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Conserved domains on  [gi|20259872|gb|AAM13283|]
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peptidylprolyl isomerase ROC4 [Arabidopsis thaliana]

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 ...
 96-254 9.07e-107

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: 305.72  E-value: 9.07e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  96 KVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKK-----YGYKGSSFHRIIKDFMIQGGDFTEGNGTGGISIY 170
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 171 GAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAfDVPKKGCRI 250
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVVI 160


                ....
gi 20259872 251 YACG 254
Cdd:cd01926 161 ADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 96-254 9.07e-107

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: 305.72  E-value: 9.07e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  96 KVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKK-----YGYKGSSFHRIIKDFMIQGGDFTEGNGTGGISIY 170
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 171 GAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAfDVPKKGCRI 250
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVVI 160


                ....
gi 20259872 251 YACG 254
Cdd:cd01926 161 ADCG 164
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 78-256 1.19e-84

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 250.52  E-value: 1.19e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872   78 SMAAEEEEVIEPQAKVTNKVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKK-----YGYKGSSFHRIIKDFM 152
Cdd:PLN03149   2 AGAGNVEWHLRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRkaglpQGYKGCQFHRVIKDFM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  153 IQGGDFTEGNGTGGISIYGAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVI-EGMKLVR 231
Cdd:PLN03149  82 IQGGDFLKGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVR 161

                        170       180
                 ....*....|....*....|....*
gi 20259872  232 TLESQETRAFDVPKKGCRIYACGEL 256
Cdd:PLN03149 162 KIENVATGPNNRPKLACVISECGEM 186
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 101-255 2.24e-58

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 182.46  E-value: 2.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872   101 VEIGGevAGRIVMGLFGEVVPKTVENFRALCtgeKKYGYKGSSFHRIIKDFMIQGGDFTeGNGTGGISIYGakFEDENF- 179
Cdd:pfam00160   1 IETNG--LGRIVIELFGDKAPKTVENFLQLC---KKGFYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20259872   180 -TLKHtGPGILSMANAG--PNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAfDVPKKGCRIYACGE 255
Cdd:pfam00160  73 lLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 94-250 1.68e-55

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 175.36  E-value: 1.68e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  94 TNKVYFDVEiggevAGRIVMGLFGEVVPKTVENFRALCtgEKKYgYKGSSFHRIIKDFMIQGGDFTeGNGTGGIsiyGAK 173
Cdd:COG0652   6 NPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYT 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20259872 174 FEDENFT-LKHTgPGILSMANA-GPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRI 250
Cdd:COG0652  74 IPDEFDPgLKHK-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 ...
 96-254 9.07e-107

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: 305.72  E-value: 9.07e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  96 KVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKK-----YGYKGSSFHRIIKDFMIQGGDFTEGNGTGGISIY 170
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 171 GAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAfDVPKKGCRI 250
Cdd:cd01926  82 GEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVVI 160


                ....
gi 20259872 251 YACG 254
Cdd:cd01926 161 ADCG 164
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 78-256 1.19e-84

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 250.52  E-value: 1.19e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872   78 SMAAEEEEVIEPQAKVTNKVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKK-----YGYKGSSFHRIIKDFM 152
Cdd:PLN03149   2 AGAGNVEWHLRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRkaglpQGYKGCQFHRVIKDFM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  153 IQGGDFTEGNGTGGISIYGAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVI-EGMKLVR 231
Cdd:PLN03149  82 IQGGDFLKGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVR 161

                        170       180
                 ....*....|....*....|....*
gi 20259872  232 TLESQETRAFDVPKKGCRIYACGEL 256
Cdd:PLN03149 162 KIENVATGPNNRPKLACVISECGEM 186
PTZ00060 PTZ00060
cyclophilin; Provisional
 88-256 7.33e-84

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 248.61  E-value: 7.33e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872   88 EPQAKVTNKVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEKKYG------YKGSSFHRIIKDFMIQGGDFTEG 161
Cdd:PTZ00060   9 FPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSsgknlhYKGSIFHRIIPQFMCQGGDITNH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  162 NGTGGISIYGAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAf 241
Cdd:PTZ00060  89 NGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS- 167

