ID TF2B_PYRIL Reviewed; 333 AA. AC A1RV37; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 96. 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=Pisl_1667; OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3). OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae; OC Pyrobaculum. OX NCBI_TaxID=384616; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4184 / JCM 9189 / GEO3; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.; RT "Complete sequence of Pyrobaculum islandicum DSM 4184."; RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000504; ABL88819.1; -; Genomic_DNA. DR RefSeq; WP_011763394.1; NC_008701.1. DR AlphaFoldDB; A1RV37; -. DR SMR; A1RV37; -. DR STRING; 384616.Pisl_1667; -. DR GeneID; 4617859; -. DR KEGG; pis:Pisl_1667; -. DR eggNOG; arCOG01981; Archaea. DR HOGENOM; CLU_043736_0_1_2; -. DR OrthoDB; 7429at2157; -. DR Proteomes; UP000002595; 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; Repeat; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..333 FT /note="Transcription initiation factor IIB" FT /id="PRO_1000080116" FT REPEAT 149..232 FT /note="1" FT REPEAT 243..324 FT /note="2" FT ZN_FING 33..64 FT /note="TFIIB-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 37 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 40 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 56 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" FT BINDING 59 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469" SQ SEQUENCE 333 AA; 37475 MW; 47826C971CAC2CCC CRC64; MSSSSPTSSG KPLKLRIDRD NEGYLSLVTD TGEVYRCPIC GNDRFVYNYE RGEIVCIVCG AVVQEQLLDL GPEWRAFTSE EKGQRARTGA PLTRLISEAL TTVIDWRDKD VSGKELDIKR KLEVIRLRKW QTRARVQTSY ERNFIQAAQE LERLRSSMGV PRPCVEQALE IYRQALEKEL VRGRSVEAMA AAALYMACRM MKMPRPLDEL VRYTKASRRE VARCYRLLLR ELNVKVPISD PVLYISRIAE QLKLSGEVVK TAIEILQKAK KAGITAGKDP AGLAAAAVYI ASLLHGDNRT QKDFAVAAGV TEVTVRNRYK ELAKTLNIKV PVK //