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Conserved domains on  [gi|606215155|ref|NP_001129261|]
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peptidyl-prolyl cis-trans isomerase A-like 4A/B/C [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 ...
 4-162 3.49e-101

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: 287.62  E-value: 3.49e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   4 SVVFFDITVDGKPLGRISIKLFADKIPKTAENFRALSTGEKG-----FRYKGSCFHRIIPGFMCQGGDFTRPNGTGDKSI 78
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  79 YGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKITI 158
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                 ....
gi 606215155 159 ADCG 162
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 ...
 4-162 3.49e-101

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: 287.62  E-value: 3.49e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   4 SVVFFDITVDGKPLGRISIKLFADKIPKTAENFRALSTGEKG-----FRYKGSCFHRIIPGFMCQGGDFTRPNGTGDKSI 78
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  79 YGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKITI 158
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                 ....
gi 606215155 159 ADCG 162
Cdd:cd01926  161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 3-163 4.78e-80

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 234.74  E-value: 4.78e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   3 NSVVFFDITVDGKPLGRISIKLFADKIPKTAENFRALSTGE------KGFRYKGSCFHRIIPGFMCQGGDFTRPNGTGDK 76
Cdd:PTZ00060  15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  77 SIYGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKI 156
Cdd:PTZ00060  95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPV 174


                 ....*..
gi 606215155 157 TIADCGQ 163
Cdd:PTZ00060 175 VVTDCGE 181
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 10-162 1.51e-47

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: 151.25  E-value: 1.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   10 ITVDGkpLGRISIKLFADKIPKTAENFRALSTgeKGFrYKGSCFHRIIPGFMCQGGDFTRPNGTGdksIYGEKFDDENL- 88
Cdd:pfam00160   1 IETNG--LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPTGTGGGG---KSIFPIPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 606215155   89 IRKHTGSGILSMANAG--PNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKITIADCG 162
Cdd:pfam00160  73 LLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 17-143 5.72e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 142.62  E-value: 5.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFRALStgEKGFrYKGSCFHRIIPGFMCQGGDFTrPNGTGDKsiyGEKFDDENLIRKHTGSG 96
Cdd:COG0652   15 KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPGLKHKRG 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 606215155  97 ILSMANA-GPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAME 143
Cdd:COG0652   88 TLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIA 135
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 4-162 3.49e-101

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: 287.62  E-value: 3.49e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   4 SVVFFDITVDGKPLGRISIKLFADKIPKTAENFRALSTGEKG-----FRYKGSCFHRIIPGFMCQGGDFTRPNGTGDKSI 78
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  79 YGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKITI 158
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                 ....
gi 606215155 159 ADCG 162
Cdd:cd01926  161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 3-163 4.78e-80

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 234.74  E-value: 4.78e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   3 NSVVFFDITVDGKPLGRISIKLFADKIPKTAENFRALSTGE------KGFRYKGSCFHRIIPGFMCQGGDFTRPNGTGDK 76
Cdd:PTZ00060  15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  77 SIYGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKI 156
Cdd:PTZ00060  95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPV 174


                 ....*..
gi 606215155 157 TIADCGQ 163
Cdd:PTZ00060 175 VVTDCGE 181
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 3-163 4.22e-67

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 202.37  E-value: 4.22e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   3 NSVVFFDITVDGKPLGRISIKLFADKIPKTAENFRALSTGEkgFR-------YKGSCFHRIIPGFMCQGGDFTRPNGTGD 75
Cdd:PLN03149  18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRkaglpqgYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  76 KSIYGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKV-KERVNIVEAMEHFGY-RNSKTS 153
Cdd:PLN03149  96 VSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVlGDGLLVVRKIENVATgPNNRPK 175

                        170
                 ....*....|
gi 606215155 154 KKITIADCGQ 163
Cdd:PLN03149 176 LACVISECGE 185
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 7-160 3.34e-56

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: 173.22  E-value: 3.34e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   7 FFDITVdgkplGRISIKLFADKIPKTAENFRALSTGEkgfRYKGSCFHRIIPGFMCQGGDFTRPNGTGdkSIYGEKFDDE 86
Cdd:cd00317    1 TLDTTK-----GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPTGTGGGG--SGPGYKFPDE 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 606215155  87 NLIRK-HTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFG-YRNSKTSKKITIAD 160
Cdd:cd00317   71 NFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 10-162 1.51e-47

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: 151.25  E-value: 1.51e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   10 ITVDGkpLGRISIKLFADKIPKTAENFRALSTgeKGFrYKGSCFHRIIPGFMCQGGDFTRPNGTGdksIYGEKFDDENL- 88
Cdd:pfam00160   1 IETNG--LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPTGTGGGG---KSIFPIPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 606215155   89 IRKHTGSGILSMANAG--PNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNSKTSKKITIADCG 162
Cdd:pfam00160  73 LLLKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 17-142 1.54e-45

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: 146.14  E-value: 1.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFRALSTgeKGFrYKGSCFHRIIPGFMCQGGDFTrPNGTGDKSIYGEKFDDE-NLIRKHTGS 95
Cdd:cd01922    6 MGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPELKHTGA 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 606215155  96 GILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAM 142
Cdd:cd01922   82 GILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM 128
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 17-143 5.72e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 142.62  E-value: 5.72e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFRALStgEKGFrYKGSCFHRIIPGFMCQGGDFTrPNGTGDKsiyGEKFDDENLIRKHTGSG 96
Cdd:COG0652   15 KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPT-GTGTGGP---GYTIPDEFDPGLKHKRG 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 606215155  97 ILSMANA-GPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAME 143
Cdd:COG0652   88 TLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIA 135
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 17-155 1.56e-42

