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Conserved domains on  [gi|564341286|ref|XP_006234395|]
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peptidyl-prolyl cis-trans isomerase G isoform X1 [Rattus norvegicus]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 240)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 8-175 1.90e-92

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


The actual alignment was detected with superfamily member cd01926:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 164  Bit Score: 285.30  E-value: 1.90e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   8 PRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKstqKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGG 87
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG---KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  88 ESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDaASKPFA 167
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                 ....*...
gi 564341286 168 EVRILSCG 175
Cdd:cd01926  157 KVVIADCG 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 ...
 8-175 1.90e-92

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: 285.30  E-value: 1.90e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   8 PRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKstqKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGG 87
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG---KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  88 ESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDaASKPFA 167
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                 ....*...
gi 564341286 168 EVRILSCG 175
Cdd:cd01926  157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 6-177 6.44e-79

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 250.92  E-value: 6.44e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   6 QRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKStqKPLHYKSCLFHRVVKDFMVQGGDFSEGNGR 85
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSSG--KNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  86 GGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAAsKP 165
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YP 170

                        170
                 ....*....|..
gi 564341286 166 FAEVRILSCGEL 177
Cdd:PTZ00060 171 KKPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 21-176 2.34e-59

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: 197.48  E-value: 2.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   21 AGRVVFELFSDVCPKTCENFRCLCTgeKGtgkstqkplHYKSCLFHRVVKDFMVQGGDFSeGNGRGGESIYggFFEDESF 100
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIF--PIPDEIF 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564341286  101 AVK-HNKEFLLSMANRG--KDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAAsKPFAEVRILSCGE 176
Cdd:pfam00160  72 PLLlKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 22-173 2.73e-47

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 164.96  E-value: 2.73e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCtgEKGtgkstqkplHYKSCLFHRVVKDFMVQGGDFsEGNGRGGEsiyGGFFEDESFA 101
Cdd:COG0652   16 GDIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDP-TGTGTGGP---GYTIPDEFDP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564341286 102 VKHNKEFLLSMAN-RGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILS 173
Cdd:COG0652   81 GLKHKRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIES 153
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 8-175 1.90e-92

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: 285.30  E-value: 1.90e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   8 PRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKstqKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGG 87
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGG---KPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  88 ESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDaASKPFA 167
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKK 156


                 ....*...
gi 564341286 168 EVRILSCG 175
Cdd:cd01926  157 KVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 6-177 6.44e-79

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 250.92  E-value: 6.44e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   6 QRPRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKStqKPLHYKSCLFHRVVKDFMVQGGDFSEGNGR 85
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSSG--KNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  86 GGESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAAsKP 165
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSG-YP 170

                        170
                 ....*....|..
gi 564341286 166 FAEVRILSCGEL 177
Cdd:PTZ00060 171 KKPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 8-177 2.01e-66

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 217.78  E-value: 2.01e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   8 PRCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKgtgKSTQKPLHYKSCLFHRVVKDFMVQGGDFSEGNGRGG 87
Cdd:PLN03149  19 PVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  88 ESIYGGFFEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVI-SGQEVVREIENQKTDAASKPF 166
Cdd:PLN03149  96 VSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPK 175

                        170
                 ....*....|.
gi 564341286 167 AEVRILSCGEL 177
Cdd:PLN03149 176 LACVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 22-173 1.71e-62

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: 205.58  E-value: 1.71e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCTGEkgtgkstqkplHYKSCLFHRVVKDFMVQGGDFSegNGRGGESIYGGFFEDESFA 101
Cdd:cd00317    7 GRIVIELYGDEAPKTVENFLSLARGG-----------FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENFP 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564341286 102 VK-HNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILS 173
Cdd:cd00317   74 LKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 21-176 2.34e-59

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: 197.48  E-value: 2.34e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   21 AGRVVFELFSDVCPKTCENFRCLCTgeKGtgkstqkplHYKSCLFHRVVKDFMVQGGDFSeGNGRGGESIYggFFEDESF 100
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIF--PIPDEIF 71

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564341286  101 AVK-HNKEFLLSMANRG--KDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAAsKPFAEVRILSCGE 176
Cdd:pfam00160  72 PLLlKHKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGD-RPVKPVKILSCGV 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 22-171 4.70e-52

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: 177.63  E-value: 4.70e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCTGEkgtgkstqkplHYKSCLFHRVVKDFMVQGGDfSEGNGRGGESIYGGFFEDE-SF 100
Cdd:cd01928   10 GDIKIELFCDDCPKACENFLALCASG-----------YYNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDEfRE 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564341286 101 AVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRI 171
Cdd:cd01928   78 TLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRI 148
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 22-173 2.25e-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: 173.03  E-value: 2.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCtgekgtgkstqKPLHYKSCLFHRVVKDFMVQGGDfSEGNGRGGESIYGGFFEDE-SF 100
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENFTTHA-----------RNGYYNNTIFHRVIKGFMIQTGD-PTGDGTGGESIWGKEFEDEfSP 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564341286 101 AVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILS 173
Cdd:cd01927   75 SLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIIN 147
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 22-173 2.73e-47

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 164.96  E-value: 2.73e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCtgEKGtgkstqkplHYKSCLFHRVVKDFMVQGGDFsEGNGRGGEsiyGGFFEDESFA 101
Cdd:COG0652   16 GDIVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDP-TGTGTGGP---GYTIPDEFDP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564341286 102 VKHNKEFLLSMAN-RGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILS 173
Cdd:COG0652   81 GLKHKRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIES 153
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 22-172 8.22e-44

