ID A0A133VM46_9EURY Unreviewed; 318 AA.
AC A0A133VM46;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:KXB07528.1};
GN ORFNames=AKJ51_01150 {ECO:0000313|EMBL:KXB07528.1};
OS candidate division MSBL1 archaeon SCGC-AAA382A20.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698280 {ECO:0000313|EMBL:KXB07528.1, ECO:0000313|Proteomes:UP000070263};
RN [1] {ECO:0000313|EMBL:KXB07528.1, ECO:0000313|Proteomes:UP000070263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA382A20 {ECO:0000313|EMBL:KXB07528.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(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 -!- 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:KXB07528.1}.
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DR EMBL; LHYE01000007; KXB07528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133VM46; -.
DR PATRIC; fig|1698280.3.peg.1082; -.
DR Proteomes; UP000070263; 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; 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; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000313|EMBL:KXB07528.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW Protein biosynthesis {ECO:0000313|EMBL:KXB07528.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070263};
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 16..49
FT /note="TFIIB-type"
FT /evidence="ECO:0000259|PROSITE:PS51134"
FT REPEAT 135..218
FT /note="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT REPEAT 229..310
FT /note="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ SEQUENCE 318 AA; 36402 MW; D989C1C50B7DB346 CRC64;
MAKANGKNSK QNEKKEKLDE ECPSCENSSL VRDYQRNIVI CEKCGRIVRE AIKDRGPEWR
AFDQDQRDEK SRGGAPMTYT IHDKGLSTKI DWKNRDGHGQ SLSPERRSRM YRLRKWQRRI
RVSDATERNL AFALSEMDRM SSQLGLPRNV REITSMIYRD AVKNQLIRGR SIEGVASAAL
YVGCRETQMP RTLEEVAEVS RVGKKEISRS YRFITRELDI HLPPIDPVNY ISRFGSKLEV
SGEVRTKAIE IIKEAQEEKL TSGRGPTGIA AASIYVAALQ SGERRTQREV AEVAQVTEVT
VRNRYKELAE ELELEINI
//