Conserved sequence motifs in the unorthodox BvgS two-component sensor protein of Bordetella pertussis

1996 ◽  
Vol 252 (1-2) ◽  
pp. 169-176 ◽  
Author(s):  
Dagmar Beier ◽  
Heike Deppisch ◽  
Roy Gross
Keyword(s):  
Bordetella Pertussis ◽  
Sequence Motifs ◽  
Conserved Sequence ◽  
Two Component ◽  
Sensor Protein ◽  
Conserved Sequence Motifs

scholarly journals Conserved sequence motifs among bacterial, eukaryotic, and archaeal phosphatases that define a new phosphohydrolase superfamily

1998 ◽  
Vol 7 (7) ◽  
pp. 1647-1652 ◽  
Author(s):  
Maria Cristina Thaller ◽  
Serena Schippa ◽  
Gian Maria Rossolini
Keyword(s):  
Sequence Motifs ◽  
Conserved Sequence ◽  
Conserved Sequence Motifs

scholarly journals Identification and Analysis of Novel Amino-Acid Sequence Repeats inBacillus anthracisstr.AmesProteome Using Computational Tools

2007 ◽  
Vol 2007 ◽  
pp. 1-23 ◽  
Author(s):  
G. R. Hemalatha ◽  
D. Satyanarayana Rao ◽  
L. Guruprasad
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
Protein Sequence ◽  
Amino Acid Residues ◽  
Sequence Motifs ◽  
Computational Tools ◽  
Conserved Sequence ◽  
Conserved Sequence Motifs ◽  
Multiple Copies ◽  
Domain 3

We have identified four repeats and ten domains that are novel in proteins encoded by theBacillus anthracisstr.Amesproteome using automated in silico methods. A “repeat” corresponds to a region comprising less than 55-amino-acid residues that occur more than once in the protein sequence and sometimes present in tandem. A “domain” corresponds to a conserved region with greater than 55-amino-acid residues and may be present as single or multiple copies in the protein sequence. These correspond to (1) 57-amino-acid-residue PxV domain, (2) 122-amino-acid-residue FxF domain, (3) 111-amino-acid-residue YEFF domain, (4) 109-amino-acid-residue IMxxH domain, (5) 103-amino-acid-residue VxxT domain, (6) 84-amino-acid-residue ExW domain, (7) 104-amino-acid-residue NTGFIG domain, (8) 36-amino-acid-residue NxGK repeat, (9) 95-amino-acid-residue VYV domain, (10) 75-amino-acid-residue KEWE domain, (11) 59-amino-acid-residue AFL domain, (12) 53-amino-acid-residue RIDVK repeat, (13) (a) 41-amino-acid-residue AGQF repeat and (b) 42-amino-acid-residue GSAL repeat. A repeat or domain type is characterized by specific conserved sequence motifs. We discuss the presence of these repeats and domains in proteins from other genomes and their probable secondary structure.

scholarly journals Conserved sequence motifs, alignment, and secondary structure for the third domain of animal 12S rRNA

1996 ◽  
Vol 13 (1) ◽  
pp. 150-169 ◽  
Author(s):  
R. E. Hickson ◽  
C. Simon ◽  
A. Cooper ◽  
G. S. Spicer ◽  
J. Sullivan ◽  
...  
Keyword(s):  
Secondary Structure ◽  
12S Rrna ◽  
Sequence Motifs ◽  
Conserved Sequence ◽  
The Third ◽  
Conserved Sequence Motifs

scholarly journals SAND, a New Protein Family: From Nucleic Acid to Protein Structure and Function Prediction

2001 ◽  
Vol 2 (4) ◽  
pp. 226-235 ◽  
Author(s):  
Amanda Cottage ◽  
Yvonne J. K. Edwards ◽  
Greg Elgar
Keyword(s):  
Genomic Sequence ◽  
Protein Family ◽  
Sequence Motifs ◽  
Est Database ◽  
Computational Tools ◽  
Conserved Sequence ◽  
Conserved Sequence Motifs ◽  
And Function ◽  
New Protein ◽  
Genomic Organisation

As a result of genome, EST and cDNA sequencing projects, there are huge numbers of predicted and/or partially characterised protein sequences compared with a relatively small number of proteins with experimentally determined function and structure. Thus, there is a considerable attention focused on the accurate prediction of gene function and structure from sequence by using bioinformatics. In the course of our analysis of genomic sequence fromFugu rubripes, we identified a novel gene,SAND, with significant sequence identity to hypothetical proteins predicted inSaccharomyces cerevisiae, Schizosaccharomyces pombe, Caenorhabditis elegans, aDrosophila melanogastergene, and mouse and human cDNAs. Here we identify a furtherSANDhomologue in human andArabidopsis thalianaby use of standard computational tools. We describe the genomic organisation ofSANDin these evolutionarily divergent species and identify sequence homologues from EST database searches confirming the expression of SAND in over 20 different eukaryotes. We confirm the expression of two different SAND paralogues in mammals and determine expression of one SAND in other vertebrates and eukaryotes. Furthermore, we predict structural properties of SAND, and characterise conserved sequence motifs in this protein family.

Conserved sequence motifs in the alpha helices of the serological variants HLA-B “DT” and HLA-B “NM5”

1994 ◽  
Vol 40 ◽  
pp. 69
Author(s):  
W.H. Hildebrand ◽  
M. Ellexson ◽  
D. Stewart ◽  
M. Lau ◽  
P. Terasaki ◽  
...  
Keyword(s):  
Sequence Motifs ◽  
Alpha Helices ◽  
Conserved Sequence ◽  
Conserved Sequence Motifs
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