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Database: UniProt
Entry: B0R9J1_HALS3
LinkDB: B0R9J1_HALS3
Original site: B0R9J1_HALS3 
ID   B0R9J1_HALS3            Unreviewed;       308 AA.
AC   B0R9J1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 2.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=Transcription initiation factor IIB {ECO:0000256|HAMAP-Rule:MF_00383};
DE            Short=TFIIB {ECO:0000256|HAMAP-Rule:MF_00383};
GN   Name=tfbH {ECO:0000313|EMBL:CAP15279.2};
GN   Synonyms=tfb {ECO:0000256|HAMAP-Rule:MF_00383};
GN   OrderedLocusNames=OE_6140R {ECO:0000313|EMBL:CAP15279.2};
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG   Plasmid PHS2 {ECO:0000313|EMBL:CAP15279.2,
OG   ECO:0000313|Proteomes:UP000001321}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium; Halobacterium salinarum NRC-34001.
OX   NCBI_TaxID=478009 {ECO:0000313|EMBL:CAP15279.2, ECO:0000313|Proteomes:UP000001321};
RN   [1] {ECO:0000313|EMBL:CAP15279.2, ECO:0000313|Proteomes:UP000001321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1 {ECO:0000313|Proteomes:UP000001321};
RC   PLASMID=Plasmid PHS2 {ECO:0000313|Proteomes:UP000001321};
RX   PubMed=18313895; DOI=.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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:0000256|HAMAP-Rule:MF_00383}.
CC   -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00383}.
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DR   EMBL; AM774417; CAP15279.2; -; Genomic_DNA.
DR   RefSeq; WP_049892660.1; NC_010369.1.
DR   AlphaFoldDB; B0R9J1; -.
DR   EnsemblBacteria; CAP15279; CAP15279; OE_6140R.
DR   GeneID; 5955078; -.
DR   KEGG; hsl:OE_6140R; -.
DR   HOGENOM; CLU_043736_0_0_2; -.
DR   PhylomeDB; B0R9J1; -.
DR   Proteomes; UP000001321; Plasmid PHS2.
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   Gene3D; 1.10.472.170; -; 1.
DR   Gene3D; 1.10.472.10; Cyclin-like; 1.
DR   HAMAP; MF_00383; TF2B_arch; 1.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR000812; TFIIB.
DR   InterPro; IPR023484; TFIIB_arc.
DR   InterPro; IPR013150; TFIIB_cyclin.
DR   InterPro; IPR013137; Znf_TFIIB.
DR   PANTHER; PTHR11618:SF13; TRANSCRIPTION INITIATION FACTOR IIB; 1.
DR   PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 1.
DR   Pfam; PF08271; TF_Zn_Ribbon; 1.
DR   Pfam; PF00382; TFIIB; 2.
DR   PRINTS; PR00685; TIFACTORIIB.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Plasmid {ECO:0000313|EMBL:CAP15279.2};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|HAMAP-Rule:MF_00383};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00383};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00383}; Zinc {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          23..61
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|Pfam:PF08271"
FT   DOMAIN          123..210
FT                   /note="Transcription factor TFIIB cyclin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00382"
FT   REPEAT          130..213
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   DOMAIN          219..298
FT                   /note="Transcription factor TFIIB cyclin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00382"
FT   REPEAT          224..305
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         27
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         43
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ   SEQUENCE   308 AA;  33951 MW;  D6E88443ACDB4926 CRC64;
     MATSEIYETT FDEDVQTDSS AKQCPECDGR VTTNTVETVC EDCGLVVDEQ RIDHGPEWRA
     FDEDERERTG APLTATRHDR GLSTEIGRGT DANGNRLSGR KRRQVARMRR EQSRGRFQSK
     AERNLAHGLG EVRRIVSALE LSEMIRDQAC QLFRSAQNED LLQGRSIEAM ATASVYGACR
     CDGLSRTLED VTDPARVEQS RVTNAYKTLN TELGLPAQPV TPSAFVPRLA SELDVSDQIR
     QRARQLAEAS ESTGATTGVQ PSGFAAACLY KAGREDGRWL TQSDIAEVAN VSVVTVRTHR
     DTLDELAV
//
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