ID A0A091MLA0_9PASS Unreviewed; 1114 AA.
AC A0A091MLA0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 35.
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=N310_10252 {ECO:0000313|EMBL:KFP75432.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP75432.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP75432.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP75432.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KK829581; KFP75432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MLA0; -.
DR Proteomes; UP000053537; 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: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:UP000053537};
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..303
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 307..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 800..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 535..610
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 307..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..389
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1049
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP75432.1"
FT NON_TER 1114
FT /evidence="ECO:0000313|EMBL:KFP75432.1"
SQ SEQUENCE 1114 AA; 124435 MW; 1738A87589AC552F CRC64;
DKHHDAAHEI IETIRWVCEE IPDLKLAMEN YVLIDYDTKS FESMQRLCDK YNRAIDSIHQ
LWKGTTQPMK LNTRPSNGLL RHILQQVYNH SVTDPEKLNN YEPFSPEVYG ETSFDLVAQM
IDEIKMTEDD LFVDLGSGVG QVVLQVAAAT NCKHHYGVEK ADIPAKYAET MDREFRKWMK
WYGKKHAEYT LERGDFLSEE WRERIANTSV IFVNNFAFGP EVDHQLKERF ANMKEGGRIV
SSKPFAPLNF RINSRNLSDI GTIMRVVELS PLKGSVSWTG KPVSYYLHTI DRTILENYFS
SLKNPKLREE QEAARRRQQR ENKSNTTTPT KVQENKVNVL HFCRVNDSGA EEEKAAANSV
KKPSPSKARK KKLSKKGRKM AGRKRGRPKK MNTASTERKT KKNQTALELL HAQTVSQTSS
SSPQDAYKSP HSPYYQLPPK VQRHSSNQLL VTPTPPALQK LLDSFKIQYL QFMAYMKTPQ
YKASLQQLLE QEKEKNAQLL GTAQQLFTHC QAQKEEIKRL FQQKLDELGV KALTYNDLIQ
AQKEISAHNQ QLKEQTKQLE KDNSELRNQS LQLLKARCEE LKLDWSTLSL ENLLKEKQAL
KNQISEKQKH CLELQISIVE LEKSQRQQEL LQLKSYTPSE ESLSVQLHNK THLSRDPEAD
HGRFQLELEC SKFPMPHMNG MSPELSMNGH ATPYEIHNAF SRPSSKQHTP QYPSSHLDQD
IVPCTPSHSS RQKADKVTSL SLPDYTRFSP AKIALRRHLN QDHGVNGKAT SHEIQRAEHV
KENGLTYPSP GIANGIKLSP QETRPSSPAA LPSAGEKVLR ERTSVSNGET ITSLPISIPL
STVQPNKLPV SIPLASVVLP SRVEKVRSTP SPVHQSRDSS TLEKQIGASS HNGISNAAGN
KPLALATSGF SYSSGSVAVN GNLTNSPAHL NHSVDQAALD DSGSLFNSVG SRSSTPQHPL
LMMQSRNSGQ NSPAQPHSAS PRLNGTAQSL VGGLQYADAQ KMFAEGSKGD LQSDAAFSDP
ENEAKRRIIF TISPNTGHVK QSPSNKHSPL PASARLDCGQ AHAQDGKKRG RRKRSSAGNL
SGNSGVSPKR KSLPTVSGLF TQPSGSPLNI NSMV
//
