NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1046887994|ref|XP_017448769|]
View 

peptidyl-prolyl cis-trans isomerase E isoform X3 [Rattus norvegicus]

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 ...
 56-214 7.38e-111

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: 314.19  E-value: 7.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  56 PQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKG-----FGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSI 130
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 131 YGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVII 210
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                  ....
gi 1046887994 211 ADCG 214
Cdd:cd01926   161 ADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 56-214 7.38e-111

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: 314.19  E-value: 7.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  56 PQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKG-----FGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSI 130
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 131 YGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVII 210
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                  ....
gi 1046887994 211 ADCG 214
Cdd:cd01926   161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 54-215 1.11e-92

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 269.02  E-value: 1.11e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  54 SNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHE------KGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGG 127
Cdd:PTZ00060   14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 128 KSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQK 207
Cdd:PTZ00060   94 ESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKP 173


                  ....*...
gi 1046887994 208 VIIADCGE 215
Cdd:PTZ00060  174 VVVTDCGE 181
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 69-215 2.96e-55

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: 2.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  69 AGRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTnhnGTGGKSIYGKKFDDENFI--LKHtG 146
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPllLKH-K 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046887994 147 PGLLSMANSG--PNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVIIADCGE 215
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 51-210 1.84e-48

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 156.10  E-value: 1.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  51 KARSNPQVYMDIkignkPAGRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKsi 130
Cdd:COG0652     2 KAAPNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP-- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 131 yGKKFDDENFI-LKHTgPGLLSMANS-GPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDG-KPKQK 207
Cdd:COG0652    71 -GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEP 148


                  ...
gi 1046887994 208 VII 210
Cdd:COG0652   149 VVI 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 ...
 56-214 7.38e-111

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: 314.19  E-value: 7.38e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  56 PQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKG-----FGFKGSSFHRIIPQFMCQGGDFTNHNGTGGKSI 130
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 131 YGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVII 210
Cdd:cd01926    81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                  ....
gi 1046887994 211 ADCG 214
Cdd:cd01926   161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 54-215 1.11e-92

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 269.02  E-value: 1.11e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  54 SNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHE------KGFGFKGSSFHRIIPQFMCQGGDFTNHNGTGG 127
Cdd:PTZ00060   14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 128 KSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQK 207
Cdd:PTZ00060   94 ESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKP 173


                  ....*...
gi 1046887994 208 VIIADCGE 215
Cdd:PTZ00060  174 VVVTDCGE 181
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 54-215 1.61e-79

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 235.89  E-value: 1.61e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  54 SNPQVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHE---KGF--GFKGSSFHRIIPQFMCQGGDFTNHNGTGGK 128
Cdd:PLN03149   17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 129 SIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEIT-DGLDVLRQIE-AQGSKDGKPKQ 206
Cdd:PLN03149   97 SIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIEnVATGPNNRPKL 176


                  ....*....
gi 1046887994 207 KVIIADCGE 215
Cdd:PLN03149  177 ACVISECGE 185
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 70-212 6.36e-57

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: 177.07  E-value: 6.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  70 GRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNHNGtgGKSIYGKKFDDENFILK-HTGPG 148
Cdd:cd00317     7 GRIVIELYGDEAPKTVENFLSLA--RGGF-YDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPDENFPLKyHHRRG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046887994 149 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQG-SKDGKPKQKVIIAD 212
Cdd:cd00317    82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 69-215 2.96e-55

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: 2.96e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  69 AGRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTnhnGTGGKSIYGKKFDDENFI--LKHtG 146
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPllLKH-K 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046887994 147 PGLLSMANSG--PNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVIIADCGE 215
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 70-210 1.72e-48

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: 155.70  E-value: 1.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  70 GRIQMLLRSDVVPMTAENFrclCTHEKGFGFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDE-NFILKHTGPG 148
Cdd:cd01927     7 GDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHDRPY 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046887994 149 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIE-AQGSKDGKPKQKVII 210
Cdd:cd01927    83 TLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIEnVKTDKNDRPYEDIKI 145
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 51-210 1.84e-48

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 156.10  E-value: 1.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  51 KARSNPQVYMDIkignkPAGRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKsi 130
Cdd:COG0652     2 KAAPNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP-- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 131 yGKKFDDENFI-LKHTgPGLLSMANS-GPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDG-KPKQK 207
Cdd:COG0652    71 -GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEP 148


                  ...
gi 1046887994 208 VII 210
Cdd:COG0652   149 VVI 151
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 70-210 1.61e-45

cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to Schizosaccharomyces pombe cyp-2. These proteins bind their respective SNW chromatin binding protein in autologous systems, in a CsA independent manner indicating interaction with a surface outside the PPIase active site. SNW proteins play a basic and broad range role in signaling.


