位置:首页 > 蛋白库 > TF2B_PYRFU
TF2B_PYRFU
ID   TF2B_PYRFU              Reviewed;         300 AA.
AC   P61998; P29095; Q51731;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Transcription initiation factor IIB {ECO:0000255|HAMAP-Rule:MF_00383};
DE            Short=TFIIB {ECO:0000255|HAMAP-Rule:MF_00383};
GN   Name=tfb {ECO:0000255|HAMAP-Rule:MF_00383}; OrderedLocusNames=PF1377;
OS   Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=186497;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zeng Q., Lewis L.M., Colangelo C.M., Dong J., Scott R.A.;
RT   "A transcription factor (TFIIB) homolog from the hyperthermophilic archaeon
RT   Pyrococcus furiosus binds Zn or Fe in an N-terminal Cys4 motif.";
RL   J. Biol. Inorg. Chem. 1:162-168(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX   PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA   Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA   DiRuggiero J., Robb F.T.;
RT   "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT   horikoshii inferred from complete genomic sequences.";
RL   Genetics 152:1299-1305(1999).
RN   [3]
RP   STRUCTURE BY NMR OF 1-50.
RX   PubMed=8564536; DOI=10.1038/nsb0296-122;
RA   Zhu W., Zeng Q., Colangelo C.M., Lewis L.M., Summers M.F., Scott R.A.;
RT   "The N-terminal domain of TFIIB from Pyrococcus furiosus forms a zinc
RT   ribbon.";
RL   Nat. Struct. Biol. 3:122-124(1996).
CC   -!- FUNCTION: Stabilizes TBP binding to an archaeal box-A promoter. Also
CC       responsible for recruiting RNA polymerase II to the pre-initiation
CC       complex (DNA-TBP-TFIIB).
CC   -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00383}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U48391; AAC43724.1; -; Genomic_DNA.
DR   EMBL; AE009950; AAL81501.1; -; Genomic_DNA.
DR   PIR; T46883; T46883.
DR   RefSeq; WP_011012524.1; NC_018092.1.
DR   PDB; 1PFT; NMR; -; A=1-49.
DR   PDBsum; 1PFT; -.
DR   AlphaFoldDB; P61998; -.
DR   SMR; P61998; -.
DR   MINT; P61998; -.
DR   STRING; 186497.PF1377; -.
DR   EnsemblBacteria; AAL81501; AAL81501; PF1377.
DR   GeneID; 41713185; -.
DR   KEGG; pfu:PF1377; -.
DR   PATRIC; fig|186497.12.peg.1440; -.
DR   eggNOG; arCOG01981; Archaea.
DR   HOGENOM; CLU_043736_0_1_2; -.
DR   OMA; RTQKDFA; -.
DR   OrthoDB; 35979at2157; -.
DR   PhylomeDB; P61998; -.
DR   EvolutionaryTrace; P61998; -.
DR   Proteomes; UP000001013; Chromosome.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0017025; F:TBP-class protein binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0070897; P:transcription preinitiation complex assembly; IEA:InterPro.
DR   CDD; cd00043; CYCLIN; 2.
DR   HAMAP; MF_00383; TF2B_arch; 1.
DR   InterPro; IPR013763; Cyclin-like.
DR   InterPro; IPR036915; Cyclin-like_sf.
DR   InterPro; IPR000812; TFIIB.
DR   InterPro; IPR023484; TFIIB_arc.
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   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..300
FT                   /note="Transcription initiation factor IIB"
FT                   /id="PRO_0000119327"
FT   REPEAT          114..197
FT                   /note="1"
FT   REPEAT          210..291
FT                   /note="2"
FT   ZN_FING         2..34
FT                   /note="TFIIB-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
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         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00469"
FT   TURN            8..10
FT                   /evidence="ECO:0007829|PDB:1PFT"
FT   STRAND          15..18
FT                   /evidence="ECO:0007829|PDB:1PFT"
FT   TURN            19..22
FT                   /evidence="ECO:0007829|PDB:1PFT"
FT   STRAND          23..29
FT                   /evidence="ECO:0007829|PDB:1PFT"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:1PFT"
SQ   SEQUENCE   300 AA;  34106 MW;  476D7CA32B2ED4C1 CRC64;
     MNKQKVCPAC ESAELIYDPE RGEIVCAKCG YVIEENIIDM GPEWRAFDAS QRERRSRTGA
     PESILLHDKG LSTEIGIDRS LSGLMREKMY RLRKWQSRLR VSDAAERNLA FALSELDRIT
     AQLKLPRHVE EEAARLYREA VRKGLIRGRS IESVMAACVY AACRLLKVPR TLDEIADIAR
     VDKKEIGRSY RFIARNLNLT PKKLFVKPTD YVNKFADELG LSEKVRRRAI EILDEAYKRG
     LTSGKSPAGL VAAALYIASL LEGEKRTQRE VAEVARVTEV TVRNRYKELV EKLKIKVPIA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024