TF2B_PYRWO
ID TF2B_PYRWO Reviewed; 300 AA.
AC P61999; P29095; Q51731;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Transcription initiation factor IIB {ECO:0000255|HAMAP-Rule:MF_00383};
DE Short=TFIIB {ECO:0000255|HAMAP-Rule:MF_00383};
GN Name=tfb {ECO:0000255|HAMAP-Rule:MF_00383};
OS Pyrococcus woesei.
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=2262;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8332505; DOI=10.1093/nar/21.12.2942;
RA Creti R., Londei P., Cammarano P.;
RT "Complete nucleotide sequence of an archaeal (Pyrococcus woesei) gene
RT encoding a homolog of eukaryotic transcription factor IIB (TFIIB).";
RL Nucleic Acids Res. 21:2942-2942(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-300.
RX PubMed=1723106; DOI=10.1007/bf02102864;
RA Creti R., Citarella F., Tiboni O., Sanangelantoni A.M., Palm P.,
RA Cammarano P.;
RT "Nucleotide sequence of a DNA region comprising the gene for elongation
RT factor 1 alpha (EF-1 alpha) from the ultrathermophilic archaeote Pyrococcus
RT woesei: phylogenetic implications.";
RL J. Mol. Evol. 33:332-342(1991).
RN [3]
RP SIMILARITY TO EUKARYOTIC TFIIB.
RX PubMed=1423586; DOI=10.1016/0092-8674(92)90347-f;
RA Ouzounis C., Sander C.;
RT "TFIIB, an evolutionary link between the transcription machineries of
RT archaebacteria and eukaryotes.";
RL Cell 71:189-190(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 101-300.
RX PubMed=9177165; DOI=10.1073/pnas.94.12.6042;
RA Kosa P.F., Ghosh G., DeDecker B.S., Sigler P.B.;
RT "The 2.1-A crystal structure of an archaeal preinitiation complex: TATA-
RT box-binding protein/transcription factor (II)B core/TATA-box.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6042-6047(1997).
CC -!- FUNCTION: Stabilizes TBP binding to an archaeal box-A promoter. Also
CC responsible for recruiting RNA polymerase II to the pre-initiation
CC complex (DNA-TBP-TFIIB).
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000255|HAMAP-
CC Rule:MF_00383}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA50006.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X70668; CAA50006.1; ALT_INIT; Genomic_DNA.
DR EMBL; X59857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S34116; S34116.
DR PDB; 1AIS; X-ray; 2.10 A; B=101-300.
DR PDB; 1D3U; X-ray; 2.40 A; B=100-300.
DR PDBsum; 1AIS; -.
DR PDBsum; 1D3U; -.
DR AlphaFoldDB; P61999; -.
DR SMR; P61999; -.
DR EvolutionaryTrace; P61999; -.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 2.
DR HAMAP; MF_00383; TF2B_arch; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR023484; TFIIB_arc.
DR InterPro; IPR023486; TFIIB_CS.
DR InterPro; IPR013150; TFIIB_cyclin.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618; PTHR11618; 1.
DR Pfam; PF08271; TF_Zn_Ribbon; 1.
DR Pfam; PF00382; TFIIB; 2.
DR PRINTS; PR00685; TIFACTORIIB.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
DR PROSITE; PS00782; TFIIB; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..300
FT /note="Transcription initiation factor IIB"
FT /id="PRO_0000119332"
FT REPEAT 114..197
FT /note="1"
FT REPEAT 210..291
FT /note="2"
FT ZN_FING 2..34
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:1AIS"
FT TURN 142..148
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 151..166
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:1AIS"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1D3U"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:1AIS"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 223..238
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 247..261
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:1AIS"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:1AIS"
SQ SEQUENCE 300 AA; 34106 MW; 476D7CA32B2ED4C1 CRC64;
MNKQKVCPAC ESAELIYDPE RGEIVCAKCG YVIEENIIDM GPEWRAFDAS QRERRSRTGA
PESILLHDKG LSTEIGIDRS LSGLMREKMY RLRKWQSRLR VSDAAERNLA FALSELDRIT
AQLKLPRHVE EEAARLYREA VRKGLIRGRS IESVMAACVY AACRLLKVPR TLDEIADIAR
VDKKEIGRSY RFIARNLNLT PKKLFVKPTD YVNKFADELG LSEKVRRRAI EILDEAYKRG
LTSGKSPAGL VAAALYIASL LEGEKRTQRE VAEVARVTEV TVRNRYKELV EKLKIKVPIA
