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Conserved domains on  [gi|145329985|ref|NP_001077978|]
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cyclophilin 5 [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 ...
 32-187 1.07e-98

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: 282.61  E-value: 1.07e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  32 HKVYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEKGVGksGKPLHYKGSKFHRIIPSFMIQGGDFTHGNGMGGE 111
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 112 SIYGQKFADENFKLKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKV 181
Cdd:cd01926   79 SIYGEKFPDENFKLKHTgpgllsmanaGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                 ....*.
gi 145329985 182 VIADSG 187
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 ...
 32-187 1.07e-98

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: 282.61  E-value: 1.07e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  32 HKVYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEKGVGksGKPLHYKGSKFHRIIPSFMIQGGDFTHGNGMGGE 111
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 112 SIYGQKFADENFKLKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKV 181
Cdd:cd01926   79 SIYGEKFPDENFKLKHTgpgllsmanaGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                 ....*.
gi 145329985 182 VIADSG 187
Cdd:cd01926  159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 33-189 1.66e-91

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 265.17  E-value: 1.66e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  33 KVYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEKgVGKSGKPLHYKGSKFHRIIPSFMIQGGDFTHGNGMGGES 112
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGES 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 113 IYGQKFADENFKLKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKVV 182
Cdd:PTZ00060  96 IYGRKFTDENFKLKHDqpgllsmanaGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVV 175


                 ....*..
gi 145329985 183 IADSGEL 189
Cdd:PTZ00060 176 VTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 44-188 5.38e-51

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: 161.27  E-value: 5.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985   44 SAGRVVIGLFGKAVPKTAENFRALCTgeKGvgksgkplHYKGSKFHRIIPSFMIQGGDFTHGNGmGGESIYGqkFADENF 123
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPTGTGG-GGKSIFP--IPDEIF 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145329985  124 --KLKHT-----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKVVIADSGE 188
Cdd:pfam00160  72 plLLKHKrgalsmantgpAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 44-183 5.21e-48

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 153.79  E-value: 5.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  44 SAGRVVIGLFGKAVPKTAENFRALCtgekgvgKSGkplHYKGSKFHRIIPSFMIQGGDFThGNGMGGEsiyGQKFADENF 123
Cdd:COG0652   14 NKGDIVIELFPDKAPKTVANFVSLA-------KEG---FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145329985 124 K-LKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSG-TPKSKVVI 183
Cdd:COG0652   80 PgLKHKrgtlamaraqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEPVVI 151
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 32-187 1.07e-98

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: 282.61  E-value: 1.07e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  32 HKVYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEKGVGksGKPLHYKGSKFHRIIPSFMIQGGDFTHGNGMGGE 111
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 112 SIYGQKFADENFKLKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKV 181
Cdd:cd01926   79 SIYGEKFPDENFKLKHTgpgllsmanaGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                 ....*.
gi 145329985 182 VIADSG 187
Cdd:cd01926  159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 33-189 1.66e-91

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 265.17  E-value: 1.66e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  33 KVYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEKgVGKSGKPLHYKGSKFHRIIPSFMIQGGDFTHGNGMGGES 112
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGES 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 113 IYGQKFADENFKLKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKVV 182
Cdd:PTZ00060  96 IYGRKFTDENFKLKHDqpgllsmanaGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVV 175


                 ....*..
gi 145329985 183 IADSGEL 189
Cdd:PTZ00060 176 VTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 34-189 7.94e-62

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 190.05  E-value: 7.94e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  34 VYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEkgVGKSGKPLHYKGSKFHRIIPSFMIQGGDFTHGNGMGGESI 113
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 114 YGQKFADENFKLKHTGP----------DTNGSQFFITTVTTSWLDGRHVVFGKVV-QGMDVVYKIE--AEGkQSGTPKSK 180
Cdd:PLN03149  99 YGSKFEDENFIAKHTGPgllsmansgpNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIEnvATG-PNNRPKLA 177


                 ....*....
gi 145329985 181 VVIADSGEL 189
Cdd:PLN03149 178 CVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 46-185 4.81e-55

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: 171.29  E-value: 4.81e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  46 GRVVIGLFGKAVPKTAENFRALCTGEkgvgksgkplHYKGSKFHRIIPSFMIQGGDFTHGNGmgGESIYGQKFADENFKL 125
Cdd:cd00317    7 GRIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPDENFPL 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145329985 126 K-----------HTGPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIE-AEGKQSGTPKSKVVIAD 185
Cdd:cd00317   75 KyhhrrgtlsmaNAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIErGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 44-188 5.38e-51

