TAF4_KLULA
ID TAF4_KLULA Reviewed; 366 AA.
AC Q6CUC6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Transcription initiation factor TFIID subunit 4;
DE AltName: Full=TBP-associated factor 4;
GN Name=TAF4; OrderedLocusNames=KLLA0C05962g;
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 [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: Functions as a component of the DNA-binding general
CC transcription factor complex TFIID. Binding of TFIID to a promoter
CC (with or without TATA element) is the initial step in pre-initiation
CC complex (PIC) formation. TFIID plays a key role in the regulation of
CC gene expression by RNA polymerase II through different activities such
CC as transcription activator interaction, core promoter recognition and
CC selectivity, TFIIA and TFIIB interaction, chromatin modification
CC (histone acetylation by TAF1), facilitation of DNA opening and
CC initiation of transcription (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The 1.2 MDa TFIID complex is composed of TATA binding protein
CC (TBP) and the 14 TBP-associated factors. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TAF4 family. {ECO:0000305}.
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DR EMBL; CR382123; CAH01314.1; -; Genomic_DNA.
DR RefSeq; XP_452463.1; XM_452463.1.
DR AlphaFoldDB; Q6CUC6; -.
DR SMR; Q6CUC6; -.
DR STRING; 28985.XP_452463.1; -.
DR EnsemblFungi; CAH01314; CAH01314; KLLA0_C05962g.
DR GeneID; 2892444; -.
DR KEGG; kla:KLLA0_C05962g; -.
DR eggNOG; KOG2341; Eukaryota.
DR HOGENOM; CLU_036634_0_0_1; -.
DR InParanoid; Q6CUC6; -.
DR OMA; YGWLTSS; -.
DR Proteomes; UP000000598; Chromosome C.
DR GO; GO:0005669; C:transcription factor TFIID complex; IEA:EnsemblFungi.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:EnsemblFungi.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:EnsemblFungi.
DR CDD; cd08045; TAF4; 1.
DR InterPro; IPR045144; TAF4.
DR InterPro; IPR007900; TAF4_C.
DR PANTHER; PTHR15138; PTHR15138; 1.
DR Pfam; PF05236; TAF4; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..366
FT /note="Transcription initiation factor TFIID subunit 4"
FT /id="PRO_0000343440"
FT DOMAIN 170..238
FT /note="Histone-fold"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 40115 MW; 0624950E3FB7D3EE CRC64;
MAKSPKRKNS EPEDLSSNKR SKSFEFGKVE NGLEPSGSDF GSDLPTPFDT MVTEQPLALP
KASSPTTNLA SPRNSSTPNL KTTSTTSKQS QKAEQKKNAG GSTGSTTAST TKPQQSDPDK
LSDALLSAGV DIREEEALLS STVARTKATG ISANNQVPSH PPFLHPKNIS DFMKRIASEQ
NFHQDFNKNT DILGLMSTAC ELYMRDVITN SLILSIHRRK GVKLNTGRRS EVSRSLRDLA
LRQKTQEERR VQRRIALGLE KQTTDARLDT EETQYRASNA TANLMIAGGN KKKYSWLTAG
SKSSSTDLKN QGNVSSAVAA RGEMGIKYRE AREEPGIVMR DLLLALENRR VGVNNVITKG
YARIRD