NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|4758950|ref|NP_000933|]
View 

peptidyl-prolyl cis-trans isomerase B precursor [Homo sapiens]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112519)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it 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:0016018|GO:0006457|GO:0003755|GO:0000413
SCOP:  4000390

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 45-203 2.08e-109

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: 310.73  E-value: 2.08e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   45 KVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKG-----FGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIY 119
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950  120 GERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSrDKPLKDVII 199
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVVI 160


                ....
gi 4758950  200 ADCG 203
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 ...
 45-203 2.08e-109

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: 310.73  E-value: 2.08e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   45 KVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKG-----FGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIY 119
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950  120 GERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSrDKPLKDVII 199
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVVI 160


                ....
gi 4758950  200 ADCG 203
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 45-205 1.70e-77

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 230.50  E-value: 1.70e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950    45 KVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGE------KGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSI 118
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGESI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   119 YGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSrDKPLKDVI 198
Cdd:PTZ00060  97 YGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS-GYPKKPVV 175


                 ....*..
gi 4758950   199 IADCGKI 205
Cdd:PTZ00060 176 VTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 58-203 5.84e-60

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: 184.77  E-value: 5.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950     58 GRVIFGLFGKTVPKTVDNFVALATgeKGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKSIYGerFPDENF--KLKHyGP 135
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFplLLKH-KR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950    136 GWVSMANAG--KDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDsRDKPLKDVIIADCG 203
Cdd:pfam00160  80 GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 43-199 4.15e-59

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 183.06  E-value: 4.15e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   43 TVKVYFDLrigdeDVGRVIFGLFGKTVPKTVDNFVALAtgEKGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKsiyGER 122
Cdd:COG0652   6 NPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYT 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758950  123 FPDENFKLKHYGPGWVSMANA-GKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVII 199
Cdd:COG0652  74 IPDEFDPGLKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVI 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 ...
 45-203 2.08e-109

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: 310.73  E-value: 2.08e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   45 KVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKG-----FGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIY 119
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950  120 GERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSrDKPLKDVII 199
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVVI 160


                ....
gi 4758950  200 ADCG 203
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 45-205 1.70e-77

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 230.50  E-value: 1.70e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950    45 KVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGE------KGFGYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSI 118
Cdd:PTZ00060  17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGESI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   119 YGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSrDKPLKDVI 198
Cdd:PTZ00060  97 YGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS-GYPKKPVV 175


                 ....*..
gi 4758950   199 IADCGKI 205
Cdd:PTZ00060 176 VTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 46-205 4.30e-73

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 219.71  E-value: 4.30e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950    46 VYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGE---KGF--GYKNSKFHRVIKDFMIQGGDFTRGDGTGGKSIYG 120
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSIYG 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   121 ERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVL-EGMEVVRKVESTKTDSRDKPLKDVII 199
Cdd:PLN03149 101 SKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLACVI 180


                 ....*.
gi 4758950   200 ADCGKI 205
Cdd:PLN03149 181 SECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 56-201 2.93e-68

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: 205.96  E-value: 2.93e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   56 DVGRVIFGLFGKTVPKTVDNFVALATGEkgfGYKNSKFHRVIKDFMIQGGDFTRGDGtgGKSIYGERFPDENFKLK-HYG 134
Cdd:cd00317   5 TKGRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPDENFPLKyHHR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758950  135 PGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIAD 201
Cdd:cd00317  80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 58-203 5.84e-60

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: 184.77  E-value: 5.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950     58 GRVIFGLFGKTVPKTVDNFVALATgeKGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKSIYGerFPDENF--KLKHyGP 135
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFplLLKH-KR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950    136 GWVSMANAG--KDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDsRDKPLKDVIIADCG 203
Cdd:pfam00160  80 GALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 43-199 4.15e-59

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 183.06  E-value: 4.15e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   43 TVKVYFDLrigdeDVGRVIFGLFGKTVPKTVDNFVALAtgEKGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKsiyGER 122
Cdd:COG0652   6 NPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYT 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4758950  123 FPDENFKLKHYGPGWVSMANA-GKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVII 199
Cdd:COG0652  74 IPDEFDPGLKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVI 151
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 64-199 3.89e-56

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: 174.96  E-value: 3.89e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   64 LFGKTVPKTVDNFVALAtgEKGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKSIYGERFPDE-NFKLKHYGPGWVSMAN 142
Cdd:cd01927  13 LFPEEAPKTVENFTTHA--RNGY-YNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLKHDRPYTLSMAN 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4758950  143 AGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVII 199
Cdd:cd01927  89 AGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKI 145
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 54-199 2.79e-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: 165.40  E-value: 2.79e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   54 DEDVGRVIFGLFGKTVPKTVDNFVALATgeKGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKSIYGERFPDE-NFKLKH 132
Cdd:cd01922   3 ETTMGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPELKH 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758950  133 YGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSrDKPLKDVII 199
Cdd:cd01922  79 TGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQT-DRPIDEVKI 144
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 64-201 4.98e-50

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: 159.89  E-value: 4.98e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   64 LFGKTVPKTVDNFVALAtgEKGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKSIYGERFPDE-NFKLKHYGPGWVSMAN 142
Cdd:cd01923  15 LHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPNLSHDGRGVLSMAN 90

