ID H8X3Y7_CANO9 Unreviewed; 1468 AA.
AC H8X3Y7;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
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 ORFNames=CORT_0C04010 {ECO:0000313|EMBL:CCG25775.1};
OS Candida orthopsilosis (strain 90-125) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1136231 {ECO:0000313|EMBL:CCG25775.1, ECO:0000313|Proteomes:UP000005018};
RN [1] {ECO:0000313|EMBL:CCG25775.1, ECO:0000313|Proteomes:UP000005018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90-125 {ECO:0000313|Proteomes:UP000005018};
RX PubMed=22563396; DOI=10.1371/journal.pone.0035750;
RA Riccombeni A., Vidanes G., Proux-Wera E., Wolfe K.H., Butler G.;
RT "Sequence and analysis of the genome of the pathogenic yeast Candida
RT orthopsilosis.";
RL PLoS ONE 7:e35750-e35750(2012).
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; HE681721; CCG25775.1; -; Genomic_DNA.
DR RefSeq; XP_003868679.1; XM_003868631.1.
DR GeneID; 14539318; -.
DR KEGG; cot:CORT_0C04010; -.
DR eggNOG; KOG3924; Eukaryota.
DR HOGENOM; CLU_004528_0_0_1; -.
DR OrthoDB; 146338at2759; -.
DR Proteomes; UP000005018; Chromosome 3.
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 CDD; cd00167; SANT; 2.
DR Gene3D; 1.10.260.170; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001005; SANT/Myb.
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 Pfam; PF13921; Myb_DNA-bind_6; 2.
DR SMART; SM00717; SANT; 4.
DR SUPFAM; SSF46689; Homeodomain-like; 4.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51569; DOT1; 1.
DR PROSITE; PS50090; MYB_LIKE; 3.
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 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 169..212
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 347..397
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 435..485
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT DOMAIN 1067..1389
FT /note="DOT1"
FT /evidence="ECO:0000259|PROSITE:PS51569"
FT REGION 22..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..818
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1468 AA; 168964 MW; 5629A7FF8817D036 CRC64;
MKCWFDYLLG KDTTPKVEEE LINNKSKQPR SHPTTMETSE TTPSNLIREL ACSDQPLSKI
VNDHSETPWT QVMQVCREIL SSGENSTNQL VERKIIVQQI LHPNKQPTPD IELDTSIKDE
VEAAITRLRR AGLDNSVIEK ICSNSNSNVI KLISNNKTKY NNGKKIWQKW TQEEDRLLWM
LRIEEKLEWD VIVSLIRSHS ENACKHRING MMLSDDVQHS SLEEEEEEEQ VSTDRSSPTL
QARITNRSSR VSNSEATSPI SANARGWKWT PAEEKLLWES IIVRNLNWNT VLPLFPNRSE
SGVKAKLWDL KKKHVCTAPK SSHSPEKSFN RMRPITGDQH FSSEEDEEPH VRQFWTDEED
ELLWELKTEK QLSWEDIVLH FEHRTQYSCQ NRFARIFERF TTKQAPTTKN PSKLQTRTTN
ESSRATNGEA DQHISTNTKR MKWTPEDEEL LWELRELHNL DWNEIYPSFP NREHTAVQTK
YFELRNKYGN IASKPKALSK KSIRASSKQR HTEIVKQIKR SASEPTEEEK LRECIEVDLT
KGNLSYCFPN YAIGDLCTRI ESHPDFVEKS LTIGEKSLMT EQVHKGDTVE EIYSDYPLRS
KSFVDLKYKE IAYTSSRKIK FKTREERLLY EAGMAYLGSG PSKRSTRRSA GCDVDFDKLE
ELEQKASRIA PPPKPKIDPE VAAARAKARL EAQERKKAER RRIYELAKAR RLANPRDYSK
KSSSPLVSLN LIKQLSESAE YFQTVTGDRQ KVQEGAKRKR TQTVLFSPVI EVKLKTRARQ
AQKWELRRKL KEEARLKREL QRKSKKLTTK KKRKLNKKGR HSFDDEYEEF SDFDLRSVEP
ESQPEEEEEE NHISPFDPPD INADTLVPLN DRHLFFKSIY EQEENVTLPE LEFRHLREDE
TAKQAMTTND GSILYDDELA ADVVGSHRKC YRDMPISFPQ YSTTPASSSN GSTNINYANS
VKIRFFLYPQ HCESFVLAEP KDNELDPVHE IIKVFMIHYA LYFDYSPTIK TYINELCHKL
ELAIEANDFS EFMYVIDTWN TLMLRLSPNE EAVARIMETG DDINAGARSL LNESEIRQVR
NEDLNLEMFY NEICFESISP VYEPIQGEVE VIEDDVDADI SIGKIEPPRN KSPQEREMNF
IKPSHYKSDL FKRLREKTSL SRYAIQQILV RVYSRIVSTD SRKLRSYKAF TAEVYGELLP
SFTSEVLEKV QLKPTQRFYD LGSGVGNTTL QAALEFGACC SGGCEIMDHA SNLTTLQENL
IQKHLAVFGL SPLNLKFALK QSFVNNEQVR QDCLASDVLI INNYLFDGDL NDAVGKLLYG
IKPGTKIISL RNFISPRYRA TFNTAFDFFS VEKHEMSDIM SVSWTANKVP YYISTVEETI
RPEYLGREEL LGELMLHAGM LSKSTTPSIG DVGDATRGIG RDYDEEDEGS ESVHAMDVDG
RGGDGVNGDG GESTPPTDHN SEPENDKN
//