TAF4_DEBHA
ID TAF4_DEBHA Reviewed; 522 AA.
AC Q6BKB1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Transcription initiation factor TFIID subunit 4;
DE AltName: Full=TBP-associated factor 4;
GN Name=TAF4; OrderedLocusNames=DEHA2F23408g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89766.2; -; Genomic_DNA.
DR RefSeq; XP_461360.2; XM_461360.1.
DR AlphaFoldDB; Q6BKB1; -.
DR STRING; 4959.XP_461360.2; -.
DR EnsemblFungi; CAG89766; CAG89766; DEHA2F23408g.
DR GeneID; 2903359; -.
DR KEGG; dha:DEHA2F23408g; -.
DR VEuPathDB; FungiDB:DEHA2F23408g; -.
DR eggNOG; KOG2341; Eukaryota.
DR HOGENOM; CLU_036634_1_0_1; -.
DR InParanoid; Q6BKB1; -.
DR OMA; QWISHIA; -.
DR OrthoDB; 1315539at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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..522
FT /note="Transcription initiation factor TFIID subunit 4"
FT /id="PRO_0000343439"
FT DOMAIN 293..379
FT /note="Histone-fold"
FT REGION 1..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..37
FT /evidence="ECO:0000255"
FT COILED 368..395
FT /evidence="ECO:0000255"
FT COMPBIAS 15..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 56663 MW; 41938B2BAFB3CF76 CRC64;
MSDVSGGESS SHKRNVDSAA NENDDMQNKR QKTEELGGHD DQLNDIFNDP LPGFGGSESN
STPYNDNAQE GELGPENFDA TLPKEGDPLD IDFDNLPTNF LEAEQATNAN NGSQVDTPSG
PGSVPNMSVT TNSASMSASP NNTPRPTPLS KTNSRSETPV GNSSRATYDG TNLKQEFGIN
GLSNKQEALN RYSQMPPTNR MNHLAPQPQG IQGLNTSSID RIPSTSTSNK EQLHTNDPSK
LNDALAAAGV DIQHEEELLM QQHLNRSSRF PSAQQPPRQR FAQTSLFSPY HVAAFMQRVA
RENGVMQNFY QDAELLELMS TSCENWLSNI ITKTIILSRH RRRGIPTITN TKQNKKTASS
SASMSNPASR SELSKELRNL AAKQKEMEER RVSKRMALGL EKDGTDPGNG DPANGKAGAE
ETLHRAANAT AAMMTMNPGR KKYSWMTANA GSGGGDDSKV ASEKDGKSKQ SSIIAARGDN
GLRFREIRSG NSVTMKDLLG ALEDERMGTE KAVLKGYAKL KD
