ID   B2AWA0_PODAN            Unreviewed;       527 AA.
AC   B2AWA0;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific {ECO:0000256|ARBA:ARBA00020987, ECO:0000256|PIRNR:PIRNR017570};
DE            EC=2.1.1.360 {ECO:0000256|ARBA:ARBA00012190, ECO:0000256|PIRNR:PIRNR017570};
DE   AltName: Full=Histone H3-K79 methyltransferase {ECO:0000256|ARBA:ARBA00029821, ECO:0000256|PIRNR:PIRNR017570};
GN   ORFNames=PODANS_7_6450 {ECO:0000313|EMBL:CAP68674.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP68674.1};
RN   [1] {ECO:0000313|EMBL:CAP68674.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP68674.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP68674.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP68674.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) 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|ARBA:ARBA00003482, ECO:0000256|PIRNR:PIRNR017570}.
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|PIRNR:PIRNR017570};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR017570}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. DOT1 family. {ECO:0000256|PIRNR:PIRNR017570}.
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DR   EMBL; CU633900; CAP68674.1; -; Genomic_DNA.
DR   RefSeq; XP_001908001.1; XM_001907966.1.
DR   AlphaFoldDB; B2AWA0; -.
DR   GeneID; 6192592; -.
DR   KEGG; pan:PODANSg5036; -.
DR   VEuPathDB; FungiDB:PODANS_7_6450; -.
DR   HOGENOM; CLU_027287_2_0_1; -.
DR   OrthoDB; 146338at2759; -.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042393; F:histone binding; IEA:InterPro.
DR   GO; GO:0140956; F:histone H3K79 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0031509; P:subtelomeric heterochromatin formation; IEA:InterPro.
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; IPR021162; Dot1.
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   PIRSF; PIRSF017570; Histone_H3-K79_MeTrfase; 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|PIRNR:PIRNR017570};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|PIRNR:PIRNR017570};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR017570};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PIRNR:PIRNR017570};
KW   Transcription {ECO:0000256|PIRNR:PIRNR017570};
KW   Transcription regulation {ECO:0000256|PIRNR:PIRNR017570};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR017570}.
FT   DOMAIN          221..527
FT                   /note="DOT1"
FT                   /evidence="ECO:0000259|PROSITE:PS51569"
FT   REGION          1..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..154
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         348..351
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT   BINDING         371..380
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT   BINDING         397
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
FT   BINDING         433..434
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017570-1"
SQ   SEQUENCE   527 AA;  59069 MW;  D8294BDF1C4B5CC5 CRC64;
     MSIFNQKSKF KVKTEVRAVK KTLPEKPKPK PTSAPPSTSR IPSSVRASPS TTSTLRASPL
     PPSARKSQIG SSRYLDPSSA LKAPSSSTSS NSRKRPRASH SPASPSFDSD SDSDSASDDD
     WQDQLDPRKR LKRLEQLRRH DPNRRVRHPK MWKGDRESEG ELLPIIHAVE VASLSEKCQP
     VMGLSRDEVG VRLRYPGSNH REKYACSILM STFYNCHLLF STKVYELVKG KDKIEGAQDI
     LTVVRHVASI YLSEEEARPF LDQNSGIYRR LERCKNLNDG KGFKEALKEY SESLFALQRK
     GVIAKNLENM RGVPQELVAF ILDQVYDRTV APKVELLAKY ENGTDNVYGE LLHPFISDIF
     ERTQLTSDMV FVDLGSGVGN VVLQAALEIG CESWGCEMME NACNLADAQK REFAARCRLW
     GVAPGKVHLE RGDFRKNEPI LESLKRADVV LVNNQAFTSQ LNDNLVNMFL DLKIGCKIVS
     LKTFVHDNKL AENDVASSIL DVEHLTYPEE YVSWTGAAGT YCISTRK
//