGSF ASAGLAGGAA AGGIFHHVVP SASSHQFGAT
LSTSGGLSSL LSLSSSSSAS PQTQQHTTAP PAPTRLTSVS SSVPLSPSQA QHSRTQSVLH
SPSPPTLLLP PPPPLHSVPS SSSSSSASTH PDVSPSSRSD PLHPSRLPQP SLHHQRIHLS
LSLSITTSST ASTSVCTTVA ASPSVPSSSL STLSSSRPFA VHYSPRLPLP PPPSVSGGGG
SMWRTQGMHG PHTAAQIPGS RLR
//
