ID   TAF4_PICGU              Reviewed;         455 AA.
AC   A5DAX7;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Transcription initiation factor TFIID subunit 4;
DE   AltName: Full=TBP-associated factor 4;
GN   Name=TAF4; ORFNames=PGUG_00432;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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; CH408155; EDK36334.2; -; Genomic_DNA.
DR   RefSeq; XP_001487055.1; XM_001487005.1.
DR   AlphaFoldDB; A5DAX7; -.
DR   STRING; 4929.XP_001487055.1; -.
DR   EnsemblFungi; EDK36334; EDK36334; PGUG_00432.
DR   GeneID; 5128568; -.
DR   KEGG; pgu:PGUG_00432; -.
DR   eggNOG; KOG2341; Eukaryota.
DR   HOGENOM; CLU_036634_1_0_1; -.
DR   InParanoid; A5DAX7; -.
DR   OMA; QWISHIA; -.
DR   OrthoDB; 1315539at2759; -.
DR   Proteomes; UP000001997; 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..455
FT                   /note="Transcription initiation factor TFIID subunit 4"
FT                   /id="PRO_0000343442"
FT   DOMAIN          247..323
FT                   /note="Histone-fold"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          314..370
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..32
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..112
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  50063 MW;  D02A46A15A6F112B CRC64;
     MSDSDGSKRP SETPDAADSD SKRQRGSSKS PVDVDEELNA ILGANGISEL EAASGNANQQ
     DIMDIDFDNL PAELLQKDDI QADRNSVGRS TSGSQTPQPI KSESMINVPQ SSQISRPIIR
     PAMPSAPVVP SSSAPVNRMN PLVQQANSIH GLNTSSIDNR TAPNFSTGHS TGQAGGNNQD
     RFHTNDPSKL NDALAAAGVD IGREEELLQQ QQYNRAPRIN VQQPSYLQSR PARQIQRTPF
     LNSYHLGTFM QRVARENGVL QSFMSDNELL ELMSASCEQW ISHIATKTVL LSRHRRRGIP
     ALKNKKLAAN QIPRSEVSKE LRNLALKQKE LEEQRVSRRI LLGLENKDAN SESNKVGAEE
     TLHRAANETA AMMTSNKKKY SWMSSGAGNG DDSKAMEREK DKQSHLLALR GDNGLRFRDI
     RTGDSVTMKD LLAALEDERM GVNKAIMKGY ARLKD