ID SET1_YARLI Reviewed; 1170 AA.
AC Q6CEK8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9Y7R4};
DE AltName: Full=COMPASS component SET1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=SET1; OrderedLocusNames=YALI0B14883g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Catalytic component of the COMPASS (Set1C) complex that
CC specifically mono-, di- and trimethylates histone H3 to form
CC H3K4me1/2/3. Binds RNAs which might negatively affect its histone
CC methyltransferase activity. COMPASS recognizes ubiquitinated H2B on one
CC face of the nucleosome which stimulates the methylation of H3 on the
CC opposing face. {ECO:0000250|UniProtKB:P38827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:P38827};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:P38827};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60272, Rhea:RHEA-
CC COMP:15537, Rhea:RHEA-COMP:15540, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:P38827};
CC -!- SUBUNIT: Component of the Set1C/COMPASS complex.
CC {ECO:0000250|UniProtKB:P38827}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- DOMAIN: The RxxxRR motif forms an adapter helix that bridges the
CC nucleosome and ubiquitin. {ECO:0000250|UniProtKB:P38827}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; CR382128; CAG83155.1; -; Genomic_DNA.
DR RefSeq; XP_500904.1; XM_500904.1.
DR AlphaFoldDB; Q6CEK8; -.
DR SMR; Q6CEK8; -.
DR STRING; 284591.Q6CEK8; -.
DR EnsemblFungi; CAG83155; CAG83155; YALI0_B14883g.
DR GeneID; 2907346; -.
DR KEGG; yli:YALI0B14883g; -.
DR VEuPathDB; FungiDB:YALI0_B14883g; -.
DR HOGENOM; CLU_274191_0_0_1; -.
DR InParanoid; Q6CEK8; -.
DR OMA; ERLPCLC; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR GO; GO:0042800; F:histone H3K4 methyltransferase activity; IBA:GO_Central.
DR GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd00590; RRM_SF; 1.
DR CDD; cd12303; RRM_spSet1p_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR017111; Set1_fungi.
DR InterPro; IPR024636; SET_assoc.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR PANTHER; PTHR45814:SF2; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF11767; SET_assoc; 1.
DR PIRSF; PIRSF037104; Histone_H3-K4_mtfrase_Set1_fun; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51572; SAM_MT43_1; 1.
DR PROSITE; PS50280; SET; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1170
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269778"
FT DOMAIN 403..489
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 1029..1146
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1154..1170
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 995..1000
FT /note="RxxxRR motif"
FT /evidence="ECO:0000250|UniProtKB:P38827"
FT COMPBIAS 13..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..835
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
SQ SEQUENCE 1170 AA; 133489 MW; 27FC52DEC9755E44 CRC64;
MANGSDTKPV PKGPRGARAD DTRTPPHPDR RGSDRDQYFS KDRSYGGRTD RDYSDYDRAY
PPPRDYDRYG GGKYGKYDKY DKYDRYDRLD SHDYPPRRDR DYDRSRDARD TDSRDYGRLP
PRDTRPPPRG GREYRYARDE RGWDRDRRDL DRDRDRDPRD RERDARDRDR DRDFRDRDHD
PRDRDPKGYR PHSLDPLPSR DRDMPPRERE RELVRERDLF SRDRDLITGV RELARSPPPP
LRDGRNRDRS NDRHDRSFDK HTRDRGTRDR DTKEKGSVIS TPQTAPTPRL TPTNGKPDLP
TSQPPAPPSP PRLKTFPKEV WETVGRKNNT RLTYDPELSK DKQKGKRGIY EEVKKGASTT
EDPRSKHPHY FKTSSKSNKK PYQRLPVPRF LYDANSIAPP PSTQIIVKGL SSLTTSKTIT
AHFKTYGELE AVNMVEDPAT GSSVGACLVR FKVTKNNYEA AHECLKKAIR GQKTGRIDQA
KYRVEPDEDG AKAKDIIKRV AARAAKKAMP VKQPPTAPAA DKSIMEKLPT PVPSARPSPK
AAQLMKTSAY IFIAGKYLPS EKVFASDIRR ILRDFGWFDV LKEGDGFYVF FDNNRDTVEC
YEAMNGRKVN GHQMAMAMIR LSRVAPKTKE SEENATEQAP KLPPKEEARK LIVQELANSL
RKDIRERVIA AAIVEFLNPA RFTHIKQDPE PSAATEPNTV NASAARVDTP EPVQSSSAIP
GFLPRFKIKR KGDPTKKKDA TKKNRKKISA RPMNHVLNDY YSDEEDSTRM STPIVPDTSA
DAAELPIRKP RKKISQSKQR IMDFSSSEGS NESEEEEEVE DDMEEEEDET AQEELQEAST
LDTSQQLTTA FGEILDWAPA HGFPQPVTAD KKGGALTTIS GFQALVKDDE DMELLQEALE
GIEPEKINGE AWTWTHKHLN EAVAKENAEF PELAAPNAFV NSTGSWKSQG YFKIPEAAKS
EYLPHRKKLN IPIDTLQMEN REKKKENASN SRVNRANNRR LVADINMQKQ LLSTETDVLN
FNQLRKRKKP VKFARSAIHN WGLYAIEPIA ANEMIIEYVG EVVRQEIADL REARYMRSGI
GSSYLFRVDE STVVDATKRG GIARFINHCC TPSCTAKIIK VEGQKRIVIY ASRDIAANEE
LTYDYKFEKE IGEERIPCLC GAPGCKGYLN
//