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: 138.36  E-value: 1.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFralSTGEKGFRYKGSCFHRIIPGFMCQGGDFTrPNGTGDKSIYGEKFDDE---NLirKHT 93
Cdd:cd01927    6 KGDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfspSL--KHD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 606215155  94 GSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEhfgyrNSKTSKK 155
Cdd:cd01927   80 RPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIE-----NVKTDKN 136
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 17-160 2.71e-41

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: 135.62  E-value: 2.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFRALStgEKGFrYKGSCFHRIIPGFMCQGGDFTrPNGTGDKSIYGEKFDDE---NLirKHT 93
Cdd:cd01923    8 KGDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfkpNL--SHD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 606215155  94 GSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAMEHFGYRNS-KTSKKITIAD 160
Cdd:cd01923   82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTdRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 17-143 1.36e-40

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: 133.72  E-value: 1.36e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFRALSTGekGFrYKGSCFHRIIPGFMCQGGDFTRPnGTGDKSIYGEKFDDEnlIR---KHT 93
Cdd:cd01928    9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPTGT-GKGGESIWGKKFEDE--FRetlKHD 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 606215155  94 GSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAME 143
Cdd:cd01928   83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLE 132
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 17-132 1.16e-34

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: 119.38  E-value: 1.16e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFRALSTgeKGFrYKGSCFHRIIPGFMCQGGDFTRpNGTGDKSIYGEKFDDENLIR-KHTGS 95
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEFHSRlRFNRR 89

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 606215155  96 GILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKV 132
Cdd:cd01925   90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV 126
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 17-134 3.87e-23

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: 89.32  E-value: 3.87e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFRALStgeKGFRYKGSCFHRIIPGFMCQGGDFTRPnGTGDKSIYGEK-------FDDENLI 89
Cdd:cd01921    6 LGDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPTGT-GAGGESIYSQLygrqarfFEPEILP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 606215155  90 R-KHTGSGILSMANAGPNTNGSQFFICTAK-TEWLDGKHVAFGKVKE 134
Cdd:cd01921   82 LlKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVE 128
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 17-143 2.31e-20

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: 82.11  E-value: 2.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  17 LGRISIKLFADKIPKTAENFraLSTGEKGFrYKGSCFHRIIPGFMCQGGDFTRPngtgdksiyGEKFDDENLIRKHTGSG 96
Cdd:cd01920    6 LGDIVVELYDDKAPITVENF--LAYVRKGF-YDNTIFHRVISGFVIQGGGFTPD---------LAQKETLKPIKNEAGNG 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 606215155  97 I------LSMA-NAGPNTNGSQFFICTAKTEWLD-----GKHVAFGKVKERVNIVEAME 143
Cdd:cd01920   74 LsntrgtIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIA 132
PTZ00221 PTZ00221
cyclophilin; Provisional
 6-143 4.16e-20

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 83.38  E-value: 4.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155   6 VFFDITVDGKPLGRISIKLFADKIPKTAENFRALSTGEKG--------FRYKGSCFHRIipgfmcqggdfTRPNGT---G 74
Cdd:PTZ00221  55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHV-----------DRNNNIivlG 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 606215155  75 D-----KSIYGEKFDDENLIRKHTGSGILSMANAGPNTNGSQFFICTAKTEWLDGKHVAFGKVKERVNIVEAME 143
Cdd:PTZ00221 124 EldsfnVSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLE 197
PRK10903 PRK10903
peptidylprolyl isomerase A;
18-140 1.03e-11

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 60.24  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  18 GRISIKLFADKIPKTAENFraLSTGEKGFrYKGSCFHRIIPGFMCQGGDFTR--PNGTGDKSIYGEKfddENLIRKHTGS 95
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNF--VDYVNSGF-YNNTTFHRVIPGFMIQGGGFTEqmQQKKPNPPIKNEA---DNGLRNTRGT 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 606215155  96 giLSMA-NAGPNTNGSQFFICTAKTEWLD-GK----HVAFGKVKERVNIVE 140
Cdd:PRK10903 112 --IAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVAD 160
PRK10791 PRK10791
peptidylprolyl isomerase B;
18-140 1.20e-10

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 56.77  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  18 GRISIKLFADKIPKTAENFraLSTGEKGFrYKGSCFHRIIPGFMCQGGDFTrpNGTGDKSIYGEKFDDENLIRKHTgSGI 97
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNF--LDYCREGF-YNNTIFHRVINGFMIQGGGFE--PGMKQKATKEPIKNEANNGLKNT-RGT 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 606215155  98 LSMANAG-PNTNGSQFFICTAKTEWLDGK--------HVAFGKVKERVNIVE 140
Cdd:PRK10791  83 LAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVD 134
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 18-159 1.26e-07

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: 48.59  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  18 GRISIKLFADKIPKTAENFRALStgEKGFrYKGSCFHRIIPGFMCQGGD-FTRPNGTGDKS------------------- 77
Cdd:cd01924    7 GTITIVLDGYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDpQGKNPGFPDPEtgksrtipleikpegqkqp 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 606215155  78 IYGE------KFDDENLIRKHTgSGILSMANA--GPNTNGSQFFICTAKTEW-------LDGKHVAFGKVKERVNIVEAM 142
Cdd:cd01924   84 VYGKtleeagRYDEQPVLPFNA-FGAIAMARTefDPNSASSQFFFLLKDNELtpsrnnvLDGRYAVFGYVTDGLDILREL 162

                        170
                 ....*....|....*..
gi 606215155 143 ehfgyrnsKTSKKITIA 159
Cdd:cd01924  163 --------KVGDKIESA 171
 
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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