TAF4_CANGA
ID TAF4_CANGA Reviewed; 336 AA.
AC Q6FNH1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-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=CAGL0J11726g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380956; CAG61174.1; -; Genomic_DNA.
DR RefSeq; XP_448223.1; XM_448223.1.
DR AlphaFoldDB; Q6FNH1; -.
DR SMR; Q6FNH1; -.
DR STRING; 5478.XP_448223.1; -.
DR EnsemblFungi; CAG61174; CAG61174; CAGL0J11726g.
DR GeneID; 2889463; -.
DR KEGG; cgr:CAGL0J11726g; -.
DR CGD; CAL0133662; CAGL0J11726g.
DR VEuPathDB; FungiDB:CAGL0J11726g; -.
DR eggNOG; KOG2341; Eukaryota.
DR HOGENOM; CLU_036634_0_0_1; -.
DR InParanoid; Q6FNH1; -.
DR OMA; YGWLTSS; -.
DR Proteomes; UP000002428; Chromosome J.
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..336
FT /note="Transcription initiation factor TFIID subunit 4"
FT /id="PRO_0000343438"
FT DOMAIN 141..209
FT /note="Histone-fold"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 336 AA; 36984 MW; B6B9C7A452B39651 CRC64;
MSSQKRPSEE STGSGTKKVK LEETKTPSLK SEASNLALPK MNDSSNNINA VPLALPKGGD
KKKKANSKTA QSGKNGGKED GTGQKQKATD PNKMQDVLIS AGVDLKEEEA LLSSTVNVSK
TQQNAVVIPP HPPFLHPDQV SNFMKKVAKT QNFNLSFTKN TEILDMMSSA CESYLRDIIT
NTIVVSRHRR KGVKVNYGRR SQVAAALRSI AINQKKEEER RMKKRIALGL EKEDYENKMD
SEETLHRASN VTATLRAGSK KQYGWLTSSI NKPASIGVKS AGKVATEIAA RGESGLKFRE
AREEPGIVMR DLLFALEHRR IGVHNIISKG YARIRD