TF2B_METTP
ID TF2B_METTP Reviewed; 337 AA.
AC A0B5T8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Mthe_0265;
OS Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS PT) (Methanosaeta thermophila).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=349307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT "Complete sequence of Methanosaeta thermophila PT.";
RL Submitted (OCT-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}.
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DR EMBL; CP000477; ABK14062.1; -; Genomic_DNA.
DR AlphaFoldDB; A0B5T8; -.
DR SMR; A0B5T8; -.
DR STRING; 349307.Mthe_0265; -.
DR PRIDE; A0B5T8; -.
DR EnsemblBacteria; ABK14062; ABK14062; Mthe_0265.
DR KEGG; mtp:Mthe_0265; -.
DR HOGENOM; CLU_043736_0_1_2; -.
DR OMA; DHDQRMK; -.
DR Proteomes; UP000000674; 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..337
FT /note="Transcription initiation factor IIB"
FT /id="PRO_1000080114"
FT REPEAT 154..237
FT /note="1"
FT REPEAT 248..329
FT /note="2"
FT ZN_FING 37..68
FT /note="TFIIB-type"
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 44
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"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ SEQUENCE 337 AA; 38703 MW; F1475DB2E705C788 CRC64;
MEEIERIREI ERTEQEKIKE RIKLQREKEK EEELDKYTVE CPECGSRALV RDYERAELVC
SECGLVIDEN FIDQGPEWRA FDHDQRMKRS RVGAPMTYTI HDKGLSTMID WRNRDSYGKT
ISSKNRAQLY RLRKWQRRIR VSNATERNLA FALSELDRMA SALGLSRNVR ETAAVIYRRA
VEKNLIRGRS IEGVAAAALY AACRQCNVPR TLDEIAEVSR VSRKEIGRTY RFVSRELSLK
LMPTSPIDYI PRFCSGLNLK GDVQAKGIEI LRQAAEKELT SGRGPTGVAA AAIYIASILC
NDRRTQREVA DVAGVTEVTI RNRYKELAEE LNIEIIL