TF2B_METM7
ID TF2B_METM7 Reviewed; 339 AA.
AC A6VI28;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=MmarC7_1038;
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 / ATCC BAA-1331;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
RL Submitted (JUN-2007) 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}.
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DR EMBL; CP000745; ABR66104.1; -; Genomic_DNA.
DR RefSeq; WP_011977417.1; NC_009637.1.
DR AlphaFoldDB; A6VI28; -.
DR SMR; A6VI28; -.
DR STRING; 426368.MmarC7_1038; -.
DR EnsemblBacteria; ABR66104; ABR66104; MmarC7_1038.
DR GeneID; 5328939; -.
DR KEGG; mmz:MmarC7_1038; -.
DR eggNOG; arCOG01981; Archaea.
DR HOGENOM; CLU_043736_0_1_2; -.
DR OMA; DHDQRMK; -.
DR OrthoDB; 35979at2157; -.
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_1000080109"
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; 38229 MW; 5B91E6587E8967D4 CRC64;
MKVESVTKEE TKKPERKIKL AIAKPEDYSN KNVILEKEEE LICPVCGSKN IIKDYERAEI
VCEMCGCVLQ QNLFDVGPEW RAFDHEQRVK RSRVGAPMTY TIHDKGLSTV IDWRNKDSYG
KDISADKRAQ LYRLRKWQRR IRVSDASERN LAFALSELDR IASKLGLPRN VRENAAVLYR
GAVEKGLIRG RSIEGVAAAA LYAACRRCKV PRTLDEIAEV SRVDRKEIGR TYRFISRELN
IRLAPTNPVD YVPRFASELK LPGEVESKAI SILQKAGEKG LTSGRGPTGV AAAAIYIASV
LQGTRRTQRE VADVAGVTEV TIRNRYKELT EHLDIDVTL