NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15229425|ref|NP_191899|]
View 

Cyclophilin-like peptidyl-prolyl cis-trans isomerase family protein [Arabidopsis thaliana]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112519)

cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0003755|GO:0006457
PubMed:  14731520|15998457|15353287

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_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 7-173 7.02e-105

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: 312.27  E-value: 7.02e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   7 PNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAGVGkstGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGTGG 86
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  87 ESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSP 166
Cdd:cd01926  78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                ....*..
gi 15229425 167 VKIIDCG 173
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 ...
 7-173 7.02e-105

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: 312.27  E-value: 7.02e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   7 PNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAGVGkstGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGTGG 86
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  87 ESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSP 166
Cdd:cd01926  78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                ....*..
gi 15229425 167 VKIIDCG 173
Cdd:cd01926 158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 5-176 4.78e-88

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 269.79  E-value: 4.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425    5 KNPNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAgVGKStGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGT 84
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSS-GKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   85 GGESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPT 164
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171

                        170
                 ....*....|..
gi 15229425  165 SPVKIIDCGETS 176
Cdd:PTZ00060 172 KPVVVTDCGELQ 183
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 22-174 2.28e-57

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: 189.00  E-value: 2.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425    22 RIVIELFADVVPKTAENFRALCTgeagvgksTGkplHFKGSSFHRVIKGFMAQGGDFsNGNGTGGESIYGgkFSDENF-- 99
Cdd:pfam00160   8 RIVIELFGDKAPKTVENFLQLCK--------KG---FYDGTTFHRVIPGFMVQGGDP-TGTGGGGKSIFP--IPDEIFpl 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229425   100 RLDHdGAGVLSMANCG--PNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSPVKIIDCGE 174
Cdd:pfam00160  74 LLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-170 5.87e-55

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 182.68  E-value: 5.87e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   1 MTKKKNPNVFLDVSIGgdpvqRIVIELFADVVPKTAENFRALCtgEAGvgkstgkplHFKGSSFHRVIKGFMAQGGDFsN 80
Cdd:COG0652   1 MKAAPNPTVTLETNKG-----DIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDP-T 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  81 GNGTGGEsiyGGKFSDENF-RLDHDgAGVLSMAN-CGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGT 158
Cdd:COG0652  64 GTGTGGP---GYTIPDEFDpGLKHK-RGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPT 139

                       170
                ....*....|...
gi 15229425 159 SDG-KPTSPVKII 170
Cdd:COG0652 140 DPGdGPLEPVVIE 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 ...
 7-173 7.02e-105

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: 312.27  E-value: 7.02e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   7 PNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAGVGkstGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGTGG 86
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  87 ESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSP 166
Cdd:cd01926  78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                ....*..
gi 15229425 167 VKIIDCG 173
Cdd:cd01926 158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 5-176 4.78e-88

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 269.79  E-value: 4.78e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425    5 KNPNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAgVGKStGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGT 84
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSS-GKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   85 GGESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPT 164
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171

                        170
                 ....*....|..
gi 15229425  165 SPVKIIDCGETS 176
Cdd:PTZ00060 172 KPVVVTDCGELQ 183
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 5-174 8.52e-72

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 228.18  E-value: 8.52e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425    5 KNPNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAgvgKSTGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGT 84
Cdd:PLN03149  17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   85 GGESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVV-EGMAVIKKMELVGTSDG-K 162
Cdd:PLN03149  94 GCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNnR 173

                        170
                 ....*....|..
gi 15229425  163 PTSPVKIIDCGE 174
Cdd:PLN03149 174 PKLACVISECGE 185
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 10-171 2.58e-65

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: 209.43  E-value: 2.58e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  10 FLDVSIGgdpvqRIVIELFADVVPKTAENFRALCTGEagvgkstgkplHFKGSSFHRVIKGFMAQGGDFSNGNGTGgeSI 89
Cdd:cd00317   1 TLDTTKG-----RIVIELYGDEAPKTVENFLSLARGG-----------FYDGTTFHRVIPGFMIQGGDPTGTGGGG--SG 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  90 YGGKFSDENF-RLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSD-GKPTSPV 167
Cdd:cd00317  63 PGYKFPDENFpLKYHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDEnGRPIKPV 142


                ....
gi 15229425 168 KIID 171
Cdd:cd00317 143 TISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 22-174 2.28e-57

