TF2B_XENLA
ID TF2B_XENLA Reviewed; 316 AA.
AC P29054; Q6AZP6;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Transcription initiation factor IIB {ECO:0000250|UniProtKB:Q00403};
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q00403};
DE AltName: Full=General transcription factor TFIIB {ECO:0000250|UniProtKB:Q00403};
GN Name=gtf2b {ECO:0000250|UniProtKB:Q00403};
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 [MRNA].
RX PubMed=1840674; DOI=10.1093/nar/19.23.6639;
RA Hisatake K., Malik S., Roeder R.G., Horikoshi M.;
RT "Conserved structural motifs between Xenopus and human TFIIB.";
RL Nucleic Acids Res. 19:6639-6639(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: General transcription factor that plays a role in
CC transcription initiation by RNA polymerase II (Pol II). Involved in the
CC pre-initiation complex (PIC) formation and Pol II recruitment at
CC promoter DNA. Together with the TATA box-bound TBP forms the core
CC initiation complex and provides a bridge between TBP and the Pol II-
CC TFIIF complex. Released from the PIC early following the onset of
CC transcription during the initiation and elongation transition and
CC reassociates with TBP during the next transcription cycle. Associates
CC with chromatin to core promoter-specific regions. Binds to two distinct
CC DNA core promoter consensus sequence elements in a TBP-independent
CC manner; these IIB-recognition elements (BREs) are localized immediately
CC upstream (BREu), 5'-[GC][GC][GA]CGCC-3', and downstream (BREd), 5'-
CC [GA]T[TGA][TG][GT][TG][TG]-3', of the TATA box element. Modulates
CC transcription start site selection. Exhibits also autoacetyltransferase
CC activity that contributes to the activated transcription.
CC {ECO:0000250|UniProtKB:Q00403}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q00403};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00403}.
CC Chromosome {ECO:0000250|UniProtKB:Q00403}. Note=Non-acetylated form
CC colocalizes with DNA in the G0/1, S and G2 phases of the cell cycle,
CC but not during mitosis. Acetylated form colocalizes at
CC transcriptionally silent mitotic chromatids during mitosis at
CC metaphase, anaphase, and telophase phases of the cell cycle.
CC {ECO:0000250|UniProtKB:Q00403}.
CC -!- DOMAIN: The zinc-binding domain is necessary for the interaction and
CC recruitment of RNA polymerase II to the core promoter, the formation of
CC a fully competent pre-initiation complex (PIC) assembly and basal
CC transcription initiation. The C-terminus is necessary and sufficient
CC for interaction with the TATA box-bound TBP complex and for the
CC formation of PIC. {ECO:0000250|UniProtKB:Q00403}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; X62868; CAA44668.1; -; mRNA.
DR EMBL; BC077495; AAH77495.1; -; mRNA.
DR PIR; S20071; S20071.
DR RefSeq; NP_001081115.1; NM_001087646.1.
DR AlphaFoldDB; P29054; -.
DR SMR; P29054; -.
DR MaxQB; P29054; -.
DR PRIDE; P29054; -.
DR GeneID; 394390; -.
DR KEGG; xla:394390; -.
DR CTD; 394390; -.
DR Xenbase; XB-GENE-6254425; gtf2b.L.
DR OMA; DHDQRMK; -.
DR OrthoDB; 729732at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 394390; Expressed in ovary and 19 other tissues.
DR GO; GO:0005694; C:chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
DR GO; GO:1990114; P:RNA polymerase II core complex assembly; ISS:UniProtKB.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0019083; P:viral transcription; ISS:UniProtKB.
DR CDD; cd00043; CYCLIN; 2.
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 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 2: Evidence at transcript level;
KW Acyltransferase; Chromosome; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..316
FT /note="Transcription initiation factor IIB"
FT /id="PRO_0000119297"
FT REPEAT 124..200
FT /note="1"
FT REPEAT 218..294
FT /note="2"
FT ZN_FING 11..42
FT /note="TFIIB-type"
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 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
SQ SEQUENCE 316 AA; 34678 MW; A1C6837888865B00 CRC64;
MASTSRIDAL PKVTCPNHPD ALLVEDYRAG DMICSECGLV VGDRVIDVGS EWRTFSNDKA
AADPSRVGDA QNPLLSGGDL TTMIGKGTGS ASFDEFGNSK YQNRRTMSSS DRAMMNAFKE
ITNMSDRINL PRNIIDRTNN LFKQVYEQKS LKGRSNDAIA SACLYIACRQ EGVPRTFKEI
CAVSRISKKE IGRCFKLILK ALETNVDLIT TGDFMSRFCS NLGLTKQVQM AATHIARKAV
ELDLVPGRSP ISVAAAAIYM ASQASAEKRT QKEIGDIAGV ADVTIRQSYR LIYPRAPDLF
PADFKFDTPV DKLPQL
