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Conserved domains on  [gi|1430737136|ref|WP_113879675|]
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peptidylprolyl isomerase [Marinobacter nauticus]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 240)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 42-195 2.95e-74

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


The actual alignment was detected with superfamily member cd01920:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 155  Bit Score: 220.78  E-value: 2.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  42 FVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGFDENLGRKQTRAPIVNEATSTLPNLRGTI 121
Cdd:cd01920     2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGTI 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737136 122 AMARTNAPDSATSQFFINVANNDFLNAGVRGPGYAVFGKVTEGMGVIDRIAGVQTGYQRGMADVPVSPVIIESA 195
Cdd:cd01920    82 AMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
 
Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 42-195 2.95e-74

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: 220.78  E-value: 2.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  42 FVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGFDENLGRKQTRAPIVNEATSTLPNLRGTI 121
Cdd:cd01920     2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGTI 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737136 122 AMARTNAPDSATSQFFINVANNDFLNAGVRGPGYAVFGKVTEGMGVIDRIAGVQTGYQRGMADVPVSPVIIESA 195
Cdd:cd01920    82 AMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 35-200 3.15e-73

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 218.12  E-value: 3.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  35 PALPEVRFVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGFDENLGRKQTRaPIVNEATSTL 114
Cdd:COG0652     4 APNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 115 PNLRGTIAMARTNAPDSATSQFFINVANNDFLNagvrgPGYAVFGKVTEGMGVIDRIAGVQTGYQrgmaDVPVSPVIIES 194
Cdd:COG0652    83 KHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLD-----GGYTVFGKVVEGMDVVDKIAAGPTDPG----DGPLEPVVIES 153


                  ....*.
gi 1430737136 195 AEEITK 200
Cdd:COG0652   154 VTIVED 159
PRK10903 PRK10903
peptidylprolyl isomerase A;
13-196 2.46e-69

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 209.70  E-value: 2.46e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  13 SVLFAFVATLLTTSPAMAQNEEPALPEVRFVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGG 92
Cdd:PRK10903    4 STLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  93 FDENLGRKQTRAPIVNEATSTLPNLRGTIAMARTNAPDSATSQFFINVANNDFLNAGVRGPGYAVFGKVTEGMGVIDRIA 172
Cdd:PRK10903   84 FTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKIS 163

                         170       180
                  ....*....|....*....|....
gi 1430737136 173 GVQTGYQRGMADVPVSPVIIESAE 196
Cdd:PRK10903  164 QVPTHDVGPYQNVPSKPVVILSAK 187
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 43-197 1.67e-55

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: 172.83  E-value: 1.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  43 VTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGFDENLGRKQTRAPIVNEAT-STLPNLRGTI 121
Cdd:pfam00160   3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEIFpLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737136 122 AMART-NAPDSATSQFFINVANNDFLNAgvrgpGYAVFGKVTEGMGVIDRIAGVQTGYQRgmadvPVSPVIIESAEE 197
Cdd:pfam00160  83 SMANTgPAPNSNGSQFFITLGPAPHLDG-----KYTVFGKVVEGMDVLEKIEKVPTDGDR-----PVKPVKILSCGV 149
 
Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 42-195 2.95e-74

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: 220.78  E-value: 2.95e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  42 FVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGFDENLGRKQTRAPIVNEATSTLPNLRGTI 121
Cdd:cd01920     2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGTI 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1430737136 122 AMARTNAPDSATSQFFINVANNDFLNAGVRGPGYAVFGKVTEGMGVIDRIAGVQTGYQRGMADVPVSPVIIESA 195
Cdd:cd01920    82 AMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 35-200 3.15e-73

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 218.12  E-value: 3.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  35 PALPEVRFVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGFDENLGRKQTRaPIVNEATSTL 114
Cdd:COG0652     4 APNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 115 PNLRGTIAMARTNAPDSATSQFFINVANNDFLNagvrgPGYAVFGKVTEGMGVIDRIAGVQTGYQrgmaDVPVSPVIIES 194
Cdd:COG0652    83 KHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLD-----GGYTVFGKVVEGMDVVDKIAAGPTDPG----DGPLEPVVIES 153


