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Conserved domains on  [gi|2086767766|ref|XP_043186690|]
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peptidyl-prolyl cis-trans isomerase, cyclophilin-type protein [Rhizoctonia solani]

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 ...
 74-237 2.95e-43

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


The actual alignment was detected with superfamily member cd01926:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 164  Bit Score: 143.55  E-value: 2.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  74 IGRLIFDL--DDSPglaKTCANFVSLCKGDKGMCKnapnKPLHYKGTAIHRIAKDFVAQGGDITRNDGSGGESIYGGKFA 151
Cdd:cd01926    14 AGRIVMELfaDVVP---KTAENFRALCTGEKGKGG----KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIYGEKFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 152 DakEGLKAKAEF-GSLAMANSGKNSNTSQFFVVLTsdpgKLAKITGKYVVFGQTRtsgEGEQVLLRLGALSGTNEQPLQP 230
Cdd:cd01926    87 D--ENFKLKHTGpGLLSMANAGPNTNGSQFFITTV----KTPWLDGKHVVFGKVV---EGMDVVKKIENVGSGNGKPKKK 157


                  ....*..
gi 2086767766 231 VWIESSG 237
Cdd:cd01926   158 VVIADCG 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 ...
 74-237 2.95e-43

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: 143.55  E-value: 2.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  74 IGRLIFDL--DDSPglaKTCANFVSLCKGDKGMCKnapnKPLHYKGTAIHRIAKDFVAQGGDITRNDGSGGESIYGGKFA 151
Cdd:cd01926    14 AGRIVMELfaDVVP---KTAENFRALCTGEKGKGG----KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIYGEKFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 152 DakEGLKAKAEF-GSLAMANSGKNSNTSQFFVVLTsdpgKLAKITGKYVVFGQTRtsgEGEQVLLRLGALSGTNEQPLQP 230
Cdd:cd01926    87 D--ENFKLKHTGpGLLSMANAGPNTNGSQFFITTV----KTPWLDGKHVVFGKVV---EGMDVVKKIENVGSGNGKPKKK 157


                  ....*..
gi 2086767766 231 VWIESSG 237
Cdd:cd01926   158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 75-239 1.55e-39

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 134.97  E-value: 1.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  75 GRLIFDL--DDSPglaKTCANFVSLCKGDKgmcKNAPNKPLHYKGTAIHRIAKDFVAQGGDITRNDGSGGESIYGGKFAD 152
Cdd:PTZ00060   30 GRIVFELfsDVTP---KTAENFRALCIGDK---VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGESIYGRKFTD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 153 AKEGLKAKAEfGSLAMANSGKNSNTSQFFVVLTSDPGklakITGKYVVFGQTrtsGEGEQVLLRLGALSGTNEQPLQPVW 232
Cdd:PTZ00060  104 ENFKLKHDQP-GLLSMANAGPNTNGSQFFITTVPCPW----LDGKHVVFGKV---IEGMEVVRAMEKEGTQSGYPKKPVV 175


                  ....*..
gi 2086767766 233 IESSGVL 239
Cdd:PTZ00060  176 VTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 73-238 2.41e-34

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: 120.44  E-value: 2.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  73 SIGRLIFDL--DDSPglaKTCANFVSLCKgdKGmcknapnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGESIYGgkF 150
Cdd:pfam00160   5 GLGRIVIELfgDKAP---KTVENFLQLCK--KG----------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--I 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 151 ADAKEGLKAKAEFGSLAMANSG--KNSNTSQFFVVLtsdpGKLAKITGKYVVFGQTRtsgEGEQVLLRLGALSGTNEQPL 228
Cdd:pfam00160  67 PDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITL----GPAPHLDGKYTVFGKVV---EGMDVLEKIEKVPTDGDRPV 139

                         170
                  ....*....|
gi 2086767766 229 QPVWIESSGV 238
Cdd:pfam00160 140 KPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 75-235 3.72e-29

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 107.18  E-value: 3.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  75 GRLIFDLDD--SPglaKTCANFVSLCKgdKGmcknapnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGEsiyGGKFAD 152
Cdd:COG0652    16 GDIVIELFPdkAP---KTVANFVSLAK--EG----------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 153 -AKEGLKAKAefGSLAMANS-GKNSNTSQFFVVLTSDPGklakITGKYVVFGQTRtsgEGEQVLLRLGALS-GTNEQPLQ 229
Cdd:COG0652    77 eFDPGLKHKR--GTLAMARAqGPNSAGSQFFIVLGDNPH----LDGGYTVFGKVV---EGMDVVDKIAAGPtDPGDGPLE 147


