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Conserved domains on  [gi|15226467|ref|NP_179709|]
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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

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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 ...
 5-170 2.15e-117

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: 328.83  E-value: 2.15e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   5 PKVFFDMTIGGAPAGKIVMELYTDKTPKTAENFRALCTGEKGVGRsgKPLHFKGSSFHRVIPNFMCQGGDFTKGNGTGGE 84
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG--KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  85 SIYGAKFEDENFERKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSGKPTKPV 164
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                ....*.
gi 15226467 165 VIADCG 170
Cdd:cd01926 159 VIADCG 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 ...
 5-170 2.15e-117

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: 328.83  E-value: 2.15e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   5 PKVFFDMTIGGAPAGKIVMELYTDKTPKTAENFRALCTGEKGVGRsgKPLHFKGSSFHRVIPNFMCQGGDFTKGNGTGGE 84
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG--KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  85 SIYGAKFEDENFERKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSGKPTKPV 164
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                ....*.
gi 15226467 165 VIADCG 170
Cdd:cd01926 159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-173 2.10e-107

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 304.46  E-value: 2.10e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467    1 MASHPKVFFDMTIGGAPAGKIVMELYTDKTPKTAENFRALCTGEKgVGRSGKPLHFKGSSFHRVIPNFMCQGGDFTKGNG 80
Cdd:PTZ00060  12 MSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   81 TGGESIYGAKFEDENFERKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSGKP 160
Cdd:PTZ00060  91 TGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYP 170

                        170
                 ....*....|...
gi 15226467  161 TKPVVIADCGEIS 173
Cdd:PTZ00060 171 KKPVVVTDCGELQ 183
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 11-171 1.13e-60

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: 185.15  E-value: 1.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467    11 MTIGGApaGKIVMELYTDKTPKTAENFRALCTgeKGvgrsgkplHFKGSSFHRVIPNFMCQGGDFTkGNGTGGESIYGak 90
Cdd:pfam00160   1 IETNGL--GRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP-- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467    91 FEDENFERKHT-GPGILSMANAGA--NTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSGKPTKPVVIA 167
Cdd:pfam00160  66 IPDEIFPLLLKhKRGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKIL 145


                  ....
gi 15226467   168 DCGE 171
Cdd:pfam00160 146 SCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-166 2.23e-55

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 171.89  E-value: 2.23e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   1 MASHPKVFFDMTiggapAGKIVMELYTDKTPKTAENFRALCtgEKGvgrsgkplHFKGSSFHRVIPNFMCQGGDFTkGNG 80
Cdd:COG0652   3 AAPNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEG--------FYDGTIFHRVIPGFMIQGGDPT-GTG 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  81 TGGEsiyGAKFEDENFERKHTGPGILSMANA-GANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSG- 158
Cdd:COG0652  67 TGGP---GYTIPDEFDPGLKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGd 143


                ....*...
gi 15226467 159 KPTKPVVI 166
Cdd:COG0652 144 GPLEPVVI 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 ...
 5-170 2.15e-117

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: 328.83  E-value: 2.15e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   5 PKVFFDMTIGGAPAGKIVMELYTDKTPKTAENFRALCTGEKGVGRsgKPLHFKGSSFHRVIPNFMCQGGDFTKGNGTGGE 84
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG--KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  85 SIYGAKFEDENFERKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSGKPTKPV 164
Cdd:cd01926  79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                ....*.
gi 15226467 165 VIADCG 170
Cdd:cd01926 159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-173 2.10e-107

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 304.46  E-value: 2.10e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467    1 MASHPKVFFDMTIGGAPAGKIVMELYTDKTPKTAENFRALCTGEKgVGRSGKPLHFKGSSFHRVIPNFMCQGGDFTKGNG 80
Cdd:PTZ00060  12 MSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   81 TGGESIYGAKFEDENFERKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSGKP 160
Cdd:PTZ00060  91 TGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYP 170

                        170
                 ....*....|...
gi 15226467  161 TKPVVIADCGEIS 173
Cdd:PTZ00060 171 KKPVVVTDCGELQ 183
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 3-172 6.10e-82

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 240.12  E-value: 6.10e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467    3 SHPKVFFDMTIGGAPAGKIVMELYTDKTPKTAENFRALCTGEkgVGRSGKPLHFKGSSFHRVIPNFMCQGGDFTKGNGTG 82
Cdd:PLN03149  17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   83 GESIYGAKFEDENFERKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVV-EGLDVVKAIEKIGSSSG-KP 160
Cdd:PLN03149  95 CVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNnRP 174