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: 161.27  E-value: 5.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985   44 SAGRVVIGLFGKAVPKTAENFRALCTgeKGvgksgkplHYKGSKFHRIIPSFMIQGGDFTHGNGmGGESIYGqkFADENF 123
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPTGTGG-GGKSIFP--IPDEIF 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145329985  124 --KLKHT-----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKVVIADSGE 188
Cdd:pfam00160  72 plLLKHKrgalsmantgpAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 44-183 5.21e-48

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 153.79  E-value: 5.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  44 SAGRVVIGLFGKAVPKTAENFRALCtgekgvgKSGkplHYKGSKFHRIIPSFMIQGGDFThGNGMGGEsiyGQKFADENF 123
Cdd:COG0652   14 NKGDIVIELFPDKAPKTVANFVSLA-------KEG---FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFD 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145329985 124 K-LKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSG-TPKSKVVI 183
Cdd:COG0652   80 PgLKHKrgtlamaraqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEPVVI 151
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 44-183 5.77e-42

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: 138.05  E-value: 5.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  44 SAGRVVIGLFGKAVPKTAENFRALCTgeKGvgksgkplHYKGSKFHRIIPSFMIQGGDFThGNGMGGESIYGQKFADE-N 122
Cdd:cd01922    5 TMGEITLELYWNHAPKTCKNFYELAK--RG--------YYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiH 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145329985 123 FKLKHTG----------PDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEAEGKQSGTPKSKVVI 183
Cdd:cd01922   74 PELKHTGagilsmanagPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 44-168 4.77e-41

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: 135.67  E-value: 4.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  44 SAGRVVIGLFGKAVPKTAENFRALCtgekgvgKSGkplHYKGSKFHRIIPSFMIQGGDFThGNGMGGESIYGQKFADE-N 122
Cdd:cd01927    5 TKGDIHIRLFPEEAPKTVENFTTHA-------RNG---YYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfS 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145329985 123 FKLKH----------TGPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIE 168
Cdd:cd01927   74 PSLKHdrpytlsmanAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIE 129
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 46-186 1.35e-37

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: 127.15  E-value: 1.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  46 GRVVIGLFGKAVPKTAENFRALCtgEKGvgksgkplHYKGSKFHRIIPSFMIQGGDFThGNGMGGESIYGQKFADE-NFK 124
Cdd:cd01923    9 GDLNLELHCDKAPKACENFIKLC--KKG--------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPN 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145329985 125 LKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIE-AEGKQSGTPKSKVVIADS 186
Cdd:cd01923   78 LSHDgrgvlsmansGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMEnVPDPGTDRPKEEIKIEDT 150
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 46-185 4.02e-37

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: 126.01  E-value: 4.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  46 GRVVIGLFGKAVPKTAENFRALCTgekgvgkSGkplHYKGSKFHRIIPSFMIQGGDFThGNGMGGESIYGQKFADENFK- 124
Cdd:cd01928   10 GDIKIELFCDDCPKACENFLALCA-------SG---YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREt 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145329985 125 LKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEA-EGKQSGTPKSKVVIAD 185
Cdd:cd01928   79 LKHDsrgvvsmannGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKlPVDKKYRPLEEIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 44-158 4.48e-33

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: 116.30  E-value: 4.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  44 SAGRVVIGLFGKAVPKTAENFRALCTGEkgvgksgkplHYKGSKFHRIIPSFMIQGGDFThGNGMGGESIYGQKFADE-N 122
Cdd:cd01925   13 TAGDIDIELWSKEAPKACRNFIQLCLEG----------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfH 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 145329985 123 FKLK----------HTGPDTNGSQFFITTVTTSWLDGRHVVFGKVV 158
Cdd:cd01925   82 SRLRfnrrglvgmaNAGDDSNGSQFFFTLDKADELNNKHTLFGKVT 127
PTZ00221 PTZ00221
cyclophilin; Provisional
 31-189 1.06e-24

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 96.48  E-value: 1.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  31 THKVYFDVEIDGKSAGRVVIGLFGKAVPKTAENFRALCTGEKGV-GKSGKPLHYKGSKFHRIipsfmiqggDFTHGNGMG 109
Cdd:PTZ00221  52 SCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdTNTGVKLDYLYTPVHHV---------DRNNNIIVL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 110 GE------SIYGQKFADENFKLKHT----------GPDTNGSQFFITTVTTSWLDGRHVVFGKVVQGMDVVYKIEA-EGK 172
Cdd:PTZ00221 123 GEldsfnvSSTGTPIADEGYRHRHTerglltmiseGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESlPLD 202

