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Database: UniProt
Entry: L8J2Z7_9CETA
LinkDB: L8J2Z7_9CETA
Original site: L8J2Z7_9CETA 
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
//
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