SET1_KLULA
ID SET1_KLULA Reviewed; 1000 AA.
AC Q6CIT4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 120.
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=KLLA0F24134g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382126; CAG98863.1; -; Genomic_DNA.
DR RefSeq; XP_456155.1; XM_456155.1.
DR PDB; 6CHG; X-ray; 2.98 A; C=848-1000.
DR PDB; 6UGM; EM; 3.70 A; M=726-1000.
DR PDB; 6UH5; EM; 3.50 A; M=726-1000.
DR PDBsum; 6CHG; -.
DR PDBsum; 6UGM; -.
DR PDBsum; 6UH5; -.
DR AlphaFoldDB; Q6CIT4; -.
DR SMR; Q6CIT4; -.
DR STRING; 28985.XP_456155.1; -.
DR PRIDE; Q6CIT4; -.
DR EnsemblFungi; CAG98863; CAG98863; KLLA0_F24134g.
DR GeneID; 2895235; -.
DR KEGG; kla:KLLA0_F24134g; -.
DR eggNOG; KOG1080; Eukaryota.
DR HOGENOM; CLU_004391_1_0_1; -.
DR InParanoid; Q6CIT4; -.
DR OMA; LHQPLNT; -.
DR Proteomes; UP000000598; Chromosome F.
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 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1000
FT /note="Histone-lysine N-methyltransferase, H3 lysine-4
FT specific"
FT /id="PRO_0000269775"
FT DOMAIN 858..975
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 984..1000
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 29..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..611
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 727..738
FT /evidence="ECO:0007829|PDB:6UH5"
FT TURN 739..742
FT /evidence="ECO:0007829|PDB:6UH5"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:6UH5"
FT HELIX 821..831
FT /evidence="ECO:0007829|PDB:6UH5"
FT TURN 832..837
FT /evidence="ECO:0007829|PDB:6UH5"
FT HELIX 851..856
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 860..864
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 866..876
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 883..887
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 889..893
FT /evidence="ECO:0007829|PDB:6CHG"
FT HELIX 894..906
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 914..918
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 921..929
FT /evidence="ECO:0007829|PDB:6CHG"
FT HELIX 931..934
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 942..950
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 953..962
FT /evidence="ECO:0007829|PDB:6CHG"
FT STRAND 993..995
FT /evidence="ECO:0007829|PDB:6UH5"
SQ SEQUENCE 1000 AA; 115018 MW; ABE3EF647FB556A5 CRC64;
MSGYYNRQYS HFHGNNDRYQ TGRYAYQENG NRYKGFQRNG SGNRRYSREG FGSQLRNNEN
ESRPIRSQSR GISEIPRNPF ATRPVVSAKY DRDEFNTKYH YYDIVSKRLR NESSFKKWKS
EKIPEHGYVT TTELIASDKQ KPILMARQPE QTSVDPRIRP MNGDAVSGSI SAKKRYRKLR
SALVRNSRIP YDSFYIGPEP PKEIIVYPSA SNQQPIAAAL SEAIIKNYFK SFGEIAHFEQ
FMDPNSALPL YVYLIKFTGP VSQPDAPYKA AYKASEKFKD APYTVSGIKF NVILNQNTVL
NSIKDKLIKQ NAARVTEVNK AKRAIAEKSS GQKPQVIRGV PYDLTQVVNN RPVLFVPAKI
TFYHRFNAAD FRYQLRKYNW AKIIDHYTGV YIVFHDLENA KACLEYESGA LVINSHRTHS
PIQIEFTFIE PKRRLQSNIT NQRDINKPRK IEYSSTEELL EASTKQILKD LHNIIKRDIL
RRLVGPIIFD TLNPANYPEV VERQKKLDDE KKKREESQKK TTIKAKPAEF DIFSLYGPAS
KTKKLKRDRK ADLGKRHLYT EESPDHQRKK KPKVEHMSHL LNDEISTRED TVDSLNVGSN
GENSPESSGY ESEDIISDES KKQSSVITTP EEDLPESAAS LPDERSKELL QYEGKYKPIA
SEFPTPVYPY DDFDLNKSKQ LSLDKFQLAL KDEEDFSILK GIVSEKSKDI TTDYTPFLPY
SMWKLYQQIE QNGIIRDNQI ALNEKEFDST LASTTGSFIA DGFKKIPDKL KSSYLLHHRR
LAQPLNTVHN HQEQNFMALN GTESTNQEAD LEQDNHNASS RLNRVFQRRF QQDIEAQRAA
IGFESDLLSL NQLTKRKKPV TFARSAIHNW GLYALEPIAA KEMIIEYVGE SIRQPVAEMR
EKRYIKSGIG SSYLFRIDEN TVIDATKRGG IARFINHCCE PSCTAKIIKV DGRKRIVIYA
LRDIGTNEEL TYDYKFERET DEGERLPCLC GAPSCKGFLN
