TF2B_DROME
ID TF2B_DROME Reviewed; 315 AA.
AC P29052; Q6AWH9; Q9VKV7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Transcription initiation factor IIB;
DE AltName: Full=General transcription factor TFIIB;
GN Name=TfIIB; ORFNames=CG5193;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1557390; DOI=10.1073/pnas.89.7.2839;
RA Yamashita S., Wada K., Horikoshi M., Gong D.W., Kokubo T., Hisatake K.,
RA Yokotani N., Malik S., Roeder R.G., Nakatani Y.;
RT "Isolation and characterization of a cDNA encoding Drosophila transcription
RT factor TFIIB.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2839-2843(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1644295; DOI=10.1101/gad.6.8.1542;
RA Wampler S.L., Kadonaga J.T.;
RT "Functional analysis of Drosophila transcription factor IIB.";
RL Genes Dev. 6:1542-1552(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RA Lira-Devito L.M., Kadonaga J.T.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R;
RA Yoon J., Oh Y., Lee K., Baek K.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: General factor that plays a major role in the activation of
CC eukaryotic genes transcribed by RNA polymerase II.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (Tafs). Associates
CC with TFIID-IIA (DA complex) to form TFIID-IIA-IIB (DAB-complex) which
CC is then recognized by polymerase II.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}.
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DR EMBL; M88164; AAA28930.1; -; mRNA.
DR EMBL; M91081; AAA28929.1; -; mRNA.
DR EMBL; U02879; AAA68626.1; -; Genomic_DNA.
DR EMBL; U35148; AAA79093.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52951.1; -; Genomic_DNA.
DR EMBL; BT011459; AAR99117.1; -; mRNA.
DR EMBL; BT015269; AAT94498.1; -; mRNA.
DR PIR; A42695; A42695.
DR RefSeq; NP_001260349.1; NM_001273420.1.
DR RefSeq; NP_476888.1; NM_057540.4.
DR AlphaFoldDB; P29052; -.
DR SMR; P29052; -.
DR BioGRID; 60511; 16.
DR DIP; DIP-17603N; -.
DR IntAct; P29052; 3.
DR STRING; 7227.FBpp0305673; -.
DR PaxDb; P29052; -.
DR PRIDE; P29052; -.
DR DNASU; 34430; -.
DR EnsemblMetazoa; FBtr0080025; FBpp0079615; FBgn0004915.
DR EnsemblMetazoa; FBtr0333489; FBpp0305673; FBgn0004915.
DR GeneID; 34430; -.
DR KEGG; dme:Dmel_CG5193; -.
DR CTD; 34430; -.
DR FlyBase; FBgn0004915; TfIIB.
DR VEuPathDB; VectorBase:FBgn0004915; -.
DR eggNOG; KOG1597; Eukaryota.
DR GeneTree; ENSGT00390000006671; -.
DR HOGENOM; CLU_043736_1_1_1; -.
DR InParanoid; P29052; -.
DR OMA; DHDQRMK; -.
DR OrthoDB; 729732at2759; -.
DR PhylomeDB; P29052; -.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; P29052; -.
DR BioGRID-ORCS; 34430; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 34430; -.
DR PRO; PR:P29052; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0004915; Expressed in cleaving embryo and 35 other tissues.
DR ExpressionAtlas; P29052; baseline and differential.
DR Genevisible; P29052; DM.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0017025; F:TBP-class protein binding; IPI:FlyBase.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IBA:GO_Central.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0051101; P:regulation of DNA binding; IDA:FlyBase.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
DR GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IDA:FlyBase.
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 Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..315
FT /note="Transcription initiation factor IIB"
FT /id="PRO_0000119299"
FT REPEAT 123..199
FT /note="1"
FT REPEAT 217..293
FT /note="2"
FT ZN_FING 10..41
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 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"
SQ SEQUENCE 315 AA; 34369 MW; AA5803F7B94BB1F4 CRC64;
MASTSRLDNN KVCCYAHPES PLIEDYRAGD MICSECGLVV GDRVIDVGSE WRTFSNEKSG
VDPSRVGGPE NPLLSGGDLS TIIGPGTGSA SFDAFGAPKY QNRRTMSSSD RSLISAFKEI
SSMADRINLP KTIVDRANNL FKQVHDGKNL KGRSNDAKAS ACLYIACRQE GVPRTFKEIC
AVSKISKKEI GRCFKLTLKA LETSVDLITT ADFMCRFCAN LDLPNMVQRA ATHIAKKAVE
MDIVPGRSPI SVAAAAIYMA SQASEHKRSQ KEIGDIAGVA DVTIRQSYKL MYPHAAKLFP
EDFKFTTPID QLPQM
