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Conserved domains on  [gi|19113324|ref|NP_596532|]
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cyclophilin family peptidyl-prolyl cis-trans isomerase Cyp4 [Schizosaccharomyces pombe]

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

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 27-186 2.05e-97

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: 279.53  E-value: 2.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  27 DTVYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGEKG-----FGYEGSIFHRVIPNFMIQGGDITKGDGTGGKSI 101
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324 102 YGSRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNrDKPLEDVK 181
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVV 159


                ....*
gi 19113324 182 IIKSG 186
Cdd:cd01926 160 IADCG 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 ...
 27-186 2.05e-97

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: 279.53  E-value: 2.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  27 DTVYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGEKG-----FGYEGSIFHRVIPNFMIQGGDITKGDGTGGKSI 101
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324 102 YGSRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNrDKPLEDVK 181
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVV 159


                ....*
gi 19113324 182 IIKSG 186
Cdd:cd01926 160 IADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 9-189 1.43e-73

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 220.10  E-value: 1.43e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324    9 LFTLF-FGLISANRGPKVtdtvYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGE------KGFGYEGSIFHRVIP 81
Cdd:PTZ00060   1 FFKLFsQSFPEMSKRPKV----FFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324   82 NFMIQGGDITKGDGTGGKSIYGSRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDI 161
Cdd:PTZ00060  77 QFMCQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEV 156

                        170       180
                 ....*....|....*....|....*...
gi 19113324  162 VKKISKAETDNrDKPLEDVKIIKSGQLS 189
Cdd:PTZ00060 157 VRAMEKEGTQS-GYPKKPVVVTDCGELQ 183
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 26-184 1.26e-63

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 193.85  E-value: 1.26e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  26 TDTVYFDLQQGDeflgrVTIGLFGKTVPKTAENFRALAtgEKGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKsiyGSR 105
Cdd:COG0652   6 NPTVTLETNKGD-----IVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324 106 FPDENFK-LSHQRpGLLSMANA-GPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKII 183
Cdd:COG0652  74 IPDEFDPgLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152


                .
gi 19113324 184 K 184
Cdd:COG0652 153 S 153
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 40-186 4.51e-62

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: 189.77  E-value: 4.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324    40 LGRVTIGLFGKTVPKTAENFRALATgeKGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKSIYGsrFPDENF--KLSHQR 117
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFplLLKHKR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113324   118 pGLLSMANAG--PDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNrDKPLEDVKIIKSG 186
Cdd:pfam00160  80 -GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCG 148
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 27-186 2.05e-97

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: 279.53  E-value: 2.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  27 DTVYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGEKG-----FGYEGSIFHRVIPNFMIQGGDITKGDGTGGKSI 101
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324 102 YGSRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNrDKPLEDVK 181
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVV 159


                ....*
gi 19113324 182 IIKSG 186
Cdd:cd01926 160 IADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 9-189 1.43e-73

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 220.10  E-value: 1.43e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324    9 LFTLF-FGLISANRGPKVtdtvYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGE------KGFGYEGSIFHRVIP 81
Cdd:PTZ00060   1 FFKLFsQSFPEMSKRPKV----FFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324   82 NFMIQGGDITKGDGTGGKSIYGSRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDI 161
Cdd:PTZ00060  77 QFMCQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEV 156

                        170       180
                 ....*....|....*....|....*...
gi 19113324  162 VKKISKAETDNrDKPLEDVKIIKSGQLS 189
Cdd:PTZ00060 157 VRAMEKEGTQS-GYPKKPVVVTDCGELQ 183
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 41-184 2.19e-66

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: 200.57  E-value: 2.19e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  41 GRVTIGLFGKTVPKTAENFRALATGEkgfGYEGSIFHRVIPNFMIQGGDITkgDGTGGKSIYGSRFPDENFKLS-HQRPG 119
Cdd:cd00317   7 GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENFPLKyHHRRG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113324 120 LLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKIIK 184
Cdd:cd00317  82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 29-188 2.02e-64

