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Conserved domains on  [gi|124512672|ref|XP_001349469|]
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peptidyl-prolyl cis-trans isomerase [Plasmodium falciparum 3D7]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 240)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 44-217 3.01e-93

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


The actual alignment was detected with superfamily member PLN03149:

Pssm-ID: 469651  Cd Length: 186  Bit Score: 270.55  E-value: 3.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  44 NPSNPVVFMDINLGNHFLGKFKFELFQNIVPRTSENFRKFCTGEHKINNLPVGYKNTTFHRVIKDFMIQGGDFVNYNGSG 123
Cdd:PLN03149  15 NPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672 124 CISIYGEHFDDENFDIKHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIDnDSLILLKKIENVSVTPYiY 203
Cdd:PLN03149  95 CVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLG-DGLLVVRKIENVATGPN-N 172

                        170
                 ....*....|....
gi 124512672 204 KPKIAINIVECGEL 217
Cdd:PLN03149 173 RPKLACVISECGEM 186
 
Name Accession Description Interval E-value
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 44-217 3.01e-93

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 270.55  E-value: 3.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  44 NPSNPVVFMDINLGNHFLGKFKFELFQNIVPRTSENFRKFCTGEHKINNLPVGYKNTTFHRVIKDFMIQGGDFVNYNGSG 123
Cdd:PLN03149  15 NPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672 124 CISIYGEHFDDENFDIKHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIDnDSLILLKKIENVSVTPYiY 203
Cdd:PLN03149  95 CVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLG-DGLLVVRKIENVATGPN-N 172

                        170
                 ....*....|....
gi 124512672 204 KPKIAINIVECGEL 217
Cdd:PLN03149 173 RPKLACVISECGEM 186
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 48-215 2.44e-89

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: 259.88  E-value: 2.44e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  48 PVVFMDINLGNHFLGKFKFELFQNIVPRTSENFRKFCTGEHKINNLPVGYKNTTFHRVIKDFMIQGGDFVNYNGSGCISI 127
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672 128 YGEHFDDENFDIKHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSVTPyiYKPKI 207
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV--EGMDVVKKIENVGSGN--GKPKK 156


                 ....*...
gi 124512672 208 AINIVECG 215
Cdd:cd01926  157 KVVIADCG 164
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 61-216 7.57e-48

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: 153.95  E-value: 7.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672   61 LGKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFvNYNGSGCISIYGehFDDENFDIK 140
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCKKGF--------YDGTTFHRVIPGFMVQGGDP-TGTGGGGKSIFP--IPDEIFPLL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124512672  141 -HDKEGLLSMANTG--PNTNGCQFFIITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSVTPyiYKPKIAINIVECGE 216
Cdd:pfam00160  75 lKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVV--EGMDVLEKIEKVPTDG--DRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 45-200 1.27e-36

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 125.67  E-value: 1.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  45 PSNPVVFMDINLGNhflgkFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFvNYNGSGC 124
Cdd:COG0652    4 APNPTVTLETNKGD-----IVIELFPDKAPKTVANFVSLAKEGF--------YDGTIFHRVIPGFMIQGGDP-TGTGTGG 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124512672 125 IsiyGEHFDDENF-DIKHDKeGLLSMANT-GPNTNGCQFFIITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSVTP 200
Cdd:COG0652   70 P---GYTIPDEFDpGLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVV--EGMDVVDKIAAGPTDP 141
 
Name Accession Description Interval E-value
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 44-217 3.01e-93

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 270.55  E-value: 3.01e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  44 NPSNPVVFMDINLGNHFLGKFKFELFQNIVPRTSENFRKFCTGEHKINNLPVGYKNTTFHRVIKDFMIQGGDFVNYNGSG 123
Cdd:PLN03149  15 NPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672 124 CISIYGEHFDDENFDIKHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIDnDSLILLKKIENVSVTPYiY 203
Cdd:PLN03149  95 CVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLG-DGLLVVRKIENVATGPN-N 172

                        170
                 ....*....|....
gi 124512672 204 KPKIAINIVECGEL 217
Cdd:PLN03149 173 RPKLACVISECGEM 186
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 48-215 2.44e-89

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: 259.88  E-value: 2.44e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  48 PVVFMDINLGNHFLGKFKFELFQNIVPRTSENFRKFCTGEHKINNLPVGYKNTTFHRVIKDFMIQGGDFVNYNGSGCISI 127
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672 128 YGEHFDDENFDIKHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSVTPyiYKPKI 207
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV--EGMDVVKKIENVGSGN--GKPKK 156


