TBP_PYRWO
ID TBP_PYRWO Reviewed; 191 AA.
AC P62001; Q57050;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=TATA-box-binding protein;
DE AltName: Full=Box A-binding protein;
DE Short=BAP;
DE AltName: Full=TATA sequence-binding protein;
DE Short=TBP;
DE AltName: Full=TATA-box factor;
GN Name=tbp;
OS Pyrococcus woesei.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=2262;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8191287; DOI=10.1126/science.8191287;
RA Rowlands T.M., Baumann P., Jackson S.P.;
RT "The TATA-binding protein: a general transcription factor in eukaryotes and
RT archaebacteria.";
RL Science 264:1326-1329(1994).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9000631; DOI=10.1006/jmbi.1996.0697;
RA DeDecker B.S., O'Brien R., Fleming P.J., Geiger J.H., Jackson S.P.,
RA Sigler P.B.;
RT "The crystal structure of a hyperthermophilic archaeal TATA-box binding
RT protein.";
RL J. Mol. Biol. 264:1072-1084(1996).
CC -!- FUNCTION: General factor that plays a role in the activation of
CC archaeal genes transcribed by RNA polymerase. Binds specifically to the
CC TATA box promoter element which lies close to the position of
CC transcription initiation.
CC -!- SIMILARITY: Belongs to the TBP family. {ECO:0000305}.
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DR EMBL; U10285; AAA73447.1; -; Unassigned_DNA.
DR PIR; A54275; A54275.
DR PDB; 1AIS; X-ray; 2.10 A; A=1-181.
DR PDB; 1D3U; X-ray; 2.40 A; A=1-181.
DR PDB; 1PCZ; X-ray; 2.20 A; A/B=1-191.
DR PDBsum; 1AIS; -.
DR PDBsum; 1D3U; -.
DR PDBsum; 1PCZ; -.
DR AlphaFoldDB; P62001; -.
DR SMR; P62001; -.
DR EvolutionaryTrace; P62001; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR CDD; cd04518; TBP_archaea; 1.
DR Gene3D; 3.30.310.10; -; 2.
DR HAMAP; MF_00408; TATA_bind_prot_arch; 1.
DR InterPro; IPR000814; TBP.
DR InterPro; IPR033711; TBP_archaea.
DR InterPro; IPR030491; TBP_CS.
DR InterPro; IPR012295; TBP_dom_sf.
DR PANTHER; PTHR10126; PTHR10126; 1.
DR Pfam; PF00352; TBP; 2.
DR PRINTS; PR00686; TIFACTORIID.
DR PROSITE; PS00351; TFIID; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..191
FT /note="TATA-box-binding protein"
FT /id="PRO_0000154023"
FT REPEAT 11..87
FT /note="1"
FT REPEAT 102..178
FT /note="2"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1PCZ"
FT STRAND 8..19
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1AIS"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1D3U"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 73..89
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:1PCZ"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1AIS"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 154..163
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:1AIS"
SQ SEQUENCE 191 AA; 21312 MW; B371491BF9282972 CRC64;
MVDMSKVKLR IENIVASVDL FAQLDLEKVL DLCPNSKYNP EEFPGIICHL DDPKVALLIF
SSGKLVVTGA KSVQDIERAV AKLAQKLKSI GVKFKRAPQI DVQNMVFSGD IGREFNLDVV
ALTLPNCEYE PEQFPGVIYR VKEPKSVILL FSSGKIVCSG AKSEADAWEA VRKLLRELDK
YGLLEEEEEE L