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: 189.00  E-value: 2.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425    22 RIVIELFADVVPKTAENFRALCTgeagvgksTGkplHFKGSSFHRVIKGFMAQGGDFsNGNGTGGESIYGgkFSDENF-- 99
Cdd:pfam00160   8 RIVIELFGDKAPKTVENFLQLCK--------KG---FYDGTTFHRVIPGFMVQGGDP-TGTGGGGKSIFP--IPDEIFpl 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15229425   100 RLDHdGAGVLSMANCG--PNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSPVKIIDCGE 174
Cdd:pfam00160  74 LLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-170 5.87e-55

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 182.68  E-value: 5.87e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   1 MTKKKNPNVFLDVSIGgdpvqRIVIELFADVVPKTAENFRALCtgEAGvgkstgkplHFKGSSFHRVIKGFMAQGGDFsN 80
Cdd:COG0652   1 MKAAPNPTVTLETNKG-----DIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDP-T 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  81 GNGTGGEsiyGGKFSDENF-RLDHDgAGVLSMAN-CGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGT 158
Cdd:COG0652  64 GTGTGGP---GYTIPDEFDpGLKHK-RGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPT 139

                       170
                ....*....|...
gi 15229425 159 SDG-KPTSPVKII 170
Cdd:COG0652 140 DPGdGPLEPVVIE 152
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 25-171 6.94e-49

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: 166.82  E-value: 6.94e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  25 IELFADVVPKTAENFRALCtgeagvgkstgKPLHFKGSSFHRVIKGFMAQGGDFSnGNGTGGESIYGGKFSDE-NFRLDH 103
Cdd:cd01923  13 LELHCDKAPKACENFIKLC-----------KKGYYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPNLSH 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15229425 104 DGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGT-SDGKPTSPVKIID 171
Cdd:cd01923  81 DGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDpGTDRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 23-171 1.95e-48

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: 165.30  E-value: 1.95e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  23 IVIELFADVVPKTAENFRALCTGEagvgkstgkplHFKGSSFHRVIKGFMAQGGDfSNGNGTGGESIYGGKFSDEnFR-- 100
Cdd:cd01928  12 IKIELFCDDCPKACENFLALCASG-----------YYNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDE-FRet 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229425 101 LDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDG-KPTSPVKIID 171
Cdd:cd01928  79 LKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKyRPLEEIRIKD 150
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 11-170 6.95e-48

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: 163.47  E-value: 6.95e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  11 LDVSIGgdpvqRIVIELFADVVPKTAENFRALCTGEagvgkstgkplHFKGSSFHRVIKGFMAQGGDfSNGNGTGGESIY 90
Cdd:cd01922   2 LETTMG-----EITLELYWNHAPKTCKNFYELAKRG-----------YYNGTIFHRLIKDFMIQGGD-PTGTGRGGASIY 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  91 GGKFSDE-NFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSPVKI 169
Cdd:cd01922  65 GKKFEDEiHPELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144


                .
gi 15229425 170 I 170
Cdd:cd01922 145 L 145
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 23-171 6.98e-44

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: 153.00  E-value: 6.98e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  23 IVIELFADVVPKTAENFRALCtgeagvgkstgKPLHFKGSSFHRVIKGFMAQGGDfSNGNGTGGESIYGGKFSDE-NFRL 101
Cdd:cd01927   9 IHIRLFPEEAPKTVENFTTHA-----------RNGYYNNTIFHRVIKGFMIQTGD-PTGDGTGGESIWGKEFEDEfSPSL 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229425 102 DHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDG-KPTSPVKIID 171
Cdd:cd01927  77 KHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNdRPYEDIKIIN 147
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 23-172 1.13e-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: 128.62  E-value: 1.13e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  23 IVIELFADVVPKTAENFRALCTGEagvgkstgkplHFKGSSFHRVIKGFMAQGGDfSNGNGTGGESIYGGKFSDE-NFRL 101
Cdd:cd01925  17 IDIELWSKEAPKACRNFIQLCLEG-----------YYDNTIFHRVVPGFIIQGGD-PTGTGTGGESIYGEPFKDEfHSRL 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229425 102 DHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKvVEGMAV---IKKMELVGTSDGKPTSPVKIIDC 172
Cdd:cd01925  85 RFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGK-VTGDTIynlLKLAEVETDKDERPVYPPKITSV 157
PTZ00221 PTZ00221
cyclophilin; Provisional
 1-173 5.50e-31

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 121.13  E-value: 5.50e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425    1 MTKKKNPN-VFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAGVGKSTGKPLHFKGSSFHRVIK--GFMAQGGD 77
Cdd:PTZ00221  46 MKEEQNSCrAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVDRnnNIIVLGEL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   78 FSNGNGTGGESIyggkfSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVG 157
Cdd:PTZ00221 126 DSFNVSSTGTPI-----ADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLP 200