                 ....*...
gi 124512672 208 AINIVECG 215
Cdd:cd01926  157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 46-217 1.16e-64

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 198.14  E-value: 1.16e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  46 SNPVVFMDINLGNHFLGKFKFELFQNIVPRTSENFRKFCTGEHK-INNLPVGYKNTTFHRVIKDFMIQGGDFVNYNGSGC 124
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVgSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672 125 ISIYGEHFDDENFDIKHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSVTPyiYK 204
Cdd:PTZ00060  94 ESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVI--EGMEVVRAMEKEGTQS--GY 169

                        170
                 ....*....|...
gi 124512672 205 PKIAINIVECGEL 217
Cdd:PTZ00060 170 PKKPVVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 62-211 6.72e-50

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: 159.35  E-value: 6.72e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  62 GKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFVNYNGSGciSIYGEHFDDENFDIK- 140
Cdd:cd00317    7 GRIVIELYGDEAPKTVENFLSLARGGF--------YDGTTFHRVIPGFMIQGGDPTGTGGGG--SGPGYKFPDENFPLKy 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124512672 141 HDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIDNDSliLLKKIENVSVTPYiYKPKIAINI 211
Cdd:cd00317   77 HHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMD--VVDKIERGDTDEN-GRPIKPVTI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 61-216 7.57e-48

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: 153.95  E-value: 7.57e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672   61 LGKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFvNYNGSGCISIYGehFDDENFDIK 140
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCKKGF--------YDGTTFHRVIPGFMVQGGDP-TGTGGGGKSIFP--IPDEIFPLL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124512672  141 -HDKEGLLSMANTG--PNTNGCQFFIITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSVTPyiYKPKIAINIVECGE 216
Cdd:pfam00160  75 lKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVV--EGMDVLEKIEKVPTDG--DRPVKPVKILSCGV 149
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 61-212 4.95e-40

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: 134.20  E-value: 4.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  61 LGKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFVNyNGSGCISIYGEHFDDE-NFDI 139
Cdd:cd01922    6 MGEITLELYWNHAPKTCKNFYELAKRGY--------YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPEL 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124512672 140 KHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIDNdslilLKKIEN-VSVTPYIYKPKIAINIV 212
Cdd:cd01922   77 KHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKG-----MKVIENmVEVQTQTDRPIDEVKIL 145
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 61-211 2.01e-39

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: 132.56  E-value: 2.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  61 LGKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFVNyNGSGCISIYGEHFDDENFD-I 139
Cdd:cd01928    9 LGDIKIELFCDDCPKACENFLALCASGY--------YNGCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFREtL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124512672 140 KHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIDN-DSLILLKKIEnvsvTPYIYKPKIAINI 211
Cdd:cd01928   80 KHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGfETLDTLEKLP----VDKKYRPLEEIRI 148
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 61-201 7.45e-39

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: 131.04  E-value: 7.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  61 LGKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFVNyNGSGCISIYGEHFDDE-NFDI 139
Cdd:cd01927    6 KGDIHIRLFPEEAPKTVENFTTHARNGY--------YNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512672 140 KHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSVTPY 201
Cdd:cd01927   77 KHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVV--KGMDVVQRIENVKTDKN 136
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 61-211 7.79e-38

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: 128.69  E-value: 7.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  61 LGKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFVNyNGSGCISIYGEHFDDE-NFDI 139
Cdd:cd01923    8 KGDLNLELHCDKAPKACENFIKLCKKGY--------YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124512672 140 KHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIDNdsLILLKKIENVSVtPYIYKPKIAINI 211
Cdd:cd01923   79 SHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGG--LETLEAMENVPD-PGTDRPKEEIKI 147
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 45-200 1.27e-36

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 125.67  E-value: 1.27e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  45 PSNPVVFMDINLGNhflgkFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFvNYNGSGC 124
Cdd:COG0652    4 APNPTVTLETNKGD-----IVIELFPDKAPKTVANFVSLAKEGF--------YDGTIFHRVIPGFMIQGGDP-TGTGTGG 69

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124512672 125 IsiyGEHFDDENF-DIKHDKeGLLSMANT-GPNTNGCQFFIITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSVTP 200
Cdd:COG0652   70 P---GYTIPDEFDpGLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVV--EGMDVVDKIAAGPTDP 141
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 61-207 1.22e-30