                  ....*.
gi 2086767766 230 PVWIES 235
Cdd:COG0652   148 PVVIES 153
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 74-237 2.95e-43

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: 143.55  E-value: 2.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  74 IGRLIFDL--DDSPglaKTCANFVSLCKGDKGMCKnapnKPLHYKGTAIHRIAKDFVAQGGDITRNDGSGGESIYGGKFA 151
Cdd:cd01926    14 AGRIVMELfaDVVP---KTAENFRALCTGEKGKGG----KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIYGEKFP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 152 DakEGLKAKAEF-GSLAMANSGKNSNTSQFFVVLTsdpgKLAKITGKYVVFGQTRtsgEGEQVLLRLGALSGTNEQPLQP 230
Cdd:cd01926    87 D--ENFKLKHTGpGLLSMANAGPNTNGSQFFITTV----KTPWLDGKHVVFGKVV---EGMDVVKKIENVGSGNGKPKKK 157


                  ....*..
gi 2086767766 231 VWIESSG 237
Cdd:cd01926   158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 75-239 1.55e-39

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 134.97  E-value: 1.55e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  75 GRLIFDL--DDSPglaKTCANFVSLCKGDKgmcKNAPNKPLHYKGTAIHRIAKDFVAQGGDITRNDGSGGESIYGGKFAD 152
Cdd:PTZ00060   30 GRIVFELfsDVTP---KTAENFRALCIGDK---VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGESIYGRKFTD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 153 AKEGLKAKAEfGSLAMANSGKNSNTSQFFVVLTSDPGklakITGKYVVFGQTrtsGEGEQVLLRLGALSGTNEQPLQPVW 232
Cdd:PTZ00060  104 ENFKLKHDQP-GLLSMANAGPNTNGSQFFITTVPCPW----LDGKHVVFGKV---IEGMEVVRAMEKEGTQSGYPKKPVV 175


                  ....*..
gi 2086767766 233 IESSGVL 239
Cdd:PTZ00060  176 VTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 72-235 1.45e-37

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: 128.54  E-value: 1.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  72 LSIGRLIFDL--DDSPglaKTCANFVSLCKGDkgmcknapnkplHYKGTAIHRIAKDFVAQGGDITRNDGsgGESIYGGK 149
Cdd:cd00317     4 TTKGRIVIELygDEAP---KTVENFLSLARGG------------FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 150 FADAKEGLKAKAEFGSLAMANSGKNSNTSQFFVVLTSDPgklaKITGKYVVFGQTRtsgEGEQVLLRLGALSGT-NEQPL 228
Cdd:cd00317    67 FPDENFPLKYHHRRGTLSMANAGPNTNGSQFFITTAPTP----HLDGKHTVFGKVV---EGMDVVDKIERGDTDeNGRPI 139


                  ....*..
gi 2086767766 229 QPVWIES 235
Cdd:cd00317   140 KPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 73-238 2.41e-34

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: 120.44  E-value: 2.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  73 SIGRLIFDL--DDSPglaKTCANFVSLCKgdKGmcknapnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGESIYGgkF 150
Cdd:pfam00160   5 GLGRIVIELfgDKAP---KTVENFLQLCK--KG----------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--I 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 151 ADAKEGLKAKAEFGSLAMANSG--KNSNTSQFFVVLtsdpGKLAKITGKYVVFGQTRtsgEGEQVLLRLGALSGTNEQPL 228
Cdd:pfam00160  67 PDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITL----GPAPHLDGKYTVFGKVV---EGMDVLEKIEKVPTDGDRPV 139

                         170
                  ....*....|
gi 2086767766 229 QPVWIESSGV 238
Cdd:pfam00160 140 KPVKILSCGV 149
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 72-237 2.07e-29

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 108.77  E-value: 2.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  72 LSIGRLIFDL--DDSPglaKTCANFVSLCKGDkgMCKNapNKPLHYKGTAIHRIAKDFVAQGGDITRNDGSGGESIYGGK 149
Cdd:PLN03149   30 IPAGRIKMELfaDIAP---KTAENFRQFCTGE--FRKA--GLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSIYGSK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 150 FADakEGLKAK-AEFGSLAMANSGKNSNTSQFFVVLTsdpgKLAKITGKYVVFGqtRTSGEGEQVLLRL-GALSGTNEQP 227
Cdd:PLN03149  103 FED--ENFIAKhTGPGLLSMANSGPNTNGCQFFITCA----KCDWLDNKHVVFG--RVLGDGLLVVRKIeNVATGPNNRP 174

