TF2B2_THEAC
ID TF2B2_THEAC Reviewed; 307 AA.
AC Q9HJM2;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcription initiation factor IIB 2 {ECO:0000255|HAMAP-Rule:MF_00383};
DE Short=TFIIB 2 {ECO:0000255|HAMAP-Rule:MF_00383};
GN Name=tfbB {ECO:0000255|HAMAP-Rule:MF_00383}; OrderedLocusNames=Ta0945;
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; CAC12074.1; -; Genomic_DNA.
DR RefSeq; WP_010901355.1; NC_002578.1.
DR AlphaFoldDB; Q9HJM2; -.
DR SMR; Q9HJM2; -.
DR STRING; 273075.Ta0945; -.
DR EnsemblBacteria; CAC12074; CAC12074; CAC12074.
DR GeneID; 1456477; -.
DR KEGG; tac:Ta0945; -.
DR eggNOG; arCOG01981; Archaea.
DR HOGENOM; CLU_043736_0_1_2; -.
DR OMA; RTQKDFA; -.
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; 1.
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..307
FT /note="Transcription initiation factor IIB 2"
FT /id="PRO_0000119339"
FT REPEAT 124..207
FT /note="1"
FT REPEAT 218..299
FT /note="2"
FT ZN_FING 7..38
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 11
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ SEQUENCE 307 AA; 34463 MW; 8C251025CBBBADD4 CRC64;
MTVEGETPKR CPECNSEHLI RDYEHGELIC ADCGAVIEDA YIDQGPEWRA FDSDQDERRA
RTGSPMTYLS HDKGLATEIS WSNKDYYGKR IPHKNRAQIY RVRKWHQRIR VSNAAERNLS
LALQLLNDIG AKLGIPKDIK ETAALIYRKA VEKNLIRGRS IESIVCASIY AACRKVNIPR
TLDEISKASE VNKKKIGKAY RHLAKELDLN LKPTTPFSYI SQFCNKLDLD KQAIVISEDI
VRQAMSMGIS SGKGPTGIAA AAIYIASVKV GKPRTQKEIA RISGVTEVTI RNRYKEISKA
LNISISE