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Conserved domains on  [gi|15226560|ref|NP_182254|]
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Cyclophilin-like peptidyl-prolyl cis-trans isomerase family protein [Arabidopsis thaliana]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10085251)

cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0006457|GO:0003755|GO:0000413
PubMed:  14731520|15998457|15353287

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 81-223 8.28e-41

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: 136.62  E-value: 8.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  81 TLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKdWALDRK----NIDTSLKHE 156
Cdd:cd00317   1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKfpdeNFPLKYHHR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226560 157 EFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMS 223
Cdd:cd00317  80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
 
Name Accession Description Interval E-value
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 81-223 8.28e-41

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: 136.62  E-value: 8.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  81 TLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKdWALDRK----NIDTSLKHE 156
Cdd:cd00317   1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKfpdeNFPLKYHHR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226560 157 EFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMS 223
Cdd:cd00317  80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 71-229 4.30e-35

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 122.20  E-value: 4.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  71 MKNVDLPRfATLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSA---EFDAVKDWALDrk 147
Cdd:COG0652   1 MKAAPNPT-VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTgtgTGGPGYTIPDE-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560 148 nIDTSLKHEEFMVGTPKAKN-EQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSVTL 226
Cdd:COG0652  78 -FDPGLKHKRGTLAMARAQGpNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTI 156


                ...
gi 15226560 227 LQD 229
Cdd:COG0652 157 VED 159
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 85-225 1.73e-31

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: 112.73  E-value: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560    85 GKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKDWALDRKN--IDTSLKHEEFMVGT 162
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDeiFPLLLKHKRGALSM 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226560   163 PKAKNE--QGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQyQPKSPIEIMSVT 225
Cdd:pfam00160  85 ANTGPApnSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPVKILSCG 148
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 87-221 6.63e-14

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 67.55  E-value: 6.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560   87 GSVTIELFKDTAPNVVDQFMKFCQDGY--------FKGFLFSRVVKHFVIQAGDSAEFD-----AVKDWALDRKNIDTsl 153
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFLKGDgtgcvSIYGSKFEDENFIA-- 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  154 KHE-EFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRV-SKGQDVVQEIEEVETDDQYQPKSPIEI 221
Cdd:PLN03149 111 KHTgPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVlGDGLLVVRKIENVATGPNNRPKLACVI 180
 
Name Accession Description Interval E-value
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 81-223 8.28e-41

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: 136.62  E-value: 8.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  81 TLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKdWALDRK----NIDTSLKHE 156
Cdd:cd00317   1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKfpdeNFPLKYHHR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226560 157 EFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMS 223
Cdd:cd00317  80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 71-229 4.30e-35

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 122.20  E-value: 4.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  71 MKNVDLPRfATLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSA---EFDAVKDWALDrk 147
Cdd:COG0652   1 MKAAPNPT-VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTgtgTGGPGYTIPDE-- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560 148 nIDTSLKHEEFMVGTPKAKN-EQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSVTL 226
Cdd:COG0652  78 -FDPGLKHKRGTLAMARAQGpNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTI 156


                ...
gi 15226560 227 LQD 229
Cdd:COG0652 157 VED 159
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 85-225 1.73e-31

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: 112.73  E-value: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560    85 GKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKDWALDRKN--IDTSLKHEEFMVGT 162
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDeiFPLLLKHKRGALSM 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15226560   163 PKAKNE--QGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQyQPKSPIEIMSVT 225
Cdd:pfam00160  85 ANTGPApnSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPVKILSCG 148
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 81-224 4.38e-28

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: 103.70  E-value: 4.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  81 TLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGD--SAEFDAVKDWALDRKN-IDTSLKHEE 157
Cdd:cd01927   1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDptGDGTGGESIWGKEFEDeFSPSLKHDR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226560 158 -FMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSV 224
Cdd:cd01927  81 pYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIINI 148
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 79-229 1.04e-23

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: 92.86  E-value: 1.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  79 FATLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGD---------SAEFDAVKDwaldrkNI 149
Cdd:cd01923   1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDptgtgrggeSIWGKPFKD------EF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560 150 DTSLKHEE----FMVGTPKAKNeqgGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSVT 225
Cdd:cd01923  75 KPNLSHDGrgvlSMANSGPNTN---GSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTS 151


                ....
gi 15226560 226 LLQD 229
Cdd:cd01923 152 VFVD 155
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 81-226 6.14e-21

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: 85.57  E-value: 6.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  81 TLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGDSA------------EFDavkdwaldrKN 148
Cdd:cd01928   4 TLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTgtgkggesiwgkKFE---------DE 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226560 149 IDTSLKHEEF-MVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYQPKSPIEIMSVTL 226
Cdd:cd01928  75 FRETLKHDSRgVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKDVTI 153
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 80-227 1.44e-18

