match no.target idtarget lengthalignment lengthprobabilityE-valuecoveragematch description
1PRK095783852335.026[-----                                            ]PRK09578periplasmic multidrug efflux lipoprotein precursor; Reviewed
2COG56331232333.430[-----                                            ]YcfLUncharacterized conserved protein YcfL
3PRK126962362530.675[-----                                            ]flgHflagellar basal body L-ring protein; Reviewed
4pfam00879521729.443[---                                              ]Defensin_propepDefensin propeptide.
5pfam08139191729.349[----                                             ]LPAM_1Prokaryotic membrane lipoprotein lipid attachment site. In prokaryotes, membrane lipoproteins are synthesized with a precursor signal peptide, which is cleaved by a specific lipoprotein signal peptidase (signal peptidase II). The peptidase recognizes a conserved sequence and cuts upstream of a cysteine residue to which a glyceride-fatty acid lipid is attached.
6PRK09810412124.464[----                                             ]PRK09810entericidin A; Provisional
7TIGR04359661722.366[----                                             ]TrbK_RP4entry exclusion lipoprotein TrbK. The characterized model example of TrbK, from incompatibility group P (IncP) plasmid RP4, is an N-terminally processed lipoprotein, localized to the periplasmic face of the plasma membrane. TrbK prevents entry through conjugation by other IncP plasmids. Unrelated, uncharacterized proteins encoded in equivalent positions in other plasmid P-type conjugative transfer regions (e.g. TIGR04360) may have analogous functions.
8PRK138831511820.771[----                                             ]PRK13883conjugal transfer protein TrbH; Provisional
9COG43141762620.192[------                                           ]NosLNitrous oxide reductase accessory protein NosL
10pfam102461053315.21E+02[                                      -----------]MRP-S35Mitochondrial ribosomal protein MRP-S35. This is a family of short mitochondrial ribosomal proteins, less than 200 amino acids long. that are highly conserved from worms to humans. The structure has previously been referred to as MRP-S18 but the current numbering fits the preferred nomenclature from these authors.