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Conserved domains on  [gi|20130249|ref|NP_611695|]
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uncharacterized protein Dmel_CG2852, isoform A [Drosophila melanogaster]

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 ...
 30-188 6.94e-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: 281.07  E-value: 6.94e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  30 KVFFDITIGGEPAGRIEIGLFGKTVPKTVENFKELALKPQGE-----GYKGSKFHRIIKDFMIQGGDFTKGDGTGGRSIY 104
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKggkpfGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249 105 GERFEDENFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDaRDRPVKDVVI 184
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVVI 160


                ....
gi 20130249 185 ANSG 188
Cdd:cd01926 161 ADCG 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 ...
 30-188 6.94e-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: 281.07  E-value: 6.94e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  30 KVFFDITIGGEPAGRIEIGLFGKTVPKTVENFKELALKPQGE-----GYKGSKFHRIIKDFMIQGGDFTKGDGTGGRSIY 104
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKggkpfGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249 105 GERFEDENFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDaRDRPVKDVVI 184
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVVI 160


                ....
gi 20130249 185 ANSG 188
Cdd:cd01926 161 ADCG 164
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 31-190 1.92e-74

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 222.40  E-value: 1.92e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249   31 VFFDITIGGEPAGRIEIGLFGKTVPKTVENFKEL-------ALKPQGegYKGSKFHRIIKDFMIQGGDFTKGDGTGGRSI 103
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFctgefrkAGLPQG--YKGCQFHRVIKDFMIQGGDFLKGDGTGCVSI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  104 YGERFEDENFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKIL-SGMNVVRQIENSATDARDRPVKDV 182
Cdd:PLN03149  99 YGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLAC 178


                 ....*...
gi 20130249  183 VIANSGTL 190
Cdd:PLN03149 179 VISECGEM 186
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 35-189 5.92e-58

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: 179.37  E-value: 5.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249    35 ITIGGepAGRIEIGLFGKTVPKTVENFKELALKPqgeGYKGSKFHRIIKDFMIQGGDFTkgdGTGGRSIYGERFEDENF- 113
Cdd:pfam00160   1 IETNG--LGRIVIELFGDKAPKTVENFLQLCKKG---FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20130249   114 -KLKHyGAGWLSMANAG--KDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDaRDRPVKDVVIANSGT 189
Cdd:pfam00160  73 lLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 43-184 4.68e-56

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 174.97  E-value: 4.68e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  43 GRIEIGLFGKTVPKTVENFKELALKPQgegYKGSKFHRIIKDFMIQGGDFTkGDGTGGRsiyGERFEDENFKLKHYGAGW 122
Cdd:COG0652  16 GDIVIELFPDKAPKTVANFVSLAKEGF---YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPGLKHKRGT 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20130249 123 LSMANA-GKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDARDRPVKDVVI 184
Cdd:COG0652  89 LAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVI 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 ...
 30-188 6.94e-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: 281.07  E-value: 6.94e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  30 KVFFDITIGGEPAGRIEIGLFGKTVPKTVENFKELALKPQGE-----GYKGSKFHRIIKDFMIQGGDFTKGDGTGGRSIY 104
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKggkpfGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249 105 GERFEDENFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDaRDRPVKDVVI 184
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVVI 160


                ....
gi 20130249 185 ANSG 188
Cdd:cd01926 161 ADCG 164
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 31-190 1.92e-74

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 222.40  E-value: 1.92e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249   31 VFFDITIGGEPAGRIEIGLFGKTVPKTVENFKEL-------ALKPQGegYKGSKFHRIIKDFMIQGGDFTKGDGTGGRSI 103
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFctgefrkAGLPQG--YKGCQFHRVIKDFMIQGGDFLKGDGTGCVSI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  104 YGERFEDENFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKIL-SGMNVVRQIENSATDARDRPVKDV 182
Cdd:PLN03149  99 YGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLAC 178


                 ....*...
gi 20130249  183 VIANSGTL 190
Cdd:PLN03149 179 VISECGEM 186
PTZ00060 PTZ00060
cyclophilin; Provisional
 30-190 4.79e-70

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 211.24  E-value: 4.79e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249   30 KVFFDITIGGEPAGRIEIGLFGKTVPKTVENFKELAL--KPQGEG----YKGSKFHRIIKDFMIQGGDFTKGDGTGGRSI 103
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIgdKVGSSGknlhYKGSIFHRIIPQFMCQGGDITNHNGTGGESI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  104 YGERFEDENFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDArDRPVKDVV 183
Cdd:PTZ00060  97 YGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS-GYPKKPVV 175


