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 1958800121  66 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 145
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90
                  ....*....|..
gi 1958800121 146 ESIYGGYFK-EN 156
Cdd:cd01926    78 KSIYGEKFPdEN 89

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800121  66 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 145
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90
                  ....*....|..
gi 1958800121 146 ESIYGGYFK-EN 156
Cdd:cd01926    78 KSIYGEKFPdEN 89

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958800121  72 IEINREpvGRIMFQLFSDICPKTCKNFLCLCsgekglgkTTGKklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIY 149
Cdd:pfam00160   1 IETNGL--GRIVIELFGDKAPKTVENFLQLC--------KKGF---YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIF 64

cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. These enzymes have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. As cyclophilins, Human hCyP-A, human cyclophilin-B (hCyP-19), S. cerevisiae Cpr1 and C. elegans Cyp-3, are inhibited by the immunosuppressive drug cyclopsporin A (CsA). CsA binds to the PPIase active site. Cyp-3. S. cerevisiae Cpr1 interacts with the Rpd3 - Sin3 complex and in addition is a component of the Set3 complex. S. cerevisiae Cpr1 has also been shown to have a role in Zpr1p nuclear transport. Human cyclophilin H associates with the [U4/U6.U5] tri-snRNP particles of the splicesome.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800121  66 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKGLGkttGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 145
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                          90
                  ....*....|..
gi 1958800121 146 ESIYGGYFK-EN 156
Cdd:cd01926    78 KSIYGEKFPdEN 89

peptidyl-prolyl isomerase H (cyclophilin H); Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800121  66 PQCHFDIEINREPVGRIMFQLFSDICPKTCKNFLCLCSGEKglgKTTGKKLCYKGSTFHRVVKNFMIQGGDFSEGNGKGG 145
Cdd:PLN03149   19 PVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                          90
                  ....*....|....
gi 1958800121 146 ESIYGGYFK-ENVV 158
Cdd:PLN03149   96 VSIYGSKFEdENFI 109

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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958800121  72 IEINREpvGRIMFQLFSDICPKTCKNFLCLCsgekglgkTTGKklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIY 149
Cdd:pfam00160   1 IETNGL--GRIVIELFGDKAPKTVENFLQLC--------KKGF---YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIF 64

cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to Schizosaccharomyces pombe cyp-2. These proteins bind their respective SNW chromatin binding protein in autologous systems, in a CsA independent manner indicating interaction with a surface outside the PPIase active site. SNW proteins play a basic and broad range role in signaling.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958800121  79 VGRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGGYFKENV 157
Cdd:cd01922     6 MGEITLELYWNHAPKTCKNFYELA-----------KRGYYNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEI 72

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        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958800121  79 VGRIMFQLFSDICPKTCKNFLCLCSGEKglgkttgkklcYKGSTFHRVVKNFMIQGGDFSeGNGKGGESIYGGYFK 154
Cdd:cd01925    14 AGDIDIELWSKEAPKACRNFIQLCLEGY-----------YDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFK 77

Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800121  80 GRIMFQLFSDICPKTCKNFLCLCsgEKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFsEGNGKGGEsiygGY-----FK 154
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEGF---------YDGTIFHRVIPGFMIQGGDP-TGTGTGGP----GYtipdeFD 79

                  ....*..
gi 1958800121 155 ENVVFCK 161
Cdd:COG0652    80 PGLKHKR 86

cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958800121  79 VGRIMFQLFSDICPKTCKNFLCLCsgekglgkttgKKLCYKGSTFHRVVKNFMIQGGDfSEGNGKGGESIYGGYFKENVV 158
Cdd:cd01921     6 LGDLVIDLFTDECPLACLNFLKLC-----------KLKYYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQLYGRQAR 73

                  .
gi 1958800121 159 F 159
Cdd:cd01921    74 F 74

peptidylprolyl isomerase B;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958800121  80 GRIMFQLFSDICPKTCKNFLCLCSgeKGLgkttgkklcYKGSTFHRVVKNFMIQGGDFSEG 140
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYCR--EGF---------YNNTIFHRVINGFMIQGGGFEPG 58