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 4758950  143 AGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIAD 201
Cdd:cd01923  91 SGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 56-201 5.18e-47

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: 152.21  E-value: 5.18e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   56 DVGRVIFGLFGKTVPKTVDNFVALATGekGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKSIYGERFPDENFK-LKHYG 134
Cdd:cd01928   8 NLGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREtLKHDS 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758950  135 PGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVIIAD 201
Cdd:cd01928  84 RGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 40-211 5.10e-41

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: 137.48  E-value: 5.10e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   40 PKVTVKVYFDLRIGDEDVGrvifgLFGKTVPKTVDNFVALATgeKGFgYKNSKFHRVIKDFMIQGGDFTrGDGTGGKSIY 119
Cdd:cd01925   2 PPTTGKVILKTTAGDIDIE-----LWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPT-GTGTGGESIY 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950  120 GERFPDE-NFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVlEGMEV--VRKVESTKTDSRDKPLKD 196
Cdd:cd01925  73 GEPFKDEfHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV-TGDTIynLLKLAEVETDKDERPVYP 151

                       170
                ....*....|....*.
gi 4758950  197 VIIADCgkiEV-EKPF 211
Cdd:cd01925 152 PKITSV---EVlENPF 164
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 57-199 8.49e-30

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: 108.20  E-value: 8.49e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   57 VGRVIFGLFGKTVPKTVDNFVALAtgeKGFGYKNSKFHRVIKDFMIQGGDFTrGDGTGGKSIYGE------RF--PDENF 128
Cdd:cd01921   6 LGDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQlygrqaRFfePEILP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758950  129 KLKHYGPGWVSMANAGKDTNGSQFFITTVK-TAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKPLKDVII 199
Cdd:cd01921  82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 43-210 1.90e-26

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 101.87  E-value: 1.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950    43 TVKVYFDLRIGDEDVGRVIFGLFGKTVPKTVDNFVALATGEKG--------FGYKNSKFHRV-IKDFMIQGGDFTrgdgT 113
Cdd:PTZ00221  52 SCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHVdRNNNIIVLGELD----S 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   114 GGKSIYGERFPDENFKLKHYGPGWVSMANAGKDTNGSQFFITTVKTAWLDGKHVVFGKVLEGMEVVRKVESTKTDSRDKP 193
Cdd:PTZ00221 128 FNVSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRP 207

                        170
                 ....*....|....*..
gi 4758950   194 LKDVIIADCGKIEVEKP 210
Cdd:PTZ00221 208 LLPVTVSFCGALTGEKP 224
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 54-201 1.09e-25

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: 97.51  E-value: 1.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   54 DEDVGRVIFGLFGKTVPKTVDNFVALAtgEKGFgYKNSKFHRVIKDFMIQGGDFTRG--DGTGGKSIYGErfPDENFKLK 131
Cdd:cd01920   3 QTSLGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTPDlaQKETLKPIKNE--AGNGLSNT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950  132 HygpGWVSMA-NAGKDTNGSQFFITTVKTAWLD-----GKHVVFGKVLEGMEVVRKVESTKTDSR----DKPLKDVIIAD 201
Cdd:cd01920  78 R---GTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYSFgsyqDVPVQDVIIES 154
PRK10903 PRK10903
peptidylprolyl isomerase A;
57-199 1.13e-17

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 77.58  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950    57 VGRVIFGLFGKTVPKTVDNFVALAtgEKGFgYKNSKFHRVIKDFMIQGGDFTRG--DGTGGKSIYGErfPDENFKLKHyg 134
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGFTEQmqQKKPNPPIKNE--ADNGLRNTR-- 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758950   135 pGWVSMA-NAGKDTNGSQFFITTVKTAWLD-GK----HVVFGKVLEGMEVVRKVESTKTDS----RDKPLKDVII 199
Cdd:PRK10903 110 -GTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHDvgpyQNVPSKPVVI 183
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 66-183 1.96e-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: 65.54  E-value: 1.96e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950   66 GKTVPKTVDNFVALAtgEKGFgYKNSKFHRVIKDFMIQGGD-FTRGDG-----TG--------------GKSIYGERF-- 123
Cdd:cd01924  15 GYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDpQGKNPGfpdpeTGksrtipleikpegqKQPVYGKTLee 91

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4758950  124 ---PDENFKLKHYGPGWVSMANAGKDTNG--SQFFI-------TTVKTAWLDGKHVVFGKVLEGMEVVRKVE 183
Cdd:cd01924  92 agrYDEQPVLPFNAFGAIAMARTEFDPNSasSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
PRK10791 PRK10791
peptidylprolyl isomerase B;
58-199 1.16e-12

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 63.32  E-value: 1.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758950    58 GRVIFGLFGKTVPKTVDNFvaLATGEKGFgYKNSKFHRVIKDFMIQGGDFTrgDGTGGKSIYGERFPDENFKLKHyGPGW 137
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNF--LDYCREGF-YNNTIFHRVINGFMIQGGGFE--PGMKQKATKEPIKNEANNGLKN-TRGT 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4758950   138 VSMANAGKDTNGS-QFFITTVKTAWLDGK--------HVVFGKVLEGMEVVRKVESTKTDS----RDKPLKDVII 199
Cdd:PRK10791  83 LAMARTQAPHSATaQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRsgmhQDVPKEDVII 157
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH