ID   TF2B_METTL              Reviewed;         339 AA.
AC   Q9P9I7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 85.
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};
OS   Methanothermococcus thermolithotrophicus (Methanococcus
OS   thermolithotrophicus).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanothermococcus.
OX   NCBI_TaxID=2186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10777522; DOI=10.1074/jbc.275.17.12393;
RA   Hausner W., Lange U., Musfeldt M.;
RT   "Transcription factor S, a cleavage induction factor of the archaeal RNA
RT   polymerase.";
RL   J. Biol. Chem. 275:12393-12399(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; AJ271467; CAB69073.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9P9I7; -.
DR   SMR; Q9P9I7; -.
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..339
FT                   /note="Transcription initiation factor IIB"
FT                   /id="PRO_0000119324"
FT   REPEAT          156..239
FT                   /note="1"
FT   REPEAT          250..331
FT                   /note="2"
FT   ZN_FING         39..70
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         46
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ   SEQUENCE   339 AA;  38377 MW;  2C23DA95C5E9A959 CRC64;
     MATKPVVKEK KKLENKKEIY KLIEHNDSSN KNVILEKEEE LICPMCGSKN IIKDYERAEI
     VCETCGCVLQ QNLFDVGPEW RAFDHEQRVK RSRVGPPMTY TIHDKGLSTV IDWRNKDSYG
     KDISADKRAQ LYRLRKWQRR IRVSDASERN LAFALSELDR IASKLGLPRN VRENAAVLYR
     GAVEKGLIRG RSIEGVAAAA LYAACRRCKV PRTLDEIAEG SRVDRKEIGR TYRFISRELN
     IRLTPTNPID YVPRFASELK LPGEVESKAI SILQKANEKG LTSGRGPTGV AAAAIYIASV
     LHGTRRTQRE VADVAGVTEV TIRNRYKELT EHLDIDVTL