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Database: UniProt/SWISS-PROT
Entry: SET1_CANAL
LinkDB: SET1_CANAL
Original site: SET1_CANAL 
ID   SET1_CANAL              Reviewed;        1040 AA.
AC   Q5ABG1; A0A1D8PCE5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   28-MAR-2018, entry version 98.
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=CAALFM_C100960CA;
GN   ORFNames=CaO19.13430, CaO19.6009;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
OC   Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
RA   Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
RA   Davis R.W., Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs
RT   aligned on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
RP   REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates
RT   allele-specific measurements and provides a simple model for repeat
RT   and indel structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   FUNCTION.
RX   PubMed=16629671; DOI=10.1111/j.1365-2958.2006.05121.x;
RA   Raman S.B., Nguyen M.H., Zhang Z., Cheng S., Jia H.Y., Weisner N.,
RA   Iczkowski K., Clancy C.J.;
RT   "Candida albicans SET1 encodes a histone 3 lysine 4 methyltransferase
RT   that contributes to the pathogenesis of invasive candidiasis.";
RL   Mol. Microbiol. 60:697-709(2006).
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, transcription elongation regulation and pathogenesis
CC       of invasive candidiasis. {ECO:0000269|PubMed:16629671}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
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; CP017623; AOW25793.1; -; Genomic_DNA.
DR   RefSeq; XP_718971.1; XM_713878.1.
DR   ProteinModelPortal; Q5ABG1; -.
DR   SMR; Q5ABG1; -.
DR   ELM; Q5ABG1; -.
DR   PRIDE; Q5ABG1; -.
DR   EnsemblFungi; AOW25793; AOW25793; CAALFM_C100960CA.
DR   GeneID; 3639280; -.
DR   KEGG; cal:CAALFM_C100960CA; -.
DR   CGD; CAL0000198993; SET1.
DR   InParanoid; Q5ABG1; -.
DR   KO; K11422; -.
DR   OMA; PSCTAKI; -.
DR   OrthoDB; EOG092C3T9B; -.
DR   PRO; PR:Q5ABG1; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IMP:CGD.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0048869; P:cellular developmental process; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IMP:CGD.
DR   GO; GO:0044416; P:induction by symbiont of host defense response; IDA:CGD.
DR   GO; GO:0009405; P:pathogenesis; IMP:CGD.
DR   GO; GO:0036166; P:phenotypic switching; IMP:CGD.
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; IPR035979; RBD_domain_sf.
DR   InterPro; IPR017111; Set1.
DR   InterPro; IPR024636; SET_assoc.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF462; PTHR22884:SF462; 3.
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; SSF54928; SSF54928; 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   1040       Histone-lysine N-methyltransferase, H3
FT                                lysine-4 specific.
FT                                /FTId=PRO_0000269767.
FT   DOMAIN      898   1015       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1024   1040       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   COMPBIAS    626    728       Glu-rich.
SQ   SEQUENCE   1040 AA;  119161 MW;  30A4796C4C7B0160 CRC64;
     MSYNNRSGGG ASGGYSRRGY HGSHRGGYRT GRSKYPEDRY LVGGMLSLNK GSHYESSDNR
     YIPNEIGSKS PENRSHRSST KDGRTPSGLS TPLSSSDKVS TPISIESING SDRNTGVNNK
     DSEFPKLSHH SDFTSTIPFS RSINPQKNFM VINDSHTPKT DKGIQSKKIR YNGEGVNHVS
     DPRIAQSNSN LQKPTKKTKK TPYKQLPQPK FVYNSDSLGP APMSTIIIWD LPISTSEPFL
     RNFVSRYGNP LEEMTFITDP TTAVPLGIVT FKFQGNPQKA SELAKNFIKT VRQDELKIDG
     ATLKIALNDN ENQLLNRKLE SAKKKMLQQR LQREQEEEKR RQKLVEEQKK QELLKKKEKE
     HQESVKKEKS VEHESTIVST RDKNLVYKPN STVLSMRHNH KIISSVILPK DLEKYIKSRP
     YILIRDKYVP TKKISSHDIK RALKKYDWTR VLSDKSGFFI VFNSLNECER CFLNEDNKKF
     FEYKLVMEMA IPEGFTNNIR ENESKSTNDV LDEATNILIK EFQTFLAKDI RERIIAPNIL
     DLLAHDKYPE LVEELKSREQ AAKPKVLVTN NQLKENALSI LEKQRQLFQQ RLPSFRMSHD
     RTQQHKPKRR NSIIPMQHAL NFDDDEDSES HSQSESEDED EDETTASRPL TPVVSTMKRE
     RSSTITSIED DIELEEREIK KQKVKVPAIE AEIAPESSPE EGEEEEKEEV EIKQEAEEVD
     IKFQPTEESP RTVYPEIPFS GDFDLNALQH TIKDSEDLLL AQEVLSETTP SGLSNIEYWS
     WKSKNRKDVQ EISQEEEYIE ELPESLQSTT GSFKSEGVRK IPEIEKIGYL PHRKRTNKPI
     KTIQYEDEDE EKPNENTNAV QSSRVNRANN RRFAADITAQ IGSESDVLSL NALTKRKKPV
     TFARSAIHNW GLYAMEPIAA KEMIIEYVGE RIRQQVAEHR EKSYLKTGIG SSYLFRIDDN
     TVIDATKKGG IARFINHCCS PSCTAKIIKV EGKKRIVIYA LRDIEANEEL TYDYKFERET
     NDEERIRCLC GAPGCKGYLN
//
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