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Conserved domains on  [gi|17552784|ref|NP_497745|]
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Peptidyl-prolyl cis-trans isomerase 9 [Caenorhabditis elegans]

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 ...
 6-172 5.45e-84

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: 249.87  E-value: 5.45e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   6 RVFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVGmtpNNKARLHYKQNEFHRIVKKFMIQGGDITEGDGRGGF 85
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKG---KGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  86 SIYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVdDKSKPLAK 165
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS-GNGKPKKK 157


                ....*..
gi 17552784 166 VLISNCG 172
Cdd:cd01926 158 VVIADCG 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 ...
 6-172 5.45e-84

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: 249.87  E-value: 5.45e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   6 RVFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVGmtpNNKARLHYKQNEFHRIVKKFMIQGGDITEGDGRGGF 85
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKG---KGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  86 SIYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVdDKSKPLAK 165
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS-GNGKPKKK 157


                ....*..
gi 17552784 166 VLISNCG 172
Cdd:cd01926 158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-174 3.99e-74

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 225.88  E-value: 3.99e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    1 MAAEKRVFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVGMTPNNKarLHYKQNEFHRIVKKFMIQGGDITEGD 80
Cdd:PTZ00060  12 MSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSSGKN--LHYKGSIFHRIIPQFMCQGGDITNHN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   81 GRGGFSIYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDnlAVDDKS 160
Cdd:PTZ00060  90 GTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAME--KEGTQS 167

                        170
                 ....*....|....*
gi 17552784  161 -KPLAKVLISNCGEL 174
Cdd:PTZ00060 168 gYPKKPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 16-173 6.32e-54

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 172.83  E-value: 6.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    16 NLIGRIEIRLFVEDAPKTCENFRALCTGEvgmtpnnkarlHYKQNEFHRIVKKFMIQGGDITEGDGRGgfsIYGRYFDDE 95
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKG-----------FYDGTTFHRVIPGFMVQGGDPTGTGGGG---KSIFPIPDE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    96 KF--KLKHsRPYLLSMANKG--PNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKsKPLAKVLISNC 171
Cdd:pfam00160  70 IFplLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPVKILSC 147


                  ..
gi 17552784   172 GE 173
Cdd:pfam00160 148 GV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-168 1.40e-46

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 154.17  E-value: 1.40e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   1 MAAEKRVFLDISVDEnliGRIEIRLFVEDAPKTCENFRALCTgevgmtpnnkaRLHYKQNEFHRIVKKFMIQGGDITeGD 80
Cdd:COG0652   1 MKAAPNPTVTLETNK---GDIVIELFPDKAPKTVANFVSLAK-----------EGFYDGTIFHRVIPGFMIQGGDPT-GT 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  81 GRGGfsiYGRYFDDE-KFKLKHsRPYLLSMAN-KGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDD 158
Cdd:COG0652  66 GTGG---PGYTIPDEfDPGLKH-KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP 141

                       170
                ....*....|
gi 17552784 159 KSKPLAKVLI 168
Cdd:COG0652 142 GDGPLEPVVI 151
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 6-172 5.45e-84

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: 249.87  E-value: 5.45e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   6 RVFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVGmtpNNKARLHYKQNEFHRIVKKFMIQGGDITEGDGRGGF 85
Cdd:cd01926   2 KVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKG---KGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  86 SIYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVdDKSKPLAK 165
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS-GNGKPKKK 157


                ....*..
gi 17552784 166 VLISNCG 172
Cdd:cd01926 158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-174 3.99e-74

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 225.88  E-value: 3.99e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    1 MAAEKRVFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVGMTPNNKarLHYKQNEFHRIVKKFMIQGGDITEGD 80
Cdd:PTZ00060  12 MSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSSGKN--LHYKGSIFHRIIPQFMCQGGDITNHN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   81 GRGGFSIYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDnlAVDDKS 160
Cdd:PTZ00060  90 GTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAME--KEGTQS 167

                        170
                 ....*....|....*
gi 17552784  161 -KPLAKVLISNCGEL 174
Cdd:PTZ00060 168 gYPKKPVVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 8-170 9.71e-60

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: 187.47  E-value: 9.71e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   8 FLDISVdenliGRIEIRLFVEDAPKTCENFRALCTGEvgmtpnnkarlHYKQNEFHRIVKKFMIQGGDITegDGRGGFSI 87
Cdd:cd00317   1 TLDTTK-----GRIVIELYGDEAPKTVENFLSLARGG-----------FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSG 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  88 YGRYFDDEKFKLK-HSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKSKPLAKV 166
Cdd:cd00317  63 PGYKFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPV 142


                ....
gi 17552784 167 LISN 170
Cdd:cd00317 143 TISD 146
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 7-174 2.79e-59

