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Conserved domains on  [gi|1268743524|ref|NP_001242013|]
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peptidyl-prolyl cis-trans isomerase CYP26 precursor [Glycine max]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112519)

cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0006457
PubMed:  14731520|15998457|15353287

Graphical summary

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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 ...
 69-234 2.38e-110

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: 313.81  E-value: 2.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  69 HKVYFDIQIHGKLAGRIVMGLYGNTVPKTAENFRALCTGEKGVGRsgKSLHYKGSTFHRIIPSFMVQGGDFTRGDGRGGE 148
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG--KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 149 SIYGDKFADENFKLKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGSPKNKV 228
Cdd:cd01926    79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                  ....*.
gi 1268743524 229 VILDSG 234
Cdd:cd01926   159 VIADCG 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 ...
 69-234 2.38e-110

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: 313.81  E-value: 2.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  69 HKVYFDIQIHGKLAGRIVMGLYGNTVPKTAENFRALCTGEKGVGRsgKSLHYKGSTFHRIIPSFMVQGGDFTRGDGRGGE 148
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG--KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 149 SIYGDKFADENFKLKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGSPKNKV 228
Cdd:cd01926    79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                  ....*.
gi 1268743524 229 VILDSG 234
Cdd:cd01926   159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 70-237 3.00e-94

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 274.03  E-value: 3.00e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  70 KVYFDIQIHGKLAGRIVMGLYGNTVPKTAENFRALCTGEKgVGRSGKSLHYKGSTFHRIIPSFMVQGGDFTRGDGRGGES 149
Cdd:PTZ00060   17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGES 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 150 IYGDKFADENFKLKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGSPKNKVV 229
Cdd:PTZ00060   96 IYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVV 175


                  ....*...
gi 1268743524 230 ILDSGELT 237
Cdd:PTZ00060  176 VTDCGELQ 183
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 82-235 3.41e-57

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: 178.60  E-value: 3.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  82 AGRIVMGLYGNTVPKTAENFRALCTgeKGvgrsgkslHYKGSTFHRIIPSFMVQGGDFTrGDGRGGESIYGdkFADENF- 160
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743524 161 -KLKHtGPGYLSMANSGE--DTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGSPKNKVVILDSGE 235
Cdd:pfam00160  73 lLLKH-KRGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 83-230 1.66e-50

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 161.88  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  83 GRIVMGLYGNTVPKTAENFRALCtgEKGvgrsgkslHYKGSTFHRIIPSFMVQGGDFTrGDGRGGEsiyGDKFADENFK- 161
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEG--------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268743524 162 LKHTgPGYLSMANS-GEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGS-PKNKVVI 230
Cdd:COG0652    82 LKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDgPLEPVVI 151
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 69-234 2.38e-110

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: 313.81  E-value: 2.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  69 HKVYFDIQIHGKLAGRIVMGLYGNTVPKTAENFRALCTGEKGVGRsgKSLHYKGSTFHRIIPSFMVQGGDFTRGDGRGGE 148
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG--KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 149 SIYGDKFADENFKLKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGSPKNKV 228
Cdd:cd01926    79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                  ....*.
gi 1268743524 229 VILDSG 234
Cdd:cd01926   159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 70-237 3.00e-94

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 274.03  E-value: 3.00e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  70 KVYFDIQIHGKLAGRIVMGLYGNTVPKTAENFRALCTGEKgVGRSGKSLHYKGSTFHRIIPSFMVQGGDFTRGDGRGGES 149
Cdd:PTZ00060   17 KVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGES 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 150 IYGDKFADENFKLKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGSPKNKVV 229
Cdd:PTZ00060   96 IYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVV 175


                  ....*...
gi 1268743524 230 ILDSGELT 237
Cdd:PTZ00060  176 VTDCGELQ 183
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 71-236 1.71e-71

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 216.24  E-value: 1.71e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  71 VYFDIQIHGKLAGRIVMGLYGNTVPKTAENFRALCTGEkgVGRSGKSLHYKGSTFHRIIPSFMVQGGDFTRGDGRGGESI 150
Cdd:PLN03149   21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSI 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 151 YGDKFADENFKLKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVL-SGMDVLYKIEAEGSESGS-PKNKV 228
Cdd:PLN03149   99 YGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNrPKLAC 178


                  ....*...
gi 1268743524 229 VILDSGEL 236
Cdd:PLN03149  179 VISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 72-232 1.14e-63

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: 195.18  E-value: 1.14e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  72 YFDIQIhgklaGRIVMGLYGNTVPKTAENFRALCTGEkgvgrsgkslHYKGSTFHRIIPSFMVQGGDFTRGDGrgGESIY 151
Cdd:cd00317     1 TLDTTK-----GRIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGP 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 152 GDKFADENFKLK-HTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIE-AEGSESGSPKNKVV 229
Cdd:cd00317    64 GYKFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIErGDTDENGRPIKPVT 143


