NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|5031987|ref|NP_005720|]
View 

peptidyl-prolyl cis-trans isomerase F, mitochondrial precursor [Homo sapiens]

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

 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 ...
 46-204 5.48e-116

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: 326.91  E-value: 5.48e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   46 PLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI 120
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987  121 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVI 200
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 5031987  201 TDCG 204
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 ...
 46-204 5.48e-116

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: 326.91  E-value: 5.48e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   46 PLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI 120
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987  121 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVI 200
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 5031987  201 TDCG 204
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 45-207 6.06e-97

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 279.42  E-value: 6.06e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987    45 NPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGE------KGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGK 118
Cdd:PTZ00060  15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   119 SIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKI 198
Cdd:PTZ00060  95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPV 174


                 ....*....
gi 5031987   199 VITDCGQLS 207
Cdd:PTZ00060 175 VVTDCGELQ 183
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 59-204 2.06e-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: 185.54  E-value: 2.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987     59 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFTNHNGtGGKSIYGsrFPDENF--TLKHVg 136
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPTGTGG-GGKSIFP--IPDEIFplLLKHK- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987    137 PGVLSMANAG--PNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCG 204
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 45-186 8.77e-56

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 174.20  E-value: 8.77e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   45 NPLVYLDVDangkpLGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKsiyGSR 124
Cdd:COG0652   6 NPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GYT 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031987  125 FPDENFT-LKHVgPGVLSMANA-GPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIES 186
Cdd:COG0652  74 IPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAA 136
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 46-204 5.48e-116

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: 326.91  E-value: 5.48e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   46 PLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI 120
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987  121 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVI 200
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 5031987  201 TDCG 204
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 45-207 6.06e-97

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 279.42  E-value: 6.06e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987    45 NPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGE------KGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGK 118
Cdd:PTZ00060  15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   119 SIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKI 198
Cdd:PTZ00060  95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPV 174


                 ....*....
gi 5031987   199 VITDCGQLS 207
Cdd:PTZ00060 175 VVTDCGELQ 183
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 45-206 3.46e-74

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 222.02  E-value: 3.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987    45 NPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGE---KGF--GYKGSTFHRVIPSFMCQAGDFTNHNGTGGKS 119
Cdd:PLN03149  18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   120 IYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHV-KEGMDVVKKIESFGSKSGRTSK-K 197
Cdd:PLN03149  98 IYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVlGDGLLVVRKIENVATGPNNRPKlA 177


                 ....*....
gi 5031987   198 IVITDCGQL 206
Cdd:PLN03149 178 CVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 60-202 2.62e-66

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: 200.57  E-value: 2.62e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   60 GRVVLELKADVVPKTAENFRALCTGEkgfGYKGSTFHRVIPSFMCQAGDFTNHNGtgGKSIYGSRFPDENFTLK-HVGPG 138
Cdd:cd00317   7 GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPDENFPLKyHHRRG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031987  139 VLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFG-SKSGRTSKKIVITD 202
Cdd:cd00317  82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 59-204 2.06e-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: 185.54  E-value: 2.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987     59 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFTNHNGtGGKSIYGsrFPDENF--TLKHVg 136
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPTGTGG-GGKSIFP--IPDEIFplLLKHK- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987    137 PGVLSMANAG--PNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCG 204
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 45-186 8.77e-56

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 174.20  E-value: 8.77e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   45 NPLVYLDVDangkpLGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKsiyGSR 124
Cdd:COG0652   6 NPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GYT 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031987  125 FPDENFT-LKHVgPGVLSMANA-GPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIES 186
Cdd:COG0652  74 IPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAA 136
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 59-196 1.71e-49

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: 158.01  E-value: 1.71e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   59 LGRVVLELKADVVPKTAENFralCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE-NFTLKHVGP 137
Cdd:cd01927   6 KGDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHDRP 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 5031987  138 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESfgSKSGRTSK 196
Cdd:cd01927  82 YTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIEN--VKTDKNDR 138
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 59-200 4.19e-48

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: 154.23  E-value: 4.19e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   59 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE-NFTLKHVGP 137
Cdd:cd01922   6 MGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPELKHTGA 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031987  138 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVI 200
Cdd:cd01922  82 GILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 59-202 2.75e-44

