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Database: UniProt
Entry: F0LLM1_THEBM
LinkDB: F0LLM1_THEBM
Original site: F0LLM1_THEBM 
ID   F0LLM1_THEBM            Unreviewed;       306 AA.
AC   F0LLM1;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Transcription initiation factor IIB {ECO:0000256|ARBA:ARBA00013932, ECO:0000256|HAMAP-Rule:MF_00383};
DE            Short=TFIIB {ECO:0000256|HAMAP-Rule:MF_00383};
GN   Name=tfb {ECO:0000256|HAMAP-Rule:MF_00383};
GN   OrderedLocusNames=TERMP_00821 {ECO:0000313|EMBL:ADT83798.1};
OS   Thermococcus barophilus (strain DSM 11836 / MP).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT83798.1, ECO:0000313|Proteomes:UP000007478};
RN   [1] {ECO:0000313|EMBL:ADT83798.1, ECO:0000313|Proteomes:UP000007478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX   PubMed=21217005; DOI=10.1128/JB.01490-10;
RA   Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT   "Complete genome sequence of the hyperthermophilic, piezophilic,
RT   heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL   J. Bacteriol. 193:1481-1482(2011).
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.
CC       {ECO:0000256|ARBA:ARBA00010857, ECO:0000256|HAMAP-Rule:MF_00383}.
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DR   EMBL; CP002372; ADT83798.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0LLM1; -.
DR   KEGG; tba:TERMP_00821; -.
DR   PATRIC; fig|391623.17.peg.823; -.
DR   eggNOG; arCOG01981; Archaea.
DR   HOGENOM; CLU_043736_0_1_2; -.
DR   Proteomes; UP000007478; 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:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd20549; CYCLIN_TFIIB_archaea_like_rpt1; 1.
DR   CDD; cd20550; CYCLIN_TFIIB_archaea_like_rpt2; 1.
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; IPR013763; Cyclin-like_dom.
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: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   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin-like; 2.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS00782; TFIIB; 1.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000313|EMBL:ADT83798.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Protein biosynthesis {ECO:0000313|EMBL:ADT83798.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007478};
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, ECO:0000256|PROSITE-
KW   ProRule:PRU00469}.
FT   DOMAIN          5..37
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REPEAT          123..206
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REPEAT          217..298
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         13
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         32
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ   SEQUENCE   306 AA;  34518 MW;  EB4AA79E0D101B66 CRC64;
     MISAEDFKKC PVCGSVRLIY DPERGEIVCT ACGYVVAQNI IDSGPEWRAF DADQRVKRGR
     VGAPMTMMIH DKGLSSTIDW KNKDIHGHDI SGTMRAKMYR LRKWQRRIRV SDAAERNLAF
     ALSELDRMAS QLGLPRNIKE MAAALYRKAV MERLIRGRSI EGVTAACLYA ACRMAKVPRT
     LDEIEEVARV DKKEIGRSYR FIARELHLRL TPTSPIDYVS RFADQLGLSE RTKNRAVKIL
     QKAIKLGLTS GRGPMGVAAA ALYIASVLEG EKKTQREVAE VAHVTEVTVR NRYKELVERL
     NIRLSL
//
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