Signature sequence

Brenner S et al. Gene expression analysis by massively parallel signature sequencing (MPSS) on microbead arrays. Nature Biotechnol 2000 18 630-634. 

S ETdomain containing H KMTs have been classified according to the presence or absence and the nature of the sequences surrounding the SET domain that are conserved within families [71, 72]. The SET domain has a unique structural fold classified as class V AdoMet-dependent methyltransferase (MTase) [69], characterized by four highly-conserved signature sequences, namely motif I... 

These proteases contain signature sequences composed of well-conserved serine,... 

FIGURE 3-32 A signature sequence in the EF-1 /EF-Tu protein family. The signature sequence (boxed) is a 12-amino-acid insertion near the amino terminus of the sequence. Residues that align in all species are shaded yellow. Both archaebacteria and eukaryotes have... 

Edman degradation 98 proteases 99 proteome 101 lateral gene transfer 107 homologous proteins 107 homolog 107 paralog 107 ortholog 107 signature sequence 109... 

Class II aminoacyl-tRNA synthetases contain a different set of three "signature sequences," two of which form an ATP-binding catalytic domain. The active site structure is built on an antiparallel (3 sheet and is surrounded by two helices (Fig. 29-9). Each class contains subgroups with inserted loops that form other domains. In the following tabulation the reference numbers refer to three-dimensional structural studies. 

Identify the signal peptide and family signature sequences of pig pancreatic ribonuclease with the given amino acid sequence ... 

Gupta RS (1998) Protein phylogenies and signature sequences a reappraisal of evolutionary relationships among Archaebacteria, Eubacteria, and Eukaryotes. Microbiol Mol Biol Rev 62 1435-1491... 

Sequence Comparisons Proteins called molecular chaperones (described in Chapter 4) assist in the process of protein folding. One class of chaperone found in organisms from bacteria to mammals is heat shock protein 90 (Hsp90). All Hsp90 chaperones contain a 10 amino acid signature sequence, which allows for ready identification of these proteins in sequence databases. Two representations of this signature sequence are shown below. 

All ABC proteins contain at least three characteristic peptide sequences the Walker A and B motifs, and the so-called ABC-signature sequence. Whereas the Walker motifs are present in several classes of ATP-binding pro-... 

The N-terminal region of NgR harbors eight canonical leucine rich repeats (LRR) that contain the LRR-signature sequence LxxLxLN/CxL. The NgR LRRs are flanked by a leucine rich repeat N-terminal subdomain (LRRNT) and a leucine rich repeat C-terminal subdomain (LRRCT), which are small protein motifs frequently found next to LRR domains. Binding studies reveal that the leucine rich domains are necessary and sufficient for ligand recognition (Fournier et al., 2002). 

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