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: 144.87  E-value: 2.75e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   59 LGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE-NFTLKHVGP 137
Cdd:cd01923   8 KGDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHDGR 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031987  138 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGS-KSGRTSKKIVITD 202
Cdd:cd01923  84 GVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDpGTDRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 59-202 3.54e-42

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: 139.49  E-value: 3.54e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   59 LGRVVLELKADVVPKTAENFRALCTGekGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDENF-TLKHVGP 137
Cdd:cd01928   9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFReTLKHDSR 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5031987  138 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESF-GSKSGRTSKKIVITD 202
Cdd:cd01928  85 GVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLpVDKKYRPLEEIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 59-174 3.38e-34

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: 119.38  E-value: 3.38e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   59 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE-NFTLKHVGP 137
Cdd:cd01925  14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRLRFNRR 89

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 5031987  138 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHV 174
Cdd:cd01925  90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV 126
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 59-201 6.87e-32

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: 113.59  E-value: 6.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   59 LGRVVLELKADVVPKTAENFRALCtgeKGFGYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE--NFT----- 131
Cdd:cd01921   6 LGDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPTG-TGAGGESIYSQLYGRQarFFEpeilp 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5031987  132 -LKHVGPGVLSMANAGPNTNGSQFFICTIK-TDWLDGKHVVFGHVKEGMDVVKKI-ESFGSKSGRTSKKIVIT 201
Cdd:cd01921  82 lLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRIK 154
PTZ00221 PTZ00221
cyclophilin; Provisional
 48-207 4.13e-22

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 90.31  E-value: 4.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987    48 VYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKG--------FGYKGSTFHRVIPSF-MCQAGDFTNHNgtggK 118
Cdd:PTZ00221  55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHVDRNNnIIVLGELDSFN----V 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   119 SIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFG-SKSGRTSKK 197
Cdd:PTZ00221 131 SSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPlDDVGRPLLP 210

                        170
                 ....*....|
gi 5031987   198 IVITDCGQLS 207
Cdd:PTZ00221 211 VTVSFCGALT 220
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 59-186 1.22e-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: 86.73  E-value: 1.22e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   59 LGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFT-------------NHNGTGGKSIYGSrf 125
Cdd:cd01920   6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTpdlaqketlkpikNEAGNGLSNTRGT-- 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5031987  126 pdenftlkhvgpgvLSMA-NAGPNTNGSQFFICTIKTDWLD-----GKHVVFGHVKEGMDVVKKIES 186
Cdd:cd01920  81 --------------IAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAG 133
PRK10791 PRK10791
peptidylprolyl isomerase B;
60-194 4.23e-14

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 67.17  E-value: 4.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987    60 GRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFtnHNGTGGKSIYGSRFPDENFTLKHVgPGV 139
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCR--EGF-YNNTIFHRVINGFMIQGGGF--EPGMKQKATKEPIKNEANNGLKNT-RGT 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5031987   140 LSMANAG-PNTNGSQFFICTIKTDWLDGK--------HVVFGHVKEGMDVVKKIEsfGSKSGRT 194
Cdd:PRK10791  83 LAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIK--GVATGRS 144
PRK10903 PRK10903
peptidylprolyl isomerase A;
60-200 8.97e-14

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 66.79  E-value: 8.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987    60 GRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFtnhngTGGKSIYGSRFPDENFT---LKHVg 136
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGF-----TEQMQQKKPNPPIKNEAdngLRNT- 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5031987   137 PGVLSMA-NAGPNTNGSQFFICTIKTDWLD-GK----HVVFGHVKEGMDVVKKI-----ESFGSKSGRTSKKIVI 200
Cdd:PRK10903 109 RGTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKIsqvptHDVGPYQNVPSKPVVI 183
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 60-185 2.05e-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: 60.15  E-value: 2.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987   60 GRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFTNHN------GTG--------------GKS 119
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDPQGKNpgfpdpETGksrtipleikpegqKQP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5031987  120 IYGSRF-----PDENFTLKHVGPGVLSMANA--GPNTNGSQFFI-------CTIKTDWLDGKHVVFGHVKEGMDVVKKIE 185
Cdd:cd01924  84 VYGKTLeeagrYDEQPVLPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
 
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