                        170
                 ....*....|....*..
gi 145329985 173 QSGTPKSKVVIADSGEL 189
Cdd:PTZ00221 203 DVGRPLLPVTVSFCGAL 219
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 44-167 1.18e-22

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: 88.94  E-value: 1.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  44 SAGRVVIGLFGKAVPKTAENFRALCtgekgvgksgKPLHYKGSKFHRIIPSFMIQGGDFThGNGMGGESIYGQK------ 117
Cdd:cd01921    5 TLGDLVIDLFTDECPLACLNFLKLC----------KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqar 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145329985 118 -FADE-NFKLKHT----------GPDTNGSQFFIT-TVTTSWLDGRHVVFGKVVQGMDVVYKI 167
Cdd:cd01921   74 fFEPEiLPLLKHSkkgtvsmvnaGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKI 136
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 44-168 3.15e-20

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: 82.49  E-value: 3.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  44 SAGRVVIGLFGKAVPKTAENFRALCtgEKGvgksgkplHYKGSKFHRIIPSFMIQGGDFT-------HGNGMGGESIYGQ 116
Cdd:cd01920    5 SLGDIVVELYDDKAPITVENFLAYV--RKG--------FYDNTIFHRVISGFVIQGGGFTpdlaqkeTLKPIKNEAGNGL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145329985 117 KFADENFKL-KHTGPDTNGSQFFITTVTTSWLD-----GRHVVFGKVVQGMDVVYKIE 168
Cdd:cd01920   75 SNTRGTIAMaRTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIA 132
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-190 2.20e-14

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 67.95  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985   1 MAKASFILLGTLFLFGAI--ASIQAKEDlkevTHKVYFdveidgKSAGRVVIGLFGKAVPKTAENFRALCTgekgvgkSG 78
Cdd:PRK10903   1 MFKSTLAAMAAVFALSALspAALAAKGD----PHVLLT------TSAGNIELELNSQKAPVSVKNFVDYVN-------SG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  79 kplHYKGSKFHRIIPSFMIQGGDFTH-------GNGMGGESIYGQKFADENFKLKHTG-PDTNGSQFFITTVTTSWLD-G 149
Cdd:PRK10903  64 ---FYNNTTFHRVIPGFMIQGGGFTEqmqqkkpNPPIKNEADNGLRNTRGTIAMARTAdKDSATSQFFINVADNAFLDhG 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 145329985 150 R----HVVFGKVVQGMDVVYKI-----EAEGKQSGTPKSKVVIADSGELP 190
Cdd:PRK10903 141 QrdfgYAVFGKVVKGMDVADKIsqvptHDVGPYQNVPSKPVVILSAKVLP 190
PRK10791 PRK10791
peptidylprolyl isomerase B;
46-183 1.13e-12

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 62.93  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  46 GRVVIGLFGKAVPKTAENFRALCtgekgvgKSGkplHYKGSKFHRIIPSFMIQGGDFThgNGMGGESIYGQKFADENFKL 125
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYC-------REG---FYNNTIFHRVINGFMIQGGGFE--PGMKQKATKEPIKNEANNGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 126 KHT----------GPDTNGSQFFITTVTTSWLDGR--------HVVFGKVVQGMDVVYKIEA-----EGKQSGTPKSKVV 182
Cdd:PRK10791  77 KNTrgtlamartqAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGvatgrSGMHQDVPKEDVI 156


                 .
gi 145329985 183 I 183
Cdd:PRK10791 157 I 157
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 29-169 2.64e-09

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: 53.99  E-value: 2.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985  29 EVTHKVYFDVEIDGKSAgrvviglfgkavPKTAENFRALCtgEKGVgksgkplhYKGSKFHRIIPSFMIQGGDFTHGNGM 108
Cdd:cd01924    2 EATDNGTITIVLDGYNA------------PVTAGNFVDLV--ERGF--------YDGMEFHRVEGGFVVQTGDPQGKNPG 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145329985 109 G--------------------GESIYGQKFA-----DENFKL----------KHTGPDTNG--SQFFI-------TTVTT 144
Cdd:cd01924   60 FpdpetgksrtipleikpegqKQPVYGKTLEeagryDEQPVLpfnafgaiamARTEFDPNSasSQFFFllkdnelTPSRN 139

                        170       180
                 ....*....|....*....|....*
gi 145329985 145 SWLDGRHVVFGKVVQGMDVVYKIEA 169
Cdd:cd01924  140 NVLDGRYAVFGYVTDGLDILRELKV 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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