TF2B2_THEVO
ID TF2B2_THEVO Reviewed; 313 AA.
AC Q979P7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Transcription initiation factor IIB 2 {ECO:0000255|HAMAP-Rule:MF_00383};
DE Short=TFIIB 2 {ECO:0000255|HAMAP-Rule:MF_00383};
GN Name=tfbB {ECO:0000255|HAMAP-Rule:MF_00383}; OrderedLocusNames=TV1113;
GN ORFNames=TVG1144753;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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; BA000011; BAB60255.1; -; Genomic_DNA.
DR RefSeq; WP_010917347.1; NC_002689.2.
DR AlphaFoldDB; Q979P7; -.
DR SMR; Q979P7; -.
DR STRING; 273116.14325351; -.
DR EnsemblBacteria; BAB60255; BAB60255; BAB60255.
DR GeneID; 1441229; -.
DR KEGG; tvo:TVG1144753; -.
DR eggNOG; arCOG01981; Archaea.
DR HOGENOM; CLU_043736_0_1_2; -.
DR OMA; RTQKDFA; -.
DR OrthoDB; 35979at2157; -.
DR PhylomeDB; Q979P7; -.
DR Proteomes; UP000001017; 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; 1.
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; 1.
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..313
FT /note="Transcription initiation factor IIB 2"
FT /id="PRO_0000119341"
FT REPEAT 130..213
FT /note="1"
FT REPEAT 224..305
FT /note="2"
FT ZN_FING 13..44
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ SEQUENCE 313 AA; 35203 MW; 09CAB21F626CDA89 CRC64;
MPYSDKMAIE SEAPKRCPEC HSEHLIRDYE HGELICADCG AVIEDSFIDQ GPEWRAFDSD
QDERRARTGS PMTYLSHDKG LATEISWSNK DYYGKRIPHK NRAQIYRVRK WHQRIRVSNA
AERNLSLALQ LLNDIGAKLG IPKDIKETSA LIYRKAVEKN LIRGRSIESI VCASIYAACR
KVNIPRTLDE IAKASEVNKK KIGKAYRHLA KELDLNLRPT TPFSYIAQFC NKLDLDKQAI
VISEDIVRQA MSMGISSGKG PTGIAAAAIY IASVKVGKPR TQKEIARISG VTEVTIRNRY
KEISKALNIS ISE