NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1183037138|gb|ORV57806|]
View 

peptidylprolyl isomerase [Mycobacterium florentinum]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-182 4.65e-70

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


:

Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 209.26  E-value: 4.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  13 QTATATLHTNRGDIKIALFGNHAPKTVANFVGLAQGtkeystqnasgspsgPFYDGAVFHRVIQGFMIQGGDPTGTGRGG 92
Cdd:COG0652     5 PNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKE---------------GFYDGTIFHRVIPGFMIQGGDPTGTGTGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  93 PGYQFADEFHPELQFdKPYLLAMANA-GPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGNDRPT 171
Cdd:COG0652    70 PGYTIPDEFDPGLKH-KRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVV--EGMDVVDKIAAGPTDPGDGPL 146

                         170
                  ....*....|.
gi 1183037138 172 DPVVIESITIS 182
Cdd:COG0652   147 EPVVIESVTIV 157
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-182 4.65e-70

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 209.26  E-value: 4.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  13 QTATATLHTNRGDIKIALFGNHAPKTVANFVGLAQGtkeystqnasgspsgPFYDGAVFHRVIQGFMIQGGDPTGTGRGG 92
Cdd:COG0652     5 PNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKE---------------GFYDGTIFHRVIPGFMIQGGDPTGTGTGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  93 PGYQFADEFHPELQFdKPYLLAMANA-GPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGNDRPT 171
Cdd:COG0652    70 PGYTIPDEFDPGLKH-KRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVV--EGMDVVDKIAAGPTDPGDGPL 146

                         170
                  ....*....|.
gi 1183037138 172 DPVVIESITIS 182
Cdd:COG0652   147 EPVVIESVTIV 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 18-178 1.18e-59

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: 182.46  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  18 TLHTNRGDIKIALFGNHAPKTVANFVGLAQGTkeystqnasgspsgpFYDGAVFHRVIQGFMIQGGDPTGTGRGGPG--Y 95
Cdd:cd00317     1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGG---------------FYDGTTFHRVIPGFMIQGGDPTGTGGGGSGpgY 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  96 QFADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGNDRPTDPVV 175
Cdd:cd00317    66 KFPDENFPLKYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVV--EGMDVVDKIERGDTDENGRPIKPVT 143


                  ...
gi 1183037138 176 IES 178
Cdd:cd00317   144 ISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 19-181 2.14e-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: 159.34  E-value: 2.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  19 LHTN-RGDIKIALFGNHAPKTVANFVGLAQGtkeystqnasgspsgPFYDGAVFHRVIQGFMIQGGD-PTGTGRGGPGYQ 96
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKK---------------GFYDGTTFHRVIPGFMVQGGDpTGTGGGGKSIFP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  97 FADEFHPELQFDKPYLLAMANAG--PGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGnDRPTDPV 174
Cdd:pfam00160  66 IPDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVV--EGMDVLEKIEKVPTDG-DRPVKPV 142


                  ....*..
gi 1183037138 175 VIESITI 181
Cdd:pfam00160 143 KILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 22-177 4.85e-32

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 113.40  E-value: 4.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  22 NRGDIKIALFGNHAPKTVANFVGLAQGTKeystqnaSGSPSGPF-YDGAVFHRVIQGFMIQGGDPTGTGRGGPGYQFADE 100
Cdd:PTZ00060   28 PAGRIVFELFSDVTPKTAENFRALCIGDK-------VGSSGKNLhYKGSIFHRIIPQFMCQGGDITNHNGTGGESIYGRK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138 101 FHPE---LQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDgNDRPTDPVVIE 177
Cdd:PTZ00060  101 FTDEnfkLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVI--EGMEVVRAMEKEGTQ-SGYPKKPVVVT 177
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 13-182 4.65e-70

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 209.26  E-value: 4.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  13 QTATATLHTNRGDIKIALFGNHAPKTVANFVGLAQGtkeystqnasgspsgPFYDGAVFHRVIQGFMIQGGDPTGTGRGG 92
Cdd:COG0652     5 PNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKE---------------GFYDGTIFHRVIPGFMIQGGDPTGTGTGG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  93 PGYQFADEFHPELQFdKPYLLAMANA-GPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGNDRPT 171
Cdd:COG0652    70 PGYTIPDEFDPGLKH-KRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVV--EGMDVVDKIAAGPTDPGDGPL 146

