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Conserved domains on  [gi|504531838|ref|WP_014718940|]
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MULTISPECIES: peptidylprolyl isomerase [Pseudomonas]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112428)

peptidylprolyl isomerase 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_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 6-163 5.29e-81

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: 236.57  E-value: 5.29e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   6 LTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPsIQNEADNGLSNDKYT 85
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKP-IKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504531838  86 VAMARTMEPHSASAQFFINVADNAFLNHSGKNvqgWGYAVFGKVTQGTDVVDKIKGVSTTSKAGHQDVPAEDVIVEKA 163
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQ---WGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
 
Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 6-163 5.29e-81

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: 236.57  E-value: 5.29e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   6 LTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPsIQNEADNGLSNDKYT 85
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKP-IKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504531838  86 VAMARTMEPHSASAQFFINVADNAFLNHSGKNvqgWGYAVFGKVTQGTDVVDKIKGVSTTSKAGHQDVPAEDVIVEKA 163
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQ---WGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PRK10791 PRK10791
peptidylprolyl isomerase B;
4-167 1.12e-74

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 220.87  E-value: 1.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   4 VKLTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPsIQNEADNGLSNDK 83
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEP-IKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  84 YTVAMARTMEPHSASAQFFINVADNAFLNHSGKNVQGWGYAVFGKVTQGTDVVDKIKGVSTTSKAGHQDVPAEDVIVEKA 163
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ....
gi 504531838 164 EIIE 167
Cdd:PRK10791 161 TVSE 164
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 2-168 3.98e-74

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 219.27  E-value: 3.98e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   2 TQVKLTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRpsIQNEADNGLSN 81
Cdd:COG0652    7 PTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGYT--IPDEFDPGLKH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  82 DKYTVAMARTMEPHSASAQFFINVADNAFLNHsgknvqgwGYAVFGKVTQGTDVVDKIKGVSTtskaGHQDVPAEDVIVE 161
Cdd:COG0652   85 KRGTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------GYTVFGKVVEGMDVVDKIAAGPT----DPGDGPLEPVVIE 152


                 ....*..
gi 504531838 162 KAEIIEA 168
Cdd:COG0652  153 SVTIVED 159
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 7-165 2.88e-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: 158.19  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838    7 TTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPsIQNEADN-GLSNDKYT 85
Cdd:pfam00160   3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFP-IPDEIFPlLLKHKRGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   86 VAMART-MEPHSASAQFFINVADNAFLNHsgknvqgwGYAVFGKVTQGTDVVDKIKGVSTtskagHQDVPAEDVIVEKAE 164
Cdd:pfam00160  82 LSMANTgPAPNSNGSQFFITLGPAPHLDG--------KYTVFGKVVEGMDVLEKIEKVPT-----DGDRPVKPVKILSCG 148


                  .
gi 504531838  165 I 165
Cdd:pfam00160 149 V 149
 
Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 6-163 5.29e-81

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: 236.57  E-value: 5.29e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   6 LTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPsIQNEADNGLSNDKYT 85
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKP-IKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504531838  86 VAMARTMEPHSASAQFFINVADNAFLNHSGKNvqgWGYAVFGKVTQGTDVVDKIKGVSTTSKAGHQDVPAEDVIVEKA 163
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQ---WGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PRK10791 PRK10791
peptidylprolyl isomerase B;
4-167 1.12e-74

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 220.87  E-value: 1.12e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   4 VKLTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPsIQNEADNGLSNDK 83
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEP-IKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  84 YTVAMARTMEPHSASAQFFINVADNAFLNHSGKNVQGWGYAVFGKVTQGTDVVDKIKGVSTTSKAGHQDVPAEDVIVEKA 163
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ....
gi 504531838 164 EIIE 167
Cdd:PRK10791 161 TVSE 164
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 2-168 3.98e-74

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 219.27  E-value: 3.98e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   2 TQVKLTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRpsIQNEADNGLSN 81
Cdd:COG0652    7 PTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGYT--IPDEFDPGLKH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  82 DKYTVAMARTMEPHSASAQFFINVADNAFLNHsgknvqgwGYAVFGKVTQGTDVVDKIKGVSTtskaGHQDVPAEDVIVE 161
Cdd:COG0652   85 KRGTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------GYTVFGKVVEGMDVVDKIAAGPT----DPGDGPLEPVVIE 152


                 ....*..
gi 504531838 162 KAEIIEA 168
Cdd:COG0652  153 SVTIVED 159
PRK10903 PRK10903
peptidylprolyl isomerase A;
2-166 1.37e-66