                         170
                  ....*....|
gi 2086767766 228 LQPVWIESSG 237
Cdd:PLN03149  175 KLACVISECG 184
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 75-235 3.72e-29

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 107.18  E-value: 3.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  75 GRLIFDLDD--SPglaKTCANFVSLCKgdKGmcknapnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGEsiyGGKFAD 152
Cdd:COG0652    16 GDIVIELFPdkAP---KTVANFVSLAK--EG----------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 153 -AKEGLKAKAefGSLAMANS-GKNSNTSQFFVVLTSDPGklakITGKYVVFGQTRtsgEGEQVLLRLGALS-GTNEQPLQ 229
Cdd:COG0652    77 eFDPGLKHKR--GTLAMARAqGPNSAGSQFFIVLGDNPH----LDGGYTVFGKVV---EGMDVVDKIAAGPtDPGDGPLE 147


                  ....*.
gi 2086767766 230 PVWIES 235
Cdd:COG0652   148 PVVIES 153
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 89-233 1.34e-26

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: 100.30  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  89 KTCANFVSLCKgdKGmcknapnkplHYKGTAIHRIAKDFVAQGGDITRNdGSGGESIYGGKFADA-KEGLKAKAEfGSLA 167
Cdd:cd01922    20 KTCKNFYELAK--RG----------YYNGTIFHRLIKDFMIQGGDPTGT-GRGGASIYGKKFEDEiHPELKHTGA-GILS 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2086767766 168 MANSGKNSNTSQFFVVLTSDPgklaKITGKYVVFGQTRtsgEGEQVLLRLGALSGTNEQPLQPVWI 233
Cdd:cd01922    86 MANAGPNTNGSQFFITLAPTP----WLDGKHTIFGRVS---KGMKVIENMVEVQTQTDRPIDEVKI 144
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 82-234 1.22e-25

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: 97.89  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  82 DDSPglaKTCANFVSLCKGDkgmcknapnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGESIYGGKFADA-KEGLKAK 160
Cdd:cd01928    19 DDCP---KACENFLALCASG------------YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEfRETLKHD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2086767766 161 AEfGSLAMANSGKNSNTSQFFVVLTSDPgklaKITGKYVVFGQTRTSGEGEQVLLRLGalSGTNEQPLQPVWIE 234
Cdd:cd01928    83 SR-GVVSMANNGPNTNGSQFFITYAKQP----HLDGKYTVFGKVIDGFETLDTLEKLP--VDKKYRPLEEIRIK 149
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 89-239 6.94e-25

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: 96.65  E-value: 6.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  89 KTCANFVSLCKGDkgmcknapnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGESIYGGKFADakeglkakaEF----- 163
Cdd:cd01925    28 KACRNFIQLCLEG------------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKD---------EFhsrlr 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 164 ----GSLAMANSGKNSNTSQFFVVLtsdpGKLAKITGKYVVFGqtRTSGEGEQVLLRLGAL-SGTNEQPLQPVWIESSGV 238
Cdd:cd01925    86 fnrrGLVGMANAGDDSNGSQFFFTL----DKADELNNKHTLFG--KVTGDTIYNLLKLAEVeTDKDERPVYPPKITSVEV 159


                  .
gi 2086767766 239 L 239
Cdd:cd01925   160 L 160
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 89-239 1.01e-23

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: 93.25  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  89 KTCANFVSLCKgdKGmcknapnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGESIYGGKFADA-KEGLKAKAEfGSLA 167
Cdd:cd01923    22 KACENFIKLCK--KG----------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPNLSHDGR-GVLS 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2086767766 168 MANSGKNSNTSQFFVVLTSDPgklaKITGKYVVFGqtRTSGeGEQVLLRLGALSG-TNEQPLQPVWIESSGVL 239
Cdd:cd01923    88 MANSGPNTNGSQFFITYRSCK----HLDGKHTVFG--RVVG-GLETLEAMENVPDpGTDRPKEEIKIEDTSVF 153
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 89-233 4.53e-20

