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Conserved domains on  [gi|20137912|sp|Q99KR7|]
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RecName: Full=Peptidyl-prolyl cis-trans isomerase F, mitochondrial; Short=PPIase F; AltName: Full=Cyclophilin D; Short=CyP-D; Short=CypD; AltName: Full=Cyclophilin F; AltName: Full=Rotamase F; Flags: Precursor

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

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 45-203 1.80e-114

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: 323.05  E-value: 1.80e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  45 PLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSI 119
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912 120 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVI 199
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 20137912 200 TDCG 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 1.80e-114

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: 323.05  E-value: 1.80e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  45 PLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSI 119
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912 120 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVI 199
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 20137912 200 TDCG 203
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 40-206 2.12e-96

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 278.27  E-value: 2.12e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912   40 SSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGE------KGFGYKGSTFHRVIPAFMCQAGDFTNHNG 113
Cdd:PTZ00060  11 EMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  114 TGGRSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKT 193
Cdd:PTZ00060  91 TGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYP 170

                        170
                 ....*....|...
gi 20137912  194 SKKIVITDCGQLS 206
Cdd:PTZ00060 171 KKPVVVTDCGELQ 183
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 58-203 2.56e-59

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: 182.84  E-value: 2.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912    58 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPAFMCQAGDFTnhnGTGGRSIYGSRFPDENF--TLKHVg 135
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFplLLKHK- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912   136 PGVLSMANAG--PNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCG 203
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 43-185 3.89e-54

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 169.97  E-value: 3.89e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  43 GNPLVYLDVgadgqPLGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQAGDFTNhNGTGGRsiyGS 122
Cdd:COG0652   5 PNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GY 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137912 123 RFPDENFT-LKHVgPGVLSMANA-GPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIES 185
Cdd:COG0652  73 TIPDEFDPgLKHK-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 ...
 45-203 1.80e-114

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: 323.05  E-value: 1.80e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  45 PLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSI 119
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912 120 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVI 199
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 20137912 200 TDCG 203
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 40-206 2.12e-96

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 278.27  E-value: 2.12e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912   40 SSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGE------KGFGYKGSTFHRVIPAFMCQAGDFTNHNG 113
Cdd:PTZ00060  11 EMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  114 TGGRSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKT 193
Cdd:PTZ00060  91 TGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYP 170

                        170
                 ....*....|...
gi 20137912  194 SKKIVITDCGQLS 206
Cdd:PTZ00060 171 KKPVVVTDCGELQ 183
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 44-205 1.57e-73

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 220.09  E-value: 1.57e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912   44 NPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGE---KGF--GYKGSTFHRVIPAFMCQAGDFTNHNGTGGRS 118
Cdd:PLN03149  18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  119 IYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHV-KEGMDVVKKIESFGSKSGKTSK-K 196
Cdd:PLN03149  98 IYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVlGDGLLVVRKIENVATGPNNRPKlA 177


                 ....*....
gi 20137912  197 IVITDCGQL 205
Cdd:PLN03149 178 CVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 59-201 7.62e-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: 199.41  E-value: 7.62e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  59 GRVVLELKADVVPKTAENFRALCTGEkgfGYKGSTFHRVIPAFMCQAGDFTNHNGTGgrSIYGSRFPDENFTLK-HVGPG 137
Cdd:cd00317   7 GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPTGTGGGG--SGPGYKFPDENFPLKyHHRRG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137912 138 VLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFG-SKSGKTSKKIVITD 201
Cdd:cd00317  82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 58-203 2.56e-59

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: 182.84  E-value: 2.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912    58 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPAFMCQAGDFTnhnGTGGRSIYGSRFPDENF--TLKHVg 135
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFplLLKHK- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912   136 PGVLSMANAG--PNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCG 203
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 43-185 3.89e-54

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 169.97  E-value: 3.89e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  43 GNPLVYLDVgadgqPLGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQAGDFTNhNGTGGRsiyGS 122
Cdd:COG0652   5 PNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GY 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20137912 123 RFPDENFT-LKHVgPGVLSMANA-GPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIES 185
Cdd:COG0652  73 TIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAA 136
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 58-195 1.97e-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: 157.62  E-value: 1.97e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  58 LGRVVLELKADVVPKTAENFralCTGEKGFGYKGSTFHRVIPAFMCQAGDFTNhNGTGGRSIYGSRFPDE-NFTLKHVGP 136
Cdd:cd01927   6 KGDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHDRP 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20137912 137 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESfgSKSGKTSK 195
Cdd:cd01927  82 YTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIEN--VKTDKNDR 138
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 58-192 2.25e-46

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: 149.99  E-value: 2.25e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  58 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPAFMCQAGDFTNhNGTGGRSIYGSRFPDE-NFTLKHVGP 136
Cdd:cd01922   6 MGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPELKHTGA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20137912 137 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGK 192
Cdd:cd01922  82 GILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDR 137
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 58-201 3.86e-43

