ID   A3LQ22_PICST            Unreviewed;      1039 AA.
AC   A3LQ22;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 89.
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=PICST_41120 {ECO:0000313|EMBL:ABN64600.2};
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN64600.2, ECO:0000313|Proteomes:UP000002258};
RN   [1] {ECO:0000313|EMBL:ABN64600.2, ECO:0000313|Proteomes:UP000002258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC   {ECO:0000313|Proteomes:UP000002258};
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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}.
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DR   EMBL; CP000496; ABN64600.2; -; Genomic_DNA.
DR   RefSeq; XP_001382629.2; XM_001382592.1.
DR   AlphaFoldDB; A3LQ22; -.
DR   STRING; 322104.A3LQ22; -.
DR   GeneID; 4837176; -.
DR   KEGG; pic:PICST_41120; -.
DR   eggNOG; KOG3924; Eukaryota.
DR   HOGENOM; CLU_004528_0_0_1; -.
DR   InParanoid; A3LQ22; -.
DR   OMA; NFIPPRY; -.
DR   OrthoDB; 146338at2759; -.
DR   Proteomes; UP000002258; Chromosome 2.
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}; 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:UP000002258};
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          667..986
FT                   /note="DOT1"
FT                   /evidence="ECO:0000259|PROSITE:PS51569"
FT   REGION          345..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          981..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          276..303
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        345..373
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..409
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..448
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        994..1013
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABN64600.2"
SQ   SEQUENCE   1039 AA;  119382 MW;  37D9E081E7B24A97 CRC64;
     VKTLTASNVW TQDEIEHFHT CIVHNATRTG MGHLIEQKSI AELNNAVTQL MSRFYWTKGE
     MTFLENHLGA GVAELCHEIP LRAKHGIVQM KSVRDLEVTI AEKKVVNLTD SSMEDTTEDD
     NLAYCIQHDL SRETLEALFP DWSLSETLDR IVFQAGPLDS IALTTGEKQI IKDSIKKQKS
     LESVQFNFPC RSKDYLVEKF KEFEFVSSRK TKFKSLSERL LYEAKWVLYS SGETFTTTRR
     SRKRALEESF ETMEKEALVS IYTKPAPKQE MTPEELEERE RRREALKESR RLANERKALL
     RKQRKEDLER RKAAGLIKAK PKSDITHSIK DLLAGSEHFQ SVIGDKKKVE EGQKRKRIQA
     VHYRPEIEPK KPSKLKVRHR QAEKSKIKLA LKLKKQQEHN KRKPKKEPKK KKKTVEEESL
     ATPETEEFIK EEIDEDEEEE EEEDTYSPFD PVDLNSDSFV PLHGRQFYAE EIYVDKPHVP
     ELKFVEVTEE SENSLISSST LTETKRIMTT NDDDIVYEDC LAADIIRSHI KNYRDLPISF
     PPLLDPSSSE RKIYPTNKVR IRFLLYPQHC ESFILAAPKT NELDPVYEII KLFMIHYALF
     FSHSSEIRRI ITEEYCQKIE HSIEENDFSD FMFVVDKWNA LMLKLSPNEE AVQSIVQSGK
     EDINAGLRSY LSEQEIRVPT SEDLKLQAFL EAVILEDLSP TFQLIKEEPS DAEKQEFVPK
     HLGDVEAPKN VSDELKDMKP DDYNLIFFTR LKEKTEISRF ATQQILLRIY SRIVSTDSRK
     LRSYKAFTAE VYGELLPSFT SEVLEKVNLL PNQKFYDLGS GVGNTTFQAA LEFGASMSGG
     CELMEHASKL TKLQEGLLQK HMAVLGLKKL NFNFALSQSF VDNDPVRDAA SDCEVLIINN
     YLFDGNLNAE VGRLLCGLKP GTKIISLRNF ISPRYRATGD TIFDFFKVEK HEMSDFLSVS
     WTANKVPYYI STVQDRILPE YLGKDESPDS DRSTPTLKSE NGSSENLAGS LTPFTATPEP
     DMFKDLSCVL GDEDDILLH
//