ID   TF2B_METB6              Reviewed;         334 AA.
AC   A7IAR4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, 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}; OrderedLocusNames=Mboo_2311;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS56825.1; -; Genomic_DNA.
DR   RefSeq; WP_012107885.1; NC_009712.1.
DR   AlphaFoldDB; A7IAR4; -.
DR   SMR; A7IAR4; -.
DR   STRING; 456442.Mboo_2311; -.
DR   PRIDE; A7IAR4; -.
DR   EnsemblBacteria; ABS56825; ABS56825; Mboo_2311.
DR   GeneID; 5409810; -.
DR   KEGG; mbn:Mboo_2311; -.
DR   eggNOG; arCOG01981; Archaea.
DR   HOGENOM; CLU_043736_0_1_2; -.
DR   OMA; DHDQRMK; -.
DR   OrthoDB; 35979at2157; -.
DR   Proteomes; UP000002408; 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..334
FT                   /note="Transcription initiation factor IIB"
FT                   /id="PRO_1000080107"
FT   REPEAT          151..234
FT                   /note="1"
FT   REPEAT          245..326
FT                   /note="2"
FT   ZN_FING         34..65
FT                   /note="TFIIB-type"
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"
FT   BINDING         41
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ   SEQUENCE   334 AA;  37847 MW;  A6C45EFF371AF499 CRC64;
     MQEVEKLKLL QSEREALKSR IKVKEQEKKA ENHTETVCPE CGGRQLVHDY ERAELVCQSC
     GLVIDDDFID RGPEWRAFDH DQRMKRSRVG APMTFTIHDK GLSTMIDWRN RDSYGRAISS
     KNRAQLYRLR KWQRRIRVSN ATERNLAFAL SELDRMASAL GLPRNVRETA AVVYRDAVDK
     NLIRGRSIEG VAAAALYAAC RQCSVPRTLD EIAEVSRVSR KEIGRTYRFI SRELGLKLLP
     TSPIDYVPRF CSGLTLKGEV QSRAVEILRQ AGERELTSGR GPTGVAAAAI YISSILGGER
     RTQREVAEVA GVTEVTIRNR YKELAEKLDI EIIL