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 2462608030 112 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 191
Cdd:cd01926     3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                  ....*.
gi 2462608030 192 YGPTFE 197
Cdd:cd01926    81 YGEKFP 86

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIVY-GKGDNGESI 191
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEGF--------YDGTIFHRVIPGFMIQGGDPTGtGTGGPGYTI 74

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 2462608030 112 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 191
Cdd:cd01926     3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                  ....*.
gi 2462608030 192 YGPTFE 197
Cdd:cd01926    81 YGEKFP 86

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608030 123 IGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVYGKGdnGESIYGPTFEE 198
Cdd:cd00317     6 KGRIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPD 69

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEEKAMKA 203
Cdd:cd01928    10 GDIKIELFCDDCPKACENFLALCASG----------YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFRET 78

                  ..
gi 2462608030 204 IK 205
Cdd:cd01928    79 LK 80

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgkagfsQRGirlHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEE 198
Cdd:cd01923     9 GDLNLELHCDKAPKACENFIKLC-------KKG---YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKD 72

cyclophilin; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 100 SAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGF-SQRGIRLHYKNSIFHRI-VQNGWIQG 177
Cdd:PTZ00221   43 SHRMKEEQNSCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdTNTGVKLDYLYTPVHHVdRNNNIIVL 122

                          90       100
                  ....*....|....*....|
gi 2462608030 178 GDIV-YGKGDNGESIYGPTF 196
Cdd:PTZ00221  123 GELDsFNVSSTGTPIADEGY 142

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 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGG 178
Cdd:cd01920     7 GDIVVELYDDKAPITVENFLAYV--RKGF--------YDNTIFHRVISGFVIQGG 51

peptidylprolyl isomerase B;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608030 124 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDivygkgdngesiYGPTFEEKAMKA 203
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYC--REGF--------YNNTIFHRVINGFMIQGGG------------FEPGMKQKATKE 66