                         170
                  ....*....|.
gi 1183037138 172 DPVVIESITIS 182
Cdd:COG0652   147 EPVVIESVTIV 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 18-178 1.18e-59

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: 182.46  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  18 TLHTNRGDIKIALFGNHAPKTVANFVGLAQGTkeystqnasgspsgpFYDGAVFHRVIQGFMIQGGDPTGTGRGGPG--Y 95
Cdd:cd00317     1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGG---------------FYDGTTFHRVIPGFMIQGGDPTGTGGGGSGpgY 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  96 QFADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGNDRPTDPVV 175
Cdd:cd00317    66 KFPDENFPLKYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVV--EGMDVVDKIERGDTDENGRPIKPVT 143


                  ...
gi 1183037138 176 IES 178
Cdd:cd00317   144 ISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 19-181 2.14e-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: 159.34  E-value: 2.14e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  19 LHTN-RGDIKIALFGNHAPKTVANFVGLAQGtkeystqnasgspsgPFYDGAVFHRVIQGFMIQGGD-PTGTGRGGPGYQ 96
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKK---------------GFYDGTTFHRVIPGFMVQGGDpTGTGGGGKSIFP 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  97 FADEFHPELQFDKPYLLAMANAG--PGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGnDRPTDPV 174
Cdd:pfam00160  66 IPDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVV--EGMDVLEKIEKVPTDG-DRPVKPV 142


                  ....*..
gi 1183037138 175 VIESITI 181
Cdd:pfam00160 143 KILSCGV 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 18-179 6.80e-50

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: 158.01  E-value: 6.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  18 TLHTNRGDIKIALFGNHAPKTVANFVglaqgtkeysTQNASGspsgpFYDGAVFHRVIQGFMIQGGDPTGTGRGGPGY-- 95
Cdd:cd01927     1 IIHTTKGDIHIRLFPEEAPKTVENFT----------THARNG-----YYNNTIFHRVIKGFMIQTGDPTGDGTGGESIwg 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  96 -QFADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGNDRPTDPV 174
Cdd:cd01927    66 kEFEDEFSPSLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVV--KGMDVVQRIENVKTDKNDRPYEDI 143


                  ....*
gi 1183037138 175 VIESI 179
Cdd:cd01927   144 KIINI 148
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 18-181 7.35e-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: 147.97  E-value: 7.35e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  18 TLHTNRGDIKIALFGNHAPKTVANFVGLAqgtkeystqnASGspsgpFYDGAVFHRVIQGFMIQGGD-PTGTGRGGPGYQ 96
Cdd:cd01928     4 TLHTNLGDIKIELFCDDCPKACENFLALC----------ASG-----YYNGCIFHRNIKGFMVQTGDpTGTGKGGESIWG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  97 --FADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGNDRPTDPV 174
Cdd:cd01928    69 kkFEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVI--DGFETLDTLEKLPVDKKYRPLEEI 146


                  ....*..
gi 1183037138 175 VIESITI 181
Cdd:cd01928   147 RIKDVTI 153
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 11-181 3.43e-45

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: 146.73  E-value: 3.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  11 PIQTATATLHTNRGDIKIALFGNHAPKTVANFVGLA-QGtkeystqnasgspsgpFYDGAVFHRVIQGFMIQGGDPTGT- 88
Cdd:cd01925     2 PPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLClEG----------------YYDNTIFHRVVPGFIIQGGDPTGTg 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  89 GRGGPGYQ--FADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIEPESQKVVdAIATTSTDG 166
Cdd:cd01925    66 TGGESIYGepFKDEFHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLL-KLAEVETDK 144

                         170
                  ....*....|....*
gi 1183037138 167 NDRPTDPVVIESITI 181
Cdd:cd01925   145 DERPVYPPKITSVEV 159
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 19-182 3.36e-44

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: 143.71  E-value: 3.36e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  19 LHTNRGDIKIALFGNHAPKTVANFVGLAQgtKEYstqnasgspsgpfYDGAVFHRVIQGFMIQGGDPTGTGRGGPGY--- 95
Cdd:cd01923     4 LHTNKGDLNLELHCDKAPKACENFIKLCK--KGY-------------YDGTIFHRSIRNFMIQGGDPTGTGRGGESIwgk 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  96 QFADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDGNDRPTDPVV 175
Cdd:cd01923    69 PFKDEFKPNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVV--GGLETLEAMENVPDPGTDRPKEEIK 146


