The nucleotide and amino acid sequences of SaAACT and SaHMGS were analyzed by bioinformatics methods, and their physical and chemical characteristics, transmembrane domain, signal peptide, and subcellular localization were predicted by corresponding bioinformatics software. Sequence assembly was performed with DNAstar (http://www.dnastar.com). Nucleotide sequences, deduced amino acid sequences and ORFs were analyzed, and sequences were compared through a BLAST database search (http://www.ncbi.nlm.nih.gov). Protein molecular weight and theoretical isoelectric point, instability index, aliphatic index and grand average of hydropathicity were calculated by ExPASy (http://www.expasy.ch/tools/). Protein conserved domains and active sites were predicted by the Conserved Domains database in NCBI (http://www.ncbi.mlm.nih.gov/Structure/cdd/wrpsb.cgi) and by Prosit (http://prosite.expasy.org/) in ExPASy. Transmembrane domains were analyzed on the TMHMM Server (http://www.cbs.-dtu.dk/services/TMHMM/). Signal peptides were analyzed by SignalP (http://www.cbs.dtu.dk/services/SignalP/). Protein subcellular localization was predicted by PSORT II (http://psort.org/).

Note: The content above has been extracted from a research article, so it may not display correctly.



Q&A
Please log in to submit your questions online.
Your question will be posted on the Bio-101 website. We will send your questions to the authors of this protocol and Bio-protocol community members who are experienced with this method. you will be informed using the email address associated with your Bio-protocol account.



We use cookies on this site to enhance your user experience. By using our website, you are agreeing to allow the storage of cookies on your computer.