Pssm-ID: 238903 [Multi-domain]  Cd Length: 146  Bit Score: 148.07  E-value: 1.61e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  70 GRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDE-NFILKHTGPG 148
Cdd:cd01922     7 GEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPELKHTGAG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046887994 149 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKDGKPKQKVII 210
Cdd:cd01922    83 ILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 70-212 7.86e-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: 144.10  E-value: 7.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  70 GRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDE-NFILKHTGPG 148
Cdd:cd01923     9 GDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHDGRG 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046887994 149 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIE-AQGSKDGKPKQKVIIAD 212
Cdd:cd01923    85 VLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMEnVPDPGTDRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 70-212 3.83e-43

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: 142.19  E-value: 3.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  70 GRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDENF-ILKHTGPG 148
Cdd:cd01928    10 GDIKIELFCDDCPKACENFLALCA--SGY-YNGCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFReTLKHDSRG 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046887994 149 LLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEA-QGSKDGKPKQKVIIAD 212
Cdd:cd01928    86 VVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKlPVDKKYRPLEEIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 69-204 1.33e-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: 125.93  E-value: 1.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  69 AGRIQMLLRSDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKKFDDE-NFILKHTGP 147
Cdd:cd01925    14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRLRFNRR 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046887994 148 GLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEIT-DGL-DVLRQIEAQGSKDGKP 204
Cdd:cd01925    90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIyNLLKLAEVETDKDERP 148
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 70-210 4.52e-27

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: 101.26  E-value: 4.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  70 GRIQMLLRSDVVPMTAENFRCLCtheKGFGFKGSSFHRIIPQFMCQGGDFTNhNGTGGKSIYGKK-------FDDE-NFI 141
Cdd:cd01921     7 GDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPTG-TGAGGESIYSQLygrqarfFEPEiLPL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046887994 142 LKHTGPGLLSMANSGPNTNGSQFFLT-CDKTDWLDGKHVVFGEITDGLDVLRQI-EAQGSKDGKPKQKVII 210
Cdd:cd01921    83 LKHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 57-214 9.12e-24

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 94.94  E-value: 9.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  57 QVYMDIKIGNKPAGRIQMLLRSDVVPMTAENFRCLCTHEKGF----GFK----GSSFHRIIPQF-MCQGGDFTNHNgtgg 127
Cdd:PTZ00221   54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdtntGVKldylYTPVHHVDRNNnIIVLGELDSFN---- 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 128 KSIYGKKFDDENFILKHTGPGLLSMANSGPNTNGSQFFLTCDKTDWLDGKHVVFGEITDGLDVLRQIEAQGSKD-GKPKQ 206
Cdd:PTZ00221  130 VSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDvGRPLL 209


                  ....*...
gi 1046887994 207 KVIIADCG 214
Cdd:PTZ00221  210 PVTVSFCG 217
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 69-212 5.09e-16

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: 72.09  E-value: 5.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  69 AGRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNHngtggksiyGKKFDDENFILKHTGPG 148
Cdd:cd01920     6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTPD---------LAQKETLKPIKNEAGNG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 149 L------LSMANSG-PNTNGSQFFLTCDKTDWLD-----GKHVVFGEITDGLDVLRQIE-----AQGSKDGKPKQKVIIA 211
Cdd:cd01920    74 LsntrgtIAMARTNaPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAgvetySFGSYQDVPVQDVIIE 153


                  .
gi 1046887994 212 D 212
Cdd:cd01920   154 S 154
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 70-196 3.54e-15

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: 70.55  E-value: 3.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  70 GRIQMLLRSDVVPMTAENFRCLCthEKGFgFKGSSFHRIIPQFMCQGGDFTNHN------GTG--------------GKS 129
Cdd:cd01924     7 GTITIVLDGYNAPVTAGNFVDLV--ERGF-YDGMEFHRVEGGFVVQTGDPQGKNpgfpdpETGksrtipleikpegqKQP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 130 IYGKKF-----DDENFILKHTGPGLLSMANS--GPNTNGSQFF-------LTCDKTDWLDGKHVVFGEITDGLDVLRQIE 195
Cdd:cd01924    84 VYGKTLeeagrYDEQPVLPFNAFGAIAMARTefDPNSASSQFFfllkdneLTPSRNNVLDGRYAVFGYVTDGLDILRELK 163


                  .
gi 1046887994 196 A 196
Cdd:cd01924   164 V 164
PRK10903 PRK10903
peptidylprolyl isomerase A;
47-208 2.06e-13

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 66.02  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  47 PAAKKARSNPQVYMDIKIGNkpagrIQMLLRSDVVPMTAENFrcLCTHEKGFgFKGSSFHRIIPQFMCQGGDFTnhngtg 126
Cdd:PRK10903   20 PAALAAKGDPHVLLTTSAGN-----IELELNSQKAPVSVKNF--VDYVNSGF-YNNTTFHRVIPGFMIQGGGFT------ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994 127 gksiygkkfddENFILKHTGPGLLSMANSG-PNTNG--------------SQFFLTCDKTDWLD-GK----HVVFGEITD 186
Cdd:PRK10903   86 -----------EQMQQKKPNPPIKNEADNGlRNTRGtiamartadkdsatSQFFINVADNAFLDhGQrdfgYAVFGKVVK 154

                         170       180
                  ....*....|....*....|..
gi 1046887994 187 GLDVLRQIEAQGSKDGKPKQKV 208
Cdd:PRK10903  155 GMDVADKISQVPTHDVGPYQNV 176
PRK10791 PRK10791
peptidylprolyl isomerase B;
78-210 3.19e-11

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 59.47  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046887994  78 SDVVPMTAENFRCLCTheKGFgFKGSSFHRIIPQFMCQGGDFtnHNGTGGKSIYGKKFDDENFILKHTgPGLLSMANSG- 156
Cdd:PRK10791   17 DDKAPETVKNFLDYCR--EGF-YNNTIFHRVINGFMIQGGGF--EPGMKQKATKEPIKNEANNGLKNT-RGTLAMARTQa 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046887994 157 PNTNGSQFFLTCDKTDWLDGK--------HVVFGEITDGLDVLRQIEA-----QGSKDGKPKQKVII 210
Cdd:PRK10791   91 PHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGvatgrSGMHQDVPKEDVII 157
 
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