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Database: UniProt
Entry: A0A2A2FJZ3_9EURY
LinkDB: A0A2A2FJZ3_9EURY
Original site: A0A2A2FJZ3_9EURY 
ID   A0A2A2FJZ3_9EURY        Unreviewed;       333 AA.
AC   A0A2A2FJZ3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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   ORFNames=CK500_02775 {ECO:0000313|EMBL:PAU84962.1};
OS   Halorubrum salipaludis.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Halorubraceae; Halorubrum.
OX   NCBI_TaxID=2032630 {ECO:0000313|EMBL:PAU84962.1, ECO:0000313|Proteomes:UP000218083};
RN   [1] {ECO:0000313|EMBL:PAU84962.1, ECO:0000313|Proteomes:UP000218083}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WN019 {ECO:0000313|EMBL:PAU84962.1,
RC   ECO:0000313|Proteomes:UP000218083};
RA   Liu D., Zhang G.;
RT   "The strain WRN001 was isolated from Binhai saline alkaline soil, Tianjin,
RT   China.";
RL   Submitted (AUG-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAU84962.1}.
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DR   EMBL; NSKC01000002; PAU84962.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2FJZ3; -.
DR   OrthoDB; 7429at2157; -.
DR   Proteomes; UP000218083; Unassembled WGS sequence.
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; 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; 2.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000313|EMBL:PAU84962.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Protein biosynthesis {ECO:0000313|EMBL:PAU84962.1};
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          34..65
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REPEAT          151..234
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REPEAT          245..326
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          75..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         57
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ   SEQUENCE   333 AA;  36945 MW;  B0194996904FBA3E CRC64;
     MTETHIRGYD SEIERDRTTE SAESTTDETE SASERTTTCP ECDGNLVTDT EHGETVCTDC
     GLVVEQDSVD RGPEWRAFDS SERDSKSRVG APTTNMMHDK GLSTNIGWQD KDAYGKSLSS
     SQRQRMQRLR TWNERFRTRD SKDRNLKQAL GEIDRMASAL GLPDNVRETA SVIYRRALSE
     NLLPGRSIEG VATAALYAAA RQAGNPRSLD EFTAVSRVDK MELTRTYRYV IRELKLEIQP
     ADPESYVPRF VSRLDLSEET QRAARELLDS AKRSGITSGK SPVGLAASAV YAAALLSNEK
     VTQSEVSAVA DISEVTIRNR YKELLDASEG LTA
//
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