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Database: UniProt
Entry: A0A151BKD3_9ARCH
LinkDB: A0A151BKD3_9ARCH
Original site: A0A151BKD3_9ARCH 
ID   A0A151BKD3_9ARCH        Unreviewed;       320 AA.
AC   A0A151BKD3;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-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=AYL33_006120 {ECO:0000313|EMBL:KYH40341.1};
OS   Candidatus Bathyarchaeota archaeon B63.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1779372 {ECO:0000313|EMBL:KYH40341.1, ECO:0000313|Proteomes:UP000075614};
RN   [1] {ECO:0000313|EMBL:KYH40341.1, ECO:0000313|Proteomes:UP000075614}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B63 {ECO:0000313|EMBL:KYH40341.1};
RA   He Y., Li M., Perumal V., Feng X., Fang J., Xie J., Sievert S., Wang F.;
RT   "Evidence for homoacetogenesis among multiple lineages of the archaeal
RT   phylum Bathyarchaeota widespread in marine sediments.";
RL   Submitted (FEB-2016) 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:KYH40341.1}.
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DR   EMBL; LUCF01000063; KYH40341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BKD3; -.
DR   PATRIC; fig|1779372.3.peg.881; -.
DR   Proteomes; UP000075614; 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:KYH40341.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Protein biosynthesis {ECO:0000313|EMBL:KYH40341.1};
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|PROSITE-ProRule:PRU00469}.
FT   DOMAIN          11..44
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REPEAT          129..212
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REPEAT          223..304
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ   SEQUENCE   320 AA;  36087 MW;  D89C8E2BBC3A94D9 CRC64;
     MVVLNMQSLS LRQWGLCPEC GSPGLVTDEW TGEVICSKCG LVILDEVLNL TPEWRAFTPE
     ERRSRRRVGA PIDYSRFDKG LSTIIRINRD TSGRPLPAEM RRRMWRIRKT HIRSRMQAPN
     IRNLMKAMSE LEMLSERLHI PSFIQEMAAV IYRKALNANL IQGRSIAAVV AAALYAACRF
     TKMSRTLKEI AESSVRSKKE ISRCYFLLIR ELGMKMPFAD PLNHISRIAE KVNISGEALS
     LAVKILREAK RKRITTGKDP VGIAATVLYI ACQLRGEKMT QMDIAAAAGV TEVTIRNRKK
     ELMERLGLSS ESLPSRSSPS
//
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