                  ....*..
gi 1183037138 176 IESITIS 182
Cdd:cd01923   147 IEDTSVF 153
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 24-176 4.21e-42

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: 138.54  E-value: 4.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  24 GDIKIALFGNHAPKTVANFVGLAQGTKeystqnasGSPSGPF-YDGAVFHRVIQGFMIQGGDPTGT--GRGGPGY--QFA 98
Cdd:cd01926    15 GRIVMELFADVVPKTAENFRALCTGEK--------GKGGKPFgYKGSTFHRVIPDFMIQGGDFTRGngTGGKSIYgeKFP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1183037138  99 DE-FHpeLQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTdGNDRPTDPVVI 176
Cdd:cd01926    87 DEnFK--LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV--EGMDVVKKIENVGS-GNGKPKKKVVI 160
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 18-176 9.09e-42

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: 137.28  E-value: 9.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  18 TLHTNRGDIKIALFGNHAPKTVANFVGLAqgTKEYstqnasgspsgpfYDGAVFHRVIQGFMIQGGDPTGTGRGGPGY-- 95
Cdd:cd01922     1 TLETTMGEITLELYWNHAPKTCKNFYELA--KRGY-------------YNGTIFHRLIKDFMIQGGDPTGTGRGGASIyg 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  96 -QFADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEViePESQKVVDAIATTSTDgNDRPTDPV 174
Cdd:cd01922    66 kKFEDEIHPELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRV--SKGMKVIENMVEVQTQ-TDRPIDEV 142


                  ..
gi 1183037138 175 VI 176
Cdd:cd01922   143 KI 144
PTZ00060 PTZ00060
cyclophilin; Provisional
 22-177 4.85e-32

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 113.40  E-value: 4.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  22 NRGDIKIALFGNHAPKTVANFVGLAQGTKeystqnaSGSPSGPF-YDGAVFHRVIQGFMIQGGDPTGTGRGGPGYQFADE 100
Cdd:PTZ00060   28 PAGRIVFELFSDVTPKTAENFRALCIGDK-------VGSSGKNLhYKGSIFHRIIPQFMCQGGDITNHNGTGGESIYGRK 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138 101 FHPE---LQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIepESQKVVDAIATTSTDgNDRPTDPVVIE 177
Cdd:PTZ00060  101 FTDEnfkLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVI--EGMEVVRAMEKEGTQ-SGYPKKPVVVT 177
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 24-176 2.02e-30

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 109.54  E-value: 2.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  24 GDIKIALFGNHAPKTVANFVGLAQGtkEYstqNASGSPSGpfYDGAVFHRVIQGFMIQGGDPTGTGRGGPGYQFADEFHP 103
Cdd:PLN03149   33 GRIKMELFADIAPKTAENFRQFCTG--EF---RKAGLPQG--YKGCQFHRVIKDFMIQGGDFLKGDGTGCVSIYGSKFED 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1183037138 104 ELQFDK---PYLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIEpESQKVVDAIATTSTDGNDRPTDPVVI 176
Cdd:PLN03149  106 ENFIAKhtgPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLG-DGLLVVRKIENVATGPNNRPKLACVI 180
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 18-178 4.57e-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: 84.42  E-value: 4.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  18 TLHTNRGDIKIALFGNHAPKTVANFVGLAQgtkeystqnasgspSGpFYDGAVFHRVIQGFMIQGGDptgtgrggpgyqf 97
Cdd:cd01920     1 EFQTSLGDIVVELYDDKAPITVENFLAYVR--------------KG-FYDNTIFHRVISGFVIQGGG------------- 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  98 adeFHPELQ---FDKP-------------YLLAMA-NAGPGTNGSQFFITVGQTPHLNRR-----HTIFGEVIepESQKV 155
Cdd:cd01920    53 ---FTPDLAqkeTLKPikneagnglsntrGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVT--EGMDV 127

                         170       180
                  ....*....|....*....|....*..
gi 1183037138 156 VDAIAT--TSTDGN--DRPTDPVVIES 178
Cdd:cd01920   128 VDKIAGveTYSFGSyqDVPVQDVIIES 154
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 19-170 2.78e-20

