ID L8J2Z7_9CETA Unreviewed; 1708 AA.
AC L8J2Z7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
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};
DE Flags: Fragment;
GN ORFNames=M91_18664 {ECO:0000313|EMBL:ELR61767.1};
OS Bos mutus (wild yak).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=72004 {ECO:0000313|EMBL:ELR61767.1, ECO:0000313|Proteomes:UP000011080};
RN [1] {ECO:0000313|EMBL:ELR61767.1, ECO:0000313|Proteomes:UP000011080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yakQH1 {ECO:0000313|Proteomes:UP000011080};
RX PubMed=22751099; DOI=10.1038/ng.2343;
RA Qiu Q., Zhang G., Ma T., Qian W., Wang J., Ye Z., Cao C., Hu Q., Kim J.,
RA Larkin D.M., Auvil L., Capitanu B., Ma J., Lewin H.A., Qian X., Lang Y.,
RA Zhou R., Wang L., Wang K., Xia J., Liao S., Pan S., Lu X., Hou H., Wang Y.,
RA Zang X., Yin Y., Ma H., Zhang J., Wang Z., Zhang Y., Zhang D., Yonezawa T.,
RA Hasegawa M., Zhong Y., Liu W., Zhang Y., Huang Z., Zhang S., Long R.,
RA Yang H., Wang J., Lenstra J.A., Cooper D.N., Wu Y., Wang J., Shi P.,
RA Wang J., Liu J.;
RT "The yak genome and adaptation to life at high altitude.";
RL Nat. Genet. 44:946-949(2012).
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 EMBL; JH880411; ELR61767.1; -; Genomic_DNA.
DR STRING; 72004.ENSBMUP00000018057; -.
DR Proteomes; UP000011080; 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:0031507; P:heterochromatin formation; IEA:InterPro.
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; 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 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:UP000011080};
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..310
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 314..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 544..616
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 314..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..395
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..891
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..984
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1607
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116..119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 139..148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 166
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT BINDING 202..203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR037123-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELR61767.1"
SQ SEQUENCE 1708 AA; 181473 MW; 5BFCD88794D51212 CRC64;
PYPIVFQDKH HDAAHEIIET IRWVCEEIPD LKLAMENYVL IDYDTKSFES MQRLCDKYNR
AIDSIHQLWK GTTQPMKLNT RPSTGLLRHI LQQVYNHSVT DPEKLNNYEP FSPEVYGETS
FDLVAQMIDE IKMTEDDLFV DLGSGVGQVV LQVAAATNCK HHYGVEKADI PAKYAETMDR
EFRKWMKWYG KKHAEYTLER GDFLSEEWRE RIANTSVVFV NNFAFGPEVD HQLKERFANM
KEGGRIVSSK PFAPLNFRIN SRNLSDIGTI MRVVELSPLK GSVSWTGKPV SYYLHTIDRT
ILENYFSSLK NPKLREEQEA ARRRQQRENK SNTTTPTKVP ESKAAVQADT PVDSGAEEEK
AGTATVKKPS PSKARKKKLN KKGRKMVGRK RGRPKKMSAT NPERKPKKTQ SSLDLLHAQT
ASRAASPLPQ DAHRPPHSPF YQLPPSVQRP TPEQLLLAPT PPALHRLLES FRIQYLQFLA
YTKTPQYKAS LQQLLDQEKE KNARLLGAAQ QLFGHCQAQK EEIKRLFQQK LDELGVKALT
YNDLIQAQKE ISAHNQQLRE QTEQLEKGNW ELRSQSLRLL KARCEELKLD WSTLSLENLL
KEKQALKSQI SEKQRHCLEL QISIVELEKS QRQQELLQLK SCVPPDEALA LQLRGKPEAE
PSRLHLELDC ARFSLPPFSS LSPELSMNGH AAGYELCSAL GRPSPKQNTP QYLASPLDQE
VVPCTPSHSG RPRLEKLSSL ALPDYTRLSP AKLVLRRHLS QDHAASGKAA ASELHPRAEH
AKENGLPYQS PGITNGIKLS PQDPRPSSPM ALQMGEKGPE KGVKERAYAS SGEAITSLPV
SIPLSTVQPS KLPVSIPLAS VVLPSRAEKA RSTPSPGPPA RESSSTLEKQ VAANTHGAGG
NAAGSKSLAL APTGFAYTGS VAISGALAGS PAPLAPGAEP PALDESSSSG SLFATVGSRS
STPQHPPLLT QPRTCGSASP APQLCSSPRL GALGPLPDSG KGDLPCEASF SDPESEAKRR
IVFTISAGAS SAKQSPSSKH SPLPSGARGD GGQGHGPDGR KRGRRKRASA GTPSLSSSVS
PKRRALPSVA GLFTQSSGSP LNLNSMVSNI NQPLEITAIS SPESSLKSSP VPYQDNDQPP
VLKKEKPLSQ TNGAHYSPLT SDEEPGSEDE PGSARRVGCS RGVGGGPDCR IERKIATISL
ESKSPPKTLE NGGSLAGRKA PLASEPVNSS KWKSTFSPIS DLGLAKAADS PLQAASALSH
NSLFAFRPGL EEPSAADAKL ATHSRKSFPG TLPGAGGLSP SSLPASGFAL GGGLAADLSL
HSFSDGASLS HKAPEAAGLG APLSFPGPRG KEGGAAESGP FVNKRQLDGL GPKGEGGLPT
CGPPDKASTA HSKAGKGRER EPDVKNGHNL FMAAATAPPA GLLSGPGLAP AASSAGGAAP
SVQTHRPFLG AFAPGPQFAL GPMSLQANLG PSVLQSLFSS VPAAGLVHVS TAATRLTNSH
AMGSFSSGVA GGAVGGVFNH AVPLASAHPF GASFGSGAAC RSATLSLTPL QAVASTPASS
FQAPSSAEPR PPPPPPHLGR PPPGQPTLHA PPHPNATLPP PPALLPANSE PVLLQNLASL
PANQAFLPAS SAASLPPANA SLSIKLASLP HKVSRPSLTV HHQPLPGLAL AQAAPVNPQA
SSTGPPAVWV SLGMPPPYAA RLAGVKPR
//