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Conserved domains on  [gi|398366463|ref|NP_010590|]
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peptidylprolyl isomerase family protein CPR5 [Saccharomyces cerevisiae S288C]

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 ...
 34-194 7.99e-88

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: 256.41  E-value: 7.99e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  34 HKVYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLT-----ISRDPkMGYLNSIFHRVIPNFMIQGGDFTHRSGIGGKS 108
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCtgekgKGGKP-FGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 109 IFGNTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSrNMPVKEV 188
Cdd:cd01926   80 IYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKV 158


                 ....*.
gi 398366463 189 IIVESG 194
Cdd:cd01926  159 VIADCG 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 ...
 34-194 7.99e-88

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: 256.41  E-value: 7.99e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  34 HKVYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLT-----ISRDPkMGYLNSIFHRVIPNFMIQGGDFTHRSGIGGKS 108
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCtgekgKGGKP-FGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 109 IFGNTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSrNMPVKEV 188
Cdd:cd01926   80 IYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKV 158


                 ....*.
gi 398366463 189 IIVESG 194
Cdd:cd01926  159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 35-196 6.91e-74

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 222.03  E-value: 6.91e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  35 KVYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLTI-----SRDPKMGYLNSIFHRVIPNFMIQGGDFTHRSGIGGKSI 109
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIgdkvgSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGESI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 110 FGNTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSrNMPVKEVI 189
Cdd:PTZ00060  97 YGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS-GYPKKPVV 175


                 ....*..
gi 398366463 190 IVESGEL 196
Cdd:PTZ00060 176 VTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 48-195 1.18e-55

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: 174.37  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463   48 GRIVMGLYGLTTPQTVENFYQLTISRdpkmGYLNSIFHRVIPNFMIQGGDFTHRSGiGGKSIFgnTFKDENFDVK-HDKP 126
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCKKG----FYDGTTFHRVIPGFMVQGGDPTGTGG-GGKSIF--PIPDEIFPLLlKHKR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366463  127 GRLSMANRG--KNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDsRNMPVKEVIIVESGE 195
Cdd:pfam00160  80 GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 35-191 1.16e-53

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 169.58  E-value: 1.16e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  35 KVYFDINHGDkqigrIVMGLYGLTTPQTVENFYQLTisrdpKMGYLN-SIFHRVIPNFMIQGGDFThRSGIGGKsifGNT 113
Cdd:COG0652    8 TVTLETNKGD-----IVIELFPDKAPKTVANFVSLA-----KEGFYDgTIFHRVIPGFMIQGGDPT-GTGTGGP---GYT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 114 FKDENF-DVKHdKPGRLSMAN-RGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVIIV 191
Cdd:COG0652   74 IPDEFDpGLKH-KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 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 ...
 34-194 7.99e-88

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: 256.41  E-value: 7.99e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  34 HKVYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLT-----ISRDPkMGYLNSIFHRVIPNFMIQGGDFTHRSGIGGKS 108
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCtgekgKGGKP-FGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 109 IFGNTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSrNMPVKEV 188
Cdd:cd01926   80 IYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKV 158


                 ....*.
gi 398366463 189 IIVESG 194
Cdd:cd01926  159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 35-196 6.91e-74

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 222.03  E-value: 6.91e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  35 KVYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLTI-----SRDPKMGYLNSIFHRVIPNFMIQGGDFTHRSGIGGKSI 109
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIgdkvgSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGESI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 110 FGNTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSrNMPVKEVI 189
Cdd:PTZ00060  97 YGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS-GYPKKPVV 175


                 ....*..
gi 398366463 190 IVESGEL 196
Cdd:PTZ00060 176 VTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 37-190 2.65e-63

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: 193.63  E-value: 2.65e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  37 YFDINhgdkqIGRIVMGLYGLTTPQTVENFYQLTISRdpkmGYLNSIFHRVIPNFMIQGGDFThrSGIGGKSIFGNTFKD 116
Cdd:cd00317    1 TLDTT-----KGRIVIELYGDEAPKTVENFLSLARGG----FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPD 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366463 117 ENFDVK-HDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVII 190
Cdd:cd00317   70 ENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTI 144
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 36-196 4.87e-60

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 186.58  E-value: 4.87e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  36 VYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLTISRDPK----MGYLNSIFHRVIPNFMIQGGDFTHRSGIGGKSIFG 111
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKaglpQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSIYG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 112 NTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVL-DGMDVVHYIENVKTDSRNMPVKEVII 190
Cdd:PLN03149 101 SKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLACVI 180