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 196.98  E-value: 2.02e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324   29 VYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGE---KGF--GYEGSIFHRVIPNFMIQGGDITKGDGTGGKSIYG 103
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSIYG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  104 SRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVL-SGYDIVKKISKAETDNRDKPLEDVKI 182
Cdd:PLN03149 101 SKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLACVI 180


                 ....*.
gi 19113324  183 IKSGQL 188
Cdd:PLN03149 181 SECGEM 186
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 26-184 1.26e-63

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 193.85  E-value: 1.26e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  26 TDTVYFDLQQGDeflgrVTIGLFGKTVPKTAENFRALAtgEKGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKsiyGSR 105
Cdd:COG0652   6 NPTVTLETNKGD-----IVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYT 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324 106 FPDENFK-LSHQRpGLLSMANA-GPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKII 183
Cdd:COG0652  74 IPDEFDPgLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152


                .
gi 19113324 184 K 184
Cdd:COG0652 153 S 153
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 40-186 4.51e-62

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: 189.77  E-value: 4.51e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324    40 LGRVTIGLFGKTVPKTAENFRALATgeKGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKSIYGsrFPDENF--KLSHQR 117
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFplLLKHKR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19113324   118 pGLLSMANAG--PDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNrDKPLEDVKIIKSG 186
Cdd:pfam00160  80 -GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCG 148
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 40-183 1.93e-61

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: 188.05  E-value: 1.93e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  40 LGRVTIGLFGKTVPKTAENFRALAtgEKGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKSIYGSRFPDE-NFKLSHQRP 118
Cdd:cd01927   6 KGDIHIRLFPEEAPKTVENFTTHA--RNGY-YNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLKHDRP 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113324 119 GLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKII 183
Cdd:cd01927  82 YTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKII 146
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 40-184 2.35e-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: 165.01  E-value: 2.35e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  40 LGRVTIGLFGKTVPKTAENFRALATgeKGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKSIYGSRFPDE-NFKLSHQRP 118
Cdd:cd01922   6 MGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPELKHTGA 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113324 119 GLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNrDKPLEDVKIIK 184
Cdd:cd01922  82 GILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQT-DRPIDEVKILK 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 40-183 4.75e-48

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: 154.50  E-value: 4.75e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  40 LGRVTIGLFGKTVPKTAENFRALAtgEKGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKSIYGSRFPDE-NFKLSHQRP 118
Cdd:cd01923   8 KGDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPNLSHDGR 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113324 119 GLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKII 183
Cdd:cd01923  84 GVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIE 148
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 40-182 4.13e-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: 151.82  E-value: 4.13e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  40 LGRVTIGLFGKTVPKTAENFRALATGekGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKSIYGSRFPDENFK-LSHQRP 118
Cdd:cd01928   9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREtLKHDSR 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113324 119 GLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKI 182
Cdd:cd01928  85 GVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRI 148
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 40-183 5.94e-45

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: 146.73  E-value: 5.94e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  40 LGRVTIGLFGKTVPKTAENFRALATgeKGFgYEGSIFHRVIPNFMIQGGDITkGDGTGGKSIYGSRFPDE-NFKLSHQRP 118
Cdd:cd01925  14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHSRLRFNRR 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19113324 119 GLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVL--SGYDIVkKISKAETDNRDKPLEDVKII 183
Cdd:cd01925  90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgdTIYNLL-KLAEVETDKDERPVYPPKIT 155
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 40-182 3.80e-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: 113.98  E-value: 3.80e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  40 LGRVTIGLFGKTVPKTAENFRALAtgeKGFGYEGSIFHRVIPNFMIQGGDITkGDGTGGKSIYG------SRF--PDENF 111
Cdd:cd01921   6 LGDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSqlygrqARFfePEILP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19113324 112 KLSHQRPGLLSMANAGPDSNGSQFFITTVK-TPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKPLEDVKI 182
Cdd:cd01921  82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 40-182 5.69e-26

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: 97.90  E-value: 5.69e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  40 LGRVTIGLFGKTVPKTAENFraLATGEKGFgYEGSIFHRVIPNFMIQGGDITKG--DGTGGKSIYGsrfpDENFKLSHQR 117
Cdd:cd01920   6 LGDIVVELYDDKAPITVENF--LAYVRKGF-YDNTIFHRVISGFVIQGGGFTPDlaQKETLKPIKN----EAGNGLSNTR 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113324 118 pGLLSMA-NAGPDSNGSQFFITTVKTPWLD-----GHHVVFGEVLSGYDIVKKISKAETDNR----DKPLEDVKI 182
Cdd:cd01920  79 -GTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYSFgsyqDVPVQDVII 152
PTZ00221 PTZ00221
cyclophilin; Provisional
 26-191 2.62e-22

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 90.70  E-value: 2.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324   26 TDTVYFDLQQGDEFLGRVTIGLFGKTVPKTAENFRALATGEKG--------FGYEGSIFHRVIPNF-MIQGGDITkgdgT 96
Cdd:PTZ00221  52 SCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHVDRNNnIIVLGELD----S 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324   97 GGKSIYGSRFPDENFKLSHQRPGLLSMANAGPDSNGSQFFITTVKTPWLDGHHVVFGEVLSGYDIVKKISKAETDNRDKP 176
Cdd:PTZ00221 128 FNVSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRP 207

                        170
                 ....*....|....*
gi 19113324  177 LEDVKIIKSGQLSQE 191
Cdd:PTZ00221 208 LLPVTVSFCGALTGE 222
PRK10903 PRK10903
peptidylprolyl isomerase A;
41-172 6.18e-17

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 74.88  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324   41 GRVTIGLFGKTVPKTAENFraLATGEKGFgYEGSIFHRVIPNFMIQGGDITKgdGTGGKSIYGSRFPDENFKLSHQRpGL 120
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNF--VDYVNSGF-YNNTTFHRVIPGFMIQGGGFTE--QMQQKKPNPPIKNEADNGLRNTR-GT 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113324  121 LSMA-NAGPDSNGSQFFITTVKTPWLDgH------HVVFGEVLSGYDIVKKISKAETDN 172
Cdd:PRK10903 112 IAMArTADKDSATSQFFINVADNAFLD-HgqrdfgYAVFGKVVKGMDVADKISQVPTHD 169
PRK10791 PRK10791
peptidylprolyl isomerase B;
41-182 3.50e-14

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 67.17  E-value: 3.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324   41 GRVTIGLFGKTVPKTAENFraLATGEKGFgYEGSIFHRVIPNFMIQGGDITKgdGTGGKSIYGSRFPDENFKLSHQRpGL 120
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNF--LDYCREGF-YNNTIFHRVINGFMIQGGGFEP--GMKQKATKEPIKNEANNGLKNTR-GT 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113324  121 LSMANAG-PDSNGSQFFITTVKTPWLDGH--------HVVFGEVLSGYDIVKKISKAETD----NRDKPLEDVKI 182
Cdd:PRK10791  83 LAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGrsgmHQDVPKEDVII 157
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 41-165 1.33e-12

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: 63.23  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113324  41 GRVTIGLFGKTVPKTAENFRALAtgEKGFgYEGSIFHRVIPNFMIQGGDITKGDGTG--------------------GKS 100
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDPQGKNPGFpdpetgksrtipleikpegqKQP 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19113324 101 IYGSRF-----PDENFKLSHQRPGLLSMANA--GPDSNGSQFFI-------TTVKTPWLDGHHVVFGEVLSGYDIVKKI 165
Cdd:cd01924  84 VYGKTLeeagrYDEQPVLPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILREL 162
 
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.
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