NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|27735045|ref|NP_775943|]
View 

probable inactive peptidyl-prolyl cis-trans isomerase-like 6 isoform 1 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 144-307 5.22e-70

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 cd01926:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 164  Bit Score: 214.43  E-value: 5.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 144 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 223
Cdd:cd01926   3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 224 YGPTFEDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNERPIHMCRI 303
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 27735045 304 TDSG 307
Cdd:cd01926 161 ADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 144-307 5.22e-70

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: 214.43  E-value: 5.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 144 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 223
Cdd:cd01926   3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 224 YGPTFEDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNERPIHMCRI 303
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 27735045 304 TDSG 307
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 127-308 3.97e-66

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 205.46  E-value: 3.97e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  127 LTEDFSAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAgFSQRGIRLHYKNSIFHRIVQNGW 206
Cdd:PTZ00060   1 FFKLFSQSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  207 IQGGDIVYGKGDNGESIYGPTFEDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQ 286
Cdd:PTZ00060  80 CQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRA 159

                        170       180
                 ....*....|....*....|..
gi 27735045  287 LELVPTQNERPIHMCRITDSGD 308
Cdd:PTZ00060 160 MEKEGTQSGYPKKPVVVTDCGE 181
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 153-307 5.99e-56

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: 178.22  E-value: 5.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045   153 SPIGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVygkGDNGESIYGPTFEDEN 232
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEI 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27735045   233 F-SVPHNKRGVLGMANKGR--HSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNERPIHMCRITDSG 307
Cdd:pfam00160  71 FpLLLKHKRGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 156-304 2.07e-38

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 133.37  E-value: 2.07e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIvYGKGDNGEsiyGPTFEDENFSV 235
Cdd:COG0652  16 GDIVIELFPDKAPKTVANFVSLA--KEGF--------YDGTIFHRVIPGFMIQGGDP-TGTGTGGP---GYTIPDEFDPG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27735045 236 PHNKRGVLGMAN-KGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQ-NERPIHMCRIT 304
Cdd:COG0652  82 LKHKRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDpGDGPLEPVVIE 152
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 144-307 5.22e-70

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: 214.43  E-value: 5.22e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 144 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 223
Cdd:cd01926   3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 224 YGPTFEDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNERPIHMCRI 303
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 27735045 304 TDSG 307
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 127-308 3.97e-66

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 205.46  E-value: 3.97e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  127 LTEDFSAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAgFSQRGIRLHYKNSIFHRIVQNGW 206
Cdd:PTZ00060   1 FFKLFSQSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  207 IQGGDIVYGKGDNGESIYGPTFEDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQ 286
Cdd:PTZ00060  80 CQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRA 159

                        170       180
                 ....*....|....*....|..
gi 27735045  287 LELVPTQNERPIHMCRITDSGD 308
Cdd:PTZ00060 160 MEKEGTQSGYPKKPVVVTDCGE 181
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 155-305 1.97e-58

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: 184.39  E-value: 1.97e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 155 IGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVYGKGdnGESIYGPTFEDENFS 234
Cdd:cd00317   6 KGRIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPDENFP 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27735045 235 VP-HNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQ-NERPIHMCRITD 305
Cdd:cd00317  74 LKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDeNGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 153-307 5.99e-56

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: 178.22  E-value: 5.99e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045   153 SPIGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVygkGDNGESIYGPTFEDEN 232
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEI 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27735045   233 F-SVPHNKRGVLGMANKGR--HSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNERPIHMCRITDSG 307
Cdd:pfam00160  71 FpLLLKHKRGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 140-308 5.32e-51

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 166.93  E-value: 5.32e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  140 KHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKagFSQRGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDN 219
Cdd:PLN03149  17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  220 GESIYGPTFEDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLI-EGTEVLKQLELVPT-QNERP 297
Cdd:PLN03149  95 CVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATgPNNRP 174

                        170
                 ....*....|.
gi 27735045  298 IHMCRITDSGD 308
Cdd:PLN03149 175 KLACVISECGE 185
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 156-305 5.87e-46

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known.


Pssm-ID: 238909 [Multi-domain]  Cd Length: 153  Bit Score: 152.59  E-value: 5.87e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 156 GRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEDENFS- 234
Cdd:cd01928  10 GDIKIELFCDDCPKACENFLALCASG----------YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREt 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27735045 235 VPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPT-QNERPIHMCRITD 305
Cdd:cd01928  79 LKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVdKKYRPLEEIRIKD 150
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 156-311 3.13e-44

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.


Pssm-ID: 238904 [Multi-domain]  Cd Length: 159  Bit Score: 148.33  E-value: 3.13e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 156 GRLIFELYCDVCPKTCKNFQVLCtgkagfsQRGirlHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEDE---N 232
Cdd:cd01923   9 GDLNLELHCDKAPKACENFIKLC-------KKG---YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfkpN 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 233 FSvpHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQ-NERPIHMCRITDSG---D 308
Cdd:cd01923  78 LS--HDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPgTDRPKEEIKIEDTSvfvD 155


                ...
gi 27735045 309 PYA 311
Cdd:cd01923 156 PFE 158
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 155-303 8.63e-39

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: 133.81  E-value: 8.63e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 155 IGRLIFELYCDVCPKTCKNFQVLCTgkagfsqrgiRLHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEDE-NF 233
Cdd:cd01922   6 MGEITLELYWNHAPKTCKNFYELAK----------RGYYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHP 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 234 SVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNERPIHMCRI 303
Cdd:cd01922  75 ELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 156-304 2.07e-38

