SET1_CANGA
ID SET1_CANGA Reviewed; 1111 AA.
AC Q6FKB1;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:P38827};
DE AltName: Full=COMPASS component SET1;
DE AltName: Full=SET domain-containing protein 1;
GN Name=SET1; OrderedLocusNames=CAGL0L12980g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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, which subsequently plays a role in telomere length
CC maintenance and transcription elongation regulation.
CC {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 -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; CR380958; CAG62307.1; -; Genomic_DNA.
DR RefSeq; XP_449333.1; XM_449333.1.
DR AlphaFoldDB; Q6FKB1; -.
DR SMR; Q6FKB1; -.
DR STRING; 5478.XP_449333.1; -.
DR EnsemblFungi; CAG62307; CAG62307; CAGL0L12980g.
DR GeneID; 2890583; -.
DR KEGG; cgr:CAGL0L12980g; -.
DR CGD; CAL0135102; CAGL0L12980g.
DR VEuPathDB; FungiDB:CAGL0L12980g; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_004391_1_0_1; -.
DR InParanoid; Q6FKB1; -.
DR OMA; LHQPLNT; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:EnsemblFungi.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:EnsemblFungi.
DR GO; GO:0003723; F:RNA binding; IEA:EnsemblFungi.
DR GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; IEA:EnsemblFungi.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; IEA:EnsemblFungi.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IEA:EnsemblFungi.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IEA:EnsemblFungi.
DR GO; GO:0090241; P:negative regulation of histone H4 acetylation; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IEA:EnsemblFungi.
DR GO; GO:1905088; P:positive regulation of synaptonemal complex assembly; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:1902275; P:regulation of chromatin organization; IEA:EnsemblFungi.
DR GO; GO:1903341; P:regulation of meiotic DNA double-strand break formation; IEA:EnsemblFungi.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IEA:EnsemblFungi.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0055092; P:sterol homeostasis; IEA:EnsemblFungi.
DR GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0007130; P:synaptonemal complex assembly; IEA:EnsemblFungi.
DR GO; GO:0000723; P:telomere maintenance; IEA:EnsemblFungi.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 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; 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; PTHR45814; 1.
DR Pfam; PF11764; N-SET; 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; SM00317; SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 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; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1111
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269768"
FT DOMAIN 969..1086
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1095..1111
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 891..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..937
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 127906 MW; 79C2294F8540340F CRC64;
MSQYRRYFDE SDPNQSRYSS RNGNGSYYQS RGSQRYNYEG QPDESGYRKD YQKSLGAGNG
QYNNRQYSRN DNGSSNNVPQ GRYTPTEYSS RRSFHHNDAE IKLPSAPSRV QYSYKARNSE
TKDPNAYRPN HTDQSYIRGR NSNGKSYGPV NIPTGPQQSR IVSNRNHNQH NVSLRPKATV
KYKNIEQLTC KYHYFDPVEK VLTHRTEMKK WTEVNKDMPE VGFVVQQETI NGQVKSVIKS
RKPDEKSTDP RKTTIPNTGN SSTKKKQRTA RKCRKELTLV PRISYDKFSL GPPPSTEVVV
FAENFSNTQM ANIPDISIKN YFRKFGELAH FASYSDPKTA LPLHLYLVKY THPSGKINDS
AKAAYQAVKS CQEQKCCILG CNFNVLLNKN NELENIMNKR ITVLSKETEK VKLQMEQEKK
SALKKSAELN KEEKGILKPL KTIPGDLRPI VNNRPALYIS RRFISVMGLR LIDFKSKLKA
YKCSRFLEHA TGFYIIFNNL EHAKLCMDAE SGKLTMASRR KRTTVPINFI LIEPFTSRFS
KKYKDVPSDS KEKVEIVRYN NKEELIDAAS KYIIEDLAKT LHTEIRKTMI GPAVFDTLQP
SNFPQLVQKR KEQEELKKAD MEKKKAEQAK SKDFNIFNLY ASYTNKPKRR QKRYLSDEEA
EEELPQKKIK PLAHLLDEVR EDSPTSGLES TDDPTEGDNM STSSSSEDED DIMDDFQNED
KKDDMFSTPE TNEEMDYHHK IDYRTENLID KEIDDASQVN ERYLPSATQF PVTVYPENTY
DSEYIDTVSL FDLQDAIKDE EDMEFLKECL PAGEDLEFDD DNGLLEYRIW KIKQMADISQ
SSTNNELRLN NQTLDKTLFE KNIPFIASEF KHIPEKLKSS YLPHKRRVHE PLNTVSHHNE
SKEQSPDIAI KEKSVNKADT GEGSLAEISS SRDNRASNRR FQQNIEAQKA ATGTESELLS
LNQLNKRKKP VTFARSAIHN WGLYALEPIN AKEMVIEYVG ERIRQPVAEM RERRYIKNGI
GSSYLFRIDE HTVIDATKKG GIARFINHCC EPSCTAKIIK VGGKRRIVIY ALRDIAANEE
LTYDYKFERE TDAEERLPCL CGAPSCKGFL N