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 201.22  E-value: 1.37e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   2 TQVKLTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPsIQNEADNGLSN 81
Cdd:PRK10903  29 PHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPP-IKNEADNGLRN 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  82 DKYTVAMARTMEPHSASAQFFINVADNAFLNHSGKNvqgWGYAVFGKVTQGTDVVDKIKGVSTTSKAGHQDVPAEDVIVE 161
Cdd:PRK10903 108 TRGTIAMARTADKDSATSQFFINVADNAFLDHGQRD---FGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVIL 184


                 ....*
gi 504531838 162 KAEII 166
Cdd:PRK10903 185 SAKVL 189
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 7-165 2.88e-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: 158.19  E-value: 2.88e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838    7 TTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPsIQNEADN-GLSNDKYT 85
Cdd:pfam00160   3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFP-IPDEIFPlLLKHKRGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   86 VAMART-MEPHSASAQFFINVADNAFLNHsgknvqgwGYAVFGKVTQGTDVVDKIKGVSTtskagHQDVPAEDVIVEKAE 164
Cdd:pfam00160  82 LSMANTgPAPNSNGSQFFITLGPAPHLDG--------KYTVFGKVVEGMDVLEKIEKVPT-----DGDRPVKPVKILSCG 148


                  .
gi 504531838  165 I 165
Cdd:pfam00160 149 V 149
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 6-162 2.43e-45

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: 145.87  E-value: 2.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   6 LTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGGFEPGMKEKKDKRPSIQNEADNGLSNDKY- 84
Cdd:cd00317    2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGSGPGYKFPDENFPLKYHHRRg 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504531838  85 TVAMARtMEPHSASAQFFINVADNAFLNHSgknvqgwgYAVFGKVTQGTDVVDKIKGVSTTSkaghQDVPAEDVIVEK 162
Cdd:cd00317   82 TLSMAN-AGPNTNGSQFFITTAPTPHLDGK--------HTVFGKVVEGMDVVDKIERGDTDE----NGRPIKPVTISD 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 4-165 3.66e-27

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: 99.80  E-value: 3.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   4 VKLTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGG---GFEPGMKEKKDKrpSIQNEADNGLS 80
Cdd:cd01923    2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGdptGTGRGGESIWGK--PFKDEFKPNLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  81 ND-KYTVAMARTmEPHSASAQFFINVADNAFLNhsGKnvqgwgYAVFGKVTQGTDVVDKIKGVSTTSKaghqDVPAEDVI 159
Cdd:cd01923   80 HDgRGVLSMANS-GPNTNGSQFFITYRSCKHLD--GK------HTVFGRVVGGLETLEAMENVPDPGT----DRPKEEIK 146


                 ....*.
gi 504531838 160 VEKAEI 165
Cdd:cd01923  147 IEDTSV 152
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 6-140 3.02e-26

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: 97.90  E-value: 3.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   6 LTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGG--------FEPGMKEKK----------DK 67
Cdd:cd01924    2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDpqgknpgfPDPETGKSRtipleikpegQK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  68 RPSIQNEADNG---------LSNDKYTVAMART-MEPHSASAQFFINVADNAFLNhSGKNVQGWGYAVFGKVTQGTDVVD 137
Cdd:cd01924   82 QPVYGKTLEEAgrydeqpvlPFNAFGAIAMARTeFDPNSASSQFFFLLKDNELTP-SRNNVLDGRYAVFGYVTDGLDILR 160


                 ...
gi 504531838 138 KIK 140
Cdd:cd01924  161 ELK 163
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 6-158 3.07e-26

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: 97.15  E-value: 3.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   6 LTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGG-FEPGMKEKKDKRPSIQNEADNGLSNDK- 83
Cdd:cd01927    2 IHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDpTGDGTGGESIWGKEFEDEFSPSLKHDRp 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504531838  84 YTVAMARTmEPHSASAQFFINVADNAFLNhsGKnvqgwgYAVFGKVTQGTDVVDKIKGVSTtskaGHQDVPAEDV 158
Cdd:cd01927   82 YTLSMANA-GPNTNGSQFFITTVATPWLD--NK------HTVFGRVVKGMDVVQRIENVKT----DKNDRPYEDI 143
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 4-165 4.58e-20

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: 81.33  E-value: 4.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   4 VKLTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGgfEPGMKEKKDKRPSIQNEADNGLSNDK 83
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTG--DPTGTGKGGESIWGKKFEDEFRETLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  84 YT----VAMARTMEPHSASaQFFINVADNAFLNhsGKnvqgwgYAVFGKVTQGTDVVDKIKgvstTSKAGHQDVPAEDVI 159
Cdd:cd01928   81 HDsrgvVSMANNGPNTNGS-QFFITYAKQPHLD--GK------YTVFGKVIDGFETLDTLE----KLPVDKKYRPLEEIR 147


