ID TF2B_METPE Reviewed; 334 AA. AC B8GJQ9; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 75. 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}; GN OrderedLocusNames=Mpal_0331; OS Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanomicrobiales; Methanoregulaceae; Methanosphaerula. OX NCBI_TaxID=521011; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c; RX PubMed=26543115; DOI=10.1128/genomea.01280-15; RA Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C., RA Yavitt J.B., Zinder S.H.; RT "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a RT Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland."; RL Genome Announc. 3:0-0(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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001338; ACL15713.1; -; Genomic_DNA. DR RefSeq; WP_012617032.1; NC_011832.1. DR AlphaFoldDB; B8GJQ9; -. DR SMR; B8GJQ9; -. DR STRING; 521011.Mpal_0331; -. DR GeneID; 7272635; -. DR KEGG; mpl:Mpal_0331; -. DR eggNOG; arCOG01981; Archaea. DR HOGENOM; CLU_043736_0_1_2; -. DR OrthoDB; 7429at2157; -. DR Proteomes; UP000002457; 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; cd20549; CYCLIN_TFIIB_archaea_like_rpt1; 1. DR CDD; cd20550; CYCLIN_TFIIB_archaea_like_rpt2; 1. DR Gene3D; 1.10.472.170; -; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 1. DR HAMAP; MF_00383; TF2B_arch; 1. DR InterPro; IPR013763; Cyclin-like_dom. 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:SF13; TRANSCRIPTION INITIATION FACTOR IIB; 1. DR PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 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; Cyclin-like; 2. DR SUPFAM; SSF57783; Zinc beta-ribbon; 1. 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_1000134236" 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; 38113 MW; FD099D74053692A5 CRC64; MQEIEKLRIL QTEREALKNR NRVIEHEKKT EDHTESVCPE CKSRQLVHDY ERAELVCQNC GLVIDDDFID RGPEWRAFDH DQRMKRSRVG APMTFTIHDK GLSTMIDWRN RDSYGRAISS KNRAQLYRLR KWQRRIRVSN ATERNLAFAL SELDRMASAL GLPRNVRETA AVVYRDAVDK NLIRGRSIEG VAAAALYAAC RQCSVPRTLD EIAEVSRVSR KEIGRTYRFI SRELGLKLLP TSPIDYVPRF CSGLTLKGEV QSRAVEILRQ AAERELTSGR GPTGVAAAAI YISSILGGER RTQREVAEVA GVTEVTIRNR YKELAEKLDI EIIL //