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Database: UniProt
Entry: A0A0U2WM50_9CREN
LinkDB: A0A0U2WM50_9CREN
Original site: A0A0U2WM50_9CREN 
ID   A0A0U2WM50_9CREN        Unreviewed;       316 AA.
AC   A0A0U2WM50;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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   ECO:0000313|EMBL:ALU12033.1};
GN   ORFNames=EYM_07380 {ECO:0000313|EMBL:ALU12033.1};
OS   Ignicoccus islandicus DSM 13165.
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=940295 {ECO:0000313|EMBL:ALU12033.1, ECO:0000313|Proteomes:UP000060778};
RN   [1] {ECO:0000313|EMBL:ALU12033.1, ECO:0000313|Proteomes:UP000060778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13165 {ECO:0000313|EMBL:ALU12033.1,
RC   ECO:0000313|Proteomes:UP000060778};
RA   Podar M.;
RT   "Comparative genomics of Ignicoccus.";
RL   Submitted (NOV-2013) 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: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; CP006867; ALU12033.1; -; Genomic_DNA.
DR   RefSeq; WP_075050433.1; NZ_CP006867.1.
DR   AlphaFoldDB; A0A0U2WM50; -.
DR   STRING; 940295.EYM_07380; -.
DR   GeneID; 30680847; -.
DR   KEGG; iis:EYM_07380; -.
DR   PATRIC; fig|940295.4.peg.1434; -.
DR   OrthoDB; 7429at2157; -.
DR   Proteomes; UP000060778; 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:ALU12033.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Protein biosynthesis {ECO:0000313|EMBL:ALU12033.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060778};
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|PROSITE-ProRule:PRU00469}.
FT   DOMAIN          14..45
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REPEAT          131..214
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REPEAT          225..306
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REGION          60..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         37
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"
SQ   SEQUENCE   316 AA;  35811 MW;  EB704183E0874877 CRC64;
     MSPDVGAQHS EEKQPLRCPV CGSTDIIFKE DTGEYVCARC GTVIMDKYID QGPEWRAFTP
     EERERRGRTG APLSPTLHDQ GISTIIDHRD RDALGRRLDA RRRMEVLRWR KWQMRTRMQT
     GMDRNLTIAM NELDKFANIL GLPKQIKEEA AVIYRKAVEK GLVRGRSIES VVAAVIYAAC
     RIHHQPRTLD EISKALGVNR KDMARCYRLM LKELKLDIPI TDPIDHIPRI GQQLGLRGDI
     IAEAINIMKK VKGHAITAGK DPAGIAAAAI YIAVMQKGER RTQKEIAQVA GVTEVTVRNR
     YKELIKILEK ENKNTQ
//
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