HAP2_KLULA
ID HAP2_KLULA Reviewed; 300 AA.
AC P53768;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Transcriptional activator HAP2;
GN Name=HAP2; OrderedLocusNames=KLLA0A00891g;
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=7828916; DOI=10.1016/0378-1119(94)00684-k;
RA Nguyen C., Bolotin-Fukuhara M., Wesolowski-Louvel M., Fukuhara H.;
RT "The respiratory system of Kluyveromyces lactis escapes from HAP2
RT control.";
RL Gene 152:113-115(1995).
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: Binds to the upstream activation site (UAS) of the CYC1 gene
CC and other genes involved in mitochondrial electron transport and
CC activates their expression. Recognizes the sequence CCAAT.
CC -!- SUBUNIT: Belongs to a heterotrimeric CCAAT-binding complex.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the NFYA/HAP2 subunit family.
CC {ECO:0000255|PROSITE-ProRule:PRU00966}.
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DR EMBL; U09272; AAA67874.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH02626.1; -; Genomic_DNA.
DR RefSeq; XP_451038.1; XM_451038.1.
DR AlphaFoldDB; P53768; -.
DR SMR; P53768; -.
DR STRING; 28985.XP_451038.1; -.
DR EnsemblFungi; CAH02626; CAH02626; KLLA0_A00891g.
DR GeneID; 2896304; -.
DR KEGG; kla:KLLA0_A00891g; -.
DR eggNOG; KOG1561; Eukaryota.
DR HOGENOM; CLU_080763_1_0_1; -.
DR InParanoid; P53768; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0016602; C:CCAAT-binding factor complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR InterPro; IPR018362; CCAAT-binding_factor_CS.
DR InterPro; IPR001289; NFYA.
DR PANTHER; PTHR12632; PTHR12632; 1.
DR Pfam; PF02045; CBFB_NFYA; 1.
DR PRINTS; PR00616; CCAATSUBUNTB.
DR SMART; SM00521; CBF; 1.
DR PROSITE; PS00686; NFYA_HAP2_1; 1.
DR PROSITE; PS51152; NFYA_HAP2_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..300
FT /note="Transcriptional activator HAP2"
FT /id="PRO_0000198782"
FT DNA_BIND 218..243
FT /note="NFYA/HAP2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00966"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 188..211
FT /note="Subunit association domain (SAD)"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..70
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 COMPBIAS 284..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 300 AA; 34499 MW; 4B468A28F88BA757 CRC64;
MPTELITYEQ NFSSGVDAEN DYPPLDSGMG SFQVSELERQ GDSHKRSNDE ISELRDETLN
GREKKLRQSE SISRNSTGNA QVEAIPHHSI NVDQSDNLLS EQENPTKVYL YDDPHLENDP
QQRQEESDAN GIMEKLTDDN SMKQVSNAKT SLETAQFLET SNSMELQRTK PHDMNIISPS
EPLEQPFYVN AKQYYRILKR RYARAKLEEN LKISRERRPY LHESRHKHAM RRPRGQGGRF
LTAAEMAEMK RKEEEGTDND SFLQEHVPKM NVLPQQLPGP VKDNNNEKSD EKPVAKEASN