                  ...
gi 1268743524 230 ILD 232
Cdd:cd00317   144 ISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 82-235 3.41e-57

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: 178.60  E-value: 3.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  82 AGRIVMGLYGNTVPKTAENFRALCTgeKGvgrsgkslHYKGSTFHRIIPSFMVQGGDFTrGDGRGGESIYGdkFADENF- 160
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1268743524 161 -KLKHtGPGYLSMANSGE--DTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGSPKNKVVILDSGE 235
Cdd:pfam00160  73 lLLKH-KRGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 83-231 9.61e-51

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: 162.32  E-value: 9.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  83 GRIVMGLYGNTVPKTAENFRALCTgeKGvgrsgkslHYKGSTFHRIIPSFMVQGGDFTrGDGRGGESIYGDKFADE-NFK 161
Cdd:cd01922     7 GEITLELYWNHAPKTCKNFYELAK--RG--------YYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPE 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 162 LKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGSPKNKVVIL 231
Cdd:cd01922    76 LKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKIL 145
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 83-230 1.66e-50

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 161.88  E-value: 1.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  83 GRIVMGLYGNTVPKTAENFRALCtgEKGvgrsgkslHYKGSTFHRIIPSFMVQGGDFTrGDGRGGEsiyGDKFADENFK- 161
Cdd:COG0652    16 GDIVIELFPDKAPKTVANFVSLA--KEG--------FYDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPg 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268743524 162 LKHTgPGYLSMANS-GEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGS-PKNKVVI 230
Cdd:COG0652    82 LKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDgPLEPVVI 151
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 83-215 4.15e-47

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: 153.00  E-value: 4.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  83 GRIVMGLYGNTVPKTAENFRALCtgekgvgRSGkslHYKGSTFHRIIPSFMVQGGDFTrGDGRGGESIYGDKFADE-NFK 161
Cdd:cd01927     7 GDIHIRLFPEEAPKTVENFTTHA-------RNG---YYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1268743524 162 LKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIE 215
Cdd:cd01927    76 LKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIE 129
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 83-233 4.67e-46

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: 150.64  E-value: 4.67e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  83 GRIVMGLYGNTVPKTAENFRALCtgEKGvgrsgkslHYKGSTFHRIIPSFMVQGGDFTrGDGRGGESIYGDKFADE-NFK 161
Cdd:cd01923     9 GDLNLELHCDKAPKACENFIKLC--KKG--------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPN 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1268743524 162 LKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIE-AEGSESGSPKNKVVILDS 233
Cdd:cd01923    78 LSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMEnVPDPGTDRPKEEIKIEDT 150
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 69-232 8.48e-44

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: 144.50  E-value: 8.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  69 HKVYFDIQIHgklagrivmgLYGNTVPKTAENFRALCTgekgvgrsgkSLHYKGSTFHRIIPSFMVQGGDFTrGDGRGGE 148
Cdd:cd01928     6 HTNLGDIKIE----------LFCDDCPKACENFLALCA----------SGYYNGCIFHRNIKGFMVQTGDPT-GTGKGGE 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 149 SIYGDKFADENFK-LKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEAEGSESGS-PKN 226
Cdd:cd01928    65 SIWGKKFEDEFREtLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYrPLE 144


                  ....*.
gi 1268743524 227 KVVILD 232
Cdd:cd01928   145 EIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 82-231 8.43e-37

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: 127.47  E-value: 8.43e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  82 AGRIVMGLYGNTVPKTAENFRALCTGEkgvgrsgkslHYKGSTFHRIIPSFMVQGGDFTrGDGRGGESIYGDKFADE-NF 160
Cdd:cd01925    14 AGDIDIELWSKEAPKACRNFIQLCLEG----------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHS 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1268743524 161 KLKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSgmDVLYKI----EAEGSESGSPKNKVVIL 231
Cdd:cd01925    83 RLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTG--DTIYNLlklaEVETDKDERPVYPPKIT 155
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 83-232 5.72e-29

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: 107.04  E-value: 5.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  83 GRIVMGLYGNTVPKTAENFRALCtgekgvgrsgKSLHYKGSTFHRIIPSFMVQGGDFTrGDGRGGESIYGDK-------F 155
Cdd:cd01921     7 GDLVIDLFTDECPLACLNFLKLC----------KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqarfF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 156 ADE-NFKLKHTGPGYLSMANSGEDTNGSQFFITTVK-TSWLDGRHVVFGKVLSGMDVLYKI-EAEGSESGSPK-----NK 227
Cdd:cd01921    76 EPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLkdiriKH 155