                        170
                 ....*....|....*
gi 20259872  242 DVPKKGCRIYACGEL 256
Cdd:PTZ00060 168 GYPKKPVVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 109-250 4.68e-67

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: 204.42  E-value: 4.68e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 109 GRIVMGLFGEVVPKTVENFRALCTGEkkyGYKGSSFHRIIKDFMIQGGDFTegNGTGGISIYGAKFEDENFTLK-HTGPG 187
Cdd:cd00317   7 GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENFPLKyHHRRG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20259872 188 ILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRI 250
Cdd:cd00317  82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 101-255 2.24e-58

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 182.46  E-value: 2.24e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872   101 VEIGGevAGRIVMGLFGEVVPKTVENFRALCtgeKKYGYKGSSFHRIIKDFMIQGGDFTeGNGTGGISIYGakFEDENF- 179
Cdd:pfam00160   1 IETNG--LGRIVIELFGDKAPKTVENFLQLC---KKGFYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20259872   180 -TLKHtGPGILSMANAG--PNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAfDVPKKGCRIYACGE 255
Cdd:pfam00160  73 lLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 94-250 1.68e-55

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 175.36  E-value: 1.68e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  94 TNKVYFDVEiggevAGRIVMGLFGEVVPKTVENFRALCtgEKKYgYKGSSFHRIIKDFMIQGGDFTeGNGTGGIsiyGAK 173
Cdd:COG0652   6 NPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYT 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20259872 174 FEDENFT-LKHTgPGILSMANA-GPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRI 250
Cdd:COG0652  74 IPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVI 151
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 109-244 5.88e-55

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: 173.80  E-value: 5.88e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 109 GRIVMGLFGEVVPKTVENFralCTGEKKYGYKGSSFHRIIKDFMIQGGDFTeGNGTGGISIYGAKFEDE-NFTLKHTGPG 187
Cdd:cd01927   7 GDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLKHDRPY 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20259872 188 ILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVP 244
Cdd:cd01927  83 TLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRP 139
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 109-250 3.40e-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: 164.24  E-value: 3.40e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 109 GRIVMGLFGEVVPKTVENFRALCTgeKKYgYKGSSFHRIIKDFMIQGGDFTeGNGTGGISIYGAKFEDE-NFTLKHTGPG 187
Cdd:cd01922   7 GEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPELKHTGAG 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20259872 188 ILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAfDVPKKGCRI 250
Cdd:cd01922  83 ILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQT-DRPIDEVKI 144
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 109-250 5.60e-50

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: 161.43  E-value: 5.60e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 109 GRIVMGLFGEVVPKTVENFRALCtgEKKYgYKGSSFHRIIKDFMIQGGDFTeGNGTGGISIYGAKFEDE-NFTLKHTGPG 187
Cdd:cd01923   9 GDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPNLSHDGRG 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20259872 188 ILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRI 250
Cdd:cd01923  85 VLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKI 147
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 109-250 5.88e-46

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: 151.05  E-value: 5.88e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 109 GRIVMGLFGEVVPKTVENFRALCTGEKkygYKGSSFHRIIKDFMIQGGDFTeGNGTGGISIYGAKFEDENF-TLKHTGPG 187
Cdd:cd01928  10 GDIKIELFCDDCPKACENFLALCASGY---YNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFReTLKHDSRG 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20259872 188 ILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRI 250
Cdd:cd01928  86 VVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRI 148
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 108-259 2.20e-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: 129.39  E-value: 2.20e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 108 AGRIVMGLFGEVVPKTVENFRALCTgeKKYgYKGSSFHRIIKDFMIQGGDFTeGNGTGGISIYGAKFEDE-NFTLKHTGP 186
Cdd:cd01925  14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHSRLRFNRR 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 187 GILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQViEG------MKLVRTLESQETRAFDVPK-KGCRIyacGELPLD 259
Cdd:cd01925  90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV-TGdtiynlLKLAEVETDKDERPVYPPKiTSVEV---LENPFD 165
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 109-250 9.26e-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: 9.26e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 109 GRIVMGLFGEVVPKTVENFRALCtgEKKYgYKGSSFHRIIKDFMIQGGDFTeGNGTGGISIYG-------AKFEDE-NFT 180
Cdd:cd01921   7 GDLVIDLFTDECPLACLNFLKLC--KLKY-YNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSqlygrqaRFFEPEiLPL 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20259872 181 LKHTGPGILSMANAGPNTNGSQFFICTVK-TSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVPKKGCRI 250
Cdd:cd01921  83 LKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 94-256 6.42e-28

