NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4505991|ref|NP_000934|]
View 

peptidyl-prolyl cis-trans isomerase C precursor [Homo sapiens]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 240)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 39-197 5.95e-99

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.


The actual alignment was detected with superfamily member cd01926:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 164  Bit Score: 284.15  E-value: 5.95e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   39 KVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKG-----YGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIY 113
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991  114 GETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATdGHDRPLTNCSI 193
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS-GNGKPKKKVVI 160


                ....
gi 4505991  194 INSG 197
Cdd:cd01926 161 ADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 39-197 5.95e-99

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.


Pssm-ID: 238907 [Multi-domain]  Cd Length: 164  Bit Score: 284.15  E-value: 5.95e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   39 KVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKG-----YGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIY 113
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991  114 GETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATdGHDRPLTNCSI 193
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS-GNGKPKKKVVI 160


                ....
gi 4505991  194 INSG 197
Cdd:cd01926 161 ADCG 164
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 40-199 5.53e-70

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 211.62  E-value: 5.53e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991    40 VFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGE-----KGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYG 114
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkagLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSIYG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   115 ETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVI-DGMTVVHSIELQATDGHDRPLTNCSI 193
Cdd:PLN03149 101 SKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLACVI 180


                 ....*.
gi 4505991   194 INSGKI 199
Cdd:PLN03149 181 SECGEM 186
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 52-197 6.66e-57

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.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 177.06  E-value: 6.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991     52 GRIVIGLFGKVVPKTVENFVALATgeKGYgYKGSKFHRVIKDFMIQGGDITTGDGTGgvsIYGETFPDENF--KLKHyGI 129
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPTGTGGGG---KSIFPIPDEIFplLLKH-KR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991    130 GWVSMANAG--PDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGhDRPLTNCSIINSG 197
Cdd:pfam00160  80 GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 50-194 1.26e-54

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 171.51  E-value: 1.26e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   50 DVGRIVIGLFGKVVPKTVENFVALAtgEKGYgYKGSKFHRVIKDFMIQGGDITtGDGTGGVsiyGETFPDENFKLKHYGI 129
Cdd:COG0652  14 NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPGLKHKR 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505991  130 GWVSMANA-GPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSII 194
Cdd:COG0652  87 GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 39-197 5.95e-99

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.


Pssm-ID: 238907 [Multi-domain]  Cd Length: 164  Bit Score: 284.15  E-value: 5.95e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   39 KVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKG-----YGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIY 113
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991  114 GETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATdGHDRPLTNCSI 193
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS-GNGKPKKKVVI 160


                ....
gi 4505991  194 INSG 197
Cdd:cd01926 161 ADCG 164
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 40-199 5.53e-70

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 211.62  E-value: 5.53e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991    40 VFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGE-----KGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYG 114
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkagLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSIYG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   115 ETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVI-DGMTVVHSIELQATDGHDRPLTNCSI 193
Cdd:PLN03149 101 SKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLACVI 180


                 ....*.
gi 4505991   194 INSGKI 199
Cdd:PLN03149 181 SECGEM 186
PTZ00060 PTZ00060
cyclophilin; Provisional
 29-181 3.34e-68

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 207.00  E-value: 3.34e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991    29 FRKRGPSVT--AKVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGE------KGYGYKGSKFHRVIKDFMIQGGD 100
Cdd:PTZ00060   5 FSQSFPEMSkrPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   101 ITTGDGTGGVSIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQA 180
Cdd:PTZ00060  85 ITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEG 164


                 .
gi 4505991   181 T 181
Cdd:PTZ00060 165 T 165
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 48-195 1.25e-61

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.


Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 189.01  E-value: 1.25e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   48 DKDVGRIVIGLFGKVVPKTVENFVALATGEkgyGYKGSKFHRVIKDFMIQGGDITtgDGTGGVSIYGETFPDENFKLK-H 126
Cdd:cd00317   3 DTTKGRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENFPLKyH 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505991  127 YGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSIIN 195
Cdd:cd00317  78 HRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 52-197 6.66e-57

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.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 177.06  E-value: 6.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991     52 GRIVIGLFGKVVPKTVENFVALATgeKGYgYKGSKFHRVIKDFMIQGGDITTGDGTGgvsIYGETFPDENF--KLKHyGI 129
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPTGTGGGG---KSIFPIPDEIFplLLKH-KR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991    130 GWVSMANAG--PDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGhDRPLTNCSIINSG 197
Cdd:pfam00160  80 GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 50-194 1.26e-54

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 171.51  E-value: 1.26e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   50 DVGRIVIGLFGKVVPKTVENFVALAtgEKGYgYKGSKFHRVIKDFMIQGGDITtGDGTGGVsiyGETFPDENFKLKHYGI 129
Cdd:COG0652  14 NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPGLKHKR 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505991  130 GWVSMANA-GPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSII 194
Cdd:COG0652  87 GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 52-195 3.89e-54

cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a WD40 domain. This group consists of several hypothetical and putative eukaryotic and bacterial proteins which have a cyclophilin domain and a WD40 domain. Function of the protein is not known.


Pssm-ID: 238908 [Multi-domain]  Cd Length: 148  Bit Score: 169.95  E-value: 3.89e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   52 GRIVIGLFGKVVPKTVENFVALAtgEKGYgYKGSKFHRVIKDFMIQGGDiTTGDGTGGVSIYGETFPDE-NFKLKHYGIG 130
Cdd:cd01927   7 GDIHIRLFPEEAPKTVENFTTHA--RNGY-YNNTIFHRVIKGFMIQTGD-PTGDGTGGESIWGKEFEDEfSPSLKHDRPY 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505991  131 WVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSIIN 195
Cdd:cd01927  83 TLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIIN 147
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 48-194 2.26e-52

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.


Pssm-ID: 238903 [Multi-domain]  Cd Length: 146  Bit Score: 165.40  E-value: 2.26e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   48 DKDVGRIVIGLFGKVVPKTVENFVALATgeKGYgYKGSKFHRVIKDFMIQGGDiTTGDGTGGVSIYGETFPDE-NFKLKH 126
Cdd:cd01922   3 ETTMGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEiHPELKH 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505991  127 YGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDgHDRPLTNCSII 194
Cdd:cd01922  79 TGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKIL 145
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 52-196 1.40e-50

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.


Pssm-ID: 238904 [Multi-domain]  Cd Length: 159  Bit Score: 161.04  E-value: 1.40e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   52 GRIVIGLFGKVVPKTVENFVALAtgEKGYgYKGSKFHRVIKDFMIQGGDiTTGDGTGGVSIYGETFPDE-NFKLKHYGIG 130
Cdd:cd01923   9 GDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGD-PTGTGRGGESIWGKPFKDEfKPNLSHDGRG 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505991  131 WVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSIINS 196
Cdd:cd01923  85 VLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDT 150
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 50-188 1.17e-47

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.


Pssm-ID: 238909 [Multi-domain]  Cd Length: 153  Bit Score: 153.75  E-value: 1.17e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   50 DVGRIVIGLFGKVVPKTVENFVALATGekGYgYKGSKFHRVIKDFMIQGGDiTTGDGTGGVSIYGETFPDENFK-LKHYG 128
Cdd:cd01928   8 NLGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDEFREtLKHDS 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991  129 IGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPL 188
Cdd:cd01928  84 RGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPL 143
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 34-202 1.53e-44

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.


Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 146.34  E-value: 1.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   34 PSVTAKVFFDVRIGDkdvgrIVIGLFGKVVPKTVENFVALATgeKGYgYKGSKFHRVIKDFMIQGGDiTTGDGTGGVSIY 113
Cdd:cd01925   2 PPTTGKVILKTTAGD-----IDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGD-PTGTGTGGESIY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991  114 GETFPDE-NFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIdGMTVVHSIELQ--ATDGHDRPL-- 188
Cdd:cd01925  73 GEPFKDEfHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVT-GDTIYNLLKLAevETDKDERPVyp 151

                       170
                ....*....|....*..
gi 4505991  189 ---TNCSIINSGKIDVK 202
Cdd:cd01925 152 pkiTSVEVLENPFDDIV 168
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 51-193 1.71e-32

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.


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 115.13  E-value: 1.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   51 VGRIVIGLFGKVVPKTVENFVALAtgeKGYGYKGSKFHRVIKDFMIQGGDiTTGDGTGGVSIYGETFPDE--------NF 122
Cdd:cd01921   6 LGDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQLYGRQarffepeiLP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505991  123 KLKHYGIGWVSMANAGPDTNGSQFFITLTKPT-WLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSI 193
Cdd:cd01921  82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGENLdYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 37-189 5.54e-29

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 108.42  E-value: 5.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991    37 TAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKG--------YGYKGSKFHRVIKdfmiQGGDITTGD-GT 107
Cdd:PTZ00221  52 SCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHVDR----NNNIIVLGElDS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   108 GGVSIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRP 187
Cdd:PTZ00221 128 FNVSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRP 207


                 ..
gi 4505991   188 LT 189
Cdd:PTZ00221 208 LL 209
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 48-181 6.24e-21

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.


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 84.80  E-value: 6.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   48 DKDVGRIVIGLFGKVVPKTVENFVALAtgEKGYgYKGSKFHRVIKDFMIQGGDITTG--DGTGGVSIYGEtfPDENFKLK 125
Cdd:cd01920   3 QTSLGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTPDlaQKETLKPIKNE--AGNGLSNT 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505991  126 HYGIgwvSMA-NAGPDTNGSQFFITLTKPTWLD-----GKHVVFGKVIDGMTVVHSIELQAT 181
Cdd:cd01920  78 RGTI---AMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVET 136
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 47-178 1.14e-13

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.


Pssm-ID: 238905  Cd Length: 176  Bit Score: 66.31  E-value: 1.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991   47 GDKDVGRIVIGlfGKVVPKTVENFVALAtgEKGYgYKGSKFHRVIKDFMIQGGD----------ITTG-----------D 105
Cdd:cd01924   4 TDNGTITIVLD--GYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDpqgknpgfpdPETGksrtipleikpE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991  106 GTGgVSIYGETF-----PDENFKLKHYGIGWVSMANAGPDTNG--SQFFITLTKPTW-------LDGKHVVFGKVIDGMT 171
Cdd:cd01924  79 GQK-QPVYGKTLeeagrYDEQPVLPFNAFGAIAMARTEFDPNSasSQFFFLLKDNELtpsrnnvLDGRYAVFGYVTDGLD 157


                ....*..
gi 4505991  172 VVHSIEL 178
Cdd:cd01924 158 ILRELKV 164
PRK10903 PRK10903
peptidylprolyl isomerase A;
51-176 3.79e-12

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 62.55  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991    51 VGRIVIGLFGKVVPKTVENFVALAtgEKGYgYKGSKFHRVIKDFMIQGGDITTG--DGTGGVSIYGETfpDENFKLKHyg 128
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGFTEQmqQKKPNPPIKNEA--DNGLRNTR-- 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4505991   129 iGWVSMA-NAGPDTNGSQFFITLTKPTWLD-GK----HVVFGKVIDGMTVVHSI 176
Cdd:PRK10903 110 -GTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKI 162
PRK10791 PRK10791
peptidylprolyl isomerase B;
52-181 2.11e-09

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 54.46  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505991    52 GRIVIGLFGKVVPKTVENFvaLATGEKGYgYKGSKFHRVIKDFMIQGGDITTG--DGTGGVSIYGETfpdeNFKLKHyGI 129
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNF--LDYCREGF-YNNTIFHRVINGFMIQGGGFEPGmkQKATKEPIKNEA----NNGLKN-TR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505991   130 GWVSMANAG-PDTNGSQFFITLTKPTWLDGK--------HVVFGKVIDGMTVVHSIELQAT 181
Cdd:PRK10791  81 GTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVAT 141
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH