PPIC

Peptidyl-prolyl cis-trans isomerase C

212 amino acids

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.

Belongs to the cyclophilin-type PPIase family.

22.811 kDa

MGPGLRPLLPLVLCVGLSALVPSAGASGFRKRGPSVTAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKGYGYKGSKFHRVIKDFMIQGGDFTRGDGTGGISIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVLDGMTVVHSIELQATDGHDRPFTDCSIVNSGKIDVKTPFVVEVSDW

PPIC

Peptidyl-prolyl cis-trans isomerase C

212 amino acids

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.

Belongs to the cyclophilin-type PPIase family.

22.763 kDa

MGPGPRLLLPLVLCVGLGALVFSSGAEGFRKRGPSVTAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSIINSGKIDVKTPFVVEIADW

Ppic

Peptidyl-prolyl cis-trans isomerase C

212 amino acids

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.

Belongs to the cyclophilin-type PPIase family.

22.794 kDa

MSPGPRLLLPAVLCLGLGALVSSSGSSGVRKRGPSVTDKVFFDVRIGDKDVGRIVIGLFGNVVPKTVENFVALATGEKGYGYKGSIFHRVIKDFMIQGGDFTARDGTGGMSIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVLDGMTVVHSIELQATDGHDRPLTDCTIVNSGKIDVKTPFVVEVPDW

ppiC

Peptidyl-prolyl cis-trans isomerase C

93 amino acids

PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates (By similarity).

Belongs to the PpiC/parvulin rotamase family.

10.232 kDa

MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVLYRN

ppiC

Peptidyl-prolyl cis-trans isomerase C

93 amino acids

PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates (By similarity).

Belongs to the PpiC/parvulin rotamase family.

10.232 kDa

MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVLYRN

ppiC

Peptidyl-prolyl cis-trans isomerase C

93 amino acids

PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates.

Belongs to the PpiC/parvulin rotamase family.

10.232 kDa

MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVLYRN

ppiC

Peptidyl-prolyl cis-trans isomerase C

93 amino acids

PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates (By similarity).

Belongs to the PpiC/parvulin rotamase family.

10.328 kDa

MAKMAAALHILVKEEKLALDLLEQIKNGGDFEKLAKKHSICPSGKKGGHLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVLYRK

ppiC

Peptidyl-prolyl cis-trans isomerase C

93 amino acids

PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates (By similarity).

Belongs to the PpiC/parvulin rotamase family.

10.328 kDa

MAKMAAALHILVKEEKLALDLLEQIKNGGDFEKLAKKHSICPSGKKGGHLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVLYRK