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Conserved domains on  [gi|896141665|ref|WP_049161430|]
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MULTISPECIES: peptidylprolyl isomerase [Actinomycetes]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10002023)

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

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0000413|GO:0003755
PubMed:  14731520|15998457
SCOP:  4000390

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 2-176 2.96e-72

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


:

Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 214.65  E-value: 2.96e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   2 ANNTHTATIHTNHGDIVVELFGNHAPKTVKNFVGLATgeqewthpqtgeknngAPLYSGTVFHRIIKDFMIQGGDPLGMG 81
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAK----------------EGFYDGTIFHRVIPGFMIQGGDPTGTG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  82 IGGPGYQFGDEIHPELQFDRpYLLAMANA-GPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDPRD 160
Cdd:COG0652   67 TGGPGYTIPDEFDPGLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVE--GMDVVDKIAAGPTDPGD 143

                        170
                 ....*....|....*.
gi 896141665 161 RPLEDVVIESIDIDEA 176
Cdd:COG0652  144 GPLEPVVIESVTIVED 159
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 2-176 2.96e-72

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 214.65  E-value: 2.96e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   2 ANNTHTATIHTNHGDIVVELFGNHAPKTVKNFVGLATgeqewthpqtgeknngAPLYSGTVFHRIIKDFMIQGGDPLGMG 81
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAK----------------EGFYDGTIFHRVIPGFMIQGGDPTGTG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  82 IGGPGYQFGDEIHPELQFDRpYLLAMANA-GPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDPRD 160
Cdd:COG0652   67 TGGPGYTIPDEFDPGLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVE--GMDVVDKIAAGPTDPGD 143

                        170
                 ....*....|....*.
gi 896141665 161 RPLEDVVIESIDIDEA 176
Cdd:COG0652  144 GPLEPVVIESVTIVED 159
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 9-170 2.68e-61

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: 186.70  E-value: 2.68e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   9 TIHTNHGDIVVELFGNHAPKTVKNFVGLATGEQewthpqtgeknngaplYSGTVFHRIIKDFMIQGGDPL--GMGIGGPG 86
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGF----------------YDGTTFHRVIPGFMIQGGDPTgtGGGGSGPG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  87 YQFGDEIHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDPRDRPLEDV 166
Cdd:cd00317   65 YKFPDENFPLKYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVE--GMDVVDKIERGDTDENGRPIKPV 142


                 ....
gi 896141665 167 VIES 170
Cdd:cd00317  143 TISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 10-173 2.58e-50

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: 158.96  E-value: 2.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   10 IHTN-HGDIVVELFGNHAPKTVKNFVGLAtgeqewthpQTGeknngapLYSGTVFHRIIKDFMIQGGDPLGMGIGG-PGY 87
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLC---------KKG-------FYDGTTFHRVIPGFMVQGGDPTGTGGGGkSIF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   88 QFGDEIHPELQFDRPYLLAMANAG--PGTNGSQFFITSVPTGWLNGKHTIFGEVkdEASQKVVDELNAVATDpRDRPLED 165
Cdd:pfam00160  65 PIPDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKV--VEGMDVLEKIEKVPTD-GDRPVKP 141


                  ....*...
gi 896141665  166 VVIESIDI 173
Cdd:pfam00160 142 VKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 13-169 9.97e-41

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 135.74  E-value: 9.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  13 NHGDIVVELFGNHAPKTVKNFVGLATGEQEwthpqtgeKNNGAPL-YSGTVFHRIIKDFMIQGGD-PLGMGIGGP---GY 87
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALCIGDKV--------GSSGKNLhYKGSIFHRIIPQFMCQGGDiTNHNGTGGEsiyGR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  88 QFGDEiHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDpRDRPLEDVV 167
Cdd:PTZ00060 100 KFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIE--GMEVVRAMEKEGTQ-SGYPKKPVV 175


                 ..
gi 896141665 168 IE 169
Cdd:PTZ00060 176 VT 177
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 2-176 2.96e-72

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 214.65  E-value: 2.96e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   2 ANNTHTATIHTNHGDIVVELFGNHAPKTVKNFVGLATgeqewthpqtgeknngAPLYSGTVFHRIIKDFMIQGGDPLGMG 81
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAK----------------EGFYDGTIFHRVIPGFMIQGGDPTGTG 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  82 IGGPGYQFGDEIHPELQFDRpYLLAMANA-GPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDPRD 160
Cdd:COG0652   67 TGGPGYTIPDEFDPGLKHKR-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVE--GMDVVDKIAAGPTDPGD 143

                        170
                 ....*....|....*.
gi 896141665 161 RPLEDVVIESIDIDEA 176
Cdd:COG0652  144 GPLEPVVIESVTIVED 159
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 9-170 2.68e-61

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: 186.70  E-value: 2.68e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   9 TIHTNHGDIVVELFGNHAPKTVKNFVGLATGEQewthpqtgeknngaplYSGTVFHRIIKDFMIQGGDPL--GMGIGGPG 86
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGF----------------YDGTTFHRVIPGFMIQGGDPTgtGGGGSGPG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  87 YQFGDEIHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDPRDRPLEDV 166
Cdd:cd00317   65 YKFPDENFPLKYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVE--GMDVVDKIERGDTDENGRPIKPV 142


                 ....
gi 896141665 167 VIES 170
Cdd:cd00317  143 TISD 146
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 9-171 5.36e-61

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: 185.74  E-value: 5.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   9 TIHTNHGDIVVELFGNHAPKTVKNFVglatgeqewTHPQTGeknngapLYSGTVFHRIIKDFMIQGGDPLGMGIGGP--- 85
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFT---------THARNG-------YYNNTIFHRVIKGFMIQTGDPTGDGTGGEsiw 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  86 GYQFGDEIHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKdeASQKVVDELNAVATDPRDRPLED 165
Cdd:cd01927   65 GKEFEDEFSPSLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVV--KGMDVVQRIENVKTDKNDRPYED 142


                 ....*.
gi 896141665 166 VVIESI 171
Cdd:cd01927  143 IKIINI 148
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 9-168 3.88e-56

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: 173.49  E-value: 3.88e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   9 TIHTNHGDIVVELFGNHAPKTVKNFVGLATgeqewthpqtgeknngAPLYSGTVFHRIIKDFMIQGGDPLGMGIGGP--- 85
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAK----------------RGYYNGTIFHRLIKDFMIQGGDPTGTGRGGAsiy 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  86 GYQFGDEIHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKdeASQKVVDELNAVATDpRDRPLED 165
Cdd:cd01922   65 GKKFEDEIHPELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVS--KGMKVIENMVEVQTQ-TDRPIDE 141


                 ...
gi 896141665 166 VVI 168
Cdd:cd01922  142 VKI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 10-173 2.58e-50

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: 158.96  E-value: 2.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   10 IHTN-HGDIVVELFGNHAPKTVKNFVGLAtgeqewthpQTGeknngapLYSGTVFHRIIKDFMIQGGDPLGMGIGG-PGY 87
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLC---------KKG-------FYDGTTFHRVIPGFMVQGGDPTGTGGGGkSIF 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   88 QFGDEIHPELQFDRPYLLAMANAG--PGTNGSQFFITSVPTGWLNGKHTIFGEVkdEASQKVVDELNAVATDpRDRPLED 165
Cdd:pfam00160  65 PIPDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKV--VEGMDVLEKIEKVPTD-GDRPVKP 141


                  ....*...
gi 896141665  166 VVIESIDI 173
Cdd:pfam00160 142 VKILSCGV 149
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 15-168 5.05e-50

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: 158.57  E-value: 5.05e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  15 GDIVVELFGNHAPKTVKNFVGLATGEQewthpqtgeKNNGAPL-YSGTVFHRIIKDFMIQGGDPL-GMGIGGP---GYQF 89
Cdd:cd01926   15 GRIVMELFADVVPKTAENFRALCTGEK---------GKGGKPFgYKGSTFHRVIPDFMIQGGDFTrGNGTGGKsiyGEKF 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896141665  90 GDEiHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDpRDRPLEDVVI 168
Cdd:cd01926   86 PDE-NFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVE--GMDVVKKIENVGSG-NGKPKKKVVI 160
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 9-173 2.23e-48

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: 154.13  E-value: 2.23e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   9 TIHTNHGDIVVELFGNHAPKTVKNFVGL-ATGeqewthpqtgeknngapLYSGTVFHRIIKDFMIQGGDPLGMGIGGP-- 85
Cdd:cd01928    4 TLHTNLGDIKIELFCDDCPKACENFLALcASG-----------------YYNGCIFHRNIKGFMVQTGDPTGTGKGGEsi 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  86 -GYQFGDEIHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDPRDRPLE 164
Cdd:cd01928   67 wGKKFEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVID--GFETLDTLEKLPVDKKYRPLE 144