                 ....*.
gi 504531838 160 VEKAEI 165
Cdd:cd01928  148 IKDVTI 153
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 6-162 1.80e-19

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: 79.50  E-value: 1.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   6 LTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGG---GFEPGMKEKKDKRpsIQNEADNGLsnd 82
Cdd:cd01922    2 LETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGdptGTGRGGASIYGKK--FEDEIHPEL--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  83 KYTVAMARTME---PHSASAQFFINVADNAFLNhsGKnvqgwgYAVFGKVTQGTDVVDKIKGVSTTSkaghqDVPAEDVI 159
Cdd:cd01922   77 KHTGAGILSMAnagPNTNGSQFFITLAPTPWLD--GK------HTIFGRVSKGMKVIENMVEVQTQT-----DRPIDEVK 143


                 ...
gi 504531838 160 VEK 162
Cdd:cd01922  144 ILK 146
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 11-160 7.22e-18

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: 75.76  E-value: 7.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  11 GDIVIELNAEKAPITVANF--------IEYVKAGHYENTVFHRVIGNFMIQGGGFEP----------GMK------EKKD 66
Cdd:cd01926   15 GRIVMELFADVVPKTAENFralctgekGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRgngtggksiyGEKfpdenfKLKH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  67 KRPSIQNEADNGlsndkytvamartmePHSASAQFFINVADNAFLNhsGKNVqgwgyaVFGKVTQGTDVVDKIKGVSTTS 146
Cdd:cd01926   95 TGPGLLSMANAG---------------PNTNGSQFFITTVKTPWLD--GKHV------VFGKVVEGMDVVKKIENVGSGN 151

                        170
                 ....*....|....
gi 504531838 147 kaghqDVPAEDVIV 160
Cdd:cd01926  152 -----GKPKKKVVI 160
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 4-133 2.81e-17

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: 74.31  E-value: 2.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   4 VKLTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQGGgfEP---GMKEKkdkrpSIQNE--ADNG 78
Cdd:cd01925    8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGG--DPtgtGTGGE-----SIYGEpfKDEF 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504531838  79 LSNDKYT----VAMARTmEPHSASAQFFINVADNAFLNhsGKNvqgwgyAVFGKVTQGT 133
Cdd:cd01925   81 HSRLRFNrrglVGMANA-GDDSNGSQFFFTLDKADELN--NKH------TLFGKVTGDT 130
PTZ00060 PTZ00060
cyclophilin; Provisional
 9-157 1.17e-13

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 65.25  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   9 NHGDIVIELNAEKAPITVANFIEYV---------KAGHYENTVFHRVIGNFMIQGGGF--EPGMKEKKDKRPSIQNEADN 77
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDItnHNGTGGESIYGRKFTDENFK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  78 GLSNDKYTVAMARTmEPHSASAQFFINVADNAFLNhsGKNVqgwgyaVFGKVTQGTDVVDKIKGVSTTSKAGHQDVPAED 157
Cdd:PTZ00060 108 LKHDQPGLLSMANA-GPNTNGSQFFITTVPCPWLD--GKHV------VFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTD 178
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 6-139 2.60e-13

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: 63.90  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838   6 LTTNHGDIVIELNAEKAPITVANFIEYVKAGHYENTVFHRVIGNFMIQ---------GGGFEPGMKEKKDKRPSIQNEAD 76
Cdd:cd01921    2 LETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQtgdptgtgaGGESIYSQLYGRQARFFEPEILP 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504531838  77 NGLSNDKYTVAMArTMEPHSASAQFFINVADNAfLNHSGKnvqgwgYAVFGKVTQGTDVVDKI 139
Cdd:cd01921   82 LLKHSKKGTVSMV-NAGDNLNGSQFYITLGENL-DYLDGK------HTVFGQVVEGFDVLEKI 136
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 11-144 9.14e-12

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 60.23  E-value: 9.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504531838  11 GDIVIELNAEKAPITVANFI-----EYVKAGH---YENTVFHRVIGNFMIQGGGFEPG--------MKEKKDKRPSIQNE 74
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRqfctgEFRKAGLpqgYKGCQFHRVIKDFMIQGGDFLKGdgtgcvsiYGSKFEDENFIAKH 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504531838  75 ADNGLsndkytVAMARTmEPHSASAQFFINVADNAFLNHsgKNVqgwgyaVFGKVT-QGTDVVDKIKGVST 144
Cdd:PLN03149 113 TGPGL------LSMANS-GPNTNGCQFFITCAKCDWLDN--KHV------VFGRVLgDGLLVVRKIENVAT 168
 
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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