ID M0E664_9EURY Unreviewed; 333 AA.
AC M0E664;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=C471_01407 {ECO:0000313|EMBL:ELZ43295.1};
OS Halorubrum saccharovorum DSM 1137.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=1227484 {ECO:0000313|EMBL:ELZ43295.1, ECO:0000313|Proteomes:UP000011514};
RN [1] {ECO:0000313|EMBL:ELZ43295.1, ECO:0000313|Proteomes:UP000011514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1137 {ECO:0000313|EMBL:ELZ43295.1,
RC ECO:0000313|Proteomes:UP000011514};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELZ43295.1}.
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DR EMBL; AOJE01000006; ELZ43295.1; -; Genomic_DNA.
DR RefSeq; WP_004045976.1; NZ_AOJE01000006.1.
DR AlphaFoldDB; M0E664; -.
DR STRING; 1227484.C471_01407; -.
DR PATRIC; fig|1227484.4.peg.286; -.
DR eggNOG; arCOG01981; Archaea.
DR OrthoDB; 7429at2157; -.
DR Proteomes; UP000011514; 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: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 Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
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..40
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..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..40
FT /note="Polar 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; 36981 MW; A877CC0460468CC2 CRC64;
MTETHIRGYN GETERDRTTE SAESTVDEAE STGEQTTTCP ECEGNLVTDT EHGETVCTDC
GLVVEQDSVD RGPEWRAFDS SERDSKSRVG APTTNMMHDK GLSTNIGWQD KDAYGKSLSS
RQRQRMQRLR TWNERFRTRD SKERNLKQAL GEIDRMASAL GLPDNVRETA SVIYRRALSE
NLLPGRSIEG VATAALYAAA RQAGNPRSLD EFTAVSRVDK MELTRTYRYV IRELKLEIQP
ADPESYVPRF VSRLDLSEET QRLARELLDG AKESGITSGK SPVGLAASAV YAAALLSNEK
VTQSQVSEVA DISEVTIRNR YKELLDASEG LTA
//