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: 83.28  E-value: 4.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  89 KTCANFVSlckgdkgMCKNApnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGESIYGGKFADA-KEGLKAKAEFgSLA 167
Cdd:cd01927    20 KTVENFTT-------HARNG-----YYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLKHDRPY-TLS 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2086767766 168 MANSGKNSNTSQFFVVLTSDPGklakITGKYVVFGQTRtsgEGEQVLLRL-GALSGTNEQPLQPVWI 233
Cdd:cd01927    86 MANAGPNTNGSQFFITTVATPW----LDNKHTVFGRVV---KGMDVVQRIeNVKTDKNDRPYEDIKI 145
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 73-239 2.72e-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: 76.23  E-value: 2.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  73 SIGRLIFDL--DDSPglaKTCANFVSLCKGDkgmcknapnkplHYKGTAIHRIAKDFVAQGGDITrNDGSGGESIYGGKF 150
Cdd:cd01921     5 TLGDLVIDLftDECP---LACLNFLKLCKLK------------YYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLY 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 151 ADAKEGLKAK-------AEFGSLAMANSGKNSNTSQFFVVLTSDpgkLAKITGKYVVFGQTRtsgEGEQVLLRLG-ALSG 222
Cdd:cd01921    69 GRQARFFEPEilpllkhSKKGTVSMVNAGDNLNGSQFYITLGEN---LDYLDGKHTVFGQVV---EGFDVLEKINdAIVD 142

                         170
                  ....*....|....*..
gi 2086767766 223 TNEQPLQPVWIESSGVL 239
Cdd:cd01921   143 DDGRPLKDIRIKHTHIL 159
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 73-235 3.20e-13

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: 65.16  E-value: 3.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  73 SIGRLIFDLDDSPGlAKTCANFVSLCKgdKGmcknapnkplHYKGTAIHRIAKDFVAQGGDITRN--DGSGGESIYGgkf 150
Cdd:cd01920     5 SLGDIVVELYDDKA-PITVENFLAYVR--KG----------FYDNTIFHRVISGFVIQGGGFTPDlaQKETLKPIKN--- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 151 aDAKEGLKAKAefGSLAMANSGK-NSNTSQFFVVLtSDPGKLAKI--TGKYVVFGQTRtsgEGEQVLLRLGALSGTN--- 224
Cdd:cd01920    69 -EAGNGLSNTR--GTIAMARTNApDSATSQFFINL-KDNASLDYQneQWGYTVFGEVT---EGMDVVDKIAGVETYSfgs 141

                         170
                  ....*....|...
gi 2086767766 225 --EQPLQPVWIES 235
Cdd:cd01920   142 yqDVPVQDVIIES 154
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 76-218 1.54e-08

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: 52.83  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766  76 RLIFDLDDSPglaKTCANFVSLCKgdkgmcKNApnkplhYKGTAIHRIAKDFVAQGGD-ITRNDG--------------- 139
Cdd:cd01924    10 TIVLDGYNAP---VTAGNFVDLVE------RGF------YDGMEFHRVEGGFVVQTGDpQGKNPGfpdpetgksrtiple 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 140 ---SG-GESIYGGKFADAKEGLKA----KAEFGSLAMANSGK--NSNTSQFFVVLtSDPGKLAKIT----GKYVVFGQTR 205
Cdd:cd01924    75 ikpEGqKQPVYGKTLEEAGRYDEQpvlpFNAFGAIAMARTEFdpNSASSQFFFLL-KDNELTPSRNnvldGRYAVFGYVT 153

                         170
                  ....*....|....*
gi 2086767766 206 tsgEGEQVL--LRLG 218
Cdd:cd01924   154 ---DGLDILreLKVG 165
PRK10903 PRK10903
peptidylprolyl isomerase A;
115-239 2.03e-03

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 37.90  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086767766 115 YKGTAIHRIAKDFVAQGGDITRN--DGSGGESIYGgkfaDAKEGLKAKAefGSLAMA-NSGKNSNTSQFFVVLTS----D 187
Cdd:PRK10903   65 YNNTTFHRVIPGFMIQGGGFTEQmqQKKPNPPIKN----EADNGLRNTR--GTIAMArTADKDSATSQFFINVADnaflD 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2086767766 188 PGKlaKITGkYVVFGQTRtsgEGEQVLLRLGALSGTNEQPLQ-----PVWIESSGVL 239
Cdd:PRK10903  139 HGQ--RDFG-YAVFGKVV---KGMDVADKISQVPTHDVGPYQnvpskPVVILSAKVL 189
 
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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