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 187.74  E-value: 2.79e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    7 VFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVgmtPNNKARLHYKQNEFHRIVKKFMIQGGDITEGDGRGGFS 86
Cdd:PLN03149  21 VFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   87 IYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVV-KGQNVVDYIDNLAVDDKSKPLAK 165
Cdd:PLN03149  98 IYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLA 177


                 ....*....
gi 17552784  166 VLISNCGEL 174
Cdd:PLN03149 178 CVISECGEM 186
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 16-173 6.32e-54

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 172.83  E-value: 6.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    16 NLIGRIEIRLFVEDAPKTCENFRALCTGEvgmtpnnkarlHYKQNEFHRIVKKFMIQGGDITEGDGRGgfsIYGRYFDDE 95
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKG-----------FYDGTTFHRVIPGFMVQGGDPTGTGGGG---KSIFPIPDE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    96 KF--KLKHsRPYLLSMANKG--PNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKsKPLAKVLISNC 171
Cdd:pfam00160  70 IFplLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPVKILSC 147


                  ..
gi 17552784   172 GE 173
Cdd:pfam00160 148 GV 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 19-170 2.61e-52

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: 168.79  E-value: 2.61e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  19 GRIEIRLFVEDAPKTCENFRALCTgevgmtpnnkaRLHYKQNEFHRIVKKFMIQGGDITeGDGRGGFSIYGRYFDDEKFK 98
Cdd:cd01927   7 GDIHIRLFPEEAPKTVENFTTHAR-----------NGYYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEFSP 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17552784  99 -LKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKSKPLAKVLISN 170
Cdd:cd01927  75 sLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIIN 147
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 19-170 3.82e-51

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: 166.07  E-value: 3.82e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  19 GRIEIRLFVEDAPKTCENFRALCtgevgmtpnnkARLHYKQNEFHRIVKKFMIQGGDITeGDGRGGFSIYGRYFDDE-KF 97
Cdd:cd01928  10 GDIKIELFCDDCPKACENFLALC-----------ASGYYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEfRE 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17552784  98 KLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKSKPLAKVLISN 170
Cdd:cd01928  78 TLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKD 150
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-168 1.40e-46

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 154.17  E-value: 1.40e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   1 MAAEKRVFLDISVDEnliGRIEIRLFVEDAPKTCENFRALCTgevgmtpnnkaRLHYKQNEFHRIVKKFMIQGGDITeGD 80
Cdd:COG0652   1 MKAAPNPTVTLETNK---GDIVIELFPDKAPKTVANFVSLAK-----------EGFYDGTIFHRVIPGFMIQGGDPT-GT 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  81 GRGGfsiYGRYFDDE-KFKLKHsRPYLLSMAN-KGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDD 158
Cdd:COG0652  66 GTGG---PGYTIPDEfDPGLKH-KRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP 141

                       170
                ....*....|
gi 17552784 159 KSKPLAKVLI 168
Cdd:COG0652 142 GDGPLEPVVI 151
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 19-168 2.14e-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: 148.72  E-value: 2.14e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  19 GRIEIRLFVEDAPKTCENFRALCtgevgmtpnnkARLHYKQNEFHRIVKKFMIQGGDITeGDGRGGFSIYGRYFDDE-KF 97
Cdd:cd01923   9 GDLNLELHCDKAPKACENFIKLC-----------KKGYYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKP 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552784  98 KLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKSKPLAKVLI 168
Cdd:cd01923  77 NLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKI 147
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 15-168 9.20e-44

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: 146.53  E-value: 9.20e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  15 ENLIGRIEIRLFVEDAPKTCENFRALCTgevgmtpnnkaRLHYKQNEFHRIVKKFMIQGGDITeGDGRGGFSIYGRYFDD 94
Cdd:cd01922   3 ETTMGEITLELYWNHAPKTCKNFYELAK-----------RGYYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFED 70

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552784  95 EKFK-LKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIdnLAVD-DKSKPLAKVLI 168
Cdd:cd01922  71 EIHPeLKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM--VEVQtQTDRPIDEVKI 144
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 19-171 2.56e-36

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: 128.24  E-value: 2.56e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  19 GRIEIRLFVEDAPKTCENFRALCTGEvgmtpnnkarlHYKQNEFHRIVKKFMIQGGDITeGDGRGGFSIYGRYFDDE-KF 97
Cdd:cd01925  15 GDIDIELWSKEAPKACRNFIQLCLEG-----------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHS 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552784  98 KLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQ--NVVDyIDNLAVDDKSKPLAKVLISNC 171
Cdd:cd01925  83 RLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTiyNLLK-LAEVETDKDERPVYPPKITSV 157
PTZ00221 PTZ00221
cyclophilin; Provisional
 6-193 2.58e-33