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 107.26  E-value: 6.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872   94 TNKVYFDVEIGGEVAGRIVMGLFGEVVPKTVENFRALCTGEK--------KYGYKGSSFHRI-IKDFMIQGGDFTEGNgt 164
Cdd:PTZ00221  52 SCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCgidtntgvKLDYLYTPVHHVdRNNNIIVLGELDSFN-- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  165 ggISIYGAKFEDENFTLKHTGPGILSMANAGPNTNGSQFFICTVKTSWLDNKHVVFGQVIEGMKLVRTLESQETRAFDVP 244
Cdd:PTZ00221 130 --VSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRP 207

                        170
                 ....*....|..
gi 20259872  245 KKGCRIYACGEL 256
Cdd:PTZ00221 208 LLPVTVSFCGAL 219
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 108-245 1.51e-21

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding.


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 87.88  E-value: 1.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 108 AGRIVMGLFGEVVPKTVENFRALCtgeKKYGYKGSSFHRIIKDFMIQGGDFTEGNGTggISIYGAKFEDENFTLKHTGpG 187
Cdd:cd01920   6 LGDIVVELYDDKAPITVENFLAYV---RKGFYDNTIFHRVISGFVIQGGGFTPDLAQ--KETLKPIKNEAGNGLSNTR-G 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20259872 188 ILSMA-NAGPNTNGSQFFICTVKTSWLDNK-----HVVFGQVIEGMKLVRTLESQETRAF----DVPK 245
Cdd:cd01920  80 TIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETYSFgsyqDVPV 147
PRK10791 PRK10791
peptidylprolyl isomerase B;
109-246 5.44e-12

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 62.16  E-value: 5.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  109 GRIVMGLFGEVVPKTVENFRALCtgeKKYGYKGSSFHRIIKDFMIQGGDFTEGNGTGGISiygAKFEDE-NFTLKHTgPG 187
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYC---REGFYNNTIFHRVINGFMIQGGGFEPGMKQKATK---EPIKNEaNNGLKNT-RG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20259872  188 ILSMANAG-PNTNGSQFFICTVKTSWLDNK--------HVVFGQVIEGMKLVRTLESQETRAF----DVPKK 246
Cdd:PRK10791  82 TLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSgmhqDVPKE 153
PRK10903 PRK10903
peptidylprolyl isomerase A;
108-257 3.75e-10

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 57.93  E-value: 3.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  108 AGRIVMGLFGEVVPKTVENFRALCtgEKKYgYKGSSFHRIIKDFMIQGGDFTegngtggisiygakfedENFTLKHTGPG 187
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGFT-----------------EQMQQKKPNPP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872  188 ILSMANAG-PNTNG--------------SQFFICTVKTSWLDN-----KHVVFGQVIEGMKLVRTLESQETRAF----DV 243
Cdd:PRK10903  97 IKNEADNGlRNTRGtiamartadkdsatSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHDVgpyqNV 176

                        170
                 ....*....|....
gi 20259872  244 PKKGCRIYACGELP 257
Cdd:PRK10903 177 PSKPVVILSAKVLP 190
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 110-234 3.54e-09

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: 54.76  E-value: 3.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 110 RIVmgLFGEVVPKTVENFRALCtgeKKYGYKGSSFHRIIKDFMIQGGDfTEGNGTGGIS--------------------- 168
Cdd:cd01924  10 TIV--LDGYNAPVTAGNFVDLV---ERGFYDGMEFHRVEGGFVVQTGD-PQGKNPGFPDpetgksrtipleikpegqkqp 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20259872 169 IYGAKFE-----DENFTLKHTGPGILSMANA--GPNTNGSQFFI-------CTVKTSWLDNKHVVFGQVIEGMKLVRTLE 234
Cdd:cd01924  84 VYGKTLEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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