SET1_ASHGO
ID SET1_ASHGO Reviewed; 975 AA.
AC Q75D88;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 129.
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=ABR136W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 655; 659 AND 671.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016815; AAS50907.2; -; Genomic_DNA.
DR RefSeq; NP_983083.2; NM_208436.2.
DR AlphaFoldDB; Q75D88; -.
DR SMR; Q75D88; -.
DR STRING; 33169.AAS50907; -.
DR EnsemblFungi; AAS50907; AAS50907; AGOS_ABR136W.
DR GeneID; 4619193; -.
DR KEGG; ago:AGOS_ABR136W; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_004391_1_0_1; -.
DR InParanoid; Q75D88; -.
DR OMA; LHQPLNT; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:EnsemblFungi.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
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:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
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; 2.
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..975
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269764"
FT DOMAIN 833..950
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 959..975
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 10..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..586
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 111600 MW; 3DA838A53513B21A CRC64;
MSGYYNHVKH QGYSRYGQNS TVRNGQHDGL RYRNPSPAHN GTNEGEGLQG SRYENAGGVT
HARRPPPVVK WGEAAFRAKY HYFDVEERKL LHLDEMKHWQ NGRLPANGYV LVADAGSKGR
PVMRERNPEE QAVDPRGARA AHTVRRVRSL LTALPRIPYD AHWVGPEPPK EVVVFPKQRE
QALSVQDPII KNFFGTFGEV AHFESFNDPN NALPLNIYLV RYINVEGNPD SPYKAAYKAV
KQFAKQDYLV SGARFAVRLN MNGFLQKTID KFVTENLQRA AKLRHEQAKQ QSTVQKVTNV
SAVPSGVPPP KIPLGLERIV NNKPILRVSA RFCALHGITS EDFKYGLKNY HWTRVINHYS
GIYIIFDDIA EAEKCLQMES LRLTFFSRRR KIPVKIKFML IEPSHQPPAS QPLTDQDEVP
KVYETEAELI EETLKHIINE LKTTLYKDIR RRLLGPTIFD ALNPGNYPDI VARRQKEEEA
KKEKEKAMVE KTKKEAPSAA AFDIFNLYGT AYKKRDGTKG KKRHVAEGRP EESSGRRRIQ
SKGTAPMAHM LNYESLKVNG TASPIKEAES ETCSSDEEDD DNFDVEMTDQ SSIKKLKRES
TATTPEQEPL QERVAGLSAE RTKELLSYPE KYRPLAGDQP EPIYPEFLIE KYDDPLLSIV
DLQRSVKDKE DMELLKKVIA YDREEVKDVI NDIEFFAWRL HRDYKEHKEN MQHQSKLSES
TYKNLLNAHG GCFKQQGFRK MPDKLKSIYL PHRRKLNQPL NTVYHHGIED FANTDNNKMD
TDPPEDTFTP EQTSSRVNRA LQRRFQQDIE AQKAAIGTES ELLSLNQLTK RKKPVTFARS
AIHNWGLYAL EPISAKEMII EYVGERIRQP VAEMREKRYL KSGIGSSYLF RVDESTVIDA
TKKGGIARFI NHCCDPSCTA KIIKVGGMKR IVIYALRDIA ANEELTYDYK FERETDDEER
LPCLCGAPNC KGFLN