                        170
                 ....*....|..
gi 15226467  161 TKPVVIADCGEI 172
Cdd:PLN03149 175 KLACVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 8-168 6.93e-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: 195.56  E-value: 6.93e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   8 FFDMTIGgapagKIVMELYTDKTPKTAENFRALCTGEkgvgrsgkplHFKGSSFHRVIPNFMCQGGDFTkgNGTGGESIY 87
Cdd:cd00317   1 TLDTTKG-----RIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGP 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  88 GAKFEDENFERK-HTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIG-SSSGKPTKPVV 165
Cdd:cd00317  64 GYKFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVT 143


                ...
gi 15226467 166 IAD 168
Cdd:cd00317 144 ISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 11-171 1.13e-60

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: 185.15  E-value: 1.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467    11 MTIGGApaGKIVMELYTDKTPKTAENFRALCTgeKGvgrsgkplHFKGSSFHRVIPNFMCQGGDFTkGNGTGGESIYGak 90
Cdd:pfam00160   1 IETNGL--GRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP-- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467    91 FEDENFERKHT-GPGILSMANAGA--NTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSGKPTKPVVIA 167
Cdd:pfam00160  66 IPDEIFPLLLKhKRGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKIL 145


                  ....
gi 15226467   168 DCGE 171
Cdd:pfam00160 146 SCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-166 2.23e-55

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 171.89  E-value: 2.23e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   1 MASHPKVFFDMTiggapAGKIVMELYTDKTPKTAENFRALCtgEKGvgrsgkplHFKGSSFHRVIPNFMCQGGDFTkGNG 80
Cdd:COG0652   3 AAPNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEG--------FYDGTIFHRVIPGFMIQGGDPT-GTG 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  81 TGGEsiyGAKFEDENFERKHTGPGILSMANA-GANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSG- 158
Cdd:COG0652  67 TGGP---GYTIPDEFDPGLKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGd 143


                ....*...
gi 15226467 159 KPTKPVVI 166
Cdd:COG0652 144 GPLEPVVI 151
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 19-168 6.78e-50

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: 157.96  E-value: 6.78e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  19 GKIVMELYTDKTPKTAENFRALCtgEKGvgrsgkplHFKGSSFHRVIPNFMCQGGDFTkGNGTGGESIYGAKFEDE-NFE 97
Cdd:cd01923   9 GDLNLELHCDKAPKACENFIKLC--KKG--------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPN 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226467  98 RKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGS-SSGKPTKPVVIAD 168
Cdd:cd01923  78 LSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDpGTDRPKEEIKIED 149
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 19-166 7.94e-50

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: 157.31  E-value: 7.94e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  19 GKIVMELYTDKTPKTAENFRALCTgeKGvgrsgkplHFKGSSFHRVIPNFMCQGGDFTkGNGTGGESIYGAKFEDE-NFE 97
Cdd:cd01922   7 GEITLELYWNHAPKTCKNFYELAK--RG--------YYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPE 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15226467  98 RKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIGSSSGKPTKPVVI 166
Cdd:cd01922  76 LKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 19-164 9.70e-50

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: 157.24  E-value: 9.70e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  19 GKIVMELYTDKTPKTAENFRALCtgekgvgRSGkplHFKGSSFHRVIPNFMCQGGDFTkGNGTGGESIYGAKFEDENFER 98
Cdd:cd01927   7 GDIHIRLFPEEAPKTVENFTTHA-------RNG---YYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEFSPS 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15226467  99 -KHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKigSSSGKPTKPV 164
Cdd:cd01927  76 lKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIEN--VKTDKNDRPY 140
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 19-168 2.95e-44

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: 143.35  E-value: 2.95e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  19 GKIVMELYTDKTPKTAENFRALCTgekgvgrSGkplHFKGSSFHRVIPNFMCQGGDFTkGNGTGGESIYGAKFEDENFER 98
Cdd:cd01928  10 GDIKIELFCDDCPKACENFLALCA-------SG---YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFRET 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15226467  99 -KHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKI-GSSSGKPTKPVVIAD 168
Cdd:cd01928  79 lKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLpVDKKYRPLEEIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 2-141 7.46e-38

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: 127.85  E-value: 7.46e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   2 ASHPKVFFDMTiggapAGKIVMELYTDKTPKTAENFRALCTGEkgvgrsgkplHFKGSSFHRVIPNFMCQGGDFTkGNGT 81
Cdd:cd01925   3 PTTGKVILKTT-----AGDIDIELWSKEAPKACRNFIQLCLEG----------YYDNTIFHRVVPGFIIQGGDPT-GTGT 66

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226467  82 GGESIYGAKFEDENFER-KHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVV 141
Cdd:cd01925  67 GGESIYGEPFKDEFHSRlRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVT 127
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 19-150 1.29e-33

