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Conserved domains on  [gi|18410386|ref|NP_567029|]
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Cyclophilin-like peptidyl-prolyl cis-trans isomerase family protein [Arabidopsis thaliana]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112519)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 59-224 1.16e-108

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: 309.19  E-value: 1.16e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  59 HKVYFDIQINGSPAGRILIGLFGNIVPKTAENFRSLCTGEKGVGnmGKPLYFKGSSFHRIIPGFMIQGGDFTRGDGRGGE 138
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386 139 SIYGDKFADENFKLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANV 218
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                ....*.
gi 18410386 219 IIFASG 224
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 ...
 59-224 1.16e-108

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: 309.19  E-value: 1.16e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  59 HKVYFDIQINGSPAGRILIGLFGNIVPKTAENFRSLCTGEKGVGnmGKPLYFKGSSFHRIIPGFMIQGGDFTRGDGRGGE 138
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386 139 SIYGDKFADENFKLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANV 218
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                ....*.
gi 18410386 219 IIFASG 224
Cdd:cd01926 159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 60-227 5.07e-93

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 270.56  E-value: 5.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386   60 KVYFDIQINGSPAGRILIGLFGNIVPKTAENFRSLCTGEKgVGNMGKPLYFKGSSFHRIIPGFMIQGGDFTRGDGRGGES 139
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGES 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  140 IYGDKFADENFKLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANVI 219
Cdd:PTZ00060  96 IYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVV 175


                 ....*...
gi 18410386  220 IFASGEVS 227
Cdd:PTZ00060 176 VTDCGELQ 183
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 65-220 3.01e-57

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: 178.60  E-value: 3.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386    65 IQINGspAGRILIGLFGNIVPKTAENFRSLCTgeKGvgnmgkplYFKGSSFHRIIPGFMIQGGDFTrGDGRGGESIYGdk 144
Cdd:pfam00160   1 IETNG--LGRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP-- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386   145 FADENF--KLKHtGPGFLSMANSG--PDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANVII 220
Cdd:pfam00160  66 IPDEIFplLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKI 144
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 73-220 7.89e-54

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 169.97  E-value: 7.89e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  73 GRILIGLFGNIVPKTAENFRSLCtgEKGvgnmgkplYFKGSSFHRIIPGFMIQGGDFTrGDGRGGEsiyGDKFADENFK- 151
Cdd:COG0652  16 GDIVIELFPDKAPKTVANFVSLA--KEG--------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPg 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18410386 152 LKHTgPGFLSMANS-GPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSG-VPKANVII 220
Cdd:COG0652  82 LKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEPVVI 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 ...
 59-224 1.16e-108

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: 309.19  E-value: 1.16e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  59 HKVYFDIQINGSPAGRILIGLFGNIVPKTAENFRSLCTGEKGVGnmGKPLYFKGSSFHRIIPGFMIQGGDFTRGDGRGGE 138
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386 139 SIYGDKFADENFKLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANV 218
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                ....*.
gi 18410386 219 IIFASG 224
Cdd:cd01926 159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 60-227 5.07e-93

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 270.56  E-value: 5.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386   60 KVYFDIQINGSPAGRILIGLFGNIVPKTAENFRSLCTGEKgVGNMGKPLYFKGSSFHRIIPGFMIQGGDFTRGDGRGGES 139
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGES 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  140 IYGDKFADENFKLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANVI 219
Cdd:PTZ00060  96 IYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVV 175


                 ....*...
gi 18410386  220 IFASGEVS 227
Cdd:PTZ00060 176 VTDCGELQ 183
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 61-226 9.83e-76

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 226.64  E-value: 9.83e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386   61 VYFDIQINGSPAGRILIGLFGNIVPKTAENFRSLCTGEKGVGnmGKPLYFKGSSFHRIIPGFMIQGGDFTRGDGRGGESI 140
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKA--GLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  141 YGDKFADENFKLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVL-SGMEVVRKIE--AQGQDSGvPKAN 217
Cdd:PLN03149  99 YGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIEnvATGPNNR-PKLA 177


                 ....*....
gi 18410386  218 VIIFASGEV 226
Cdd:PLN03149 178 CVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 62-220 2.13e-62

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: 191.32  E-value: 2.13e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  62 YFDIQIngspaGRILIGLFGNIVPKTAENFRSLCTGEkgvgnmgkplYFKGSSFHRIIPGFMIQGGDFTRGDGrgGESIY 141
Cdd:cd00317   1 TLDTTK-----GRIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGP 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386 142 GDKFADENFKLK-HTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQG-QDSGVPKANVI 219
Cdd:cd00317  64 GYKFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVT 143


