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Conserved domains on  [gi|15227585|ref|NP_181157|]
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Cyclophilin-like peptidyl-prolyl cis-trans isomerase family protein [Arabidopsis thaliana]

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 ...
 13-159 7.34e-96

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 cd01922:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 146  Bit Score: 273.64  E-value: 7.34e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  13 TLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGSKFEDEINKELKHTG 92
Cdd:cd01922   1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227585  93 AGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNtDRPIHEVKILR 159
Cdd:cd01922  81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQT-DRPIDEVKILK 146
 
Name Accession Description Interval E-value
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 13-159 7.34e-96

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: 273.64  E-value: 7.34e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  13 TLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGSKFEDEINKELKHTG 92
Cdd:cd01922   1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227585  93 AGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNtDRPIHEVKILR 159
Cdd:cd01922  81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQT-DRPIDEVKILK 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-164 1.43e-73

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 217.35  E-value: 1.43e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   1 MSARPEgspPEVTLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGEsiyGSKF 80
Cdd:COG0652   1 MKAAPN---PTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  81 EDEINKELKHTgAGILSMANA-GPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRPIHEVKILR 159
Cdd:COG0652  75 PDEFDPGLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIES 153


                ....*
gi 15227585 160 TKVID 164
Cdd:COG0652 154 VTIVE 158
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 14-162 8.00e-64

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: 192.47  E-value: 8.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585    14 LETS-MGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGskFEDEINKELKHTG 92
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFP--IPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227585    93 AGILSMANAG--PNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNtDRPIHEVKILRTKV 162
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 19-147 3.90e-47

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 151.54  E-value: 3.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   19 GPFTVEMYYKHSPRTCRNFLEL------SRRG---YYDNVLFHRIVKDFIVQGGDPT-GTGRGGESIYGSKFEDEiNKEL 88
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALcigdkvGSSGknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFKL 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15227585   89 KHTGAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDN 147
Cdd:PTZ00060 109 KHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS 167
 
Name Accession Description Interval E-value
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 13-159 7.34e-96

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: 273.64  E-value: 7.34e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  13 TLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGSKFEDEINKELKHTG 92
Cdd:cd01922   1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227585  93 AGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNtDRPIHEVKILR 159
Cdd:cd01922  81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQT-DRPIDEVKILK 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 12-162 4.87e-74

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: 218.82  E-value: 4.87e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  12 VTLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGSKFEDEINKELKHT 91
Cdd:cd01923   2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15227585  92 GAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRPIHEVKILRTKV 162
Cdd:cd01923  82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSV 152
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-164 1.43e-73

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 217.35  E-value: 1.43e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   1 MSARPEgspPEVTLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGEsiyGSKF 80
Cdd:COG0652   1 MKAAPN---PTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  81 EDEINKELKHTgAGILSMANA-GPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRPIHEVKILR 159
Cdd:COG0652  75 PDEFDPGLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIES 153


                ....*
gi 15227585 160 TKVID 164
Cdd:COG0652 154 VTIVE 158
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 13-158 2.96e-72

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: 213.86  E-value: 2.96e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  13 TLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGSKFEDEINKELKHTG 92
Cdd:cd01927   1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227585  93 AGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRPIHEVKIL 158
Cdd:cd01927  81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKII 146
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 12-157 7.23e-72

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: 213.07  E-value: 7.23e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  12 VTLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGSKFEDEINKELKHT 91
Cdd:cd01928   3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227585  92 GAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRPIHEVKI 157
Cdd:cd01928  83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRI 148
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 13-158 9.58e-71

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: 209.81  E-value: 9.58e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  13 TLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGeSIYGSKFEDEINKELKHTG 92
Cdd:cd00317   1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227585  93 AGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRPIHEVKIL 158
Cdd:cd00317  80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTIS 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 12-164 4.83e-66

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: 199.12  E-value: 4.83e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  12 VTLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGSKFEDEINKELKHT 91
Cdd:cd01925   8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRLRFN 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227585  92 GAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVcRGMEV--IKRLGSVQTDNTDRPIHEVKILRTKVID 164
Cdd:cd01925  88 RRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV-TGDTIynLLKLAEVETDKDERPVYPPKITSVEVLE 161
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 14-162 8.00e-64

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: 192.47  E-value: 8.00e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585    14 LETS-MGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYGskFEDEINKELKHTG 92
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFP--IPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15227585    93 AGILSMANAG--PNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNtDRPIHEVKILRTKV 162
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCGV 149
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 19-157 1.35e-54

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: 169.75  E-value: 1.35e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  19 GPFTVEMYYKHSPRTCRNFLELS--RRG------YYDNVLFHRIVKDFIVQGGDPT-GTGRGGESIYGSKFEDEiNKELK 89
Cdd:cd01926  15 GRIVMELFADVVPKTAENFRALCtgEKGkggkpfGYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKFPDE-NFKLK 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15227585  90 HTGAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNtDRPIHEVKI 157
Cdd:cd01926  94 HTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVVI 160
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 14-164 1.93e-52

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: 164.44  E-value: 1.93e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  14 LETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESIYG-------SKFEDEINK 86
Cdd:cd01921   2 LETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSqlygrqaRFFEPEILP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15227585  87 ELKHTGAGILSMANAGPNTNGSQFFITLAPQ-PSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRPIHEVKILRTKVID 164
Cdd:cd01921  82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRIKHTHILD 160
PTZ00060 PTZ00060
cyclophilin; Provisional
 19-147 3.90e-47

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 151.54  E-value: 3.90e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   19 GPFTVEMYYKHSPRTCRNFLEL------SRRG---YYDNVLFHRIVKDFIVQGGDPT-GTGRGGESIYGSKFEDEiNKEL 88
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALcigdkvGSSGknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDE-NFKL 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15227585   89 KHTGAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDN 147
Cdd:PTZ00060 109 KHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS 167
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 19-151 3.15e-44

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 144.21  E-value: 3.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   19 GPFTVEMYYKHSPRTCRNFL-----ELSRRGY---YDNVLFHRIVKDFIVQGGD-PTGTGRGGESIYGSKFEDEiNKELK 89
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRqfctgEFRKAGLpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGCVSIYGSKFEDE-NFIAK 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15227585   90 HTGAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVC-RGMEVIKRLGSVQTDNTDRP 151
Cdd:PLN03149 112 HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRP 174
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 13-157 2.60e-29

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: 105.22  E-value: 2.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  13 TLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRGGESiyGSKFEDEINKELKHTg 92
Cdd:cd01920   1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKET--LKPIKNEAGNGLSNT- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15227585  93 AGILSMA-NAGPNTNGSQFFITLAPQPSLD-----GKHTIFGRVCRGMEVIKRLGSVQTDN----TDRPIHEVKI 157
Cdd:cd01920  78 RGTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYSfgsyQDVPVQDVII 152
PRK10903 PRK10903
peptidylprolyl isomerase A;
10-163 1.05e-22

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 89.13  E-value: 1.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   10 PEVTLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRggESIYGSKFEDEINKELK 89
Cdd:PRK10903  29 PHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQ--QKKPNPPIKNEADNGLR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   90 HTgAGILSMA-NAGPNTNGSQFFITLAPQPSLD-GK----HTIFGRVCRGMEVIKRLGSVQTDNT----DRPIHEVKILR 159
Cdd:PRK10903 107 NT-RGTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHDVgpyqNVPSKPVVILS 185


                 ....
gi 15227585  160 TKVI 163
Cdd:PRK10903 186 AKVL 189
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 19-140 7.58e-19

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: 78.64  E-value: 7.58e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585  19 GPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGDPTGTGRG---------------------GESIYG 77
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleikpegqKQPVYG 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15227585  78 SKFE-----DEINKELKHTgAGILSMANA--GPNTNGSQFFITL-------APQPSLDGKHTIFGRVCRGMEVIKRL 140
Cdd:cd01924  87 KTLEeagryDEQPVLPFNA-FGAIAMARTefDPNSASSQFFFLLkdneltpSRNNVLDGRYAVFGYVTDGLDILREL 162
PRK10791 PRK10791
peptidylprolyl isomerase B;
12-162 3.38e-16

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 71.41  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   12 VTLETSMGPFTVEMYYKHSPRTCRNFLELSRRGYYDNVLFHRIVKDFIVQGGdptGTGRG-GESIYGSKFEDEINKELKH 90
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGmKQKATKEPIKNEANNGLKN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   91 TgAGILSMANAG-PNTNGSQFFITLAPQPSLDGK--------HTIFGRVCRGMEVIKRLGSVQTDNT----DRPIHEVKI 157
Cdd:PRK10791  79 T-RGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSgmhqDVPKEDVII 157


                 ....*
gi 15227585  158 LRTKV 162
Cdd:PRK10791 158 ESVTV 162
PTZ00221 PTZ00221
cyclophilin; Provisional
 72-157 9.85e-15

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 69.13  E-value: 9.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227585   72 GESIYGSKFEDEINKElKHTGAGILSMANAGPNTNGSQFFITLAPQPSLDGKHTIFGRVCRGMEVIKRLGSVQTDNTDRP 151
Cdd:PTZ00221 129 NVSSTGTPIADEGYRH-RHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRP 207


                 ....*.
gi 15227585  152 IHEVKI 157
Cdd:PTZ00221 208 LLPVTV 213
 
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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