GenomeNet

Database: UniProt
Entry: Q6FKB1
LinkDB: Q6FKB1
Original site: Q6FKB1 
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   10-APR-2019, entry version 105.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-4 specific;
DE            EC=2.1.1.43;
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 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBUNIT: Component of the COMPASS (Set1C) complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; CR380958; CAG62307.1; -; Genomic_DNA.
DR   RefSeq; XP_449333.1; XM_449333.1.
DR   ProteinModelPortal; 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   EuPathDB; FungiDB:CAGL0L12980g; -.
DR   eggNOG; KOG1080; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   InParanoid; Q6FKB1; -.
DR   KO; K11422; -.
DR   OMA; PSCTAKI; -.
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:0030466; P:chromatin silencing at silent mating-type cassette; IEA:EnsemblFungi.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IEA:EnsemblFungi.
DR   GO; GO:0044648; P:histone H3-K4 dimethylation; IEA:EnsemblFungi.
DR   GO; GO:0080182; P:histone H3-K4 trimethylation; 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:0045944; P:positive regulation of transcription by RNA polymerase II; 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:0000723; P:telomere maintenance; IEA:EnsemblFungi.
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; IPR017111; Set1.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF462; PTHR22884:SF462; 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   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; Complete proteome; Methyltransferase;
KW   Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1   1111       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000269768.
FT   DOMAIN      969   1086       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1095   1111       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
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
//
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