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: 142.17  E-value: 3.86e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  58 LGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQAGDFTNhNGTGGRSIYGSRFPDE-NFTLKHVGP 136
Cdd:cd01923   8 KGDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHDGR 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20137912 137 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGS-KSGKTSKKIVITD 201
Cdd:cd01923  84 GVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDpGTDRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 58-198 5.64e-41

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: 136.41  E-value: 5.64e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  58 LGRVVLELKADVVPKTAENFRALCTGekGFgYKGSTFHRVIPAFMCQAGDFTNhNGTGGRSIYGSRFPDENF-TLKHVGP 136
Cdd:cd01928   9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFReTLKHDSR 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20137912 137 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFgsKSGKTSKKIV 198
Cdd:cd01928  85 GVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKL--PVDKKYRPLE 144
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 58-173 1.36e-33

cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) domain similar to Caenorhabditis elegans cyclophilin 16. C. elegans CeCYP-16, compared to the archetypal cyclophilin Human cyclophilin A has, a reduced peptidylprolyl cis- trans isomerase activity, is cyclosporin insensitive and shows an altered substrate preference favoring, hydrophobic, acidic or amide amino acids. Most members of this subfamily have a glutamate residue in the active site at the position equivalent to a tryptophan (W121 in Human cyclophilin A), which has been shown to be important for cyclophilin binding.


Pssm-ID: 238906 [Multi-domain]  Cd Length: 171  Bit Score: 117.84  E-value: 1.36e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  58 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPAFMCQAGDFTNhNGTGGRSIYGSRFPDE-NFTLKHVGP 136
Cdd:cd01925  14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRLRFNRR 89

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 20137912 137 GVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHV 173
Cdd:cd01925  90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV 126
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 58-200 2.23e-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: 109.74  E-value: 2.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  58 LGRVVLELKADVVPKTAENFRALCtgeKGFGYKGSTFHRVIPAFMCQAGDFTNhNGTGGRSIYGSRFPDE--NFT----- 130
Cdd:cd01921   6 LGDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPTG-TGAGGESIYSQLYGRQarFFEpeilp 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20137912 131 -LKHVGPGVLSMANAGPNTNGSQFFICTIK-TDWLDGKHVVFGHVKEGMDVVKKI-ESFGSKSGKTSKKIVIT 200
Cdd:cd01921  82 lLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRIK 154
PTZ00221 PTZ00221
cyclophilin; Provisional
 47-206 1.07e-22

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 91.85  E-value: 1.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912   47 VYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKG--------FGYKGSTFHRVIPAF-MCQAGDFTNHNgtggR 117
Cdd:PTZ00221  55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHVDRNNnIIVLGELDSFN----V 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  118 SIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFG-SKSGKTSKK 196
Cdd:PTZ00221 131 SSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPlDDVGRPLLP 210

                        170
                 ....*....|
gi 20137912  197 IVITDCGQLS 206
Cdd:PTZ00221 211 VTVSFCGALT 220
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 58-185 2.15e-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: 85.96  E-value: 2.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  58 LGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQAGDFT-------------NHNGTGGRSIYGSrf 124
Cdd:cd01920   6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTpdlaqketlkpikNEAGNGLSNTRGT-- 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20137912 125 pdenftlkhvgpgvLSMA-NAGPNTNGSQFFICTIKTDWLD-----GKHVVFGHVKEGMDVVKKIES 185
Cdd:cd01920  81 --------------IAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAG 133
PRK10903 PRK10903
peptidylprolyl isomerase A;
37-199 1.71e-14

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 68.72  E-value: 1.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912   37 GANSSSGNPLVYLDVGAdgqplGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQAGDFT------- 109
Cdd:PRK10903  21 AALAAKGDPHVLLTTSA-----GNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGFTeqmqqkk 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  110 ------NHNGTGGRSIYGSrfpdenftlkhvgpgvLSMA-NAGPNTNGSQFFICTIKTDWLD-GK----HVVFGHVKEGM 177
Cdd:PRK10903  93 pnppikNEADNGLRNTRGT----------------IAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGM 156

                        170       180
                 ....*....|....*....|....*..
gi 20137912  178 DVVKKI-----ESFGSKSGKTSKKIVI 199
Cdd:PRK10903 157 DVADKIsqvptHDVGPYQNVPSKPVVI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
59-185 5.28e-13

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 64.09  E-value: 5.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912   59 GRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPAFMCQAGDFtnHNGTGGRSIYGSRFPDENFTLKHVgPGV 138
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCR--EGF-YNNTIFHRVINGFMIQGGGF--EPGMKQKATKEPIKNEANNGLKNT-RGT 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20137912  139 LSMANAG-PNTNGSQFFICTIKTDWLDGK--------HVVFGHVKEGMDVVKKIES 185
Cdd:PRK10791  83 LAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKG 138
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 59-184 8.79e-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: 58.22  E-value: 8.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912  59 GRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQAGDFTNHN------GTG--------------GRS 118
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDPQGKNpgfpdpETGksrtipleikpegqKQP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20137912 119 IYGSRF-----PDENFTLKHVGPGVLSMANA--GPNTNGSQFFI-------CTIKTDWLDGKHVVFGHVKEGMDVVKKIE 184
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.
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