ID A0A094F4H1_9PEZI Unreviewed; 1258 AA.
AC A0A094F4H1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|RuleBase:RU271113};
DE EC=2.1.1.360 {ECO:0000256|RuleBase:RU271113};
DE AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|RuleBase:RU271113};
GN ORFNames=V498_07952 {ECO:0000313|EMBL:KFY83588.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY83588.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY83588.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-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|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|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:KFY83588.1}.
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DR EMBL; JPKA01002478; KFY83588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094F4H1; -.
DR HOGENOM; CLU_265104_0_0_1; -.
DR Proteomes; UP000029270; 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 Gene3D; 1.10.260.170; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR025789; DOT1_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR47349:SF1; AER328WP; 1.
DR PANTHER; PTHR47349; CHROMOSOME 8, WHOLE GENOME SHOTGUN SEQUENCE; 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|RuleBase:RU271113};
KW Methyltransferase {ECO:0000256|RuleBase:RU271113};
KW Nucleus {ECO:0000256|RuleBase:RU271113};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU271113};
KW Transferase {ECO:0000256|RuleBase:RU271113}.
FT DOMAIN 927..1258
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 138422 MW; 838C238B004E7888 CRC64;
MASQKPRQSN SDDESSRACR QDVPKATVAS QTQSSTDATK NISPTTITTG EAPRSWYGGG
SWPRIKSNPS IQVVKESIMA GKSNNNSRSA DVALFEQRTP PEAPPVKATV SRPASMDPGK
SKETLEIVSG ECSIKDTATG SYNTANELVT HSVKPTEDQS KSTDTVVEPG LDNPKPESDD
VVEQQKATGW LEWLRPTKVQ HSFQHGVATT EETAPPPMDE PQQPPNVNKT KQTHPSTSTV
ASDSQQNSVT SQHKRIEQNS RWPGLWPVSN SSTTVARPEE NNSEQEPIKP DLIVGKVDGQ
RNNATATGSS WAFWSKQVPS ATRQTTNSDE LGEIAVTGQP SQEHPVAAVS NGPENAKAGS
GTQPHQAKLS RAELPTKTAA VTSSSSTKSF APNLLLPSFR NTYHLAESPS IIQQIARLLF
RSHQPPTNHL FVIKDPPRIK KAIAIGIHGL FPAALLRTVI GQPTGTSIRF ANHGASAIER
WAEKRGFQCD IEKIALEGEG KIGERVDHLW KLLLNWVEHV RQADFILVSC HSQGVPVAMM
LTAKLINLGV VTSAKIGVCA MAGVSLGPFT DYKSRLFSGS AAELFDFADL DSEVSRSYHE
SLSVALKYGV RVTYVGSIDD QLVSLESAVF SPVDHPYIYR SVFVDGRIHA PDFITNLVGF
ALKLRNLGVS DHQLIKALSA PLAGSLYSGE GHSRLYDEEA IYDLSVQFAL ETTSVNQNVD
LKVQRSAANS NSNPFQLPWS MRGLLEEDVV KTELDQEAKE LLLQFEEWKP TTKVLKDVNS
KQKIRTESVP VKASPGTTKR VPSRSQSEAR LASSLPRSKP LGQTSRSSRK DSYSTKLSLP
ERSASRKRSP VYQRIQSDTS EDEGQESPPV NKRQRLTPGE LDDPTRTLPS RKQFSQIDST
LLIHAADIAS HKLGYRAAFG DSDLEGAPVR LQYPGSSIGE RYELVFKKDS FDPVEEILGV
IKDFTDFFLD DENAKPFVDP DTGIIRRLER ARNLGSLEGF KSALVDYNSA VESLRQEEDI
TKILDKKHSV SESLVVRIMA QTYDRAVSPK VDLLRKYENG TNEIYGELKS NLVYKILAET
KITSEQVFVD LGSGVANVVL QAALQVGCES WGCEIMENAC SIAEAQKAEF EARCRLWGLQ
PGLTRLERGD FMVNEEMRAA LQRADVVLVN NEVFTPELNV SLVNLFLDLK EGCKIVSLKS
FVPENRKISN YNNNDPSNIL NVAKKSYSTK SVSWKDEGGN YYISTKDSTR LQLYGDRS
//
