ID   TAF4_LODEL              Reviewed;         550 AA.
AC   A5DYN3;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Transcription initiation factor TFIID subunit 4;
DE   AltName: Full=TBP-associated factor 4;
GN   Name=TAF4; ORFNames=LELG_02470;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981526; EDK44291.1; -; Genomic_DNA.
DR   RefSeq; XP_001525912.1; XM_001525862.1.
DR   AlphaFoldDB; A5DYN3; -.
DR   SMR; A5DYN3; -.
DR   STRING; 379508.A5DYN3; -.
DR   PRIDE; A5DYN3; -.
DR   EnsemblFungi; EDK44291; EDK44291; LELG_02470.
DR   GeneID; 5233367; -.
DR   KEGG; lel:LELG_02470; -.
DR   VEuPathDB; FungiDB:LELG_02470; -.
DR   eggNOG; KOG2341; Eukaryota.
DR   HOGENOM; CLU_036634_1_0_1; -.
DR   InParanoid; A5DYN3; -.
DR   OrthoDB; 1315539at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IEA:InterPro.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
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   Coiled coil; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..550
FT                   /note="Transcription initiation factor TFIID subunit 4"
FT                   /id="PRO_0000343441"
FT   DOMAIN          316..396
FT                   /note="Histone-fold"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          165..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          380..412
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        165..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  57630 MW;  788FCB218214B322 CRC64;
     MSEDLKRSAS DIQDELAQSP KRVKFNDPPQ IDDVNKYDAN NVNANANVNA NANVNANAND
     SNSNNFASIA SNVTTNPIDF TVTQPQPVSP EIQNPITTLL QTDPGVGASK DLLTTNGSAI
     NITKNADTNN IETNTASINP VSNTNTNTKP ASVDTVDIKS VSANTADTAT DTKPVSADNA
     DTATDTKPVS ADTADTADTD ADAKPASANT SNTTNANTAG TGASNTDVAN SSSATTSTGD
     AKPQVQGANE TGSNQHDQRD SSKLNDAIAA AGVDIQKEEE LLQQRQLNRK PGAPSEKQDG
     SKSQTQVPLL NPYHLSAFLA KVSKTHQIHQ NFLEDGNLLN LISDACEDWL SHIASKALIL
     SRHRRRGTQF SLKKGGLSSL TQLSQQRSAV SKELRNLALR QKEMEEKRVQ KRIVLGLEKS
     SGNGTDDAAN GKPGSEETLH RAANATAAMM ATGKKKYSWM SSGGGGAGSI GSLGDDARGS
     GVGIGGGGVG GGDSKTKQSA ILSARGDNGL RYRDLRSTNA IVLKDLLNAL EGEKKGTQHA
     ITKGYAKLRD