                .
gi 18410386 220 I 220
Cdd:cd00317 144 I 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 65-220 3.01e-57

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: 178.60  E-value: 3.01e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386    65 IQINGspAGRILIGLFGNIVPKTAENFRSLCTgeKGvgnmgkplYFKGSSFHRIIPGFMIQGGDFTrGDGRGGESIYGdk 144
Cdd:pfam00160   1 IETNG--LGRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP-- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386   145 FADENF--KLKHtGPGFLSMANSG--PDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANVII 220
Cdd:pfam00160  66 IPDEIFplLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKI 144
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 73-220 7.89e-54

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 169.97  E-value: 7.89e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  73 GRILIGLFGNIVPKTAENFRSLCtgEKGvgnmgkplYFKGSSFHRIIPGFMIQGGDFTrGDGRGGEsiyGDKFADENFK- 151
Cdd:COG0652  16 GDIVIELFPDKAPKTVANFVSLA--KEG--------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPg 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18410386 152 LKHTgPGFLSMANS-GPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSG-VPKANVII 220
Cdd:COG0652  82 LKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEPVVI 151
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 73-220 3.75e-51

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: 162.70  E-value: 3.75e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  73 GRILIGLFGNIVPKTAENFRSLCTgekgvgnMGkplYFKGSSFHRIIPGFMIQGGDFTrGDGRGGESIYGDKFADE-NFK 151
Cdd:cd01922   7 GEITLELYWNHAPKTCKNFYELAK-------RG---YYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPE 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18410386 152 LKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQGQDSGVPKANVII 220
Cdd:cd01922  76 LKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 73-205 1.10e-48

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: 156.47  E-value: 1.10e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  73 GRILIGLFGNIVPKTAENFRSLCtgekgvgnmgKPLYFKGSSFHRIIPGFMIQGGDFTrGDGRGGESIYGDKFADE-NFK 151
Cdd:cd01927   7 GDIHIRLFPEEAPKTVENFTTHA----------RNGYYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 18410386 152 LKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIE 205
Cdd:cd01927  76 LKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIE 129
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 73-220 3.38e-46

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: 150.64  E-value: 3.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  73 GRILIGLFGNIVPKTAENFRSLCtgEKGvgnmgkplYFKGSSFHRIIPGFMIQGGDFTrGDGRGGESIYGDKFADE-NFK 151
Cdd:cd01923   9 GDLNLELHCDKAPKACENFIKLC--KKG--------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPN 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386 152 LKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIE-AQGQDSGVPKANVII 220
Cdd:cd01923  78 LSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMEnVPDPGTDRPKEEIKI 147
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 73-220 5.20e-45

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known.


Pssm-ID: 238909 [Multi-domain]  Cd Length: 153  Bit Score: 147.58  E-value: 5.20e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  73 GRILIGLFGNIVPKTAENFRSLCTGEkgvgnmgkplYFKGSSFHRIIPGFMIQGGDFTrGDGRGGESIYGDKFADEnFK- 151
Cdd:cd01928  10 GDIKIELFCDDCPKACENFLALCASG----------YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDE-FRe 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18410386 152 -LKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEA-QGQDSGVPKANVII 220
Cdd:cd01928  78 tLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKlPVDKKYRPLEEIRI 148
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 72-194 4.39e-38

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: 130.16  E-value: 4.39e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  72 AGRILIGLFGNIVPKTAENFRSLCTGEkgvgnmgkplYFKGSSFHRIIPGFMIQGGDFTrGDGRGGESIYGDKFADE-NF 150
Cdd:cd01925  14 AGDIDIELWSKEAPKACRNFIQLCLEG----------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHS 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 18410386 151 KLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKV 194
Cdd:cd01925  83 RLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV 126
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 73-220 1.85e-28

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: 105.12  E-value: 1.85e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  73 GRILIGLFGNIVPKTAENFRSLCtgekgvgnmgKPLYFKGSSFHRIIPGFMIQGGDFTrGDGRGGESIYGDK-------F 145
Cdd:cd01921   7 GDLVIDLFTDECPLACLNFLKLC----------KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqarfF 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18410386 146 ADE-NFKLKHTGPGFLSMANSGPDSNGSQFFIT-TVTTSWLDGHHVVFGKVLSGMEVVRKI-EAQGQDSGVPKANVII 220
Cdd:cd01921  76 EPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 55-220 1.84e-26

