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Search results 1 to 74 out of 74 for Rbfa

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Hits by Strain

Type Details Score
Gene
79863 | RBFA
Type: gene
Organism: human
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Gene
733470 | rbfa
Type: gene
Organism: frog, western clawed
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Gene
606936 | RBFA
Type: gene
Organism: dog, domestic
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Gene
468594 | RBFA
Type: gene
Organism: chimpanzee
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Gene
307235 | Rbfa
Type: gene
Organism: rat
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Gene
510927 | RBFA
Type: gene
Organism: cattle
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Gene
420806 | RBFA
Type: gene
Organism: chicken
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Gene
100037330 | rbfa
Type: gene
Organism: zebrafish
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Gene
699220 | RBFA
Type: gene
Organism: macaque, rhesus
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Protein Coding Gene
MGI:1915981 | Rbfa
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Domain
IPR000238 | RbfA
Type: Family
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].Ribosome-binding factor A [](gene rbfA) is a bacterial protein that associates with free 30S ribosomal subunits. It does not associate with 30S subunits that are part of 70S ribosomes or polysomes. It is essential for efficient processing of 16S rRNA. Ribosome-binding factor A is a protein of from 13 to 15 Kd which is found in most bacteria. A putative chloroplastic form seems to exist in plants.
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Gene
100506070 | RBFADN
Type: gene
Organism: human
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Publication
9422595 | -
First Author: Bylund GO
Year: 1998
Journal: J Bacteriol
Title: RimM and RbfA are essential for efficient processing of 16S rRNA in Escherichia coli.
Volume: 180
Issue: 1
Pages: 73-82
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Protein
Q6P3B9
Organism: Mus musculus/domesticus
Length: 350  
Fragment?: false
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Protein
Q3UKZ0
Organism: Mus musculus/domesticus
Length: 350  
Fragment?: false
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Publication
11297922 | -
First Author: Ramakrishnan V
Year: 2001
Journal: Curr Opin Struct Biol
Title: Atomic structures at last: the ribosome in 2000.
Volume: 11
Issue: 2
Pages: 144-54
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Publication
11290319 | -
First Author: Maguire BA
Year: 2001
Journal: Cell
Title: The ribosome in focus.
Volume: 104
Issue: 6
Pages: 813-6
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Publication
11114498 | -
First Author: Chandra Sanyal S
Year: 2000
Journal: Curr Opin Struct Biol
Title: The end of the beginning: structural studies of ribosomal proteins.
Volume: 10
Issue: 6
Pages: 633-6
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Protein Coding Gene
MGP_CAROLIEiJ_G0022433 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0024590 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0024557 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0024528 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0024555 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0024324 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1915981 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0025002 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0023797 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0024294 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0024424 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0024390 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0024508 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0024420 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0025051 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0023542 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0023859 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0019161 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0023348 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
- | J:73796
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Function or Process or Component Unknown following Literature Review
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Publication
- | J:57656
     
First Author: Lennon G
Year: 1999
Journal: Database Download
Title: WashU-HHMI Mouse EST Project
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
21102555 | -
First Author: Goto S
Year: 2011
Journal: EMBO J
Title: RsgA releases RbfA from 30S ribosome during a late stage of ribosome biosynthesis.
Volume: 30
Issue: 1
Pages: 104-14
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Publication
25904134 | -
First Author: Jeganathan A
Year: 2015
Journal: RNA
Title: The C-terminal helix in the YjeQ zinc-finger domain catalyzes the release of RbfA during 30S ribosome subunit assembly.
Volume: 21
Issue: 6
Pages: 1203-16
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Publication
35682734 | J:325995
 
First Author: Averina OA
Year: 2022
Journal: Int J Mol Sci
Title: Mitochondrial rRNA Methylation by Mettl15 Contributes to the Exercise and Learning Capability in Mice.
Volume: 23
Issue: 11
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Publication
14973029 | -
First Author: Daigle DM
Year: 2004
Journal: J Bacteriol
Title: Studies of the interaction of Escherichia coli YjeQ with the ribosome in vitro.
Volume: 186
Issue: 5
Pages: 1381-7
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Publication
15466596 | -
First Author: Himeno H
Year: 2004
Journal: Nucleic Acids Res
Title: A novel GTPase activated by the small subunit of ribosome.
Volume: 32
Issue: 17
Pages: 5303-9
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Publication
15828870 | -
First Author: Campbell TL
Year: 2005
Journal: Biochem J
Title: Characterization of the Bacillus subtilis GTPase YloQ and its role in ribosome function.
Volume: 389
Issue: Pt 3
Pages: 843-52
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Publication
21960487 | -
First Author: Jomaa A
Year: 2011
Journal: RNA
Title: Cryo-electron microscopy structure of the 30S subunit in complex with the YjeQ biogenesis factor.
Volume: 17
Issue: 11
Pages: 2026-38
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Protein Domain
IPR004881 | Ribosome_biogen_GTPase_RsgA
Type: Family
Description: This entry contains Escherichia coli (strain K12) RsgA, which plays a role in the late maturation steps of the functional core of the 30S ribosomal subunit. It removes RbfA from mature, but not immature, 30S ribosomes in a GTP-dependent manner [, ], and binds the 30S subunit making contact with the head, platform and rRNA helix 44 [, ]. RsgA (sometimes known as YjeQ or EngC) is an unusual circulary permuted GTPase that catalyzes rapid hydrolysis of GTP with a slow catalytic turnover. It is dispensible for viability, but important for overall fitness. The intrinsic GTPase activity is stimulated by the presence of 30S (160-fold increase in kcat) or 70S (96 fold increase in kcat) ribosomes []. The GTPase is inhibited by aminoglycoside antibiotics such as neomycin and paromycin []streptomycin and spectinomycin []. This inhibition is not due to competition for binding sites on the 30S or 70S ribosome []. A mitochondrial version of RsgA has been characterized from Arabidopsis[].
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Publication
21788480 | -
First Author: Guo Q
Year: 2011
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for the function of a small GTPase RsgA on the 30S ribosomal subunit maturation revealed by cryoelectron microscopy.
Volume: 108
Issue: 32
Pages: 13100-5
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Publication
15266054 | -
First Author: Tzafrir I
Year: 2004
Journal: Plant Physiol
Title: Identification of genes required for embryo development in Arabidopsis.
Volume: 135
Issue: 3
Pages: 1206-20
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Publication
12628255 | -
First Author: Huang YJ
Year: 2003
Journal: J Mol Biol
Title: Solution NMR structure of ribosome-binding factor A (RbfA), a cold-shock adaptation protein from Escherichia coli.
Volume: 327
Issue: 2
Pages: 521-36
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Protein Domain
IPR023799 | RbfA_dom_sf
Type: Homologous_superfamily
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].Ribosome-binding factor A [](gene rbfA) is a bacterial protein that associates with free 30S ribosomal subunits. It does not associate with 30S subunits that are part of 70S ribosomes or polysomes. It is essential for efficient processing of 16S rRNA. Ribosome-binding factor A is a protein of from 13 to 15 Kd which is found in most bacteria. A putative chloroplastic form seems to exist in plants.The structural domain of RbfA has an α-β fold containing three helices and three β-strands: alpha1-beta1-beta2-alpha2-alpha3-beta3. The structure has type-II KH-domain fold topology, related to conserved KH sequence family proteins whose beta-α-α-beta subunits are characterised by a helix-turn-helix motif with sequence signature GxxG at the turn. In RbfA, this beta-α-α-beta subunit is characterised by a helix-kink-helix motif in which the GxxG sequence is replaced by a conserved AxG sequence [].
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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