TBF1_CANAL
ID TBF1_CANAL Reviewed; 886 AA.
AC Q5AHJ5; A0A1D8PH36; Q5AHX1;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Transcription factor TBF1;
GN Name=TBF1; OrderedLocusNames=CAALFM_C204200WA;
GN ORFNames=CaO19.801, CaO19.8420;
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 FUNCTION.
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 [5]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=20231876; DOI=10.1371/journal.pbio.1000329;
RA Lavoie H., Hogues H., Mallick J., Sellam A., Nantel A., Whiteway M.;
RT "Evolutionary tinkering with conserved components of a transcriptional
RT regulatory network.";
RL PLoS Biol. 8:E1000329-E1000329(2010).
RN [6]
RP INDUCTION.
RX PubMed=21257795; DOI=10.1128/ec.00278-10;
RA Hussein B., Huang H., Glory A., Osmani A., Kaminskyj S., Nantel A.,
RA Bachewich C.;
RT "G1/S transcription factor orthologues Swi4p and Swi6p are important but
RT not essential for cell proliferation and influence hyphal development in
RT the fungal pathogen Candida albicans.";
RL Eukaryot. Cell 10:384-397(2011).
CC -!- FUNCTION: Essential transcriptional activator that binds the telomeric
CC double-stranded TTAGGG repeat and negatively regulates telomere length.
CC Involved in the regulation of gene expression. Bind both the promoters
CC of ribosomal protein genes and the rDNA locus and activates
CC transcription at these loci. Recruits FHL1 and IFH1 to promoters.
CC {ECO:0000269|PubMed:18342603, ECO:0000269|PubMed:20231876}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC Chromosome, telomere {ECO:0000250}.
CC -!- INDUCTION: Expression is under the control of transcription factors
CC SWI4 and SWI6. {ECO:0000269|PubMed:21257795}.
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DR EMBL; CP017624; AOW27446.1; -; Genomic_DNA.
DR RefSeq; XP_720925.2; XM_715832.2.
DR AlphaFoldDB; Q5AHJ5; -.
DR SMR; Q5AHJ5; -.
DR BioGRID; 1220307; 3.
DR STRING; 237561.Q5AHJ5; -.
DR PRIDE; Q5AHJ5; -.
DR GeneID; 3637327; -.
DR KEGG; cal:CAALFM_C204200WA; -.
DR CGD; CAL0000179754; TBF1.
DR VEuPathDB; FungiDB:C2_04200W_A; -.
DR eggNOG; ENOG502QRT9; Eukaryota.
DR HOGENOM; CLU_008791_2_1_1; -.
DR InParanoid; Q5AHJ5; -.
DR OrthoDB; 1108443at2759; -.
DR PRO; PR:Q5AHJ5; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IBA:GO_Central.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF08558; TRF; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; Coiled coil; DNA-binding; Nucleus;
KW Reference proteome; Telomere; Transcription; Transcription regulation.
FT CHAIN 1..886
FT /note="Transcription factor TBF1"
FT /id="PRO_0000422810"
FT DOMAIN 648..703
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 674..699
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..41
FT /evidence="ECO:0000255"
FT COILED 747..835
FT /evidence="ECO:0000255"
FT COMPBIAS 21..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..855
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 886 AA; 100905 MW; 6E549EBCD33F0184 CRC64;
MSDQLEKDIE ESIANLDYQQ NQEHHETEQD KDKEHQDVEK QSSEEETKGI EHVTDSNTDV
IGVTKSQDTE EVIENSPVDP QLKEQQESTT KMSLSERDLV DEIDELFTNS TKTVTENNQP
SETNKRAYES VETPQELTPN DKRQKLDANT ETSVPTELES VNNHNEQSQP IEPTQERQPS
TTETTYSISV PVSTANEVER ASSSINEQED LEMIAKQYQQ ATNLEIERAM EGHGDGGQHF
STQENGQPSG SSLISSIVPS DSELLNTNQA YAAYTSLSSQ LEQHTSASAM LSSATLSALP
LSIIAPVYLP PRIQLLINTL PTLDNLATQL LRTVATSPYQ KIIDLASNPD TSAGATYRDL
TSLFEFTKRL YSEDDPFLTV EHIAPGMWKE GEETPSIFKP KQQSIESTLR KVNLATFLAA
TLGTMEIGFF YLNESFLDVF CPSNNLDPSN ALSNLGGYQN GLQSTDSPVG ARVGKLLKPQ
ATLYLDLKTQ AYISAIEAGE RSKEEILEDI LPDDLHVYLM SRRNAKLLSP TETDFVWRCK
QRKELLLNYT EETPLSEQYD WFTFLRDLFD YVSKNIAYLI WGKMGKTMKN RREDTPHTQE
LLDNTTGSTQ MPNQLSSSSG QASSTPSVVD PNKMLVSEMR EANIAVPKPS QRRAWSREEE
KALRHALELK GPHWATILEL FGQGGKISEA LKNRTQVQLK DKARNWKKFF LRSGLEIPSY
LRGVTGGVDD GKRKKDNVTK KTAAAPVPNM SEQLQQQQQR QQEKQEKQQQ EEQQAQQSEQ
QQEPQQEQQQ EQQQEQQQEQ QQEQQQEQQQ EQQQEQQQEQ QQEQREETQQ TEQEQPDQPQ
EEQQQEKEQP DQQQQEKEQP DQQQPDQQHP DRQQQEQIQQ PESSDK
