ID A0A367XVM0_9ASCO Unreviewed; 1331 AA.
AC A0A367XVM0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 08-NOV-2023, entry version 21.
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=DOT1_1 {ECO:0000313|EMBL:RCK57459.1};
GN ORFNames=Cantr_06179 {ECO:0000313|EMBL:RCK57459.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK57459.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK57459.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK57459.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) 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 -!- ACTIVITY REGULATION: Ubiquitination of histone H2B to form H2BK123ub1
CC is required for efficient DOT1 methyltransferase activity on histone
CC H3. {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCK57459.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QLNQ01000028; RCK57459.1; -; Genomic_DNA.
DR STRING; 5486.A0A367XVM0; -.
DR Proteomes; UP000253472; 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 Gene3D; 1.10.260.170; -; 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};
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:UP000253472};
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 964..1286
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 19..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1288..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1331 AA; 152677 MW; 16E9E1F65C10A17E CRC64;
MATPTEEEGI KSKELHIQAD KGTPDSTIPA HAHLHTPDMS DYSCDESKLS SEADETQEDT
PVWTEELDET LKELVSQPIT FSHVLTRFPE FDWEFIGTKI VESKINRASW KKKLLAYDLL
FKKQGVFELE NRDHLFDAFD MLKSHDWDDG EIEQFVCCFY EDLTTARVQA GLPNKSLKDV
TKVLNQVQPR VFWTPAEEQL VRENLDDMDG LSKGLFYRTE NAIRKKTIIF RKTKRPDTGL
QKYASSPMTF SEILKMFPNQ DWRELSRKLT SKAKDSNWSK KIGCYCLLYH FEEYGTSKVG
AELLEVIGQA RTEFQAFSKG IFKAFSLNSF GKCSRSLFEK LYSLFLYDLT KETCKELVPR
DIVAHMKNFV SAFDPRCQNL SPGEIDFLEK NTSMDLNELM QNLPCRTKDG ISRALESLLN
PEPEADPLLD ELVEHDLTLE TIKAYFPKDE FQDILNEIRI HPKFNADTFT KGETKLMNDL
ALKNTPVDKC IQAFPARDEE FLRRMYHESK YITGRKKKFT SPEERLLYEA RWTVSSMGNT
TTSNRDKRAQ KRSADFEEIA KLEEKFAVKR SKKLKPELSE KELALRRERQ EKRRLEKEKA
AEEKQKKIQL QRLQKQEREP KPKKQTESME LKMLLEAAEY FQSTVGDRKT VREGEKRRKV
KAEYYEPEAA PSHAPVKLKT THRQAMKNNL KKVMQLKAKE EEAKLKKKEK PQSKRSKSRR
ALDDYTIAEL ETHYEIKEET PVPDDTPSKY DPPDILADSY VELKGRHLFV SEFYDENPVV
PKLEFVNISQ QERDNSHDKS MSPGKAVMTA NDDKILFDDN LALELVIAHV RSYRDMPVGF
PPRFIPDTKE INPLNIVRIR FLLYPEHCEL FILGSPKSNE LDPAQEIAKV FMIHYSLYFS
HSEELKNIII EDYCKKLETS IDNSDFAEFM SVIDNWNALM LHLSPNTESC QRIVESGADI
NEAPKQGLHD IETKPPTSSD LKIHKFYQEI LYETVSPSYQ EVQNTLGESS DTLAADATSP
STAEVEVPTN VSKDSKVVKP DNYNADFFRR LREKTEISRY AMQQLLLRVY SRIVSTDSKK
LRSYKAFTAE VYGELLPSFT SEVLEKVNLS PGQRFYDLGS GVGNTTFQAA LEFGAAPSGG
CEIMDHASHL TKLQTGLLQK HLAVLGLTPL NLNFELHASF VNNERVTRSC LDCDVLIINN
YLFDGALNAE VGRMLVGLQP GTKIISLRNF ISPRYRATGD TVFDYLRVEK HEMSDVMSVS
WTANKVPYYI STVQETILSE YLRDDGSVHG GASSSDRSSS KSVSPLAVDF SESREDALMM
TPPTDSETQK E
//
