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Database: UniProt
Entry: U3AGF4_9EURY
LinkDB: U3AGF4_9EURY
Original site: U3AGF4_9EURY 
ID   U3AGF4_9EURY            Unreviewed;       316 AA.
AC   U3AGF4;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=MBEHAL_2623 {ECO:0000313|EMBL:GAD53863.1};
OS   Halarchaeum acidiphilum MH1-52-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae.
OX   NCBI_TaxID=1261545 {ECO:0000313|EMBL:GAD53863.1, ECO:0000313|Proteomes:UP000016986};
RN   [1] {ECO:0000313|EMBL:GAD53863.1, ECO:0000313|Proteomes:UP000016986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16109 {ECO:0000313|EMBL:GAD53863.1,
RC   ECO:0000313|Proteomes:UP000016986};
RA   Shimane Y., Minegishi H., Nishi S., Echigo A., Shuto A., Konishi M.,
RA   Ito T., Ohkuma M., Ohta Y., Nagano Y., Tsubouchi T., Mori K., Usui K.,
RA   Kamekura M., Usami R., Takaki Y., Hatada Y.;
RT   "Whole genome sequencing of Halarchaeum acidiphilum strain MH1-52-1.";
RL   Submitted (SEP-2013) 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:GAD53863.1}.
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DR   EMBL; BATA01000117; GAD53863.1; -; Genomic_DNA.
DR   RefSeq; WP_021780825.1; NZ_BATA01000117.1.
DR   AlphaFoldDB; U3AGF4; -.
DR   eggNOG; arCOG01981; Archaea.
DR   OrthoDB; 7429at2157; -.
DR   Proteomes; UP000016986; 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; 1.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   3: Inferred from homology;
KW   Initiation factor {ECO:0000313|EMBL:GAD53863.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Protein biosynthesis {ECO:0000313|EMBL:GAD53863.1};
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|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00469}.
FT   DOMAIN          21..50
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REPEAT          136..219
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REPEAT          230..311
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         28
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         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ   SEQUENCE   316 AA;  35514 MW;  BE91371B5639D61F CRC64;
     MERSIREQDG EQTEQDDGEV VSAQCPECES TNIVTDQGER LCQDCGLVLE EDNIDHGPEW
     RAFNSSERDQ KSRVGAPTTQ TMHDKGLTTQ IDWKDKDAYG RSISSKKRSQ MHRLRKWQER
     IRTKDAGERN LQFALSEIDR MASALGVPRS VREVASVIYR RALKEDLIRG RSIEGVATAC
     LYAACRKESI PRSLEEVAEV SRVGKKEIGR TYRYIAQELS LEMEPVDPKQ YVPRFASELD
     ASEETIAKAN EIIDTSAEQG LLSGKSPIGF AAAAIYAAGL LCNDKMTQRE VADVANVTEV
     TIRNRYQEQI EAMGFE
//
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