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Conserved domains on  [gi|1034614705|ref|XP_016859842|]
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peptidyl-prolyl cis-trans isomerase-like 3 isoform X1 [Homo sapiens]

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 ...
 1-158 3.07e-79

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 cd01928:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 153  Bit Score: 231.94  E-value: 3.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   1 MSVTLHTDVGDIKIEVFCERTPKTCE--------------MESRCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRG 66
Cdd:cd01928     1 MSVTLHTNLGDIKIELFCDDCPKACEnflalcasgyyngcIFHRNIKGFMVQTGD-------PTG-----------TGKG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  67 GNSIWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVnEKTYR 146
Cdd:cd01928    63 GESIWGKKFEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYR 141

                         170
                  ....*....|..
gi 1034614705 147 PLNDVHIKDITI 158
Cdd:cd01928   142 PLEEIRIKDVTI 153
 
Name Accession Description Interval E-value
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 1-158 3.07e-79

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: 231.94  E-value: 3.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   1 MSVTLHTDVGDIKIEVFCERTPKTCE--------------MESRCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRG 66
Cdd:cd01928     1 MSVTLHTNLGDIKIELFCDDCPKACEnflalcasgyyngcIFHRNIKGFMVQTGD-------PTG-----------TGKG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  67 GNSIWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVnEKTYR 146
Cdd:cd01928    63 GESIWGKKFEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYR 141

                         170
                  ....*....|..
gi 1034614705 147 PLNDVHIKDITI 158
Cdd:cd01928   142 PLEEIRIKDVTI 153
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 3-158 3.61e-42

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 137.99  E-value: 3.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   3 VTLHTDVGDIKIEVFCERTPKTCEM-----ES---------RCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRGGn 68
Cdd:COG0652     9 VTLETNKGDIVIELFPDKAPKTVANfvslaKEgfydgtifhRVIPGFMIQGGD-------PTG-----------TGTGG- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  69 siWGKKFEDEYSEYLKHnVRGVVSMAN-NGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTyRP 147
Cdd:COG0652    70 --PGYTIPDEFDPGLKH-KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGD-GP 145

                         170
                  ....*....|.
gi 1034614705 148 LNDVHIKDITI 158
Cdd:COG0652   146 LEPVVIESVTI 156
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 10-158 2.55e-36

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: 122.75  E-value: 2.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  10 GDIKIEVFCERTPKTCE--------------MESRCVPQAGVQWRDLgslqppppgfkqvfclslprTGRGGNSIWGKKF 75
Cdd:pfam00160   7 GRIVIELFGDKAPKTVEnflqlckkgfydgtTFHRVIPGFMVQGGDP--------------------TGTGGGGKSIFPI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  76 EDEYSEYLKHNVRGVVSMANNG--PNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtyRPLNDVHI 153
Cdd:pfam00160  67 PDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD--RPVKPVKI 144


                  ....*
gi 1034614705 154 KDITI 158
Cdd:pfam00160 145 LSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 10-155 6.79e-26

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 97.22  E-value: 6.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  10 GDIKIEVFCERTPKTCE-MESRCVPqagvqwrDLGSLQPPPPGFK-QVFCLSLPR-----------TGRGGNSIWGKKFE 76
Cdd:PTZ00060   30 GRIVFELFSDVTPKTAEnFRALCIG-------DKVGSSGKNLHYKgSIFHRIIPQfmcqggditnhNGTGGESIYGRKFT 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034614705  77 DEYSEyLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKlpVNEKTYRPLNDVHIKD 155
Cdd:PTZ00060  103 DENFK-LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEK--EGTQSGYPKKPVVVTD 178
 
Name Accession Description Interval E-value
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 1-158 3.07e-79

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: 231.94  E-value: 3.07e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   1 MSVTLHTDVGDIKIEVFCERTPKTCE--------------MESRCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRG 66
Cdd:cd01928     1 MSVTLHTNLGDIKIELFCDDCPKACEnflalcasgyyngcIFHRNIKGFMVQTGD-------PTG-----------TGKG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  67 GNSIWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVnEKTYR 146
Cdd:cd01928    63 GESIWGKKFEDEFRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYR 141

                         170
                  ....*....|..
gi 1034614705 147 PLNDVHIKDITI 158
Cdd:cd01928   142 PLEEIRIKDVTI 153
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 3-165 1.12e-55

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: 172.21  E-value: 1.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   3 VTLHTDVGDIKIEVFCERTPKTCE--------------MESRCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRGGN 68
Cdd:cd01923     2 VRLHTNKGDLNLELHCDKAPKACEnfiklckkgyydgtIFHRSIRNFMIQGGD-------PTG-----------TGRGGE 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  69 SIWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNeKTYRPL 148
Cdd:cd01923    64 SIWGKPFKDEFKPNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDP-GTDRPK 142

