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Database: UniProt
Entry: A0A133VM46_9EURY
LinkDB: A0A133VM46_9EURY
Original site: A0A133VM46_9EURY 
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
//
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