                        170
                 ....*....|....*..
gi 15229425  158 TSD-GKPTSPVKIIDCG 173
Cdd:PTZ00221 201 LDDvGRPLLPVTVSFCG 217
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 23-153 1.05e-26

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


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 106.27  E-value: 1.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  23 IVIELFADVVPKTAENFRALCtgeagvgkstgKPLHFKGSSFHRVIKGFMAQGGDfSNGNGTGGESIY---GGK----FS 95
Cdd:cd01921   9 LVIDLFTDECPLACLNFLKLC-----------KLKYYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYsqlYGRqarfFE 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  96 DE-NFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQ-PHLDGKHVVFGKVVEGMAVIKKM 153
Cdd:cd01921  77 PEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGENlDYLDGKHTVFGQVVEGFDVLEKI 136
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 22-167 3.76e-18

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: 81.72  E-value: 3.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  22 RIVIELFADVVPKTAENFRALCtgEAGvgkstgkplHFKGSSFHRVIKGFMAQGGDFS-------NGNGTGGESIYGGKf 94
Cdd:cd01920   8 DIVVELYDDKAPITVENFLAYV--RKG---------FYDNTIFHRVISGFVIQGGGFTpdlaqkeTLKPIKNEAGNGLS- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  95 sdenfrldhDGAGVLSMANCG-PNTNGSQFFILFKRQPHLD-----GKHVVFGKVVEGMAVIKKMELV--GTSDGKPTSP 166
Cdd:cd01920  76 ---------NTRGTIAMARTNaPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVetYSFGSYQDVP 146


                .
gi 15229425 167 V 167
Cdd:cd01920 147 V 147
PRK10791 PRK10791
peptidylprolyl isomerase B;
23-158 1.20e-10

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 60.24  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   23 IVIELFADVVPKTAENFRALCTGEagvgkstgkplHFKGSSFHRVIKGFMAQGGDFSNGNgtgGESIYGGKFSDENFRLD 102
Cdd:PRK10791  11 IVIKTFDDKAPETVKNFLDYCREG-----------FYNNTIFHRVINGFMIQGGGFEPGM---KQKATKEPIKNEANNGL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229425  103 HDGAGVLSMANCG-PNTNGSQFFI-------LFKRQPHLDG-KHVVFGKVVEGMAVIKKMELVGT 158
Cdd:PRK10791  77 KNTRGTLAMARTQaPHSATAQFFInvvdndfLNFSGESLQGwGYCVFAEVVEGMDVVDKIKGVAT 141
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 21-155 4.79e-10

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: 58.99  E-value: 4.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  21 QRIVIELFADVVPKTAENFRALCtgEAGVgkstgkplhFKGSSFHRVIKGFMAQGGD-FSNGNG-----TG--------- 85
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLV--ERGF---------YDGMEFHRVEGGFVVQTGDpQGKNPGfpdpeTGksrtiplei 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425  86 -----GESIYGGKFS-----DENFRLDHDGAGVLSMANC--GPNTNGSQFFILFK-------RQPHLDGKHVVFGKVVEG 146
Cdd:cd01924  76 kpegqKQPVYGKTLEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFLLKdneltpsRNNVLDGRYAVFGYVTDG 155


                ....*....
gi 15229425 147 MAVIKKMEL 155
Cdd:cd01924 156 LDILRELKV 164
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-170 5.73e-10

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 59.09  E-value: 5.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425    1 MTKKKNPNVFLDVSIGgdpvqRIVIELFADVVPKTAENFRALCtgEAGvgkstgkplHFKGSSFHRVIKGFMAQGGDFSN 80
Cdd:PRK10903  23 LAAKGDPHVLLTTSAG-----NIELELNSQKAPVSVKNFVDYV--NSG---------FYNNTTFHRVIPGFMIQGGGFTE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229425   81 GNGTGGESIYGGKFSDENFRldhDGAGVLSMANCG-PNTNGSQFFILFKRQPHLD-GK----HVVFGKVVEGMAVIKKME 154
Cdd:PRK10903  87 QMQQKKPNPPIKNEADNGLR---NTRGTIAMARTAdKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKIS 163

                        170       180
                 ....*....|....*....|.
gi 15229425  155 LVGTSD-----GKPTSPVKII 170
Cdd:PRK10903 164 QVPTHDvgpyqNVPSKPVVIL 184
 
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