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 122.67  E-value: 2.58e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    6 RVFLDISVDENLIGRIEIRLFVEDAPKTCENFRALCTGEVGMTPNNKARLHYKQNEFHRIVKKF-MIQGGDITEGdgrgG 84
Cdd:PTZ00221  54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVDRNNnIIVLGELDSF----N 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   85 FSIYGRYFDDEKFKLKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKSKPLA 164
Cdd:PTZ00221 130 VSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLL 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 17552784  165 KVLISNCGELVKKKKPLK-----------TDEELAAALEE 193
Cdd:PTZ00221 210 PVTVSFCGALTGEKPPGRqqllaaaddsaSSEHVACAAEE 249
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 15-169 5.21e-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: 5.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  15 ENLIGRIEIRLFVEDAPKTCENFRALCtgevgmtpnnKARlHYKQNEFHRIVKKFMIQGGDITeGDGRGGFSIYG----- 89
Cdd:cd01921   3 ETTLGDLVIDLFTDECPLACLNFLKLC----------KLK-YYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSqlygr 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  90 --RYFDDEKF-KLKHSRPYLLSMANKGPNSNSSQFFITTA-AAPHCNGKHVVFGEVVKGQNVVDYIDNLAVDDKSKPLAK 165
Cdd:cd01921  71 qaRFFEPEILpLLKHSKKGTVSMVNAGDNLNGSQFYITLGeNLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKD 150


                ....
gi 17552784 166 VLIS 169
Cdd:cd01921 151 IRIK 154
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 19-156 9.27e-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: 75.94  E-value: 9.27e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  19 GRIEIRLFVEDAPKTCENFRALCtgevgmtpnNKArlHYKQNEFHRIVKKFMIQGGDIT-EGDGRGGF------SIYGry 91
Cdd:cd01920   7 GDIVVELYDDKAPITVENFLAYV---------RKG--FYDNTIFHRVISGFVIQGGGFTpDLAQKETLkpikneAGNG-- 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552784  92 fddekfkLKHSRpYLLSMA-NKGPNSNSSQFFITTA---AAPHCNGK--HVVFGEVVKGQNVVDYIDNLAV 156
Cdd:cd01920  74 -------LSNTR-GTIAMArTNAPDSATSQFFINLKdnaSLDYQNEQwgYTVFGEVTEGMDVVDKIAGVET 136
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 19-159 2.95e-09

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: 55.53  E-value: 2.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  19 GRIEIRLFVEDAPKTCENFRALCTGEVgmtpnnkarlhYKQNEFHRIVKKFMIQGGD----------------------- 75
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLVERGF-----------YDGMEFHRVEGGFVVQTGDpqgknpgfpdpetgksrtiplei 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784  76 ITEGDGRggfSIYGRYF-----DDEKFKLKHSRPYLLSMAN--KGPNSNSSQFFI-------TTAAAPHCNGKHVVFGEV 141
Cdd:cd01924  76 KPEGQKQ---PVYGKTLeeagrYDEQPVLPFNAFGAIAMARteFDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYV 152

                       170
                ....*....|....*...
gi 17552784 142 VKGQnvvDYIDNLAVDDK 159
Cdd:cd01924 153 TDGL---DILRELKVGDK 167
PRK10791 PRK10791
peptidylprolyl isomerase B;
19-155 6.40e-09

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 54.08  E-value: 6.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   19 GRIEIRLFVEDAPKTCENFRALCTGEVgmtpnnkarlhYKQNEFHRIVKKFMIQGGDITEGDGRGgfSIYGRYFDDEKFK 98
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCREGF-----------YNNTIFHRVINGFMIQGGGFEPGMKQK--ATKEPIKNEANNG 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552784   99 LKHSRPYLLSMANKGPNSNSSQFFITTAAAPHCNGK--------HVVFGEVVKGQNVVDYIDNLA 155
Cdd:PRK10791  76 LKNTRGTLAMARTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVA 140
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-167 7.96e-09

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 54.46  E-value: 7.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784    1 MAA--EKRVFLDISVdenliGRIEIRLFVEDAPKTCENFralctgeVGMTPNNkarlHYKQNEFHRIVKKFMIQGgdite 78
Cdd:PRK10903  23 LAAkgDPHVLLTTSA-----GNIELELNSQKAPVSVKNF-------VDYVNSG----FYNNTTFHRVIPGFMIQG----- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552784   79 gdgrGGFSiygryfddEKFKLKHSRPYLLSMANKG---------------PNSNSSQFFITTAAAPHCN-GK----HVVF 138
Cdd:PRK10903  82 ----GGFT--------EQMQQKKPNPPIKNEADNGlrntrgtiamartadKDSATSQFFINVADNAFLDhGQrdfgYAVF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 17552784  139 GEVVKGQNVVDYIDNLAVDD-------KSKPL----AKVL 167
Cdd:PRK10903 150 GKVVKGMDVADKISQVPTHDvgpyqnvPSKPVvilsAKVL 189
 
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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