                  ....*.
gi 1430737136 195 AEEITK 200
Cdd:COG0652   154 VTIVED 159
PRK10903 PRK10903
peptidylprolyl isomerase A;
13-196 2.46e-69

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 209.70  E-value: 2.46e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  13 SVLFAFVATLLTTSPAMAQNEEPALPEVRFVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGG 92
Cdd:PRK10903    4 STLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  93 FDENLGRKQTRAPIVNEATSTLPNLRGTIAMARTNAPDSATSQFFINVANNDFLNAGVRGPGYAVFGKVTEGMGVIDRIA 172
Cdd:PRK10903   84 FTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKIS 163

                         170       180
                  ....*....|....*....|....
gi 1430737136 173 GVQTGYQRGMADVPVSPVIIESAE 196
Cdd:PRK10903  164 QVPTHDVGPYQNVPSKPVVILSAK 187
PRK10791 PRK10791
peptidylprolyl isomerase B;
40-194 2.48e-57

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 178.11  E-value: 2.48e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  40 VRFVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGFDENLGRKQTRAPIVNEATSTLPNLRG 119
Cdd:PRK10791    2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTRG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737136 120 TIAMARTNAPDSATSQFFINVANNDFLN---AGVRGPGYAVFGKVTEGMGVIDRIAGVQTGYQRGMADVPVSPVIIES 194
Cdd:PRK10791   82 TLAMARTQAPHSATAQFFINVVDNDFLNfsgESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIES 159
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 43-197 1.67e-55

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: 172.83  E-value: 1.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  43 VTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGFDENLGRKQTRAPIVNEAT-STLPNLRGTI 121
Cdd:pfam00160   3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEIFpLLLKHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1430737136 122 AMART-NAPDSATSQFFINVANNDFLNAgvrgpGYAVFGKVTEGMGVIDRIAGVQTGYQRgmadvPVSPVIIESAEE 197
Cdd:pfam00160  83 SMANTgPAPNSNGSQFFITLGPAPHLDG-----KYTVFGKVVEGMDVLEKIEKVPTDGDR-----PVKPVKILSCGV 149
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 42-194 4.40e-46

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: 148.95  E-value: 4.40e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  42 FVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGGF-DENLGRKQTRAPIVNEAT-STLPNLRG 119
Cdd:cd00317     2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPtGTGGGGSGPGYKFPDENFpLKYHHRRG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1430737136 120 TIAMARTNaPDSATSQFFINVANNDFLNagvrgPGYAVFGKVTEGMGVIDRIAGVQTGYQrgmaDVPVSPVIIES 194
Cdd:cd00317    82 TLSMANAG-PNTNGSQFFITTAPTPHLD-----GKHTVFGKVVEGMDVVDKIERGDTDEN----GRPIKPVTISD 146
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 44-195 7.73e-29

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: 104.85  E-value: 7.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  44 TTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGG--FDENLGRKQTRAPIVNEATSTLPNLR-GT 120
Cdd:cd01927     4 TTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDptGDGTGGESIWGKEFEDEFSPSLKHDRpYT 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1430737136 121 IAMArtNA-PDSATSQFFINVANNDFLNAgvrgpGYAVFGKVTEGMGVIDRIAGVQTGYQrgmaDVPVSPVIIESA 195
Cdd:cd01927    84 LSMA--NAgPNTNGSQFFITTVATPWLDN-----KHTVFGRVVKGMDVVQRIENVKTDKN----DRPYEDIKIINI 148
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 40-192 3.01e-27

