ID B9LP13_HALLT Unreviewed; 333 AA.
AC B9LP13;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 91.
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=Hlac_1513 {ECO:0000313|EMBL:ACM57101.1};
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348 {ECO:0000313|EMBL:ACM57101.1, ECO:0000313|Proteomes:UP000000740};
RN [1] {ECO:0000313|EMBL:ACM57101.1, ECO:0000313|Proteomes:UP000000740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34
RC {ECO:0000313|Proteomes:UP000000740};
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001365; ACM57101.1; -; Genomic_DNA.
DR RefSeq; WP_015910241.1; NC_012029.1.
DR AlphaFoldDB; B9LP13; -.
DR GeneID; 7401439; -.
DR KEGG; hla:Hlac_1513; -.
DR eggNOG; arCOG01981; Archaea.
DR HOGENOM; CLU_043736_0_0_2; -.
DR Proteomes; UP000000740; Chromosome 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000000740};
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 33..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..39
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..37
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; 36946 MW; DA5CB51EBA2906C7 CRC64;
MTETHIRGYN GETERDRSTE STESTAEEAE STEERTTTCP ECEGNLITDT EHGETVCSEC
GLVVEQDSVD RGPEWRAFDS SERDSKSRVG APTTNMMHDK GLSTNIGWQD KDAYGKSLSS
RQRQRMQRLR TWNERFRTRD SKERNLKQAL GEIDRMASAL GLPDNVRETA SVIYRRALSE
NLLPGRSIEG VATAALYAAA RQAGNPRSLD EISAVSRVDK MELTRTYRYV IRELKLEIQP
ADPGSYVPRF VSRLGLSEET QRVARELLDS AKRAGITSGK SPVGLAASAV YAAALLSNEK
VTQSQVSEVA DISEVTIRNR YKELLDASEG LTA
//