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 102.25  E-value: 1.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386   55 EGVTHKVYFDIQINGSPAGRILIGLFGNIVPKTAENFRSLCTGEKGV-GNMGKPLYFKGSSFHRIipgfmiqggDFTRGD 133
Cdd:PTZ00221  49 EQNSCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdTNTGVKLDYLYTPVHHV---------DRNNNI 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  134 GRGGE------SIYGDKFADENFKLKHTGPGFLSMANSGPDSNGSQFFITTVTTSWLDGHHVVFGKVLSGMEVVRKIEAQ 207
Cdd:PTZ00221 120 IVLGEldsfnvSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESL 199

                        170
                 ....*....|....
gi 18410386  208 GQDS-GVPKANVII 220
Cdd:PTZ00221 200 PLDDvGRPLLPVTV 213
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 72-220 1.52e-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: 84.42  E-value: 1.52e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  72 AGRILIGLFGNIVPKTAENFRSLCtgEKGVgnmgkplyFKGSSFHRIIPGFMIQGGDFTRGdgrGGESIYGDKFADE-NF 150
Cdd:cd01920   6 LGDIVVELYDDKAPITVENFLAYV--RKGF--------YDNTIFHRVISGFVIQGGGFTPD---LAQKETLKPIKNEaGN 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386 151 KLKHTGpGFLSMANSG-PDSNGSQFFITTVTTSWLD-----GHHVVFGKVLSGMEVVRKIE-----AQGQDSGVPKANVI 219
Cdd:cd01920  73 GLSNTR-GTIAMARTNaPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAgvetySFGSYQDVPVQDVI 151


                .
gi 18410386 220 I 220
Cdd:cd01920 152 I 152
PRK10903 PRK10903
peptidylprolyl isomerase A;
72-226 1.66e-16

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 74.49  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386   72 AGRILIGLFGNIVPKTAENFRSLCtgekgvgNMGkplYFKGSSFHRIIPGFMIQGGDFTrgdgrggesiygdkfadENFK 151
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYV-------NSG---FYNNTTFHRVIPGFMIQGGGFT-----------------EQMQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  152 LKHTGP--------------GFLSMA-NSGPDSNGSQFFITTVTTSWLDgH------HVVFGKVLSGMEVVRKI-EAQGQ 209
Cdd:PRK10903  90 QKKPNPpikneadnglrntrGTIAMArTADKDSATSQFFINVADNAFLD-HgqrdfgYAVFGKVVKGMDVADKIsQVPTH 168

                        170       180
                 ....*....|....*....|.
gi 18410386  210 DSGvPKANV----IIFASGEV 226
Cdd:PRK10903 169 DVG-PYQNVpskpVVILSAKV 188
PRK10791 PRK10791
peptidylprolyl isomerase B;
73-220 2.95e-14

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 67.94  E-value: 2.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386   73 GRILIGLFGNIVPKTAENFRSLCTGEkgvgnmgkplYFKGSSFHRIIPGFMIQGGDFTRGdgrGGESIYGDKFADE-NFK 151
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCREG----------FYNNTIFHRVINGFMIQGGGFEPG---MKQKATKEPIKNEaNNG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  152 LKHTgPGFLSMANSG-PDSNGSQFFITTVTTSWLDGH--------HVVFGKVLSGMEVVRKIEA-----QGQDSGVPKAN 217
Cdd:PRK10791  76 LKNT-RGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGvatgrSGMHQDVPKED 154


                 ...
gi 18410386  218 VII 220
Cdd:PRK10791 155 VII 157
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 57-206 3.93e-11

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: 59.76  E-value: 3.93e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386  57 VTHKVYFDIQINGSPAgriliglfgnivPKTAENFRSLCtgEKGVgnmgkplyFKGSSFHRIIPGFMIQGGD-FTRGDGR 135
Cdd:cd01924   3 ATDNGTITIVLDGYNA------------PVTAGNFVDLV--ERGF--------YDGMEFHRVEGGFVVQTGDpQGKNPGF 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18410386 136 G-------------------GESIYGDKFA-----DENFKLKHTGPGFLSMANS--GPDSNGSQFFI-------TTVTTS 182
Cdd:cd01924  61 PdpetgksrtipleikpegqKQPVYGKTLEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNN 140

                       170       180
                ....*....|....*....|....
gi 18410386 183 WLDGHHVVFGKVLSGMEVVRKIEA 206
Cdd:cd01924 141 VLDGRYAVFGYVTDGLDILRELKV 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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