ID A0A2Y9LI14_ENHLU Unreviewed; 1706 AA.
AC A0A2Y9LI14;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-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|PIRNR:PIRNR037123};
GN Name=LOC111161720 {ECO:0000313|RefSeq:XP_022381305.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022381305.1};
RN [1] {ECO:0000313|RefSeq:XP_022381305.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022381305.1};
RG RefSeq;
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 -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-79' of histone H3.
CC {ECO:0000256|PIRNR:PIRNR037123}.
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|PIRNR:PIRNR037123, 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|PIRNR:PIRNR037123,
CC ECO:0000256|RuleBase:RU271113}.
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DR RefSeq; XP_022381305.1; XM_022525597.1.
DR STRING; 391180.A0A2Y9LI14; -.
DR KEGG; elk:111161720; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000248482; 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:0000077; P:DNA damage checkpoint signaling; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0031507; P:heterochromatin formation; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; IPR021169; DOT1L/grappa.
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 PIRSF; PIRSF037123; Histone_H3-K79_MeTrfase_met; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51569; DOT1; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037123}; Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|PIRNR:PIRNR037123};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037123};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRNR:PIRNR037123};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037123}.
FT DOMAIN 16..330
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 333..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1570..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 564..636
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 333..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..415
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1601
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136..139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 159..168
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 186
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 222..223
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
SQ SEQUENCE 1706 AA; 180755 MW; AF19E321B0609D82 CRC64;
MGEKLELRLK SPVGAEPAVY PWPLPVYDKH HDAAHEIIET IRWVCEEIPD LKLAMENYVL
IDYDTKSFES MQRLCDKYNR AIDSIHQLWK GTTQPMKLNT RPSNGLLRHI LQQVYNHSVT
DPEKLNNYEP FSPEVYGETS FDLVAQMIDE IKMTEDDLFV DLGSGVGQVV LQVAAATNCK
HHYGVEKADI PAKYAETMDR EFRKWMKWYG KKHAEYTLER GDFLSEEWRE RIANTSVIFV
NNFAFGPEVD HQLKERFANM KEGGRIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLK
GSVSWTGKPV SYYLHTIDRT ILENYFSSLK NPKLREEQEA ARRRQQREGK SATTTPTKGP
ESKAAAPADA PMDSGAEEEK AGATTIKKPS PSKARKKKLN KKGRKMAGRK RGRPKKMSTA
NPERKPKKSQ TALDLLHAQA APQTAAPSPQ DAYKSPHSPF YQLPPSVQRR PPDQLLLAPT
PPALQKLLES FKIQYLQFLA YTKTAQYKAS LQQLLDQEKE KNARLLGAAQ QLFGHCQAQK
EEIKRLFQQK LDELGVKALT YNDLIQAQKE ISAHNQQLRE QTEQLQKDNG ELRTQSLRLL
KARCEELKLD WSTLSLENLL KEKQALRTQI SEKQRHCLEL QISIVELEKS QRRQELLQLK
SCVPPDDGLS AHLRGKGALG RELEAEPGRL HLDLDGPKFS LPHLSSASPE LSMNGHVAGY
EVCGALSRPS SKQNTPQYLA SPLDQDVVPC TPSHGGRPRL EKMAGLALPD YTRLSPAKLV
LRRHLSQDHA AGGKPAAGEL HPRAEHAKEN GLPYQSPGIA NGIKLSPQDP RPSSPAALQM
TGERGSEKGV KERAYASSGE AITSLPVSIP LSTVQPSKLP VSIPLASVVL PSRAEKVRST
PSPVSQTRES SSTLEKQMGA NAHGTGSKSL APAPAGFYTG SGAVSGALAG SPAPLAPGAE
PGALDEVSSS GSLFASVGSC GSAPQHPPLL PQSRGSAAAS PAHPLCASPR LSSAAQGPLP
EANKGDLPSE AGVSDPEGEA KRRIVFTISA GGGAKQSPPG KPSPLPTGAR GDSGQGHGPD
SRKRGRRKRA AAGTPSLSSG VSPKRRALPS VAGLFTQSSG SPLNLTSMVS NINQPLEITA
ISSPESLKSS PVPYQDNDQP PILKKEKPLS QTNGAHYSPL TSDEEQGSED EPGSARIERK
IATISLESKS PPKTLESGGG LTGRKPAPAS EPANSSKWKS TFSPISDLGL AKCADSPLQA
SSALSQNSLF TFRPPLEEPG LADAKLAAHP RKGFPGALAG SGGLSPSSNP PNGFAFSGGL
TADLSLHSFS DGASLSHKIP EAASLSGPLS FPTPRGKEGA AAEPGTFVNK RQLDGLSGPK
GREAGEPGLP ACGPPDKASL THSKPGKGRD REPDLKNGHN LFISAATVPP GGLLSGPGLA
TAASSTVSAA PSAQTHRPFL GTFAPGPQFA LGPMSLQANL GSSVLQSLFS SVPAAAGLVH
VSSAATRLTN SHAMGSFSSG VAGGAVGGVF NHAVPSASAR PFGASFGGGA ACRSGTLGLT
ALQAVAGAPA SSFQAPPPPP QGQPALPAPP PPNAALPPAP ALLPANPEPV LLQNLASLPA
NQAFLPAASA ASLQPANASL SVKLASLPHK APRPSFTVHH QPLPGLALAQ AAPVIPQASS
TGPSAVWVSL GMPPPYAARL AGVKPR
//
