ID   TAF4_YEAS7              Reviewed;         388 AA.
AC   A6ZM67;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Transcription initiation factor TFIID subunit 4;
DE   AltName: Full=MPT-1;
DE   AltName: Full=TAF suppressor gene 2 protein;
DE   AltName: Full=TAFII-48;
DE   AltName: Full=TBP-associated factor 4;
DE   AltName: Full=TBP-associated factor 48 kDa;
GN   Name=TAF4; Synonyms=MPT1, TAF48, TSG2; ORFNames=SCY_4179;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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: TAF4 heterodimerizes with TAF12, forming ultimately an octamer
CC       consisting of a TAF6/TAF9 heterotetramer core flanked by TAF4/TAF12
CC       dimers on either side, similar to the histone H2A/H2B/H3/H4 octamer.
CC       The 1.2 MDa TFIID complex is composed of TATA binding protein (TBP) and
CC       the 14 TBP-associated factors. One copy of each TAF1, TAF2, TAF3, TAF7,
CC       TAF8, TAF11, TAF13, two copies of each TAF4, TAF5, TAF6, TAF9, TAF10,
CC       TAF12, and three copies of TAF14 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TAF4 family. {ECO:0000305}.
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DR   EMBL; AAFW02000020; EDN64397.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZM67; -.
DR   SMR; A6ZM67; -.
DR   PRIDE; A6ZM67; -.
DR   EnsemblFungi; EDN64397; EDN64397; SCY_4179.
DR   HOGENOM; CLU_036634_0_0_1; -.
DR   Proteomes; UP000007060; 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; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..388
FT                   /note="Transcription initiation factor TFIID subunit 4"
FT                   /id="PRO_0000343445"
FT   DOMAIN          193..261
FT                   /note="Histone-fold"
FT   REGION          1..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          279..297
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50105"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50105"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P50105"
SQ   SEQUENCE   388 AA;  42306 MW;  7DFAC01C7AF060CD CRC64;
     MANSPKKPSD GTGVSASDTP KYQHTVPETK PAFNLSPGKA SELSHSLPSP SQIKSTAHVS
     STHNDAAGNT DDSVLPKNVS PTTNLRVESN GDTNNMFSSP AGLALPKKDD KKKNKGTSKA
     DSKDGKASNS SGQNAQQQSD PNKMQDVLFS AGIDVREEEA LLNSSINASK SQVQTNNVKI
     PNHLPFLHPE QVSNYMRKVG KEQNFNLTPT KNPEILDMMS SACENYMRDI LTNAIVISRH
     RRKAVKINSG RRSEVSAALR AIALIQKKEE ERRVKKRIAL GLEKEDYENK IDSEETLHRA
     SNVTAGLRAG SKKQYGWLTS SVNKPTSLGA KSSGKVASDI TARGESGLKF REAREEPGIV
     MRDLLFALEN RRNGVQTIIS KGYAKIRD