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: 82.77  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  19 LHTNRGDIKIALFGNHAPKTVANFVGLAQgTKeystqnasgspsgpFYDGAVFHRVIQGFMIQGGD-------PTGTGRG 91
Cdd:cd01921     2 LETTLGDLVIDLFTDECPLACLNFLKLCK-LK--------------YYNFCLFYNVQKDFIAQTGDptgtgagGESIYSQ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  92 GPGYQ---FADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQ-TPHLNRRHTIFGEVIepESQKVVDAIATTSTDGN 167
Cdd:cd01921    67 LYGRQarfFEPEILPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVV--EGFDVLEKINDAIVDDD 144


                  ...
gi 1183037138 168 DRP 170
Cdd:cd01921   145 GRP 147
PRK10791 PRK10791
peptidylprolyl isomerase B;
18-182 3.03e-17

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 74.88  E-value: 3.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  18 TLHTNRGDIKIALFGNHAPKTVANFVglaqgtkEYSTQNasgspsgpFYDGAVFHRVIQGFMIQGGD-PTGTGRGGPGYQ 96
Cdd:PRK10791    3 TFHTNHGDIVIKTFDDKAPETVKNFL-------DYCREG--------FYNNTIFHRVINGFMIQGGGfEPGMKQKATKEP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  97 FADEFHPELQFDKPYLLAMANAGPGTNGSQFFITVGQTPHLNRR--------HTIFGEVIepESQKVVDAIATTSTDGN- 167
Cdd:PRK10791   68 IKNEANNGLKNTRGTLAMARTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVV--EGMDVVDKIKGVATGRSg 145

                         170
                  ....*....|....*...
gi 1183037138 168 ---DRPTDPVVIESITIS 182
Cdd:PRK10791  146 mhqDVPKEDVIIESVTVS 163
PRK10903 PRK10903
peptidylprolyl isomerase A;
19-181 1.62e-12

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 62.55  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  19 LHTNRGDIKIALFGNHAPKTVANFVGLAQgtkeystqnasgspSGpFYDGAVFHRVIQGFMIQGG----DPTGTGRGGPG 94
Cdd:PRK10903   33 LTTSAGNIELELNSQKAPVSVKNFVDYVN--------------SG-FYNNTTFHRVIPGFMIQGGgfteQMQQKKPNPPI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  95 YQFADEFHPELQFDkpylLAMA-NAGPGTNGSQFFITVGQTPHLNR-----RHTIFGEVIepESQKVVDAIATTSTDG-- 166
Cdd:PRK10903   98 KNEADNGLRNTRGT----IAMArTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVV--KGMDVADKISQVPTHDvg 171

                         170
                  ....*....|....*..
gi 1183037138 167 --NDRPTDPVVIESITI 181
Cdd:PRK10903  172 pyQNVPSKPVVILSAKV 188
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 21-149 1.96e-08

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


Pssm-ID: 238905  Cd Length: 176  Bit Score: 51.29  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  21 TNRGDIKIALFGNHAPKTVANFVGLAQgtkeystqnasgspSGpFYDGAVFHRVIQGFMIQGGDPTGTGRggpgyQFAD- 99
Cdd:cd01924     4 TDNGTITIVLDGYNAPVTAGNFVDLVE--------------RG-FYDGMEFHRVEGGFVVQTGDPQGKNP-----GFPDp 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138 100 ----------EFHPELQFDKPY----------------------LLAMANA--GPGTNGSQFFITVGQ-------TPHLN 138
Cdd:cd01924    64 etgksrtiplEIKPEGQKQPVYgktleeagrydeqpvlpfnafgAIAMARTefDPNSASSQFFFLLKDneltpsrNNVLD 143

                         170
                  ....*....|.
gi 1183037138 139 RRHTIFGEVIE 149
Cdd:cd01924   144 GRYAVFGYVTD 154
PTZ00221 PTZ00221
cyclophilin; Provisional
 24-176 4.74e-06

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 45.25  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1183037138  24 GDIKIALFGNHAPKTVANFVGLAQGtkEYSTQNASGSPSGpfYDGAVFHRV-IQGFMIQGGDPTGTGRGGPGYQFADEFH 102
Cdd:PTZ00221   67 GRLVFELFEDVVPETVENFRALITG--SCGIDTNTGVKLD--YLYTPVHHVdRNNNIIVLGELDSFNVSSTGTPIADEGY 142

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1183037138 103 PELQFDKPyLLAMANAGPGTNGSQFFITVGQTPHLNRRHTIFGEVIEPESqkVVDAIATTSTDGNDRPTDPVVI 176
Cdd:PTZ00221  143 RHRHTERG-LLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLS--LLEKLESLPLDDVGRPLLPVTV 213
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH