ID   BRF2_XENLA              Reviewed;         396 AA.
AC   Q66IW8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Transcription factor IIIB 50 kDa subunit;
DE   AltName: Full=B-related factor 2;
DE            Short=BRF-2;
GN   Name=brf2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: General activator of RNA polymerase III transcription. Factor
CC       exclusively required for RNA polymerase III transcription of genes with
CC       promoter elements upstream of the initiation sites. Contributes to the
CC       regulation of gene expression; functions as activator in the absence of
CC       oxidative stress. Down-regulates expression of target genes in response
CC       to oxidative stress. Overexpression protects cells against apoptosis in
CC       response to oxidative stress. {ECO:0000250|UniProtKB:Q9HAW0}.
CC   -!- SUBUNIT: Component of TFIIIB complexes. Interacts with TBP and forms a
CC       ternary complex with TBp and target DNA sequences.
CC       {ECO:0000250|UniProtKB:Q9HAW0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAW0}.
CC   -!- PTM: In response to oxidative stress, a Cys-residue is reversibly
CC       oxidized to cysteine sulfenic acid. This impairs formation of a ternary
CC       complex with TBP and DNA and down-regulates expression of target genes
CC       in response to oxidative stress. {ECO:0000250|UniProtKB:Q9HAW0}.
CC   -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC081158; AAH81158.1; -; mRNA.
DR   RefSeq; NP_001087739.1; NM_001094270.1.
DR   AlphaFoldDB; Q66IW8; -.
DR   SMR; Q66IW8; -.
DR   DNASU; 447563; -.
DR   GeneID; 447563; -.
DR   KEGG; xla:447563; -.
DR   CTD; 447563; -.
DR   Xenbase; XB-GENE-964413; brf2.S.
DR   OrthoDB; 1518547at2759; -.
DR   Proteomes; UP000186698; Chromosome 3S.
DR   Bgee; 447563; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000126; C:transcription factor TFIIIB complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001006; F:RNA polymerase III type 3 promoter sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0006359; P:regulation of transcription by RNA polymerase III; ISS:UniProtKB.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR000812; TFIIB.
DR   InterPro; IPR013137; Znf_TFIIB.
DR   PANTHER; PTHR11618; PTHR11618; 1.
DR   Pfam; PF08271; TF_Zn_Ribbon; 1.
DR   SUPFAM; SSF47954; SSF47954; 2.
DR   PROSITE; PS51134; ZF_TFIIB; 1.
PE   2: Evidence at transcript level;
KW   Activator; Metal-binding; Nucleus; Oxidation; Reference proteome; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..396
FT                   /note="Transcription factor IIIB 50 kDa subunit"
FT                   /id="PRO_0000337192"
FT   REPEAT          173..249
FT                   /note="2"
FT   ZN_FING         3..36
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         10
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         31
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   MOD_RES         342
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HAW0"
SQ   SEQUENCE   396 AA;  44430 MW;  D0473E8FA1E020CA CRC64;
     MSGAKRCPDC GSSEIVEDAH YSQDQLVCAD CGCILSEGLI TTTVSEETSL QAVRYSDSTG
     ENDSVTYCMK RGIIRVRDLC RVLRLPDGFV DTALSYYKQA VGLPLYRLVS IEKKEIIVGC
     CVYITCRQQQ WPITMGTICS LIYAKKELFA SLFMDIVQVL KVDVPSISLQ NLVKSHCRSF
     KLFKDSSEVP PQYAEKLDTV SERTVQTVEL AYETWLVTGR HPIPMITAAA YISWQSFQPS
     RRLSCSLSRF CKLSDVDMPP PSTIRLKELQ ETLIKLAYHL PWLKILSLNR KNIVQHLGDL
     LKHRALLLRR ALAVTEAELS KGTEASSSTD QLNSTLVFLP PCVSNPKKRS RSIAFPCGDL
     DITGDEEISD SEIEQYLRTP AEMKDYQQVQ SCISSV