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Database: UniProt
Entry: J2ZVB6_9EURY
LinkDB: J2ZVB6_9EURY
Original site: J2ZVB6_9EURY 
ID   J2ZVB6_9EURY            Unreviewed;       319 AA.
AC   J2ZVB6;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
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=HSB1_47950 {ECO:0000313|EMBL:EJN56978.1};
OS   Halogranum salarium B-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae.
OX   NCBI_TaxID=1210908 {ECO:0000313|EMBL:EJN56978.1, ECO:0000313|Proteomes:UP000007813};
RN   [1] {ECO:0000313|EMBL:EJN56978.1, ECO:0000313|Proteomes:UP000007813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-1 {ECO:0000313|EMBL:EJN56978.1,
RC   ECO:0000313|Proteomes:UP000007813};
RX   PubMed=23144405; DOI=10.1128/JB.01815-12;
RA   Kim K.K., Lee K.C., Lee J.S.;
RT   "Draft Genome Sequence of the Extremely Halophilic Archaeon Halogranum
RT   salarium B-1T.";
RL   J. Bacteriol. 194:6659-6659(2012).
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:EJN56978.1}.
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DR   EMBL; ALJD01000017; EJN56978.1; -; Genomic_DNA.
DR   AlphaFoldDB; J2ZVB6; -.
DR   PATRIC; fig|1210908.3.peg.4465; -.
DR   eggNOG; arCOG01981; Archaea.
DR   OrthoDB; 7429at2157; -.
DR   Proteomes; UP000007813; 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   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:EJN56978.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00383};
KW   Protein biosynthesis {ECO:0000313|EMBL:EJN56978.1};
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          22..52
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51134"
FT   REPEAT          138..221
FT                   /note="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REPEAT          232..313
FT                   /note="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
FT   BINDING         29
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"
FT   BINDING         47
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00383"
SQ   SEQUENCE   319 AA;  35553 MW;  C8264CE40474F92A CRC64;
     MTETTTEIGI ERTSEKEAPT KSLRTCPECD GKIVQDSEHG ESSCEECGLV VDEMQVDRGP
     EWQAYNADDR SEKSRVGAPT TQLMHDKGLS TTIGWKNTDG YGKTIPDRKR ARLQRLRTWD
     ERFRTKDAHE RNLKQALTEI RRMASALGLP EPPRETAGIL YRRAVKDNLL PGRSIEGMAT
     ACLYAATRQH GSPRTLTTFA DVSRVKRLRI QRAYNYLSRE LGLQIEPENP SKYVPQFASS
     LDVSKEATRE AHELLEVATA NGIHSGKSPA GLAAAALYAA SHLTNEGLTQ KEVSNEAHVS
     RVTIRNRYQE LLEVYGAQG
//
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