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InterPro is a database of protein families, protein domains and functional sites in which identifiable features found in known proteins can be applied to new protein sequences [2] in order to functionally characterise them.
The general purpose of the Pfam database is to provide a complete and accurate classification of protein families and domains. [5] Originally, the rationale behind creating the database was to have a semi-automated method of curating information on known protein families to improve the efficiency of annotating genomes. [6]
Stockholm format is a multiple sequence alignment format used by Pfam, Rfam and Dfam, to disseminate protein, RNA and DNA sequence alignments. [1] [2] [3] The alignment editors Ralee, [4] Belvu and Jalview support Stockholm format as do the probabilistic database search tools, Infernal and HMMER, and the phylogenetic analysis tool Xrate.
A large group of two component regulator proteins appear to have the same N-terminal structure of 14 tandem repeats.These repeats show homology to members of INTERPRO and INTERPRO indicating that they are likely to form a beta-propeller.
Fel d 1 is a secretoglobin protein complex that, in cats, is encoded by the CH1 (chain 1/Fel d 1-A) and CH2 (chain 2/Fel d 1-B) genes. [2] [3] Among cats, Fel d 1 is produced largely in their saliva and by the sebaceous glands located in their skin. It is the primary allergen present on cats and kittens.
These proteins contain between 1 and 7 Kazal-type inhibitor repeats. [4] [5] The structure of the Kazal repeat includes a large quantity of extended chain, 2 short alpha-helices and a 3-stranded anti-parallel beta sheet. [4] The inhibitor makes 11 contacts with its enzyme substrate: unusually, 8 of these important residues are hypervariable. [5]
Some of those who are making the trek, like Samantha Balsham, tell Yahoo Life that the effort is worth it to make sure their vote counts. At 19 years old, this presidential election is the first ...
The structure is a disulfide rich alpha+beta fold. Bovine pancreatic trypsin inhibitor is an extensively studied model structure. Certain family members are similar to the tick anticoagulant peptide (TAP, ).