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: 116.67  E-value: 1.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  19 GKIVMELYTDKTPKTAENFRALCtgekgvgrsgKPLHFKGSSFHRVIPNFMCQGGDFTkGNGTGGESIYG-------AKF 91
Cdd:cd01921   7 GDLVIDLFTDECPLACLNFLKLC----------KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSqlygrqaRFF 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15226467  92 EDENFER-KHTGPGILSMANAGANTNGSQFFICTVK-TDWLDGKHVVFGQVVEGLDVVKAI 150
Cdd:cd01921  76 EPEILPLlKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKI 136
PTZ00221 PTZ00221
cyclophilin; Provisional
 6-173 5.43e-30

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 109.96  E-value: 5.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467    6 KVFFDMTIGGAPAGKIVMELYTDKTPKTAENFRALCTGEKGV-GRSGKPLHFKGSSFHRVipnfmcqggDFTKGNGTGGE 84
Cdd:PTZ00221  54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdTNTGVKLDYLYTPVHHV---------DRNNNIIVLGE 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   85 ------SIYGAKFEDENFERKHTGPGILSMANAGANTNGSQFFICTVKTDWLDGKHVVFGQVVEGLDVVKAIEKIG-SSS 157
Cdd:PTZ00221 125 ldsfnvSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPlDDV 204

                        170
                 ....*....|....*.
gi 15226467  158 GKPTKPVVIADCGEIS 173
Cdd:PTZ00221 205 GRPLLPVTVSFCGALT 220
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 18-164 4.42e-24

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: 92.12  E-value: 4.42e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  18 AGKIVMELYTDKTPKTAENFRALCtgekgvgRSGkplHFKGSSFHRVIPNFMCQGGDFTkgngtggesiygakfedENFE 97
Cdd:cd01920   6 LGDIVVELYDDKAPITVENFLAYV-------RKG---FYDNTIFHRVISGFVIQGGGFT-----------------PDLA 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  98 RKHTGPGILSMANAG-ANTNG--------------SQFFICTVKTDWLD-----GKHVVFGQVVEGLDVVKAIE--KIGS 155
Cdd:cd01920  59 QKETLKPIKNEAGNGlSNTRGtiamartnapdsatSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAgvETYS 138


                ....*....
gi 15226467 156 SSGKPTKPV 164
Cdd:cd01920 139 FGSYQDVPV 147
PRK10903 PRK10903
peptidylprolyl isomerase A;
18-166 2.94e-17

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 75.26  E-value: 2.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   18 AGKIVMELYTDKTPKTAENFRALCTgekgvgrSGkplHFKGSSFHRVIPNFMCQGGDFTKG--NGTGGESIygaKFEDEN 95
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYVN-------SG---FYNNTTFHRVIPGFMIQGGGFTEQmqQKKPNPPI---KNEADN 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   96 FERKHTgpGILSMA-NAGANTNGSQFFICTVKTDWLD-GK----HVVFGQVVEGLDVVKAI-----EKIGSSSGKPTKPV 164
Cdd:PRK10903 104 GLRNTR--GTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKIsqvptHDVGPYQNVPSKPV 181


                 ..
gi 15226467  165 VI 166
Cdd:PRK10903 182 VI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
19-159 4.22e-12

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 61.01  E-value: 4.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   19 GKIVMELYTDKTPKTAENFRALCtgekgvgRSGkplHFKGSSFHRVIPNFMCQGGDFTKGNgtgGESIYGAKFEDENFER 98
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYC-------REG---FYNNTIFHRVINGFMIQGGGFEPGM---KQKATKEPIKNEANNG 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467   99 KHTGPGILSMANAGA-NTNGSQFFICTVKTDWLDGK--------HVVFGQVVEGLDVVKAIEkiGSSSGK 159
Cdd:PRK10791  76 LKNTRGTLAMARTQApHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIK--GVATGR 143
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 19-154 8.02e-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: 55.14  E-value: 8.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  19 GKIVMELYTDKTPKTAENFRALCtgEKGVgrsgkplhFKGSSFHRVIPNFMCQGGD-FTKGNG-----TG---------- 82
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLV--ERGF--------YDGMEFHRVEGGFVVQTGDpQGKNPGfpdpeTGksrtipleik 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15226467  83 ----GESIYGAKFEDENFERKHT-----GPGILSMANA--GANTNGSQFFI-------CTVKTDWLDGKHVVFGQVVEGL 144
Cdd:cd01924  77 pegqKQPVYGKTLEEAGRYDEQPvlpfnAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGL 156

                       170
                ....*....|
gi 15226467 145 DVVKAIeKIG 154
Cdd:cd01924 157 DILREL-KVG 165
 
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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