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 133.37  E-value: 2.07e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIvYGKGDNGEsiyGPTFEDENFSV 235
Cdd:COG0652  16 GDIVIELFPDKAPKTVANFVSLA--KEGF--------YDGTIFHRVIPGFMIQGGDP-TGTGTGGP---GYTIPDEFDPG 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27735045 236 PHNKRGVLGMAN-KGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQ-NERPIHMCRIT 304
Cdd:COG0652  82 LKHKRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDpGDGPLEPVVIE 152
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 156-303 2.04e-36

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: 127.96  E-value: 2.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEDE-NFS 234
Cdd:cd01927   7 GDIHIRLFPEEAPKTVENFTTHA--RNGY--------YNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPS 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 235 VPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLELVPT-QNERPIHMCRI 303
Cdd:cd01927  76 LKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTdKNDRPYEDIKI 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 156-304 4.58e-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: 125.16  E-value: 4.58e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 156 GRLIFELYCDVCPKTCKNFQVLCtgkagfsqrgIRLHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEDENFS- 234
Cdd:cd01925  15 GDIDIELWSKEAPKACRNFIQLC----------LEGYYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEFHSr 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27735045 235 VPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGT--EVLKQLELVPTQNERPIHMCRIT 304
Cdd:cd01925  84 LRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTiyNLLKLAEVETDKDERPVYPPKIT 155
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 155-304 5.39e-30

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: 111.66  E-value: 5.39e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 155 IGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDiVYGKGDNGESIYGPT------- 227
Cdd:cd01921   6 LGDLVIDLFTDECPLACLNFLKLCKLK----------YYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQLygrqarf 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 228 FEDE-NFSVPHNKRGVLGMANKGRHSNGSQFYITL-QATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNE-RPIHMCRIT 304
Cdd:cd01921  75 FEPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLgENLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDgRPLKDIRIK 154
PTZ00221 PTZ00221
cyclophilin; Provisional
 132-298 8.96e-30

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 113.43  E-value: 8.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  132 SAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGF-SQRGIRLHYKNSIFHRI-VQNGWIQG 209
Cdd:PTZ00221  43 SHRMKEEQNSCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdTNTGVKLDYLYTPVHHVdRNNNIIVL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  210 GDIV-YGKGDNGESIygptfEDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLE 288
Cdd:PTZ00221 123 GELDsFNVSSTGTPI-----ADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLE 197

                        170
                 ....*....|.
gi 27735045  289 LVP-TQNERPI 298
Cdd:PTZ00221 198 SLPlDDVGRPL 208
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 156-297 5.22e-17

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: 76.71  E-value: 5.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGdivyGKGDNGESIygPTFE---DEN 232
Cdd:cd01920   7 GDIVVELYDDKAPITVENFLAYV--RKGF--------YDNTIFHRVISGFVIQGG----GFTPDLAQK--ETLKpikNEA 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27735045 233 FSVPHNKRGVLGMA-NKGRHSNGSQFYITLQATPYLDRK-----FVAFGQLIEGTEVLKQLELVPTQNERP 297
Cdd:cd01920  71 GNGLSNTRGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETYSFGS 141
PRK10903 PRK10903
peptidylprolyl isomerase A;
156-297 5.59e-10

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 57.93  E-value: 5.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  156 GRLIFELYCDVCPKTCKNFqvLCTGKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIvygKGDNGESIYGPTFEDENFSV 235
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNF--VDYVNSGF--------YNNTTFHRVIPGFMIQGGGF---TEQMQQKKPNPPIKNEADNG 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27735045  236 PHNKRGVLGMANKG-RHSNGSQFYITLQATPYLD---RKF--VAFGQLIEGTEVLKQLELVPTQNERP 297
Cdd:PRK10903 105 LRNTRGTIAMARTAdKDSATSQFFINVADNAFLDhgqRDFgyAVFGKVVKGMDVADKISQVPTHDVGP 172
PRK10791 PRK10791
peptidylprolyl isomerase B;
156-292 4.17e-08

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 51.76  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045  156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDivYGKGDNGESIYGPTFEDENFSV 235
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYC--REGF--------YNNTIFHRVINGFMIQGGG--FEPGMKQKATKEPIKNEANNGL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27735045  236 pHNKRGVLGMA-NKGRHSNGSQFYITLQATPYLDRK--------FVAFGQLIEGTEVLKQLELVPT 292
Cdd:PRK10791  77 -KNTRGTLAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVAT 141
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 168-289 4.24e-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: 52.06  E-value: 4.24e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27735045 168 PKTCKNFqvlctgkAGFSQRGIrlhYKNSIFHRIVQNGWIQGGDiVYGKGDN---------------------GESIYGP 226
Cdd:cd01924  19 PVTAGNF-------VDLVERGF---YDGMEFHRVEGGFVVQTGD-PQGKNPGfpdpetgksrtipleikpegqKQPVYGK 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27735045 227 TFE-----DENFSVPHNKRGVLGMAN--KGRHSNGSQFYITLQA-------TPYLDRKFVAFGQLIEGTEVLKQLEL 289
Cdd:cd01924  88 TLEeagryDEQPVLPFNAFGAIAMARteFDPNSASSQFFFLLKDneltpsrNNVLDGRYAVFGYVTDGLDILRELKV 164
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH