TF2B_PYRAR
ID TF2B_PYRAR Reviewed; 333 AA.
AC A4WMA6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Pars_1976;
OS Pyrobaculum arsenaticum (strain DSM 13514 / JCM 11321 / PZ6).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=340102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700994 / DSM 13514 / JCM 11321 / PZ6;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum arsenaticum DSM 13514.";
RL Submitted (APR-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; CP000660; ABP51523.1; -; Genomic_DNA.
DR AlphaFoldDB; A4WMA6; -.
DR SMR; A4WMA6; -.
DR STRING; 340102.Pars_1976; -.
DR EnsemblBacteria; ABP51523; ABP51523; Pars_1976.
DR KEGG; pas:Pars_1976; -.
DR HOGENOM; CLU_043736_0_1_2; -.
DR OMA; RTQKDFA; -.
DR PhylomeDB; A4WMA6; -.
DR Proteomes; UP000001567; 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; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..333
FT /note="Transcription initiation factor IIB"
FT /id="PRO_1000080115"
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; 37473 MW; 9D31DB6955D05AE7 CRC64;
MSSTSLPSSG KPLKLRINRD SEGYLSLVTE SGEIYRCPIC GNDRFVYNYE RGEVVCIVCG
AVVQEQLLDL GPEWRAFTSE EKGQRARTGA PLTRLISEAL TTVIDWRDKD VSGRELDIKR
KLEVIRLRKW QTRARVQTSY ERNFIQAAQE LERLKSSMGV PRPCVEQALE IYRQALEKEL
VRGRSVEAMA AAALYMACRM MRMPRPLDEL VRYTKASRRE VARCYRLLLR ELNVKVPISD
PVLYISRIAE QLKLSGEVVK AAIDILQRAK KAGITAGKDP AGLAAAAVYI ASLMHGDNRT
QKDFAVAAGV TEVTVRNRYK ELAKALNIKV PVK