                  ....*
gi 1268743524 228 VVILD 232
Cdd:cd01921   156 THILD 160
PTZ00221 PTZ00221
cyclophilin; Provisional
 65-237 8.99e-28

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 106.11  E-value: 8.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  65 EGVTHKVYFDIQIHGKLAGRIVMGLYGNTVPKTAENFRALCTGEKGV-GRSGKSLHYKGSTFHRIipsfmvqggDFTRGD 143
Cdd:PTZ00221   49 EQNSCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdTNTGVKLDYLYTPVHHV---------DRNNNI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 144 GRGGE------SIYGDKFADENFKLKHTGPGYLSMANSGEDTNGSQFFITTVKTSWLDGRHVVFGKVLSGMDVLYKIEA- 216
Cdd:PTZ00221  120 IVLGEldsfnvSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESl 199

                         170       180
                  ....*....|....*....|.
gi 1268743524 217 EGSESGSPKNKVVILDSGELT 237
Cdd:PTZ00221  200 PLDDVGRPLLPVTVSFCGALT 220
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 82-215 1.17e-20

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: 84.80  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  82 AGRIVMGLYGNTVPKTAENFRALCtgekgvgRSGkslHYKGSTFHRIIPSFMVQGGDFTRGdgrGGESIYGDKFADE-NF 160
Cdd:cd01920     6 LGDIVVELYDDKAPITVENFLAYV-------RKG---FYDNTIFHRVISGFVIQGGGFTPD---LAQKETLKPIKNEaGN 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1268743524 161 KLKHTGpGYLSMANSGE-DTNGSQFFITTVKTSWLD-----GRHVVFGKVLSGMDVLYKIE 215
Cdd:cd01920    73 GLSNTR-GTIAMARTNApDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIA 132
PRK10903 PRK10903
peptidylprolyl isomerase A;
82-231 3.92e-17

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 76.42  E-value: 3.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  82 AGRIVMGLYGNTVPKTAENFRALCTgekgvgrSGkslHYKGSTFHRIIPSFMVQGGDFTrgdgrggesiygdkfadENFK 161
Cdd:PRK10903   37 AGNIELELNSQKAPVSVKNFVDYVN-------SG---FYNNTTFHRVIPGFMIQGGGFT-----------------EQMQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 162 LKHTGP--------------GYLSMANSGE-DTNGSQFFITTVKTSWLD-GR----HVVFGKVLSGMDVLYKI-----EA 216
Cdd:PRK10903   90 QKKPNPpikneadnglrntrGTIAMARTADkDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKIsqvptHD 169

                         170
                  ....*....|....*
gi 1268743524 217 EGSESGSPKNKVVIL 231
Cdd:PRK10903  170 VGPYQNVPSKPVVIL 184
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 84-216 1.04e-13

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.


Pssm-ID: 238905  Cd Length: 176  Bit Score: 67.08  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  84 RIVmgLYGNTVPKTAENFRALCtgEKGVgrsgkslhYKGSTFHRIIPSFMVQGGD-FTRGDGRG---------------- 146
Cdd:cd01924    10 TIV--LDGYNAPVTAGNFVDLV--ERGF--------YDGMEFHRVEGGFVVQTGDpQGKNPGFPdpetgksrtipleikp 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 147 ---GESIYGDKFA-----DENFKLKHTGPGYLSMANSGEDTNG--SQFFI-------TTVKTSWLDGRHVVFGKVLSGMD 209
Cdd:cd01924    78 egqKQPVYGKTLEeagryDEQPVLPFNAFGAIAMARTEFDPNSasSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLD 157


                  ....*..
gi 1268743524 210 VLYKIEA 216
Cdd:cd01924   158 ILRELKV 164
PRK10791 PRK10791
peptidylprolyl isomerase B;
83-230 3.04e-11

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 59.85  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524  83 GRIVMGLYGNTVPKTAENFRALCtgekgvgRSGkslHYKGSTFHRIIPSFMVQGGDFTRGdgrGGESIYGDKFADE-NFK 161
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYC-------REG---FYNNTIFHRVINGFMIQGGGFEPG---MKQKATKEPIKNEaNNG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1268743524 162 LKHTgPGYLSMANSGEDTNGS-QFFITTVKTSWLDGR--------HVVFGKVLSGMDVLYKIEA-----EGSESGSPKNK 227
Cdd:PRK10791   76 LKNT-RGTLAMARTQAPHSATaQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGvatgrSGMHQDVPKED 154


                  ...
gi 1268743524 228 VVI 230
Cdd:PRK10791  155 VII 157
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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