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: 79.70  E-value: 1.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  80 ATLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGD---------SAEFDAVKDwaldrkNID 150
Cdd:cd01925   8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDptgtgtggeSIYGEPFKD------EFH 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560 151 TSLK-HEEFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSkGQDV--VQEIEEVETDDQYQPKSPIEIMSVTLL 227
Cdd:cd01925  82 SRLRfNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVT-GDTIynLLKLAEVETDKDERPVYPPKITSVEVL 160
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 81-222 1.19e-17

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: 76.42  E-value: 1.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  81 TLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGD---------SAEFDAVKDwaldrkNIDT 151
Cdd:cd01922   1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDptgtgrggaSIYGKKFED------EIHP 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226560 152 SLKHE-EFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQyQPKSPIEIM 222
Cdd:cd01922  75 ELKHTgAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTD-RPIDEVKIL 145
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 81-224 6.08e-15

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: 69.39  E-value: 6.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  81 TLDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAG-------DSAEFDAVKDWAldrkniDTSL 153
Cdd:cd01920   1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGgftpdlaQKETLKPIKNEA------GNGL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560 154 KHEEFMVGTPK-AKNEQGGFEFFIvsaQIKDlNEKL---------TVFGRVSKGQDVVQEIEEVET--DDQYQ--PKSPI 219
Cdd:cd01920  75 SNTRGTIAMARtNAPDSATSQFFI---NLKD-NASLdyqneqwgyTVFGEVTEGMDVVDKIAGVETysFGSYQdvPVQDV 150


                ....*
gi 15226560 220 EIMSV 224
Cdd:cd01920 151 IIESA 155
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 87-222 2.92e-14

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: 68.05  E-value: 2.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  87 GSVTIELFKDTAPNVVDQFMKFC--------QDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKDWAL-DRKNIDTS--LKH 155
Cdd:cd01926  15 GRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIyGEKFPDENfkLKH 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226560 156 E-EFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETdDQYQPKSPIEIM 222
Cdd:cd01926  95 TgPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS-GNGKPKKKVVIA 161
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 87-221 6.63e-14

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 67.55  E-value: 6.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560   87 GSVTIELFKDTAPNVVDQFMKFCQDGY--------FKGFLFSRVVKHFVIQAGDSAEFD-----AVKDWALDRKNIDTsl 153
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFLKGDgtgcvSIYGSKFEDENFIA-- 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  154 KHE-EFMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRV-SKGQDVVQEIEEVETDDQYQPKSPIEI 221
Cdd:PLN03149 111 KHTgPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVlGDGLLVVRKIENVATGPNNRPKLACVI 180
PTZ00060 PTZ00060
cyclophilin; Provisional
 87-221 2.42e-13

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 66.02  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560   87 GSVTIELFKDTAPNVVDQFMKFC---------QDGYFKGFLFSRVVKHFVIQAGDSAEFDAVKDWAL-DRKNIDT--SLK 154
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGESIyGRKFTDEnfKLK 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15226560  155 HEE-FMVGTPKAKNEQGGFEFFIVSAQIKDLNEKLTVFGRVSKGQDVVQEIEEVETDDQYqPKSPIEI 221
Cdd:PTZ00060 110 HDQpGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGY-PKKPVVV 176
PRK10903 PRK10903
peptidylprolyl isomerase A;
82-227 2.63e-12

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 63.32  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560   82 LDTGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGD-SAEFDAVKDWALDRKNIDTSLKHEEFMV 160
Cdd:PRK10903  33 LTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGfTEQMQQKKPNPPIKNEADNGLRNTRGTI 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226560  161 GTPK-AKNEQGGFEFFIVSAQIKDLNE-----KLTVFGRVSKGQDVVQEIEEVETDD--QYQ--PKSPIEIMSVTLL 227
Cdd:PRK10903 113 AMARtADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHDvgPYQnvPSKPVVILSAKVL 189
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 84-206 2.12e-03

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: 37.81  E-value: 2.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560  84 TGKGSVTIELFKDTAPNVVDQFMKFCQDGYFKGFLFSRVVKHFVIQAGD-------------------------SAEFDA 138
Cdd:cd01924   4 TDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDpqgknpgfpdpetgksrtipleikpEGQKQP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226560 139 VKDWALDRKNIDTS----LKHEEFMVGTPKAKNEQ--GGFEFFI-------VSAQIKDLNEKLTVFGRVSKGQDVVQEIE 205
Cdd:cd01924  84 VYGKTLEEAGRYDEqpvlPFNAFGAIAMARTEFDPnsASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163


                .
gi 15226560 206 E 206
Cdd:cd01924 164 V 164
 
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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