ID   ABF1_KLUMA              Reviewed;         496 AA.
AC   P33293;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=ARS-binding factor 1;
DE   AltName: Full=Bidirectionally acting factor;
GN   Name=ABF1; Synonyms=BAF1;
OS   Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=4911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26548 / CBS 6556 / NRRL Y-7571;
RX   PubMed=7916634; DOI=10.1016/0167-4781(93)90187-i;
RA   Oberye E.H.H., Maurer K., Mager W.H., Planta R.J.;
RT   "Structure of the ABF1-homologue from Kluyveromyces marxianus.";
RL   Biochim. Biophys. Acta 1173:233-236(1993).
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}.
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DR   EMBL; Z19865; CAA79673.1; -; Genomic_DNA.
DR   PIR; S33791; S33791.
DR   AlphaFoldDB; P33293; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; Transcription; Transcription regulation.
FT   CHAIN           1..496
FT                   /note="ARS-binding factor 1"
FT                   /id="PRO_0000064806"
FT   REGION          82..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        102..118
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..489
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         402
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   496 AA;  55807 MW;  8F1E0560D9C2E58F CRC64;
     MSLYEYNDPI INKDLAQADP VMGQNRTFPT LEAWYDVIND YEFQSRCPII LKNSHKTKHF
     TFACHLKSCP FKILLSHQGP VSVQNGDGSP GVGVGDEHGH HHHHNMHAHH HHHHQNGHTN
     GHGNSGDDVS EQEAQQDDED DDAAVTAAIA AAVAAVADSQ ETIKGPFAVT KIEPYHNHPL
     ESNLSLQRFV LTKIPKILQV DLKFDAILES LCNDEDNTVA KFRVAQYVEE SGIIDIIKQR
     YGLTDAEMDK KMLSNIARRV TTDKARFVLK RKKEGVYMLP NGHQISGADQ HQHQLQHQHQ
     HQHQHQHQHQ HQHQSQDQHQ NQHQQHVGND NHVYQDRIHS QSDQDEAGVH NLDDNNVRVA
     AAAAAAAAAA LQSRDSHVSE ELKLNCGTGQ DEDGIEDDNH SSKRQLHRSD RDRVAEALKM
     ATRDILSNQN VDSDVNVDVD LVTGHKQLSP HDDMAEQLRL LSSHLKEVEA EENVSDSNLK
     KDDVQDENIQ PELRGQ