ID A0A094DWX3_9PEZI Unreviewed; 1266 AA.
AC A0A094DWX3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=V497_01903 {ECO:0000313|EMBL:KFY63955.1};
OS Pseudogymnoascus sp. VKM F-4516 (FW-969).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420910 {ECO:0000313|EMBL:KFY63955.1, ECO:0000313|Proteomes:UP000029268};
RN [1] {ECO:0000313|EMBL:KFY63955.1, ECO:0000313|Proteomes:UP000029268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4516 (FW-969) {ECO:0000313|Proteomes:UP000029268};
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:KFY63955.1}.
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DR EMBL; JPJZ01000411; KFY63955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094DWX3; -.
DR HOGENOM; CLU_265104_0_0_1; -.
DR OrthoDB; 1331863at2759; -.
DR Proteomes; UP000029268; 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 CDD; cd02440; AdoMet_MTases; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000029268};
KW S-adenosyl-L-methionine {ECO:0000256|RuleBase:RU271113};
KW Transferase {ECO:0000256|RuleBase:RU271113}.
FT DOMAIN 935..1266
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 80..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..877
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 138856 MW; D132E5369B45C305 CRC64;
MASQKPRQSN SDDESTRASH QDAPKATAAS LTQPNTDETK NISAVTTFSG EVPPRSWYGG
GSWPRIKSNP SIQVVKESIM AGKSGNNSRA AGAALFEQRT PAEAQISKAS PSRPPSMDPG
KSKETLKLVP GESSTDNTTM GNNGTAKTKT IPHSAKPIED QSESTNTVVE PELDNVKLES
DAVIEEQKAT GWLEWLRPTK VQNSPQRGLA TAEDSVPRLD APQQPPSVNK TKSLDPSAPT
VASDRQENDP TDQHRQPEAN SRWQGLWPVS NSSSTVARPE ENNSQQEPVK PDLNMGKDNE
QSNNATTTGS SWAFWSRQVP SATRQTTNSK ELGEIAVTGE PSQEHPVAAL SNGPENTKVG
PGTPLNQAKL SKAEMPSKTA AANSASSTKS FAPNLLLPSF RNTYQLAESP SIIQQIARLL
FRSHQPPTNH LFVIKDPPKI KKAIAIGIHG LFPAALLRTV IGQPTGTSIK FANHGASAIE
RWAERQGFQC DIEKIALEGE GKIAERVDHL WKLLLNWVEH VRQADFILVS CHSQGVPVAM
MLTAKLINLG VVSSAKIGVC AMAGVSLGPF TDYKSRLFSG SAAELFDFAD LDSEVSRSYH
ESLSVAMKYG VRVTYVGSID DQLVSLESAV FSPVDHPYIY RSVFVDGRIH APDFITNLVG
FALKLRNLGV SDHQLIKALS APLAGSLYSG EGHSRLYDEE AIYDLSVQFA LETTSVNQNV
GLKVQRSAAN GNSNPFQLPW SMRGLLEEDV VKTELDQEAK ELLLQFEEWK PTTKVLKDVK
YRLEVINSKQ KIRTETVPVK ASPGTISRTP SRSQSEARLA SSLPRSKSSG QASRSSRKDN
YSTKLSLPER SISRKRSPVY QRIESDSSED ESQESPPVNK RQRLTPGELD DPARSLPSRK
QFSQIDSTLL IHAADIASHK LGYRAAFGGT DLEEAPVGLQ YPGSSIAERY ELVFKKDSFD
PVEEILGVIK DFTDFFLDDE NAKPFVDPDT GIIRRLERAR NLGSLEGFKS ALIDYNSAVE
SLRLGKDIAS ILDKKHGVSE SLVVRIMAQT YDRAVSPKVD LLRKYENGTN EIYGELKSNL
VYKILAETKI TSKQVFVDLG SGVANVVLQA ALQVGCESWG CEIMENACSI AEAQKAEFEA
RCRLWGLQPG LTRLERGDFM VNEDIREALQ RADVVLVNNE VFTPELNVSL VNLFLDLKEG
CKIVSLKSFV PENRKISNYN NNDPSNILDV AKKAYSTKSV SWKDEGGNYY IATKDSTRLQ
SYGDRS
//
