ID   TF2B3_HALSA             Reviewed;         317 AA.
AC   Q9HHK5;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Transcription initiation factor IIB 3 {ECO:0000255|HAMAP-Rule:MF_00383};
DE            Short=TFIIB 3 {ECO:0000255|HAMAP-Rule:MF_00383};
GN   Name=tfbC {ECO:0000255|HAMAP-Rule:MF_00383}; OrderedLocusNames=VNG_6351G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OG   Plasmid pNRC200.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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   -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00383}.
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DR   EMBL; AE004438; AAG20975.1; -; Genomic_DNA.
DR   RefSeq; WP_010904186.1; NZ_BK010831.1.
DR   AlphaFoldDB; Q9HHK5; -.
DR   SMR; Q9HHK5; -.
DR   EnsemblBacteria; AAG20975; AAG20975; VNG_6351G.
DR   GeneID; 5955012; -.
DR   KEGG; hal:VNG_6351G; -.
DR   PATRIC; fig|64091.14.peg.2315; -.
DR   HOGENOM; CLU_043736_0_0_2; -.
DR   InParanoid; Q9HHK5; -.
DR   OMA; ISHHYID; -.
DR   OrthoDB; 35979at2157; -.
DR   PhylomeDB; Q9HHK5; -.
DR   Proteomes; UP000000554; Plasmid pNRC200.
DR   GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
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:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd00043; CYCLIN; 2.
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   3: Inferred from homology;
KW   Metal-binding; Plasmid; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..317
FT                   /note="Transcription initiation factor IIB 3"
FT                   /id="PRO_0000119313"
FT   REPEAT          136..219
FT                   /note="1"
FT   REPEAT          230..311
FT                   /note="2"
FT   ZN_FING         21..50
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          62..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         28
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         42
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ   SEQUENCE   317 AA;  35904 MW;  40DB6D6E8F8C9B86 CRC64;
     MERATREREK EQREQAQTND EAQQCPECNS ANVITDQSER VCEDCGLVLE DDQIDHGPEW
     RAFNSSERDQ KSRVGAPTTK TMHDKGLTTQ IDWKDKDAYG RSLDAKKRNQ MNRLRKWQER
     IRTKDAGERN LQFALSEIDR MASALGVPRS VREVASVIYR RALKEDLIRG RSIEGVATAC
     LYAACRQEGI PRTLEEVTEV ARIDQKEIGR TYRYVAQELS LEIQPTDPKE YLPRFASDLE
     LSEEVIAKAR EIIDTSAEQG LLSGKSPSGF AAAAIYAASL LCNEKKTQRE VANVANVTEV
     TIRNRYQEQI EAMGFGV