TF2B1_THEVO
ID TF2B1_THEVO Reviewed; 312 AA.
AC Q979Q3;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-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=TV1107;
GN ORFNames=TVG1139885;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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; BA000011; BAB60249.1; -; Genomic_DNA.
DR RefSeq; WP_010917341.1; NC_002689.2.
DR AlphaFoldDB; Q979Q3; -.
DR SMR; Q979Q3; -.
DR STRING; 273116.14325345; -.
DR EnsemblBacteria; BAB60249; BAB60249; BAB60249.
DR GeneID; 1441223; -.
DR KEGG; tvo:TVG1139885; -.
DR eggNOG; arCOG01981; Archaea.
DR HOGENOM; CLU_043736_0_1_2; -.
DR OMA; DHDQRMK; -.
DR PhylomeDB; Q979Q3; -.
DR Proteomes; UP000001017; 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; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..312
FT /note="Transcription initiation factor IIB 1"
FT /id="PRO_0000119340"
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; 35266 MW; FBFA56FB1CA9E11A CRC64;
MVENQKKKKI EEIERCPECG STNLIRDYEH GELVCGECGA VIEDSYIDQG PEWRAFDSEQ
NESRARAGSP MTFTIHDKGL STDISWKNKD SYGRSIPTRN RAQLYRLRKW QKRIKVSNAA
ERNLSQALQE LERMAFNLSI PNDVRETAAV IYRKAVKQNM IRGRSIEGVV AGALYAACRI
TNVPRTLGEI ASVTRVKKKE IGRTYRIMSR YLKLNIMPSK AEDYISRFCS KLKLSMDTRN
KALEILRDAE NVGLTSGKGP TGVAAAAIYI ASLITGERRT QRAVAEVAGV TEVTIRNRYK
ELTEKLKLNV EQ