                         170
                  ....*....|....*..
gi 1034614705 149 NDVHIKDITIHANPFAQ 165
Cdd:cd01923   143 EEIKIEDTSVFVDPFEE 159
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 4-155 9.81e-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: 146.64  E-value: 9.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   4 TLHTDVGDIKIEVFCERTPKTCE-MESRCvpqAGVQWRDLgSLQPPPPGFkqVFCLSLPRTGRGGNSIWGKKFEDEYSEY 82
Cdd:cd00317     1 TLDTTKGRIVIELYGDEAPKTVEnFLSLA---RGGFYDGT-TFHRVIPGF--MIQGGDPTGTGGGGSGPGYKFPDENFPL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034614705  83 LKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtYRPLNDVHIKD 155
Cdd:cd00317    75 KYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDEN-GRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 3-158 3.61e-42

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 137.99  E-value: 3.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   3 VTLHTDVGDIKIEVFCERTPKTCEM-----ES---------RCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRGGn 68
Cdd:COG0652     9 VTLETNKGDIVIELFPDKAPKTVANfvslaKEgfydgtifhRVIPGFMIQGGD-------PTG-----------TGTGG- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  69 siWGKKFEDEYSEYLKHnVRGVVSMAN-NGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKTyRP 147
Cdd:COG0652    70 --PGYTIPDEFDPGLKH-KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGD-GP 145

                         170
                  ....*....|.
gi 1034614705 148 LNDVHIKDITI 158
Cdd:COG0652   146 LEPVVIESVTI 156
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 4-156 2.57e-37

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: 125.27  E-value: 2.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   4 TLHTDVGDIKIEVFCERTPKTCE--------------MESRCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRGGNS 69
Cdd:cd01927     1 IIHTTKGDIHIRLFPEEAPKTVEnfttharngyynntIFHRVIKGFMIQTGD-------PTG-----------DGTGGES 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  70 IWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNeKTYRPLN 149
Cdd:cd01927    63 IWGKEFEDEFSPSLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTD-KNDRPYE 141


                  ....*..
gi 1034614705 150 DVHIKDI 156
Cdd:cd01927   142 DIKIINI 148
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 10-158 2.55e-36

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: 122.75  E-value: 2.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  10 GDIKIEVFCERTPKTCE--------------MESRCVPQAGVQWRDLgslqppppgfkqvfclslprTGRGGNSIWGKKF 75
Cdd:pfam00160   7 GRIVIELFGDKAPKTVEnflqlckkgfydgtTFHRVIPGFMVQGGDP--------------------TGTGGGGKSIFPI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  76 EDEYSEYLKHNVRGVVSMANNG--PNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEKtyRPLNDVHI 153
Cdd:pfam00160  67 PDEIFPLLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD--RPVKPVKI 144


                  ....*
gi 1034614705 154 KDITI 158
Cdd:pfam00160 145 LSCGV 149
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-153 1.38e-35

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: 120.72  E-value: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   4 TLHTDVGDIKIEVFCERTPKTCEMES--------------RCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRGGNS 69
Cdd:cd01922     1 TLETTMGEITLELYWNHAPKTCKNFYelakrgyyngtifhRLIKDFMIQGGD-------PTG-----------TGRGGAS 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  70 IWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKlpVNEKTYRPLN 149
Cdd:cd01922    63 IYGKKFEDEIHPELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVE--VQTQTDRPID 140


                  ....
gi 1034614705 150 DVHI 153
Cdd:cd01922   141 EVKI 144
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 2-163 2.23e-35

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: 120.92  E-value: 2.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   2 SVTLHTDVGDIKIEVFCERTPKTCE------MES--------RCVPQAGVQWRDlgslqppPPGfkqvfclslprTGRGG 67
Cdd:cd01925     7 KVILKTTAGDIDIELWSKEAPKACRnfiqlcLEGyydntifhRVVPGFIIQGGD-------PTG-----------TGTGG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  68 NSIWGKKFEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVI-DGLETLDELEKLPVNEKTyR 146
Cdd:cd01925    69 ESIYGEPFKDEFHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIYNLLKLAEVETDKDE-R 147

                         170
                  ....*....|....*..
gi 1034614705 147 PLNDVHIKDITIHANPF 163
Cdd:cd01925   148 PVYPPKITSVEVLENPF 164
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 7-155 1.24e-31

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: 111.19  E-value: 1.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   7 TDVGDIKIEVFCERTPKTCE-MESRCVPQAGVQwrdlgslqPPPPGFK-QVFCLSLP-----------RTGRGGNSIWGK 73
Cdd:cd01926    12 EPAGRIVMELFADVVPKTAEnFRALCTGEKGKG--------GKPFGYKgSTFHRVIPdfmiqggdftrGNGTGGKSIYGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  74 KFEDEYSEyLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVneKTYRPLNDVHI 153
Cdd:cd01926    84 KFPDENFK-LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS--GNGKPKKKVVI 160


                  ..
gi 1034614705 154 KD 155
Cdd:cd01926   161 AD 162
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 5-163 3.48e-26

cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis.


