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LOCUS WP_003113919 174 aa linear BCT 18-FEB-2025 [Pseudomonas]. ACCESSION WP_003113919 VERSION WP_003113919.1 KEYWORDS RefSeq. SOURCE Pseudomonas ORGANISM Pseudomonas Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae. REFERENCE 1 (residues 1 to 174) AUTHORS Llorens,C., Futami,R., Renaud,G. and Moya,A. TITLE Bioinformatic flowchart and database to investigate the origins and diversity of clan AA peptidases JOURNAL Biol Direct 4, 3 (2009) PUBMED 19173708 REMARK Publication Status: Online-Only REFERENCE 2 (residues 1 to 174) AUTHORS Rawlings,N.D. and Barrett,A.J. TITLE Families of aspartic peptidases, and those of unknown catalytic mechanism JOURNAL Methods Enzymol 248, 105-120 (1995) PUBMED 7674916 REFERENCE 3 (residues 1 to 174) AUTHORS Davies,D.R. TITLE The structure and function of the aspartic proteinases JOURNAL Annu Rev Biophys Biophys Chem 19, 189-215 (1990) PUBMED 2194475 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: Conserved Domain (CDD) Evidence Accession :: Domain architecture ID 11466443 Evidence Source :: NCBI SPARCLE ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..174 /organism="Pseudomonas" /db_xref="taxon:286" Protein 1..174 /product="retropepsin-like aspartic protease family protein" /EC_number="3.4.23.-" /GO_function="GO:0004190 - aspartic-type endopeptidase activity [Evidence IEA]" /GO_process="GO:0006508 - proteolysis [Evidence IEA]" /calculated_mol_wt=18668 Region 23..172 /region_name="COG3577" /note="Predicted aspartyl protease [General function prediction only]" /db_xref="CDD:442797" ORIGIN 1 mtqrapgqrl grimlvlawi aglalatryf gvwedrqrnp nqapqsihgd gyvelrlass 61 rqghyllngq ingqgvtfll dtgatqvavp ealaarlale rgapitlsta ngratgwrtr 121 ldqlqlgdir lsgvaaliap gmdgdevllg msalkqleft qrdgtlvlrq ntsp