ID   BRF2_XENTR              Reviewed;         519 AA.
AC   A4QNR3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) 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}.
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DR   EMBL; BC136234; AAI36235.1; -; mRNA.
DR   RefSeq; NP_001096549.1; NM_001103079.1.
DR   AlphaFoldDB; A4QNR3; -.
DR   SMR; A4QNR3; -.
DR   STRING; 8364.ENSXETP00000060533; -.
DR   PaxDb; A4QNR3; -.
DR   DNASU; 100125194; -.
DR   GeneID; 100125194; -.
DR   KEGG; xtr:100125194; -.
DR   CTD; 55290; -.
DR   Xenbase; XB-GENE-964408; brf2.
DR   eggNOG; KOG1598; Eukaryota.
DR   InParanoid; A4QNR3; -.
DR   OrthoDB; 1518547at2759; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000126; C:transcription factor TFIIIB complex; ISS:UniProtKB.
DR   GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
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:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
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; IPR013150; TFIIB_cyclin.
DR   InterPro; IPR013137; Znf_TFIIB.
DR   PANTHER; PTHR11618; PTHR11618; 1.
DR   Pfam; PF00382; TFIIB; 1.
DR   SUPFAM; SSF47954; SSF47954; 1.
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..519
FT                   /note="Transcription factor IIIB 50 kDa subunit"
FT                   /id="PRO_0000337193"
FT   REPEAT          173..249
FT                   /note="2"
FT   ZN_FING         3..36
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   REGION          465..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         462
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HAW0"
SQ   SEQUENCE   519 AA;  57126 MW;  55564CD7F1E36AF6 CRC64;
     MSGAKQCPDC GSSDIVEDAH YSQDQVVCAD CGCILSEGLI TTTAAEESHL QAVRFADSTG
     ENDSMTVSKL RGIVRVRNIC RVLRLPDGFS DTAVSYYEQA YKHPLYHSVS IEKKEIIVGC
     CVYITCRQHQ WPITMATICS LVYAKKELFA SIFLSIVQVL KLDVPSVSLQ NLVMSHCRSF
     KLFKDSCEVP SHYAEKLDTV SERTVQTVEL AYETWLVTGR HPIPIITAAA YISWQSLLPA
     RRLSCSLSRF CKLSDVDLPP PSAIRLRELQ GTLIKLSVYL PWLKVLSLNK KTVVQHLGDL
     LRHRVFLLRK ALAVTEAELS RGTLADTEAQ LSRGTLADTE AQLSRGTLAD TEAQLSRGTL
     ADTEAQLSRG TLADTEAQLS RGTLADTEAQ LSRGTLADTE AQLSRGTLAD TEAQLSRGTL
     ADTVAQLSRG TLADTEAQLS RGTKALSSND QPNSTFVFLP PCVSNPRKRS RSIPFPRGHL
     DITGDEDISD SEIEQYLRTP AEMKEFEQAL NRDDELPNA