TF2B_ENCCU
ID TF2B_ENCCU Reviewed; 312 AA.
AC Q8SRP3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Transcription initiation factor IIB;
DE AltName: Full=General transcription factor TFIIB;
GN OrderedLocusNames=ECU06_1100i;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- FUNCTION: General factor that plays a major role in the activation of
CC eukaryotic genes transcribed by RNA polymerase II. {ECO:0000250}.
CC -!- SUBUNIT: Associates with TFIID-IIA (DA complex) to form TFIID-IIA-IIB
CC (DAB-complex) which is then recognized by polymerase II.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; AL590446; CAD25470.1; -; Genomic_DNA.
DR RefSeq; NP_585866.1; NM_001041488.1.
DR AlphaFoldDB; Q8SRP3; -.
DR SMR; Q8SRP3; -.
DR STRING; 284813.Q8SRP3; -.
DR PRIDE; Q8SRP3; -.
DR GeneID; 859291; -.
DR KEGG; ecu:ECU06_1100i; -.
DR VEuPathDB; MicrosporidiaDB:ECU06_1100i; -.
DR HOGENOM; CLU_043736_1_1_1; -.
DR InParanoid; Q8SRP3; -.
DR OMA; RTQKDFA; -.
DR OrthoDB; 729732at2759; -.
DR Proteomes; UP000000819; Chromosome VI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
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; 1.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 3: Inferred from homology;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..312
FT /note="Transcription initiation factor IIB"
FT /id="PRO_0000119305"
FT REPEAT 120..196
FT /note="1"
FT REPEAT 213..290
FT /note="2"
FT ZN_FING 10..42
FT /note="TFIIB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT BINDING 17
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 312 AA; 35165 MW; E1577DCD36EC987C CRC64;
MKTLPKFKPF VQTCSDCGET QNIVEDYKNG YHVCGRCGCI VGNRIIDEGS EWRSFGDSNK
VDPCRIGSAS NPYLESEQLD TMISTGGGMN SYVLSKIQMK NSMRGPERAL KHGMNLITAF
CERSNLSRTI IDRAHYIFKN IEERKLLKGK NVEGIVAACI YIACRQEECP RTFKEISVMT
AVQKREIGRC FKLISPHLER MATMSTENII ARFCSDLNLN IKIQKIATEI AKAAHELGCL
AGKSPDSIAA AVIYMVTNLF PEEKKIQKDI QFVTNVTEVT IKNTYKELLT FKYDIIPENM
VNKESIDKLP GY