ID Q7SX98_DANRE Unreviewed; 316 AA.
AC Q7SX98;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE RecName: Full=Transcription initiation factor IIB {ECO:0000256|ARBA:ARBA00013932};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
DE AltName: Full=General transcription factor TFIIB {ECO:0000256|ARBA:ARBA00031706};
GN Name=gtf2b {ECO:0000313|EMBL:AAH55569.1,
GN ECO:0000313|ZFIN:ZDB-GENE-030131-3544};
GN Synonyms=wu:fc44c11 {ECO:0000313|RefSeq:NP_955991.1}, zgc:66258
GN {ECO:0000313|RefSeq:NP_955991.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAH55569.1};
RN [1] {ECO:0000313|EMBL:AAH55569.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:AAH55569.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:NP_955991.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20047469;
RA Anelli V., Santoriello C., Distel M., Koster R.W., Ciccarelli F.D.,
RA Mione M.;
RT "Global repression of cancer gene expression in a zebrafish model of
RT melanoma is linked to epigenetic regulation.";
RL Zebrafish 6:417-424(2009).
RN [3] {ECO:0000313|RefSeq:NP_955991.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24156918;
RA Gu Q., Yang X., He X., Li Q., Cui Z.;
RT "Generation and characterization of a transgenic zebrafish expressing the
RT reverse tetracycline transactivator.";
RL J. Genet. Genomics 40:523-531(2013).
RN [4] {ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [5] {ECO:0000313|RefSeq:NP_955991.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000780};
CC -!- SIMILARITY: Belongs to the TFIIB family.
CC {ECO:0000256|ARBA:ARBA00010857}.
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DR EMBL; BC055569; AAH55569.1; -; mRNA.
DR RefSeq; NP_955991.1; NM_199697.1.
DR GeneID; 324823; -.
DR KEGG; dre:324823; -.
DR AGR; ZFIN:ZDB-GENE-030131-3544; -.
DR CTD; 2959; -.
DR ZFIN; ZDB-GENE-030131-3544; gtf2b.
DR OrthoDB; 38673at2759; -.
DR PhylomeDB; Q7SX98; -.
DR Proteomes; UP000000437; Chromosome 2.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097550; C:transcription preinitiation complex; IBA:GO_Central.
DR GO; GO:0016407; F:acetyltransferase activity; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:1990114; P:RNA polymerase II core complex assembly; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IBA:GO_Central.
DR CDD; cd20551; CYCLIN_TFIIB_rpt1; 1.
DR CDD; cd20552; CYCLIN_TFIIB_rpt2; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR InterPro; IPR013763; Cyclin-like_dom.
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:SF13; TRANSCRIPTION INITIATION FACTOR IIB; 1.
DR PANTHER; PTHR11618; TRANSCRIPTION INITIATION FACTOR IIB-RELATED; 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; Cyclin-like; 2.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS00782; TFIIB; 2.
DR PROSITE; PS51134; ZF_TFIIB; 1.
PE 1: Evidence at protein level;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Cyclin {ECO:0000256|ARBA:ARBA00023127};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00469};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q7SX98};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00023315};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00469};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00469}.
FT DOMAIN 11..42
FT /note="TFIIB-type"
FT /evidence="ECO:0000259|PROSITE:PS51134"
SQ SEQUENCE 316 AA; 34836 MW; 589958282C810BDB CRC64;
MASTSRGDSL PKVQCPNHPD ALLVEDYRAG DMICPECGLV VRDRVIDVGS EWRTFSNEKA
TKDPSRVGDA QNPLLNGGDL TTMISKGTGA ASFDEFGNSK YQNRRTMSSS DRAMLNAFKE
ITTMADRINL PRNIIDRTNN LFKQVYEQKS LKGRSNDAIA SACLYIACRQ EGVPRTFKEI
CAVSRISKKE IGRCFKLILK ALETSVDLIT TGDFMSRFCS NLGLPKQVQM AATYIARKAV
ELDLVPGRSP ISVAAAAIYM ASQASAEKKT QKEIGDIAGV ADVTIRQSYR LIYPRAADLF
PPDFKFDTPV DKLPQL
//