                 ....*..
gi 20130249  184 IANSGTL 190
Cdd:PTZ00060 176 VTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 32-186 7.62e-65

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: 196.72  E-value: 7.62e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  32 FFDITIGgepagRIEIGLFGKTVPKTVENFKELAlkpQGEGYKGSKFHRIIKDFMIQGGDFTkGDGTGGrSIYGERFEDE 111
Cdd:cd00317   1 TLDTTKG-----RIVIELYGDEAPKTVENFLSLA---RGGFYDGTTFHRVIPGFMIQGGDPT-GTGGGG-SGPGYKFPDE 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20130249 112 NFKLK-HYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDARDRPVKDVVIAN 186
Cdd:cd00317  71 NFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 35-189 5.92e-58

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: 179.37  E-value: 5.92e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249    35 ITIGGepAGRIEIGLFGKTVPKTVENFKELALKPqgeGYKGSKFHRIIKDFMIQGGDFTkgdGTGGRSIYGERFEDENF- 113
Cdd:pfam00160   1 IETNG--LGRIVIELFGDKAPKTVENFLQLCKKG---FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20130249   114 -KLKHyGAGWLSMANAG--KDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDaRDRPVKDVVIANSGT 189
Cdd:pfam00160  73 lLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 43-184 4.68e-56

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 174.97  E-value: 4.68e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  43 GRIEIGLFGKTVPKTVENFKELALKPQgegYKGSKFHRIIKDFMIQGGDFTkGDGTGGRsiyGERFEDENFKLKHYGAGW 122
Cdd:COG0652  16 GDIVIELFPDKAPKTVANFVSLAKEGF---YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPGLKHKRGT 88

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20130249 123 LSMANA-GKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDARDRPVKDVVI 184
Cdd:COG0652  89 LAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVI 151
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 43-186 3.28e-54

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: 169.95  E-value: 3.28e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  43 GRIEIGLFGKTVPKTVENFKELAlkpQGEGYKGSKFHRIIKDFMIQGGDFTkGDGTGGRSIYGERFEDE-NFKLKHYGAG 121
Cdd:cd01927   7 GDIHIRLFPEEAPKTVENFTTHA---RNGYYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLKHDRPY 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130249 122 WLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDARDRPVKDVVIAN 186
Cdd:cd01927  83 TLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIIN 147
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 43-184 7.62e-52

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: 163.86  E-value: 7.62e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  43 GRIEIGLFGKTVPKTVENFKELALKPQgegYKGSKFHRIIKDFMIQGGDFTkGDGTGGRSIYGERFEDE-NFKLKHYGAG 121
Cdd:cd01922   7 GEITLELYWNHAPKTCKNFYELAKRGY---YNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPELKHTGAG 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20130249 122 WLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDaRDRPVKDVVI 184
Cdd:cd01922  83 ILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKI 144
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 43-184 4.63e-48

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: 154.50  E-value: 4.63e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  43 GRIEIGLFGKTVPKTVENFKELALKPQgegYKGSKFHRIIKDFMIQGGDFTkGDGTGGRSIYGERFEDE-NFKLKHYGAG 121
Cdd:cd01923   9 GDLNLELHCDKAPKACENFIKLCKKGY---YDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPNLSHDGRG 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20130249 122 WLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDARDRPVKDVVI 184
Cdd:cd01923  85 VLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKI 147
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 43-184 2.36e-44

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: 144.89  E-value: 2.36e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  43 GRIEIGLFGKTVPKTVENFkeLALKPQGEgYKGSKFHRIIKDFMIQGGDFTkGDGTGGRSIYGERFEDENFK-LKHYGAG 121
Cdd:cd01928  10 GDIKIELFCDDCPKACENF--LALCASGY-YNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREtLKHDSRG 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20130249 122 WLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDARDRPVKDVVI 184
Cdd:cd01928  86 VVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRI 148
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 25-179 2.42e-43

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: 142.88  E-value: 2.42e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  25 PKVTEKVFFDITiggepAGRIEIGLFGKTVPKTVENFKELALkpqgEG-YKGSKFHRIIKDFMIQGGDFTkGDGTGGRSI 103
Cdd:cd01925   2 PPTTGKVILKTT-----AGDIDIELWSKEAPKACRNFIQLCL----EGyYDNTIFHRVVPGFIIQGGDPT-GTGTGGESI 71