                 ....*....
gi 896141665 165 DVVIESIDI 173
Cdd:cd01928  145 EIRIKDVTI 153
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 5-175 7.82e-48

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: 153.28  E-value: 7.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   5 THTATIHTNHGDIVVELFGNHAPKTVKNFVGLATGEqewthpqtgeknngapLYSGTVFHRIIKDFMIQGGDPLGMGIGG 84
Cdd:cd01925    5 TGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEG----------------YYDNTIFHRVVPGFIIQGGDPTGTGTGG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  85 P---GYQFGDEIHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDEASQKVVdELNAVATDPRDR 161
Cdd:cd01925   69 EsiyGEPFKDEFHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLL-KLAEVETDKDER 147

                        170
                 ....*....|....
gi 896141665 162 PLEDVVIESIDIDE 175
Cdd:cd01925  148 PVYPPKITSVEVLE 161
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 10-173 3.09e-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: 148.72  E-value: 3.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  10 IHTNHGDIVVELFGNHAPKTVKNFVGLAtgeqewthpqtgeKNNgapLYSGTVFHRIIKDFMIQGGDPLGMGIGGP---G 86
Cdd:cd01923    4 LHTNKGDLNLELHCDKAPKACENFIKLC-------------KKG---YYDGTIFHRSIRNFMIQGGDPTGTGRGGEsiwG 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  87 YQFGDEIHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDPRDRPLEDV 166
Cdd:cd01923   68 KPFKDEFKPNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVG--GLETLEAMENVPDPGTDRPKEEI 145


                 ....*..
gi 896141665 167 VIESIDI 173
Cdd:cd01923  146 KIEDTSV 152
PTZ00060 PTZ00060
cyclophilin; Provisional
 13-169 9.97e-41

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 135.74  E-value: 9.97e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  13 NHGDIVVELFGNHAPKTVKNFVGLATGEQEwthpqtgeKNNGAPL-YSGTVFHRIIKDFMIQGGD-PLGMGIGGP---GY 87
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALCIGDKV--------GSSGKNLhYKGSIFHRIIPQFMCQGGDiTNHNGTGGEsiyGR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  88 QFGDEiHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDpRDRPLEDVV 167
Cdd:PTZ00060 100 KFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIE--GMEVVRAMEKEGTQ-SGYPKKPVV 175


                 ..
gi 896141665 168 IE 169
Cdd:PTZ00060 176 VT 177
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 15-168 2.67e-36

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 124.18  E-value: 2.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  15 GDIVVELFGNHAPKTVKNFVGLATGEQewthpqtgeKNNGAPL-YSGTVFHRIIKDFMIQGGDPL-GMGIGGP---GYQF 89
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCTGEF---------RKAGLPQgYKGCQFHRVIKDFMIQGGDFLkGDGTGCVsiyGSKF 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896141665  90 GDEiHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDEAsQKVVDELNAVATDPRDRPLEDVVI 168
Cdd:PLN03149 104 EDE-NFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDG-LLVVRKIENVATGPNNRPKLACVI 180
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 10-168 1.07e-26

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: 98.95  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  10 IHTNHGDIVVELFGNHAPKTVKNFVGLAtgeqewthpqtgeKNNgapLYSGTVFHRIIKDFMIQGGDPLGMGIGGP---- 85
Cdd:cd01921    2 LETTLGDLVIDLFTDECPLACLNFLKLC-------------KLK---YYNFCLFYNVQKDFIAQTGDPTGTGAGGEsiys 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  86 ---GYQ---FGDEIHPELQFDRPYLLAMANAGPGTNGSQFFIT-SVPTGWLNGKHTIFGEVKDeaSQKVVDELNAVATDP 158
Cdd:cd01921   66 qlyGRQarfFEPEILPLLKHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVE--GFDVLEKINDAIVDD 143

                        170
                 ....*....|
gi 896141665 159 RDRPLEDVVI 168
Cdd:cd01921  144 DGRPLKDIRI 153
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 9-170 1.31e-24

