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CBF1_CANAL
ID   CBF1_CANAL              Reviewed;         251 AA.
AC   Q5A1E3; A0A1D8PML4;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Transcriptional regulator CBF1;
GN   Name=CBF1; OrderedLocusNames=CAALFM_C406580WA;
GN   ORFNames=CaO19.10394, CaO19.2876;
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   IDENTIFICATION, AND FUNCTION.
RX   PubMed=11481675; DOI=10.1002/yea.757;
RA   Eck R., Stoyan T., Kunkel W.;
RT   "The centromere-binding factor Cbf1p from Candida albicans complements the
RT   methionine auxotrophic phenotype of Saccharomyces cerevisiae.";
RL   Yeast 18:1047-1052(2001).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14659878; DOI=10.1016/j.gene.2003.09.005;
RA   Biswas K., Rieger K.J., Morschhauser J.;
RT   "Functional characterization of CaCBF1, the Candida albicans homolog of
RT   centromere binding factor 1.";
RL   Gene 323:43-55(2003).
RN   [6]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=18342603; DOI=10.1016/j.molcel.2008.02.006;
RA   Hogues H., Lavoie H., Sellam A., Mangos M., Roemer T., Purisima E.,
RA   Nantel A., Whiteway M.;
RT   "Transcription factor substitution during the evolution of fungal ribosome
RT   regulation.";
RL   Mol. Cell 29:552-562(2008).
RN   [7]
RP   INDUCTION.
RX   PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA   Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA   Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT   "A recently evolved transcriptional network controls biofilm development in
RT   Candida albicans.";
RL   Cell 148:126-138(2012).
CC   -!- FUNCTION: Transcription factor that binds ribosomal protein gene
CC       promoters and rDNA locus with TBF1. Necessary for the expression of
CC       genes involved in assimilation of inorganic sulfate. Also required for
CC       the expression of respiratory genes and glycolytic genes. Does not bind
CC       to centromeres and is not necessary for efficient chromosome
CC       segregationas as does S.cerevisiae CBF1. {ECO:0000269|PubMed:11481675,
CC       ECO:0000269|PubMed:14659878, ECO:0000269|PubMed:18342603}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17106}.
CC   -!- INDUCTION: Repressed during biofilm formation.
CC       {ECO:0000269|PubMed:22265407}.
CC   -!- DISRUPTION PHENOTYPE: Leads to auxotrophy for sulfur amino acids.
CC       {ECO:0000269|PubMed:14659878}.
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DR   EMBL; CP017626; AOW29381.1; -; Genomic_DNA.
DR   RefSeq; XP_019330942.1; XM_019475397.1.
DR   AlphaFoldDB; Q5A1E3; -.
DR   SMR; Q5A1E3; -.
DR   BioGRID; 1225818; 1.
DR   STRING; 237561.Q5A1E3; -.
DR   PRIDE; Q5A1E3; -.
DR   GeneID; 3642779; -.
DR   KEGG; cal:CAALFM_C406580WA; -.
DR   CGD; CAL0000186329; CBF1.
DR   VEuPathDB; FungiDB:C4_06580W_A; -.
DR   eggNOG; KOG1318; Eukaryota.
DR   HOGENOM; CLU_046871_2_0_1; -.
DR   InParanoid; Q5A1E3; -.
DR   OMA; QSSHQEI; -.
DR   OrthoDB; 1471388at2759; -.
DR   PRO; PR:Q5A1E3; -.
DR   Proteomes; UP000000559; Chromosome 4.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..251
FT                   /note="Transcriptional regulator CBF1"
FT                   /id="PRO_0000426067"
FT   DOMAIN          152..200
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          190..223
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..100
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   251 AA;  29153 MW;  5479B57AE244BD24 CRC64;
     MVKSHKRTLE KDEEHQEKKK ANKISKDDME IDAELLTQQA SDSAHTDTAT AAVAAVNNEQ
     GKELEQTESS TNQTSALDKD DKETKDNLNP REETQSSHQE IDIPKDQLTN QQNLADQHQQ
     YQYHQQLAQT NFKTEPTNSA KPPHGSEEWH RQRRENHKEV ERKRRESINT GIRELARLIP
     TTDTNKAQIL QRAVEYIKRL KENENNNIEK WTLEKLLTEQ AVSELSASNE KLKHELESAY
     REIEQLKRGK K
 
 
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