                 ....*.
gi 398366463 191 VESGEL 196
Cdd:PLN03149 181 SECGEM 186
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 48-191 1.93e-56

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: 176.11  E-value: 1.93e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  48 GRIVMGLYGLTTPQTVENFyqLTISRDpkmGYLNS-IFHRVIPNFMIQGGDFTHrSGIGGKSIFGNTFKDE-NFDVKHDK 125
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENF--TTHARN---GYYNNtIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398366463 126 PGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVIIV 191
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKII 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 48-195 1.18e-55

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: 174.37  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463   48 GRIVMGLYGLTTPQTVENFYQLTISRdpkmGYLNSIFHRVIPNFMIQGGDFTHRSGiGGKSIFgnTFKDENFDVK-HDKP 126
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCKKG----FYDGTTFHRVIPGFMVQGGDPTGTGG-GGKSIF--PIPDEIFPLLlKHKR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398366463  127 GRLSMANRG--KNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDsRNMPVKEVIIVESGE 195
Cdd:pfam00160  80 GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 35-191 1.16e-53

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 169.58  E-value: 1.16e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  35 KVYFDINHGDkqigrIVMGLYGLTTPQTVENFYQLTisrdpKMGYLN-SIFHRVIPNFMIQGGDFThRSGIGGKsifGNT 113
Cdd:COG0652    8 TVTLETNKGD-----IVIELFPDKAPKTVANFVSLA-----KEGFYDgTIFHRVIPGFMIQGGDPT-GTGTGGP---GYT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 114 FKDENF-DVKHdKPGRLSMAN-RGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVIIV 191
Cdd:COG0652   74 IPDEFDpGLKH-KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIE 152
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 36-193 1.16e-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: 161.81  E-value: 1.16e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  36 VYFDINHGDkqigrIVMGLYGLTTPQTVENFYQLTisrdpKMGYLN-SIFHRVIPNFMIQGGDFTHrSGIGGKSIFGNTF 114
Cdd:cd01923    2 VRLHTNKGD-----LNLELHCDKAPKACENFIKLC-----KKGYYDgTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 115 KDE-NFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVIIVES 193
Cdd:cd01923   71 KDEfKPNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDT 150
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 44-191 5.72e-48

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: 154.61  E-value: 5.72e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  44 DKQIGRIVMGLYGLTTPQTVENFYQLTisrdpKMGYLN-SIFHRVIPNFMIQGGDFTHrSGIGGKSIFGNTFKDE-NFDV 121
Cdd:cd01922    3 ETTMGEITLELYWNHAPKTCKNFYELA-----KRGYYNgTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPEL 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 122 KHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSrNMPVKEVIIV 191
Cdd:cd01922   77 KHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQT-DRPIDEVKIL 145
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 48-190 8.30e-45

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: 146.81  E-value: 8.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  48 GRIVMGLYGLTTPQTVENFYQLTISrdpkmGYLN-SIFHRVIPNFMIQGGDFTHrSGIGGKSIFGNTFKDENFD-VKHDK 125
Cdd:cd01928   10 GDIKIELFCDDCPKACENFLALCAS-----GYYNgCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFREtLKHDS 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398366463 126 PGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVII 190
Cdd:cd01928   84 RGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRI 148
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 29-185 6.57e-34

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: 119.38  E-value: 6.57e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  29 DPEITHKVYFDINHGDKQIGrivmgLYGLTTPQTVENFYQLTISrdpkmGYL-NSIFHRVIPNFMIQGGDFTHrSGIGGK 107
Cdd:cd01925    1 EPPTTGKVILKTTAGDIDIE-----LWSKEAPKACRNFIQLCLE-----GYYdNTIFHRVVPGFIIQGGDPTG-TGTGGE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 108 SIFGNTFKDE-NFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVL-DGMDVVHYIENVKTDSRNMPV 185
Cdd:cd01925   70 SIYGEPFKDEfHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIYNLLKLAEVETDKDERPV 149
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 38-190 9.20e-27

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: 100.60  E-value: 9.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  38 FDINHGDkqigrIVMGLYGLTTPQTVENFyqLTISRdpKMGYLNSIFHRVIPNFMIQGGDFThrSGIGGKSIFgNTFKDE 117
Cdd:cd01920    2 FQTSLGD-----IVVELYDDKAPITVENF--LAYVR--KGFYDNTIFHRVISGFVIQGGGFT--PDLAQKETL-KPIKNE 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 118 NFDVKHDKPGRLSMANRGKNTNG-SQFFITTVPCPWLD-----GKHVVFGEVLDGMDVVHYIENVKTDSR----NMPVKE 187
Cdd:cd01920   70 AGNGLSNTRGTIAMARTNAPDSAtSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYSFgsyqDVPVQD 149


