ABF1_KLULA
ID ABF1_KLULA Reviewed; 494 AA.
AC P26375; Q6CLH5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=ARS-binding factor 1;
DE AltName: Full=Bidirectionally acting factor;
GN Name=ABF1; Synonyms=BAF1; OrderedLocusNames=KLLA0F02970g;
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].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=1594441; DOI=10.1093/nar/20.9.2211;
RA Goncalves P.M., Maurer K., Mager W.H., Planta R.J.;
RT "Kluyveromyces contains a functional ABF1-homologue.";
RL Nucleic Acids Res. 20:2211-2215(1992).
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: General regulatory factor (GRF) that contributes to
CC transcriptional activation of a large number of genes, as well as to
CC DNA replication, silencing and telomere structure. Involved in the
CC transcription activation of a subset of ribosomal protein genes. Binds
CC the ARS-elements found in many promoters. Binds to the sequence 5'-
CC TCN(7)ACG-3'.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Extensively phosphorylated on Ser and Thr residues. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45792.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X64462; CAA45792.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CR382126; CAG97922.1; -; Genomic_DNA.
DR PIR; S22654; S22654.
DR RefSeq; XP_455214.1; XM_455214.1.
DR AlphaFoldDB; P26375; -.
DR STRING; 28985.XP_455214.1; -.
DR EnsemblFungi; CAG97922; CAG97922; KLLA0_F02970g.
DR GeneID; 2894945; -.
DR KEGG; kla:KLLA0_F02970g; -.
DR eggNOG; ENOG502QSTW; Eukaryota.
DR HOGENOM; CLU_031229_0_0_1; -.
DR InParanoid; P26375; -.
DR OMA; HRNKHFT; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0000113; C:nucleotide-excision repair factor 4 complex; IEA:EnsemblFungi.
DR GO; GO:0003688; F:DNA replication origin binding; IEA:EnsemblFungi.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:EnsemblFungi.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:EnsemblFungi.
DR GO; GO:0044374; F:sequence-specific DNA binding, bending; IEA:EnsemblFungi.
DR GO; GO:0006338; P:chromatin remodeling; IEA:EnsemblFungi.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:EnsemblFungi.
DR GO; GO:0070911; P:global genome nucleotide-excision repair; IEA:EnsemblFungi.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
DR InterPro; IPR006774; BAF1_ABF1.
DR Pfam; PF04684; BAF1_ABF1; 2.
PE 3: Inferred from homology;
KW Activator; DNA damage; DNA repair; DNA replication; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..494
FT /note="ARS-binding factor 1"
FT /id="PRO_0000064805"
FT REGION 82..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 400
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT CONFLICT 131..138
FT /note="Missing (in Ref. 1; CAA45792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 55259 MW; 24BF02085E40F394 CRC64;
MSLYEYKHPI INKDLAAPDP VSAQKRSFPT LEAWYDVIND YEFQSRCPII LKNSHKNKHF
TFACHLKSCP FKILLSYQGA NNSGSSEDGS PHGLSGDGGS SSSGSNHHNG HTNLAEDGRA
EDEDDDEDDD AAVTAAIAAA VAAVADSQET IKGPFVVTKI EPYHNHPLES NLSLQRFVLS
KIPKILQVDL KFDAILESLC NDDDNTVAKF RVAQYVEESG ILDIIKQRYG LTEAEMDKKM
LSNIARRVTT YKARFVLKRK KDGVYAMPTA HQLTGGDHHQ VQHHHHPSIP AHHQHQLPEG
QQRDVQHHHQ QQQQQLQHQE QHQSHVDSGH NVYQNRIGSI SDNDDSAIHN LDDTNVRVAA
AAAAAAAALQ SRENHDTEDL KRTLEQVQDD ESLDVGVPDS KRQLHRRERD RVAEALKMAT
RDILSNQSVD SDVNVDVDLV TGHKQLSPHD DMAEQLRLLS SHLKEVEAEE NVSDNNLKKD
DIPDENIQPE LRGQ
