ID   TF2B2_HALVD             Reviewed;         332 AA.
AC   Q9YGA5; D4GZP0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Transcription initiation factor IIB 2 {ECO:0000255|HAMAP-Rule:MF_00383};
DE            Short=TFIIB 2 {ECO:0000255|HAMAP-Rule:MF_00383};
GN   Name=tfb2 {ECO:0000255|HAMAP-Rule:MF_00383}; Synonyms=tfb9;
GN   OrderedLocusNames=HVO_1676;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=10476041; DOI=10.1046/j.1365-2958.1999.01551.x;
RA   Thompson D.K., Palmer J.R., Daniels C.J.;
RT   "Expression and heat-responsive regulation of a TFIIB homologue from the
RT   archaeon Haloferax volcanii.";
RL   Mol. Microbiol. 33:1081-1092(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
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:0000255|HAMAP-Rule:MF_00383}.
CC   -!- INDUCTION: By heat shock (60 degrees Celsius), with a 2-fold increase
CC       (at protein level). {ECO:0000269|PubMed:10476041}.
CC   -!- MISCELLANEOUS: There are 6-12 TFIIB paralogs in this organism.
CC   -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00383}.
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DR   EMBL; AF143693; AAD43074.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE05068.1; -; Genomic_DNA.
DR   PIR; T44261; T44261.
DR   RefSeq; WP_004041566.1; NZ_AOHU01000029.1.
DR   AlphaFoldDB; Q9YGA5; -.
DR   SMR; Q9YGA5; -.
DR   STRING; 309800.C498_03735; -.
DR   EnsemblBacteria; ADE05068; ADE05068; HVO_1676.
DR   GeneID; 8924391; -.
DR   KEGG; hvo:HVO_1676; -.
DR   eggNOG; arCOG01981; Archaea.
DR   HOGENOM; CLU_043736_0_0_2; -.
DR   OMA; TKMMHDK; -.
DR   OrthoDB; 35979at2157; -.
DR   Proteomes; UP000008243; Chromosome.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd00043; CYCLIN; 1.
DR   HAMAP; MF_00383; TF2B_arch; 1.
DR   InterPro; IPR013763; Cyclin-like.
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; PTHR11618; 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; SSF47954; 2.
DR   PROSITE; PS00782; TFIIB; 2.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..332
FT                   /note="Transcription initiation factor IIB 2"
FT                   /id="PRO_0000119319"
FT   REPEAT          149..232
FT                   /note="1"
FT   REPEAT          243..324
FT                   /note="2"
FT   ZN_FING         33..63
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ   SEQUENCE   332 AA;  37282 MW;  BAA4118B60EF3323 CRC64;
     MSDTITTRTY SADAKSRDVR PRESERDETQ QDETQVCPEC SGHLVTDEEH GETICEDCGL
     VVEDTVVDRG PEWRAFDSAE RDSKSRVGAP TTKMMHDKGL STNIGWQNKD AYGKSLSPRQ
     REQMQRLRTW NERFRTRDSK ERNLKQALGE IDRMASALGL PENVRETASV IYRRALNDDL
     LPGRSIEGVA TSALYASARM AGTPRSLDEL EKVSRVDKME LTRTYRYIVR ELKLEIKPAD
     PEQYVPRFAS ELGLSDEAER QARQLLRDAK ETGIHSGKSP VGLAAAAVYA AALLTNEKVT
     QSEVSTVADI SEVTIRNRYK ELLEVQDGTL LA