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: 93.28  E-value: 1.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   9 TIHTNHGDIVVELFGNHAPKTVKNFVGLAtgeqewthpqtgekNNGapLYSGTVFHRIIKDFMIQGGdplGMGIGGPGYQ 88
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYV--------------RKG--FYDNTIFHRVISGFVIQGG---GFTPDLAQKE 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  89 FGDEIHPE----LQFDRpYLLAMA-NAGPGTNGSQFFITSVPTGWLN-----GKHTIFGEVkdEASQKVVDELNAVATDP 158
Cdd:cd01920   62 TLKPIKNEagngLSNTR-GTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEV--TEGMDVVDKIAGVETYS 138

                        170
                 ....*....|....*.
gi 896141665 159 R----DRPLEDVVIES 170
Cdd:cd01920  139 FgsyqDVPVQDVIIES 154
PRK10791 PRK10791
peptidylprolyl isomerase B;
9-175 7.99e-18

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 76.03  E-value: 7.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665   9 TIHTNHGDIVVELFGNHAPKTVKNFVGLATGEqewthpqtgeknngapLYSGTVFHRIIKDFMIQGG--DPlGMGIGGPG 86
Cdd:PRK10791   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREG----------------FYNNTIFHRVINGFMIQGGgfEP-GMKQKATK 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  87 YQFGDEIHPELQFDRPYLLAMANAGPGTNGSQFFITSVPTGWLNGK--------HTIFGEVKDeaSQKVVDELNAVATDP 158
Cdd:PRK10791  66 EPIKNEANNGLKNTRGTLAMARTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVE--GMDVVDKIKGVATGR 143

                        170       180
                 ....*....|....*....|.
gi 896141665 159 ----RDRPLEDVVIESIDIDE 175
Cdd:PRK10791 144 sgmhQDVPKEDVIIESVTVSE 164
PTZ00221 PTZ00221
cyclophilin; Provisional
 15-168 8.95e-15

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 69.51  E-value: 8.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  15 GDIVVELFGNHAPKTVKNFVGLATGEQEwTHPQTGEKNNgaplYSGTVFHRI-IKDFMIQGGDPLGMGIGGPGYQFGDEI 93
Cdd:PTZ00221  67 GRLVFELFEDVVPETVENFRALITGSCG-IDTNTGVKLD----YLYTPVHHVdRNNNIIVLGELDSFNVSSTGTPIADEG 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896141665  94 HPELQFDRPyLLAMANAGPGTNGSQFFITSVPTGWLNGKHTIFGEVKDEASqkVVDELNAVATDPRDRPLEDVVI 168
Cdd:PTZ00221 142 YRHRHTERG-LLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLS--LLEKLESLPLDDVGRPLLPVTV 213
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 12-141 1.01e-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: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  12 TNHGDIVVELFGNHAPKTVKNFVGLAtgeqewthpqtgEKNngapLYSGTVFHRIIKDFMIQGGDPLGMGIGGPGYQFGD 91
Cdd:cd01924    4 TDNGTITIVLDGYNAPVTAGNFVDLV------------ERG----FYDGMEFHRVEGGFVVQTGDPQGKNPGFPDPETGK 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  92 ------EIHPELQFDRPY----------------------LLAMANA--GPGTNGSQFFI-------TSVPTGWLNGKHT 134
Cdd:cd01924   68 srtiplEIKPEGQKQPVYgktleeagrydeqpvlpfnafgAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYA 147


                 ....*..
gi 896141665 135 IFGEVKD 141
Cdd:cd01924  148 VFGYVTD 154
PRK10903 PRK10903
peptidylprolyl isomerase A;
12-173 1.26e-09

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 54.85  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  12 TNHGDIVVELFGNHAPKTVKNFVGLAtgeqewthpqtgekNNGapLYSGTVFHRIIKDFMIQGGDPLG-MGIGGPGYQFG 90
Cdd:PRK10903  35 TSAGNIELELNSQKAPVSVKNFVDYV--------------NSG--FYNNTTFHRVIPGFMIQGGGFTEqMQQKKPNPPIK 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896141665  91 DEIHPELQFDRPyLLAMA-NAGPGTNGSQFFITSVPTGWLN-GK----HTIFGEVKDeaSQKVVDELNAVATDP----RD 160
Cdd:PRK10903  99 NEADNGLRNTRG-TIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVK--GMDVADKISQVPTHDvgpyQN 175

                        170
                 ....*....|...
gi 896141665 161 RPLEDVVIESIDI 173
Cdd:PRK10903 176 VPSKPVVILSAKV 188
 
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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