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20130249 104 YGERFEDE-NFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKIL--SGMNVVRqIENSATDARDRPV 179
Cdd:cd01925  72 YGEPFKDEfHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgdTIYNLLK-LAEVETDKDERPV 149
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 43-184 2.86e-29

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: 106.66  E-value: 2.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  43 GRIEIGLFGKTVPKTVENFKELA-LKpqgeGYKGSKFHRIIKDFMIQGGDFTkGDGTGGRSIYGER-------FEDE-NF 113
Cdd:cd01921   7 GDLVIDLFTDECPLACLNFLKLCkLK----YYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqarfFEPEiLP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20130249 114 KLKHYGAGWLSMANAGKDTNGSQFFITTKQ-TSWLDGRHVVFGKILSGMNVVRQIENSATDARDRPVKDVVI 184
Cdd:cd01921  82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 28-190 9.82e-22

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 89.16  E-value: 9.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249   28 TEKVFFDITIGGEPAGRIEIGLFGKTVPKTVENFKELAlkpQGEG-----------YKGSKFHRI-IKDFMIQGGDFTkg 95
Cdd:PTZ00221  52 SCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALI---TGSCgidtntgvkldYLYTPVHHVdRNNNIIVLGELD-- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249   96 dgTGGRSIYGERFEDENFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDAR 175
Cdd:PTZ00221 127 --SFNVSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDV 204

                        170
                 ....*....|....*
gi 20130249  176 DRPVKDVVIANSGTL 190
Cdd:PTZ00221 205 GRPLLPVTVSFCGAL 219
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 42-184 8.18e-21

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: 8.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  42 AGRIEIGLFGKTVPKTVENFKELALKpqGEgYKGSKFHRIIKDFMIQGGDFTKG--DGTGGRSIYGErfedENFKLKHyG 119
Cdd:cd01920   6 LGDIVVELYDDKAPITVENFLAYVRK--GF-YDNTIFHRVISGFVIQGGGFTPDlaQKETLKPIKNE----AGNGLSN-T 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20130249 120 AGWLSMA-NAGKDTNGSQFFITTKQTSWLD-----GRHVVFGKILSGMNVVRQIENSATDAR----DRPVKDVVI 184
Cdd:cd01920  78 RGTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYSFgsyqDVPVQDVII 152
PRK10903 PRK10903
peptidylprolyl isomerase A;
42-191 3.27e-17

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 76.03  E-value: 3.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249   42 AGRIEIGLFGKTVPKTVENFKELAlkpqGEG-YKGSKFHRIIKDFMIQGGDFTKgDGTGGRSIYGERFEDENfKLKHYgA 120
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYV----NSGfYNNTTFHRVIPGFMIQGGGFTE-QMQQKKPNPPIKNEADN-GLRNT-R 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  121 GWLSMA-NAGKDTNGSQFFITTKQTSWLD-GR----HVVFGKILSGMNVVRQIENSATDA----RDRPVKDVVIANSGTL 190
Cdd:PRK10903 110 GTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHDvgpyQNVPSKPVVILSAKVL 189


                 .
gi 20130249  191 P 191
Cdd:PRK10903 190 P 190
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 43-168 3.52e-13

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: 64.77  E-value: 3.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249  43 GRIEIGLFGKTVPKTVENFKELALKpqgEGYKGSKFHRIIKDFMIQGGD-FTKGDG-----TG--------------GRS 102
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLVER---GFYDGMEFHRVEGGFVVQTGDpQGKNPGfpdpeTGksrtipleikpegqKQP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249 103 IYGERFE-----DENFKLKHYGAGWLSMANAGKDTNG--SQFFI-------TTKQTSWLDGRHVVFGKILSGMNVVRQIE 168
Cdd:cd01924  84 VYGKTLEeagryDEQPVLPFNAFGAIAMARTEFDPNSasSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
PRK10791 PRK10791
peptidylprolyl isomerase B;
43-186 9.80e-10

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 55.23  E-value: 9.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20130249   43 GRIEIGLFGKTVPKTVENFKELAlkpQGEGYKGSKFHRIIKDFMIQGGDFTKgdGTGGRSIYGERFEDENFKLKHyGAGW 122
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYC---REGFYNNTIFHRVINGFMIQGGGFEP--GMKQKATKEPIKNEANNGLKN-TRGT 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20130249  123 LSMANAGKDTNGS-QFFITTKQTSWLDGR--------HVVFGKILSGMNVVRQIENSATDA----RDRPVKDVVIAN 186
Cdd:PRK10791  83 LAMARTQAPHSATaQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRsgmhQDVPKEDVIIES 159
 
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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