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: 100.97  E-value: 3.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  40 VRFVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQaGGFDENLGRKQTR---APIVNEATSTLP- 115
Cdd:cd01928     3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQ-TGDPTGTGKGGESiwgKKFEDEFRETLKh 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1430737136 116 NLRGTIAMArTNAPDSATSQFFINVANNDFLNAgvrgpGYAVFGKVTEGMGVIDRIAGVQTGYQ-RGMADVPVSPVII 192
Cdd:cd01928    82 DSRGVVSMA-NNGPNTNGSQFFITYAKQPHLDG-----KYTVFGKVIDGFETLDTLEKLPVDKKyRPLEEIRIKDVTI 153
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 40-196 1.05e-24

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: 94.40  E-value: 1.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  40 VRFVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQaGGFDENLGRKQTR---APIVNEATSTLPN 116
Cdd:cd01923     2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQ-GGDPTGTGRGGESiwgKPFKDEFKPNLSH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 117 L-RGTIAMARTnAPDSATSQFFINVANNDFLNAgvrgpGYAVFGKVTEGMGVIDRIAGVQTgyqrGMADVPVSPVIIESA 195
Cdd:cd01923    81 DgRGVLSMANS-GPNTNGSQFFITYRSCKHLDG-----KHTVFGRVVGGLETLEAMENVPD----PGTDRPKEEIKIEDT 150


                  .
gi 1430737136 196 E 196
Cdd:cd01923   151 S 151
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 47-192 1.37e-23

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: 91.93  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  47 GSFVLQLRPDVAPKTVENFLAY-------VNSGF-YDGTIFHRVIPGFMVQAGGF-----------------DENLGRKQ 101
Cdd:cd01926    15 GRIVMELFADVVPKTAENFRALctgekgkGGKPFgYKGSTFHRVIPDFMIQGGDFtrgngtggksiygekfpDENFKLKH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 102 TRApivneatstlpnlrGTIAMArtNA-PDSATSQFFINVANNDFLNAgvrgpGYAVFGKVTEGMGVIDRIAGVQTGyqr 180
Cdd:cd01926    95 TGP--------------GLLSMA--NAgPNTNGSQFFITTVKTPWLDG-----KHVVFGKVVEGMDVVKKIENVGSG--- 150

                         170
                  ....*....|..
gi 1430737136 181 gmADVPVSPVII 192
Cdd:cd01926   151 --NGKPKKKVVI 160
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 33-196 6.16e-23

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: 90.49  E-value: 6.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  33 EEPALPEVRFVTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQaGGFDENLGRKQTR---APIVNE 109
Cdd:cd01925     1 EPPTTGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQ-GGDPTGTGTGGESiygEPFKDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 110 ATSTLP-NLRGTIAMARTNaPDSATSQFFINVANNDFLNAgvrgpGYAVFGKVTeGMGVID--RIAGVQTGYQrgmaDVP 186
Cdd:cd01925    80 FHSRLRfNRRGLVGMANAG-DDSNGSQFFFTLDKADELNN-----KHTLFGKVT-GDTIYNllKLAEVETDKD----ERP 148

                         170
                  ....*....|
gi 1430737136 187 VSPVIIESAE 196
Cdd:cd01925   149 VYPPKITSVE 158
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 44-187 1.48e-22

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: 88.75  E-value: 1.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  44 TTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGgfdENLGRKQTRAPIVNEATS--TLPNLR--- 118
Cdd:cd01922     4 TTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGG---DPTGTGRGGASIYGKKFEdeIHPELKhtg 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 119 -GTIAMArTNAPDSATSQFFINVANNDFLNAgvrgpGYAVFGKVTEGMGVIDRIAGVQTGYQRGMADVPV 187
Cdd:cd01922    81 aGILSMA-NAGPNTNGSQFFITLAPTPWLDG-----KHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 43-171 1.99e-22

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: 89.04  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  43 VTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQAGG--------FDENLGRKQT----------RA 104
Cdd:cd01924     3 ATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDpqgknpgfPDPETGKSRTipleikpegqKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 105 PIVNEATST----------LPNLRGTIAMART-NAPDSATSQFFINVANNDFLNAG--VRGPGYAVFGKVTEGMGVIDRI 171
Cdd:cd01924    83 PVYGKTLEEagrydeqpvlPFNAFGAIAMARTeFDPNSASSQFFFLLKDNELTPSRnnVLDGRYAVFGYVTDGLDILREL 162
PTZ00060 PTZ00060
cyclophilin; Provisional
 12-199 3.18e-19

