-- dump date 20120504_141507 -- class Genbank::CDS -- table cds_note -- id note YP_005815737.1 Note the Pfam PF08282;haloacid dehalogenase-like hydrolase motif YP_005815740.1 extended C terminus compared to CTB_1051 YP_005815742.1 Note the Pfam PF01784, NIF3 (NGG1p interacting factor 3) YP_005815749.1 insertion leading to frameshift. possibly able to express from alternative start codon. YP_005815765.1 Note the Pfam PF03631;Ribonuclease BN-like family YP_005815768.1 members of this family of proteins have a broad spectrum of activity YP_005815769.1 note the PFAM motif to yrdC domain PF01300 YP_005815786.1 truncated compared to serotype B protein CTB_1531. alternative start codon may be used. YP_005815792.1 Note the motifs for calcium binding and calmodulin-binding domain. YP_005815794.1 remnant of larger cytotoxin gene. Possibly still active - serovar D retains function in CT166 [Carlson et al (2004) Infect. Immun 72 (12):7063-72]. YP_005815795.1 remnant of larger cytotoxin gene. Possibly still active - serovar D retains function in CT166 [Carlson et al (2004) Infect. Immun 72 (12):7063-72]. YP_005815796.1 remnant of larger cytotoxin gene. Possibly still active - serovar D retains function in CT166 [Carlson et al (2004) Infect. Immun 72 (12):7063-72]. YP_005815797.1 remnant of larger cytotoxin gene. Possibly still active - serovar D retains function in CT166 [Carlson et al (2004) Infect. Immun 72 (12):7063-72]. YP_005815806.1 Note the alternate possible translational start site at codon 27. YP_005815821.1 carries characteristic twin membrane spanning domains YP_005815825.1 carries characteristic twin membrane spanning domains YP_005815843.1 carries characteristic twin membrane spanning domains YP_005815852.1 carries characteristic twin membrane spanning domains YP_005815853.1 carries characteristic twin membrane spanning domains YP_005815854.1 carries characteristic twin membrane spanning domains YP_005815855.1 carries characteristic twin membrane spanning domains YP_005815856.1 carries characteristic twin membrane spanning domains YP_005815857.1 carries characteristic twin membrane spanning domains YP_005815858.1 carries characteristic twin membrane spanning domains YP_005815859.1 carries characteristic twin membrane spanning domains YP_005815918.1 carries characteristic twin membrane spanning domains YP_005815989.1 carries characteristic twin membrane spanning domains YP_005816095.1 recognizes the termination signals UGA and UAA during protein translation a specificity which is dependent on amino acid residues residing in loops of the L-shaped tRNA-like molecule of RF2; in some organisms control of PrfB protein levels is maintained through a +1 ribosomal frameshifting mechanism; this protein is similar to release factor 1 YP_005816096.1 Note the Pfam PF02201;SWIB-MDM2 domain. YP_005816183.1 note the tetratricopeptide repeat motifs YP_005816187.1 pseudo in SeroD intact in Sero A YP_005816256.1 member of the CHLPN 76 kD protein family of proteins YP_005816257.1 member of the CHLPN 76 kD protein family of proteins YP_005816272.1 Note the PFAM domain PF04085 MreC (murein formation C) is involved in the rod shape determination in E. coli. YP_005816283.1 Similar to many proposed 5-formyltetrahydrofolate cyclo-ligase YP_005816319.1 Note the COG0719 motif associated with, SufB, an ABC-type transport system protein YP_005816335.1 note the PF07719 Tetratricopeptide repeat motif YP_005816355.1 note the NifU-like protein domains: PF01592;NifU-like N terminal domain and PF01106, NifU-like domain YP_005816371.1 Note the PF01161;Phosphatidylethanolamine-binding motif YP_005816389.1 Note the PF00149;Calcineurin-like phosphoesterase motif YP_005816402.1 Note the PF04055;Radical SAM superfamily motif YP_005816404.1 Note the Pfam PF02410;Domain of unknown function associated with iojap superfamily proteins YP_005816406.1 Note the Pfam PF00293;NUDIX domain YP_005816449.1 carries characteristic twin membrane spanning domains YP_005816498.1 note that the product of this CDS has been proposed to be a putative type III secretion system translocator