TF2B1_THEAC
ID TF2B1_THEAC Reviewed; 312 AA.
AC Q9HJM7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Transcription initiation factor IIB 1 {ECO:0000255|HAMAP-Rule:MF_00383};
DE Short=TFIIB 1 {ECO:0000255|HAMAP-Rule:MF_00383};
GN Name=tfbA {ECO:0000255|HAMAP-Rule:MF_00383}; OrderedLocusNames=Ta0940;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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). {ECO:0000255|HAMAP-Rule:MF_00383}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000255|HAMAP-
CC Rule:MF_00383}.
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DR EMBL; AL445066; CAC12069.1; -; Genomic_DNA.
DR RefSeq; WP_010901349.1; NC_002578.1.
DR AlphaFoldDB; Q9HJM7; -.
DR SMR; Q9HJM7; -.
DR STRING; 273075.Ta0940; -.
DR EnsemblBacteria; CAC12069; CAC12069; CAC12069.
DR GeneID; 1456473; -.
DR KEGG; tac:Ta0940; -.
DR eggNOG; arCOG01981; Archaea.
DR HOGENOM; CLU_043736_0_1_2; -.
DR OMA; DHDQRMK; -.
DR OrthoDB; 35979at2157; -.
DR Proteomes; UP000001024; Chromosome.
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 3: Inferred from homology;
KW Metal-binding; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..312
FT /note="Transcription initiation factor IIB 1"
FT /id="PRO_0000119338"
FT REPEAT 129..212
FT /note="1"
FT REPEAT 223..304
FT /note="2"
FT ZN_FING 12..43
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ SEQUENCE 312 AA; 35100 MW; 85BE5459CA526837 CRC64;
MVENTKKKKV EEIERCPECG STNLIRDYEH GELVCGECGA VIEDAYIDQG PEWRAFDSEQ
NESRARAGSP MTYTIHDKGL STDISWKNKD SYGRSIPTRN RAQLYRLRKW QKRIKVSNAA
ERNLSQALQE LERMASNLSI PDDVKETAAV IYRKAVKQNM IRGRSIEGVV AGALYAACRI
TNVPRTLGEI ASVTRVKKKE IGRTYRIMSR YLKLNIMPSK AEDYISRFCS KLKLSMDTRN
KALEILRSAE NAGLTSGKGP TGVAAAAIYI ASLMTGERRT QRAVAEVAGV TEVTIRNRYK
ELTEKLQLNV EQ