BDF1_CANAL
ID BDF1_CANAL Reviewed; 732 AA.
AC Q5A4W8; A0A1D8PMV0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Bromodomain-containing factor 1;
GN Name=BDF1; OrderedLocusNames=CAALFM_C500200CA;
GN ORFNames=CaO19.8593, CaO19.978;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; 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., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA 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 aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME 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 allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION.
RX PubMed=12455696; DOI=10.1128/ec.1.5.787-798.2002;
RA Bensen E.S., Filler S.G., Berman J.;
RT "A forkhead transcription factor is important for true hyphal as well as
RT yeast morphogenesis in Candida albicans.";
RL Eukaryot. Cell 1:787-798(2002).
RN [5]
RP INDUCTION.
RX PubMed=16039996; DOI=10.1016/j.bbrc.2005.07.018;
RA Singh V., Sinha I., Sadhale P.P.;
RT "Global analysis of altered gene expression during morphogenesis of Candida
RT albicans in vitro.";
RL Biochem. Biophys. Res. Commun. 334:1149-1158(2005).
RN [6]
RP INDUCTION.
RX PubMed=15796975; DOI=10.1016/j.femsle.2005.02.014;
RA Marchais V., Kempf M., Licznar P., Lefrancois C., Bouchara J.P., Robert R.,
RA Cottin J.;
RT "DNA array analysis of Candida albicans gene expression in response to
RT adherence to polystyrene.";
RL FEMS Microbiol. Lett. 245:25-32(2005).
RN [7]
RP INDUCTION.
RX PubMed=17164403; DOI=10.1074/mcp.m600210-mcp200;
RA Fernandez-Arenas E., Cabezon V., Bermejo C., Arroyo J., Nombela C.,
RA Diez-Orejas R., Gil C.;
RT "Integrated proteomics and genomics strategies bring new insight into
RT Candida albicans response upon macrophage interaction.";
RL Mol. Cell. Proteomics 6:460-478(2007).
CC -!- FUNCTION: Transcription factor involved in the expression of a broad
CC class of genes including snRNAs. Required for sporulation and DNA-
CC damage repair. Prevents the spreading of SIR silencing at telomeres and
CC protects histone H4, but not H3, from deacetylation (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- INDUCTION: Expression is regulated by FKH2 and repressed upon adherence
CC to polystyrene and interaction with macrophages.
CC {ECO:0000269|PubMed:12455696, ECO:0000269|PubMed:15796975,
CC ECO:0000269|PubMed:16039996, ECO:0000269|PubMed:17164403}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AOW29466.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP017627; AOW29466.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_716816.2; XM_711723.2.
DR PDB; 5N13; X-ray; 1.20 A; A=386-491.
DR PDB; 5N15; X-ray; 2.37 A; A/B/C/D=193-327.
DR PDB; 5N16; X-ray; 1.76 A; A/B/C/D=193-327.
DR PDB; 5N17; X-ray; 1.60 A; A/B=193-327.
DR PDB; 5N18; X-ray; 1.45 A; A/B=386-491.
DR PDBsum; 5N13; -.
DR PDBsum; 5N15; -.
DR PDBsum; 5N16; -.
DR PDBsum; 5N17; -.
DR PDBsum; 5N18; -.
DR AlphaFoldDB; Q5A4W8; -.
DR SMR; Q5A4W8; -.
DR STRING; 237561.Q5A4W8; -.
DR PRIDE; Q5A4W8; -.
DR GeneID; 3641592; -.
DR KEGG; cal:CAALFM_C500200CA; -.
DR CGD; CAL0000183583; BDF1.
DR eggNOG; KOG1474; Eukaryota.
DR HOGENOM; CLU_001499_4_0_1; -.
DR InParanoid; Q5A4W8; -.
DR OrthoDB; 619848at2759; -.
DR PHI-base; PHI:7195; -.
DR PRO; PR:Q5A4W8; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1270.220; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR027353; NET_dom.
DR InterPro; IPR038336; NET_sf.
DR Pfam; PF17035; BET; 1.
DR Pfam; PF00439; Bromodomain; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
DR PROSITE; PS51525; NET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bromodomain; Coiled coil; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Repeat; Sporulation; Transcription;
KW Transcription regulation.
FT CHAIN 1..732
FT /note="Bromodomain-containing factor 1"
FT /id="PRO_0000426053"
FT DOMAIN 226..298
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 403..475
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 593..672
FT /note="NET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00857"
FT REGION 1..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 529..569
FT /evidence="ECO:0000255"
FT COMPBIAS 1..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..579
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:5N17"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:5N17"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:5N15"
FT TURN 240..244
FT /evidence="ECO:0007829|PDB:5N17"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:5N17"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:5N17"
FT HELIX 273..291
FT /evidence="ECO:0007829|PDB:5N17"
FT HELIX 296..312
FT /evidence="ECO:0007829|PDB:5N17"
FT HELIX 386..400
FT /evidence="ECO:0007829|PDB:5N13"
FT HELIX 402..404
FT /evidence="ECO:0007829|PDB:5N13"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:5N13"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:5N13"
FT TURN 417..421
FT /evidence="ECO:0007829|PDB:5N13"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:5N13"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:5N13"
FT HELIX 435..443
FT /evidence="ECO:0007829|PDB:5N13"
FT HELIX 450..467
FT /evidence="ECO:0007829|PDB:5N13"
FT HELIX 473..489
FT /evidence="ECO:0007829|PDB:5N13"
SQ SEQUENCE 732 AA; 82552 MW; 03BCA3F0C3D63819 CRC64;
MSETFPETNT PVQTPSTESF VNKMNAGDKT IGNNIFSQDS DSNQQSSHQE PLSPPNPSPT
PEKRQLDDEV DNSIEPESKK QKVEEETEAS QTGVIQTEVS ETVPEIESSV NKDSEPVNGV
SEESENTNNE QEKPQEEAPE ENPQEEVPEA KPQEEASGEN PQEIPNDKPQ DDEPDIQEVD
PPKPVVPVFT EPAPKPPQEP DMNNLPENPI PQHQAKFVLN TIKAVKRNRE AVPFLHPVDT
VKLNVPFYYN YIPRPMDLST IERKINLKAY EDVSQVVDDF NLMVKNCKKF NGEAAGISKM
ATNIQAQFEK LMVKVPPKEL PAGTNVAEAT SVATSPTTNK RKSVAESSSS HQHRDSVAAA
RPKRTIHPPK SKELPYETKP KNKKVAAELR FCNQTIKELM SKKHYNYNFP FLAPVDTVAL
NIPNYNEIVK QPMDLGTIQS KLANNEYENA DDFEKDVRLV FKNCYLFNPE GTDVNMMGHR
LEAVFDKKWA NKPVPEPTPQ NSDVSDREYS SEEEDNVEIS EAMLSEIPAI QVMENQIIRM
RKELDELKKE HLKKLREQQA ARKKKKQQKG KRRAPKAKHT KDTQHQVQAP PEPPKLTPPQ
PVVTYEMKKQ VSEMVPNLSD KKLNALIKII QDDVQISNDD EVELDMDQLE DRTVLKLYDF
LFGDKALKNS AGKKKKPVAN NNLDELAHLR SQLALFDEGV NGQQGSDNGF MKVVNQEESS
EDEASSESSE EE
