cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509663 250 NPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDG-FVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGE 328
Cdd:cd01924    1 GEATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGgFVVQTGDPQGKNPGFPDPETGKSRTIPLEIKPEGQ 80

                         90
                 ....*....|
gi 186509663 329 KTPFYGSTLE 338
Cdd:cd01924   81 KQPVYGKTLE 90

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509663 250 NPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDG-FVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGE 328
Cdd:cd01924    1 GEATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGgFVVQTGDPQGKNPGFPDPETGKSRTIPLEIKPEGQ 80

                         90
                 ....*....|
gi 186509663 329 KTPFYGSTLE 338
Cdd:cd01924   81 KQPVYGKTLE 90

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186509663  258 FRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGDPEGPaegfiDPSTEKTRTVPLEI 323
Cdd:pfam00160   9 IVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRViPGFMVQGGDPTGT-----GGGGKSIFPIPDEI 70

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509663 250 NPNIEDCVFRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRSDG-FVVQTGDPEGPAEGFIDPSTEKTRTVPLEIMVTGE 328
Cdd:cd01924    1 GEATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGgFVVQTGDPQGKNPGFPDPETGKSRTIPLEIKPEGQ 80

                         90
                 ....*....|
gi 186509663 329 KTPFYGSTLE 338
Cdd:cd01924   81 KQPVYGKTLE 90

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186509663 260 IVLDGYNAPVTAGNFVDLVERHFYDGMEIQR-SDGFVVQTGDPEGPAEGFIDPStektRTVPLEIMV 325
Cdd:cd00317   11 IELYGDEAPKTVENFLSLARGGFYDGTTFHRvIPGFMIQGGDPTGTGGGGSGPG----YKFPDENFP 73

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 186509663 258 FRIVLDGYNAPVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGdpegpaeGFIDPSTEK 315
Cdd:cd01920    9 IVVELYDDKAPITVENFLAYVRKGFYDNTIFHRViSGFVIQGG-------GFTPDLAQK 60

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 186509663 267 APVTAGNFVDLVERHFYDGMEIQRS-DGFVVQTGDPEGPAEG 307
Cdd:cd01925   26 APKACRNFIQLCLEGYYDNTIFHRVvPGFIIQGGDPTGTGTG 67