TF3B_KLULA
ID TF3B_KLULA Reviewed; 556 AA.
AC P46070; Q6CXU9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Transcription factor IIIB 70 kDa subunit;
DE Short=TFIIIB;
DE AltName: Full=B-related factor 1;
DE Short=BRF-1;
GN Name=TDS4; Synonyms=BRF1; OrderedLocusNames=KLLA0A05434g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7995525; DOI=10.1101/gad.8.23.2879;
RA Khoo B., Brophy B., Jackson S.P.;
RT "Conserved functional domains of the RNA polymerase III general
RT transcription factor BRF.";
RL Genes Dev. 8:2879-2890(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: General activator of RNA polymerase III transcription.
CC Interacts with TBP. Binds to Pol III subunit C34 and to the TAU135
CC component of TFIIIC.
CC -!- SUBUNIT: TFIIIB comprises the TATA-binding protein (TBP), the B-related
CC factor (BRF) and a 70 kDa polypeptide.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; Z47203; CAA87399.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH02828.1; -; Genomic_DNA.
DR PIR; A55483; A55483.
DR RefSeq; XP_451240.1; XM_451240.1.
DR AlphaFoldDB; P46070; -.
DR SMR; P46070; -.
DR STRING; 28985.XP_451240.1; -.
DR EnsemblFungi; CAH02828; CAH02828; KLLA0_A05434g.
DR GeneID; 2896820; -.
DR KEGG; kla:KLLA0_A05434g; -.
DR eggNOG; KOG1598; Eukaryota.
DR HOGENOM; CLU_010293_3_3_1; -.
DR InParanoid; P46070; -.
DR OMA; AEPPCKV; -.
DR Proteomes; UP000000598; Chromosome A.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000126; C:transcription factor TFIIIB complex; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000994; F:RNA polymerase III core binding; IEA:EnsemblFungi.
DR GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IEA:InterPro.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:EnsemblFungi.
DR GO; GO:0001156; F:TFIIIC-class transcription factor complex binding; IEA:EnsemblFungi.
DR GO; GO:0001112; P:DNA-templated transcription open complex formation; IEA:EnsemblFungi.
DR GO; GO:0006359; P:regulation of transcription by RNA polymerase III; IEA:EnsemblFungi.
DR GO; GO:0070898; P:RNA polymerase III preinitiation complex assembly; IEA:EnsemblFungi.
DR GO; GO:0070893; P:transposon integration; IEA:EnsemblFungi.
DR CDD; cd00043; CYCLIN; 2.
DR InterPro; IPR029529; Brf1.
DR InterPro; IPR011665; BRF1_TBP-bd_dom.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR000812; TFIIB.
DR InterPro; IPR023486; TFIIB_CS.
DR InterPro; IPR013150; TFIIB_cyclin.
DR InterPro; IPR013137; Znf_TFIIB.
DR PANTHER; PTHR11618; PTHR11618; 1.
DR PANTHER; PTHR11618:SF4; PTHR11618:SF4; 1.
DR Pfam; PF07741; BRF1; 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 Activator; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..556
FT /note="Transcription factor IIIB 70 kDa subunit"
FT /id="PRO_0000119344"
FT REPEAT 98..174
FT /note="1"
FT REPEAT 193..272
FT /note="2"
FT ZN_FING 8..41
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT REGION 98..272
FT /note="Interaction with TBP and with the Pol III subunit
FT C34"
FT REGION 284..556
FT /note="Interaction with TBP"
FT REGION 287..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT CONFLICT 49..50
FT /note="VT -> LA (in Ref. 1; CAA87399)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="R -> H (in Ref. 1; CAA87399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 62284 MW; BF5FF4B516D27A3D CRC64;
MASTLQVSSR KCKNCGSTDF VRDISNTTNE LICKVCGLVT EENSIVSEVT FGEASNGAAV
IQGAFVSANQ AHPTFMSHSG QNALMSRETT LNNARRKLKA VSYALNIPEY VTDAAFQWYR
LALSNNFVQG RKSQNVIAAC LYIACRKERT HHMLIDFSSR LQVSVYSIGA TFLKLAKKLQ
IVKLPLADPS LFIQHFAEKL ELGDKKIKVI RDAVKLAQTM SRDWMYEGRR PAGIAGACLL
LACRMNNLRR THSEIVAISH VAEETLQQRL NEFKNTTSAK LSVKEFRDDE TEVNEGERSA
ESKPPSFDKN RLKEKKIKDS LDTKEMLETS EEAVSRNPIL TQVLGAQELS SKEVLYYLKK
LSERRKAEFS RIKATHGIDG EDLHKTEKDK KRSLDEIDGY SLEKDPYRPR NLHLLPTTAS
LLSKVSDHPE NLDDVDDAEL DSHLLDEEAS KLKERIWIDI NGDYLIEQES KRLKQEADLA
SGNTSLRKKR SKRTNRNQSS ASIVKVQVDG LPLDVSVDDA DAVDVVAAGG VKNLLQKTTF
SKKINYDAIN GLFGQK