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 97.41  E-value: 3.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   5 LHTDVGDIKIEVFCERTPKTCE-----MESR---CVPQAGVQWRDLGSLQPPPPgfkqvfclslprTGRGGNSIWGKK-- 74
Cdd:cd01921     2 LETTLGDLVIDLFTDECPLACLnflklCKLKyynFCLFYNVQKDFIAQTGDPTG------------TGAGGESIYSQLyg 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  75 -----FEDEYSEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQ-PHLDMKYTVFGKVIDGLETLDELEKLPVNEKtYRPL 148
Cdd:cd01921    70 rqarfFEPEILPLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKINDAIVDDD-GRPL 148

                         170
                  ....*....|....*
gi 1034614705 149 NDVHIKDITIHANPF 163
Cdd:cd01921   149 KDIRIKHTHILDDPF 163
PTZ00060 PTZ00060
cyclophilin; Provisional
 10-155 6.79e-26

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 97.22  E-value: 6.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  10 GDIKIEVFCERTPKTCE-MESRCVPqagvqwrDLGSLQPPPPGFK-QVFCLSLPR-----------TGRGGNSIWGKKFE 76
Cdd:PTZ00060   30 GRIVFELFSDVTPKTAEnFRALCIG-------DKVGSSGKNLHYKgSIFHRIIPQfmcqggditnhNGTGGESIYGRKFT 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034614705  77 DEYSEyLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKlpVNEKTYRPLNDVHIKD 155
Cdd:PTZ00060  103 DENFK-LKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEK--EGTQSGYPKKPVVVTD 178
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 8-136 4.25e-22

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 87.20  E-value: 4.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   8 DVGDIKIEVFCERTPKTCE-MESRCvpqAGvQWRDLGSlqppPPGFKQV--------FCLS----LPRTGRGGNSIWGKK 74
Cdd:PLN03149   31 PAGRIKMELFADIAPKTAEnFRQFC---TG-EFRKAGL----PQGYKGCqfhrvikdFMIQggdfLKGDGTGCVSIYGSK 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034614705  75 FEDEySEYLKHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVI-DGLETLDELE 136
Cdd:PLN03149  103 FEDE-NFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIE 164
PTZ00221 PTZ00221
cyclophilin; Provisional
 84-153 3.90e-15

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 70.28  E-value: 3.90e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  84 KHNVRGVVSMANNGPNTNGSQFFITYGKQPHLDMKYTVFGKVIDGLETLDELEKLPVNEkTYRPLNDVHI 153
Cdd:PTZ00221  145 RHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDD-VGRPLLPVTV 213
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-158 3.37e-13

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: 63.23  E-value: 3.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705   4 TLHTDVGDIKIEVFCERTPKTCE--------------MESRCVPQAGVQWrdlGSLQPPppgFKQVFCLSlPRTGRGGNS 69
Cdd:cd01920     1 EFQTSLGDIVVELYDDKAPITVEnflayvrkgfydntIFHRVISGFVIQG---GGFTPD---LAQKETLK-PIKNEAGNG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  70 IwgkkfedeyseylkHNVRGVVSMA-NNGPNTNGSQFFITYGKQPHLDMK-----YTVFGKVIDGLETLDELEKLPVNek 143
Cdd:cd01920    74 L--------------SNTRGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETY-- 137

                         170
                  ....*....|....*
gi 1034614705 144 TYRPLNDVHIKDITI 158
Cdd:cd01920   138 SFGSYQDVPVQDVII 152
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 86-136 1.55e-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: 1.55e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034614705  86 NVRGVVSMAN--NGPNTNGSQFFITYGKQ-------PHLDMKYTVFGKVIDGLETLDELE 136
Cdd:cd01924   104 NAFGAIAMARteFDPNSASSQFFFLLKDNeltpsrnNVLDGRYAVFGYVTDGLDILRELK 163
PRK10903 PRK10903
peptidylprolyl isomerase A;
86-158 7.58e-07

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 46.76  E-value: 7.58e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034614705  86 NVRGVVSMANNG-PNTNGSQFFITYGKQPHL-----DMKYTVFGKVIDGLETLDELEKLPVneKTYRPLNDVHIKDITI 158
Cdd:PRK10903  107 NTRGTIAMARTAdKDSATSQFFINVADNAFLdhgqrDFGYAVFGKVVKGMDVADKISQVPT--HDVGPYQNVPSKPVVI 183
 
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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