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 81.04  E-value: 3.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  12 MSVLFAFvatlltTSPAMAQNeepalPEVRFVTT-----EGSFVLQLRPDVAPKTVENFLAYV---------NSGFYDGT 77
Cdd:PTZ00060    1 FFKLFSQ------SFPEMSKR-----PKVFFDISidnapAGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  78 IFHRVIPGFMVQAGGF-----------------DENLGRKQTRApivneatstlpnlrGTIAMArtNA-PDSATSQFFIN 139
Cdd:PTZ00060   70 IFHRIIPQFMCQGGDItnhngtggesiygrkftDENFKLKHDQP--------------GLLSMA--NAgPNTNGSQFFIT 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1430737136 140 VANNDFLNAgvrgpGYAVFGKVTEGMGVIDRI--AGVQTGYqrgmadvPVSPVIIESAEEIT 199
Cdd:PTZ00060  134 TVPCPWLDG-----KHVVFGKVIEGMEVVRAMekEGTQSGY-------PKKPVVVTDCGELQ 183
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 43-171 3.51e-16

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: 72.37  E-value: 3.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  43 VTTEGSFVLQLRPDVAPKTVENFLAYVNSGFYDGTIFHRVIPGFMVQ------AGGFDENLGRKQTRAPIVNEATSTLPN 116
Cdd:cd01921     3 ETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQtgdptgTGAGGESIYSQLYGRQARFFEPEILPL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 117 LR----GTIAMArTNAPDSATSQFFINVANN-DFLNagvrGPgYAVFGKVTEGMGVIDRI 171
Cdd:cd01921    83 LKhskkGTVSMV-NAGDNLNGSQFYITLGENlDYLD----GK-HTVFGQVVEGFDVLEKI 136
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 35-177 1.28e-15

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 71.41  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  35 PALPEVRFVTTEGS-----FVLQLRPDVAPKTVENFLAYVNSGF--------YDGTIFHRVIPGFMVQAGGF-------- 93
Cdd:PLN03149   16 PKNPVVFFDVTIGGipagrIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFlkgdgtgc 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  94 ---------DENLGRKQTRApivneatstlpnlrGTIAMARTnAPDSATSQFFINVANNDFLNAgvrgpGYAVFGKVT-E 163
Cdd:PLN03149   96 vsiygskfeDENFIAKHTGP--------------GLLSMANS-GPNTNGCQFFITCAKCDWLDN-----KHVVFGRVLgD 155

                         170
                  ....*....|....
gi 1430737136 164 GMGVIDRIAGVQTG 177
Cdd:PLN03149  156 GLLVVRKIENVATG 169
PTZ00221 PTZ00221
cyclophilin; Provisional
 47-192 9.56e-04

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 39.08  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136  47 GSFVLQLRPDVAPKTVENFLAYV--------NSGF---YDGTIFHRVIPGFMVQAGGFDENLGRKQTRAPIVNEATSTLP 115
Cdd:PTZ00221   67 GRLVFELFEDVVPETVENFRALItgscgidtNTGVkldYLYTPVHHVDRNNNIIVLGELDSFNVSSTGTPIADEGYRHRH 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1430737136 116 NLRGTIAMArTNAPDSATSQFFINVANN---DFLNagvrgpgyAVFGKVTEGMGVIDRIAGV---QTGYqrgmadvPVSP 189
Cdd:PTZ00221  147 TERGLLTMI-SEGPHTSGSVFGITLGPSpslDFKQ--------VVFGKAVDDLSLLEKLESLpldDVGR-------PLLP 210


                  ...
gi 1430737136 190 VII 192
Cdd:PTZ00221  211 VTV 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.
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