                 ...
gi 398366463 188 VII 190
Cdd:cd01920  150 VII 152
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 47-190 1.65e-24

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: 95.10  E-value: 1.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  47 IGRIVMGLYGLTTPQTVENFYQLTisrdpKMGYLN-SIFHRVIPNFMIQGGDFTHrSGIGGKSIFGNT-------FKDE- 117
Cdd:cd01921    6 LGDLVIDLFTDECPLACLNFLKLC-----KLKYYNfCLFYNVQKDFIAQTGDPTG-TGAGGESIYSQLygrqarfFEPEi 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366463 118 NFDVKHDKPGRLSMANRGKNTNGSQFFITTVP-CPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMPVKEVII 190
Cdd:cd01921   80 LPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 33-196 1.32e-21

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 89.54  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  33 THKVYFDINHGDKQIGRIVMGLYGLTTPQTVENFYQLTISR---DP----KMGYLNSIFHRVIPNF-MIQGGDFTHRsgi 104
Cdd:PTZ00221  52 SCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGScgiDTntgvKLDYLYTPVHHVDRNNnIIVLGELDSF--- 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 105 gGKSIFGNTFKDENFDVKHDKPGRLSMANRGKNTNGSQFFITTVPCPWLDGKHVVFGEVLDGMDVVHYIENVKTDSRNMP 184
Cdd:PTZ00221 129 -NVSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRP 207

                        170
                 ....*....|..
gi 398366463 185 VKEVIIVESGEL 196
Cdd:PTZ00221 208 LLPVTVSFCGAL 219
PRK10903 PRK10903
peptidylprolyl isomerase A;
48-190 5.69e-19

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 81.04  E-value: 5.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  48 GRIVMGLYGLTTPQTVENFYQLTISrdpkmGYLN-SIFHRVIPNFMIQGGDFThrSGIGGKSIfGNTFKDENFDVKHDKP 126
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNFVDYVNS-----GFYNnTTFHRVIPGFMIQGGGFT--EQMQQKKP-NPPIKNEADNGLRNTR 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398366463 127 GRLSMANRG-KNTNGSQFFITTVPCPWLD-GK----HVVFGEVLDGMDVVHYIENVKTDS----RNMPVKEVII 190
Cdd:PRK10903 110 GTIAMARTAdKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHDvgpyQNVPSKPVVI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
36-190 1.40e-15

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 71.41  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  36 VYFDINHGDkqigrIVMGLYGLTTPQTVENFyqLTISRDPKmgYLNSIFHRVIPNFMIQGGDFthRSGIGGKSIFGNTFK 115
Cdd:PRK10791   2 VTFHTNHGD-----IVIKTFDDKAPETVKNF--LDYCREGF--YNNTIFHRVINGFMIQGGGF--EPGMKQKATKEPIKN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 116 DENFDVKHDKpGRLSMA-NRGKNTNGSQFFITTVPCPWLDGK--------HVVFGEVLDGMDVVHYIENVKTDSRNM--- 183
Cdd:PRK10791  71 EANNGLKNTR-GTLAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSGMhqd 149


                 ....*...
gi 398366463 184 -PVKEVII 190
Cdd:PRK10791 150 vPKEDVII 157
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 43-174 1.70e-06

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: 46.67  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463  43 GDKQIGRIVmgLYGLTTPQTVENFYQLTisrdpKMGYLNSI-FHRVIPNFMIQGGD-FTHRSGIG--------------- 105
Cdd:cd01924    4 TDNGTITIV--LDGYNAPVTAGNFVDLV-----ERGFYDGMeFHRVEGGFVVQTGDpQGKNPGFPdpetgksrtipleik 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398366463 106 ----GKSIFGNTFK-----DENFDVKHDKPGRLSMANRGKNTNG--SQFFI-------TTVPCPWLDGKHVVFGEVLDGM 167
Cdd:cd01924   77 pegqKQPVYGKTLEeagryDEQPVLPFNAFGAIAMARTEFDPNSasSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGL 156


                 ....*..
gi 398366463 168 DVVHYIE 174
Cdd:cd01924  157 DILRELK 163
 
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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