CBF1_KLULA
ID CBF1_KLULA Reviewed; 359 AA.
AC P49379; Q6CV96;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Centromere-binding protein 1;
DE Short=CBP-1;
DE AltName: Full=Centromere promoter factor 1;
DE AltName: Full=Centromere-binding factor 1;
GN Name=CBF1; Synonyms=CPF1; OrderedLocusNames=KLLA0B13761g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7859301; DOI=10.1007/bf00309548;
RA Mulder W., Winkler A.A., Scholten I.H.J.M., Zonneveld B.J.M.,
RA de Winde J.H., de Steensma H.Y., Grivell L.A.;
RT "Centromere promoter factors (CPF1) of the yeasts Saccharomyces cerevisiae
RT and Kluyveromyces lactis are functionally exchangeable, despite low overall
RT homology.";
RL Curr. Genet. 26:198-207(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Required for chromosome stability and methionine prototrophy.
CC It is involved in chromosomal segregation. Binds to a highly conserved
CC DNA sequence (5'-RTCACRTG-3'), called CDEI, found in centromeres and in
CC several promoters (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA as a dimer. {ECO:0000250}.
CC -!- INTERACTION:
CC P49379; Q6CPM4: KLLA0_E03807g; NbExp=3; IntAct=EBI-15956272, EBI-15956087;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53618.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X76028; CAA53618.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR382122; CAH02536.1; -; Genomic_DNA.
DR PIR; S48231; S48231.
DR RefSeq; XP_452143.1; XM_452143.1.
DR AlphaFoldDB; P49379; -.
DR SMR; P49379; -.
DR DIP; DIP-59576N; -.
DR IntAct; P49379; 4.
DR STRING; 28985.XP_452143.1; -.
DR PRIDE; P49379; -.
DR EnsemblFungi; CAH02536; CAH02536; KLLA0_B13761g.
DR GeneID; 2897533; -.
DR KEGG; kla:KLLA0_B13761g; -.
DR eggNOG; KOG1318; Eukaryota.
DR HOGENOM; CLU_046871_0_1_1; -.
DR InParanoid; P49379; -.
DR OMA; HEENMES; -.
DR Proteomes; UP000000598; Chromosome B.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 Centromere; Chromosome; DNA-binding; Nucleus; Reference proteome.
FT CHAIN 1..359
FT /note="Centromere-binding protein 1"
FT /id="PRO_0000127160"
FT DOMAIN 249..297
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..160
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 341
FT /note="E -> Q (in Ref. 1; CAA53618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39826 MW; B2232E4B6FAEE6F0 CRC64;
MSGKRSYQDD QLDVEEANKR HQMVDTLLRG SEDKDGDNDN SVYDDLLQDP EEVEKENKEN
RDGDKVGDDE HDVVKGESEG QAAEQSSADQ NDENINVDVD PSVTAVARAA QHASQRREAG
DEDEDEDEEE EEDEDDHVDI DDVDKDPDAV IDEDDDEEDE DQAQRRRGKK NIEGTGESND
SERATKIGES GSSNETAGAD GSGDREDGSQ PDGTEHDDEE NGGAGAGGAA PRRGRKPGTE
TGSTAWKQQR KESHKEVERR RRQNINTAIE KLSDLLPVKE TSKAAILSRA AEYIQKMKET
ETANIEKWTL QKLLGEQQVS SLTSANDKLE QELSKAYKNL EELKKKLKEA GIEDPTEEE