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: 110.90  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  61 LGKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFVNyNGSGCISIYGEHFDDE-NFDI 139
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCLEGY--------YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRL 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124512672 140 KHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIdNDSLILLKKIENVSV---TPYIYKPKI 207
Cdd:cd01925   85 RFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVT-GDTIYNLLKLAEVETdkdERPVYPPKI 154
PTZ00221 PTZ00221
cyclophilin; Provisional
 50-217 7.31e-28

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 105.72  E-value: 7.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  50 VFMDINLGNHFLGKFKFELFQNIVPRTSENFRKFCTGE---HKINNLPVGYKNTTFHRV-IKDFMIQGGDFVNYNgsgcI 125
Cdd:PTZ00221  55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGScgiDTNTGVKLDYLYTPVHHVdRNNNIIVLGELDSFN----V 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672 126 SIYGEHFDDENFDIKHDKEGLLSMANTGPNTNGCQFFIITKKCEWLDGKNVVFGRIIDNdsLILLKKIENVSVTPyIYKP 205
Cdd:PTZ00221 131 SSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDD--LSLLEKLESLPLDD-VGRP 207

                        170
                 ....*....|..
gi 124512672 206 KIAINIVECGEL 217
Cdd:PTZ00221 208 LLPVTVSFCGAL 219
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 61-198 7.44e-17

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: 74.68  E-value: 7.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  61 LGKFKFELFQNIVPRTSENFRKFCtgehKINNlpvgYKNTTFHRVIKDFMIQGGDfVNYNGSGCISIYGE-------HFD 133
Cdd:cd01921    6 LGDLVIDLFTDECPLACLNFLKLC----KLKY----YNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQlygrqarFFE 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124512672 134 DE-NFDIKHDKEGLLSMANTGPNTNGCQFFI-ITKKCEWLDGKNVVFGRIIdnDSLILLKKIENVSV 198
Cdd:cd01921   77 PEiLPLLKHSKKGTVSMVNAGDNLNGSQFYItLGENLDYLDGKHTVFGQVV--EGFDVLEKINDAIV 141
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 61-199 1.92e-15

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: 70.55  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  61 LGKFKFELFQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFvNYNGSGCISiyGEHFDDENFDIK 140
Cdd:cd01920    6 LGDIVVELYDDKAPITVENFLAYVRKGF--------YDNTIFHRVISGFVIQGGGF-TPDLAQKET--LKPIKNEAGNGL 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124512672 141 HDKEGLLSMANTG-PNTNGCQFFIITKKCEWLDGKN-----VVFGRIIDNdsLILLKKIENVSVT 199
Cdd:cd01920   75 SNTRGTIAMARTNaPDSATSQFFINLKDNASLDYQNeqwgyTVFGEVTEG--MDVVDKIAGVETY 137
PRK10791 PRK10791
peptidylprolyl isomerase B;
69-163 1.27e-06

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 46.76  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  69 FQNIVPRTSENFRKFCTGEHkinnlpvgYKNTTFHRVIKDFMIQGGDFVnyNGSGCISIYGEHFDDENFDIKHDKeGLLS 148
Cdd:PRK10791  16 FDDKAPETVKNFLDYCREGF--------YNNTIFHRVINGFMIQGGGFE--PGMKQKATKEPIKNEANNGLKNTR-GTLA 84

                         90
                 ....*....|....*.
gi 124512672 149 MANTG-PNTNGCQFFI 163
Cdd:PRK10791  85 MARTQaPHSATAQFFI 100
PRK10903 PRK10903
peptidylprolyl isomerase A;
62-201 3.18e-06

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 45.99  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672  62 GKFKFELFQNIVPRTSENFRKFctgehkINNlpvG-YKNTTFHRVIKDFMIQGGDFvnyNGSGCISIYGEHFDDENFDIK 140
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNFVDY------VNS---GfYNNTTFHRVIPGFMIQGGGF---TEQMQQKKPNPPIKNEADNGL 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124512672 141 HDKEGLLSMANTG-PNTNGCQFFIITKKCEWLD-GKN----VVFGRIIdnDSLILLKKIENV---SVTPY 201
Cdd:PRK10903 106 RNTRGTIAMARTAdKDSATSQFFINVADNAFLDhGQRdfgyAVFGKVV--KGMDVADKISQVpthDVGPY 173
 
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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