GenomeNet

Database: UniProt
Entry: Q6CIT4
LinkDB: Q6CIT4
Original site: Q6CIT4 
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   10-APR-2019, entry version 107.
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=KLLA0F24134g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC
OS   1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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 /
RC   WM37;
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; 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   PDBsum; 6CHG; -.
DR   ProteinModelPortal; 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   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000066111; -.
DR   InParanoid; Q6CIT4; -.
DR   KO; K11422; -.
DR   OMA; PSCTAKI; -.
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: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   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; Chromosome; Complete proteome;
KW   Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1   1000       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000269775.
FT   DOMAIN      858    975       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN      984   1000       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   HELIX       851    856       {ECO:0000244|PDB:6CHG}.
FT   STRAND      860    864       {ECO:0000244|PDB:6CHG}.
FT   STRAND      866    876       {ECO:0000244|PDB:6CHG}.
FT   STRAND      883    887       {ECO:0000244|PDB:6CHG}.
FT   STRAND      889    893       {ECO:0000244|PDB:6CHG}.
FT   HELIX       894    906       {ECO:0000244|PDB:6CHG}.
FT   STRAND      914    918       {ECO:0000244|PDB:6CHG}.
FT   STRAND      921    929       {ECO:0000244|PDB:6CHG}.
FT   HELIX       931    934       {ECO:0000244|PDB:6CHG}.
FT   STRAND      942    950       {ECO:0000244|PDB:6CHG}.
FT   STRAND      953    962       {ECO:0000244|PDB:6CHG}.
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
//
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