Proteases in the MEROPS protease database have been subdivided into families and clans on the basis of evolutionary relationships (http://merops.sanger.ac.uk) (Rawlings et al., 2014). A protease clan refers to proteases derived from a single common ancestor, and clans are subdivided into families. A protease family refers to a sub-group of proteases that share sequence similarity, either throughout the entire protein sequence or only within the catalytic domain. The Arabidopsis thaliana genome encodes 879 known and putative proteases, corresponding to approximately 3.2% of all Arabidopsis protein-coding genes (The Arabidopsis Information Resource). These proteases are distributed over 60 families that belong to around 30 different clans
Since we have already known the amino sequence of the protein in previous step, we can narrow down the targeting ubiquitin ligase based on existing research data such as papers, NCBI data.
The newly formed ookinete survives in the harsh protease rich environment of the midgut due to protease resistant covering (Gass and Yeates, 1979). Carter and Kumar (1985) observed that ookinete surface proteins are responsible for protecting ookinetes from protease enzymes attack (Carter et al., 1988). These and other parasite surface proteins are also candidates for an antizygote-ookinete transmission-blocking
Researchers at George Washington University have been working on a vaccine to prevent infection from the hookworm parasite for years and sought out volunteers that would let these parasitic worms burrow into their skin. In order to effectively study the hookworm, the researchers needed to find healthy volunteers that would allow the hookworm parasites to infiltrate their bodies and live in there for several months and also diseased participants to compare the data that they would collect. However, people weren’t interested in doing the clinical trial when they found out they would have parasites sucking on their blood through their intestines. After searching for months, the GW team found a small group of volunteers to take on the task
Primase and helicase proteins are the essential components of the DNA replication machinery required for the synthesis of short RNA primers and the unwinding of the DNA, respectively. When these activities are encoded on the same polypeptide chain, as seen in many double-stranded DNA viruses, their proximity is hypothesized to confer several functional advantages. The aim of this study was to investigate the origin and evolutionary relationships of different combinations of primase-helicase bifunctional proteins that are prevalent in the virus world but also present sporadically in bacteria, archaea and eukaryotes. For this purpose, sequence analysis, phylogenetic relationships and coevolution of primase and helicase domains of the bifunctional
One of the biggest advances has come from molecular analysis of common ancestry. Compiling molecular phylogenies that focus
This alarm anti-protease is secreted at the site of injury in response to primary cytokines like interleukin-1 (IL-1) and tumour necrosis factor (TNF), making them possibly the first line of defence in the anti-proteinase network (Sallenave, 2000). Elafin is produced mainly by epithelia in the skin, upper gastrointestinal tract, female reproductive tract, lungs and in low levels in serum. Its secretion is upregulated in the presence of inflammatory stimuli or conditions such as psoriasis and acute respiratory distress syndrome (Shaw, 2011), although some research have shown that uncontrolled protease activity may lead to its proteolytic cleavage (Small, 2015). This was confirmed in a study by Guyot et al which demonstrated that the involvement of purified NE in
For the sake of discussing the protein product formed by each locus, it is inherent that the terms hypothetical protein and putative protein be defined. A protein’s existence can be predicted. However, there may be no evidence, experimentally, to prove its expression, in vivo. Such a protein is called a hypothetical protein. Hypothetical proteins have less similarity with known proteins that have been annotated. On the contrary, putative proteins are more similar to characterized proteins in their levels conserved amino acid residues. Both FACI_IFERC00001G1223 and FACI_IFERC00001G1220 have protein products that are hypothetical. It must be added that, initially a search of the entire Ferroplasma genome was done. The data from this ‘whole-genome research’ was very helpful in assisting with the formulation of hypotheses pertaining to protein products, which should be observed for the various loci during this Genomic annotation assessment. As stated earlier, the proteins which were encoded for by the loci associated
Apolipoprotein(A) is a homologue of plasminogen and contains several copies of KRINGLE 4 plasminogen, a single copy of KRINGLE 5 plasminogen and an inactive protease domain (2).
Just as members in the same family often resemble each other, similarly structured molecules are often grouped in the same category. There are several methods of comparing amino acid sequencing and determining how closely they are related. A simple example is the sequence-comparison method. Sequence databases are searched for a specific amino acid sequence of unknown characteristics. A set of molecules that are similar in structure can give insight into the properties of the unknown sequence of amino acids.
HUPO promotes proteomics study through international collaborations to better understand various aspects of human well-being by supporting related research into plants, livestock and pathogens. The general goal of the Biology/Disease branch of the Human Protein Project (B/D-HPP), initiated by the Human Proteome Organization, is to explore the impact that proteomic approach, exemplified by mass spectrometry technologies, can have when applied to a focused area of biology, in collaboration with specific experts in that particular field.
To understand how coevolving Gag residues can alter binding interactions between Gag polyprotein and HIV-1 protease, Ozen et al. studied the interactions between wildtype and mutant I50V/A71V protease with Gag polyprotein with mutated p1 to p6 cleavage sites. While the overall backbone conformation of the Gag-protease complex is conserved n all coevolved structures, when superposed onto the wildtype Gag-protease complex, minor structural changes were found at contact surfaces between the Gag polyprotein and HIV-1 surfaces. This coincides with how Deshmukh et al. found regions of high mutational propensities at short-lived contacts between surface-exposed residues on the Gag polyprotein and HIV-1 proteases (Deshmukh et al, 2016; Ozen et al, 2014).
D.Thompson, Desmond G.Higginsand and Toby J.Gibson [1] innovated pairwise alignment of very closely related sequence can be carried out very accurately, and this guarantees a mathematically optimal alignment. It is very useful starting point for as it helps define the major blocks of similarity manual refinement. W J Wilbur and David J Lipman [2] developed a global algorithm for comparing two Amino acid sequences, and also the algorithm involves the construction of an optimal alignment. It is an algorithm for fast alignment and comparison of two nuclide acid and amino acid sequence, the number of protein molecules and nucleic acid fragments for which the sequences have been determined has grown into the thousands, it has become clear that
Proteus Mirabilis is a motile bacterium that exists freely in water and soil; it may also be said to be a parasite that colonizes the human urinary tract. It exists in flagella or rod form as a gram-negative bacterium that displays uropathogenic virulence. Proteus Mirabilis is known to persist and live in people due to its unique virulence factors. Patients who have structural modifications within their urinary tract such as internal catheters are often deemed to be at high risk of contracting diseases such as pyelonephritis and cystitis, which are caused by Proteus Mirabilis (Jacobsen &Shirtliff, 2011). Individuals who have long-term catheters in their tracts face a high risk of suffering from urea hydrolysis and kidney/
EST sequences with vector sequence were edited using Phrap “cross-match” application. Contig Assembly Program 3 (Cap3) was used to assemble the sequences obtained from sequencing for analysis while Consed/Autofinish software was used to control the sequence assembly. All sequences were assembled separately into contigs. BLAST of sequences was conducted to determine the gene homology in order to connect their functions. Unique sequences were analysed for biological characteristics as well as functional annotation using program BLAST2GO. New genes can then be identified eventually.