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


Pssm-ID: 238903 [Multi-domain]  Cd Length: 146  Bit Score: 154.61  E-value: 8.22e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCTgeKGtgkstqkplHYKSCLFHRVVKDFMVQGGDfSEGNGRGGESIYGGFFEDE-SF 100
Cdd:cd01922    7 GEITLELYWNHAPKTCKNFYELAK--RG---------YYNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEiHP 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564341286 101 AVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDaASKPFAEVRIL 172
Cdd:cd01922   75 ELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKIL 145
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 22-173 1.58e-42

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: 151.41  E-value: 1.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCtgEKGtgkstqkplHYKSCLFHRVVKDFMVQGGDFSeGNGRGGESIYGGFFEDE-SF 100
Cdd:cd01923    9 GDLNLELHCDKAPKACENFIKLC--KKG---------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKP 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564341286 101 AVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRILS 173
Cdd:cd01923   77 NLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIED 149
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 21-174 4.83e-35

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: 130.93  E-value: 4.83e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  21 AGRVVFELFSDVCPKTCENFRCLCTGEkgtgkstqkplHYKSCLFHRVVKDFMVQGGDFSeGNGRGGESIYGGFFEDESF 100
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCLEG-----------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEFH 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564341286 101 A-VKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQViSGQEV--VREIENQKTDAASKPFAEVRILSC 174
Cdd:cd01925   82 SrLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKV-TGDTIynLLKLAEVETDKDERPVYPPKITSV 157
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 22-171 4.49e-31

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: 119.37  E-value: 4.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCtgekgtgkstqKPLHYKSCLFHRVVKDFMVQGGDfSEGNGRGGESIYGG-------F 94
Cdd:cd01921    7 GDLVIDLFTDECPLACLNFLKLC-----------KLKYYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQlygrqarF 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564341286  95 FEDESF-AVKHNKEFLLSMANRGKDTNGSQFFIT-TKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPFAEVRI 171
Cdd:cd01921   75 FEPEILpLLKHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 9-177 8.17e-26

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 106.88  E-value: 8.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286   9 RCFFDIAINNQPAGRVVFELFSDVCPKTCENFRCLCTGEKGTGKSTQKPLHYKSCLFHRV--VKDFMVQGGDFSEGNGRG 86
Cdd:PTZ00221  54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVdrNNNIIVLGELDSFNVSST 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  87 GESIyggffEDESFAVKHNKEFLLSMANRGKDTNGSQFFITTKPTPHLDGHHVVFGQVISGQEVVREIENQKTDAASKPF 166
Cdd:PTZ00221 134 GTPI-----ADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPL 208

                        170
                 ....*....|.
gi 564341286 167 AEVRILSCGEL 177
Cdd:PTZ00221 209 LPVTVSFCGAL 219
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 21-169 3.14e-17

cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) domain similar to the cytosolic E. coli cyclophilin A and Streptomyces antibioticus SanCyp18. Compared to the archetypal cyclophilin Human cyclophilin A, these have reduced affinity for cyclosporin A. E. coli cyclophilin A has a similar peptidylprolyl cis- trans isomerase activity to the human cyclophilin A. Most members of this subfamily contain a phenylalanine residue at the position equivalent to Human cyclophilin W121, where a tyrptophan has been shown to be important for cyclophilin binding.


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 79.41  E-value: 3.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  21 AGRVVFELFSDVCPKTCENFRCLCtgEKGtgkstqkplHYKSCLFHRVVKDFMVQGGDFSEGngrGGESIYGGFFEDESF 100
Cdd:cd01920    6 LGDIVVELYDDKAPITVENFLAYV--RKG---------FYDNTIFHRVISGFVIQGGGFTPD---LAQKETLKPIKNEAG 71

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564341286 101 AVKHNKEFLLSMA-NRGKDTNGSQFFITTKPTPHLD-----GHHVVFGQVISGQEVVREIENQKTdAASKPFAEV 169
Cdd:cd01920   72 NGLSNTRGTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVET-YSFGSYQDV 145
PRK10903 PRK10903
peptidylprolyl isomerase A;
21-160 7.44e-09

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 56.00  E-value: 7.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  21 AGRVVFELFSDVCPKTCENFrclcTGEKGTGkstqkplHYKSCLFHRVVKDFMVQGGDFsegNGRGGESIYGGFFEDESF 100
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNF----VDYVNSG-------FYNNTTFHRVIPGFMIQGGGF---TEQMQQKKPNPPIKNEAD 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564341286 101 AVKHNKEFLLSMANRG-KDTNGSQFFITTKPTPHLDgH------HVVFGQVISGQEVVREIENQKTD 160
Cdd:PRK10903 103 NGLRNTRGTIAMARTAdKDSATSQFFINVADNAFLD-HgqrdfgYAVFGKVVKGMDVADKISQVPTH 168
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 60-155 4.11e-08

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: 53.60  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  60 YKSCLFHRVVKDFMVQGGDfSEGNGRG---------------------GESIYG------GFFEDESFAVKHNKEfLLSM 112
Cdd:cd01924   34 YDGMEFHRVEGGFVVQTGD-PQGKNPGfpdpetgksrtipleikpegqKQPVYGktleeaGRYDEQPVLPFNAFG-AIAM 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564341286 113 ANRGKDTNG--SQFFI-------TTKPTPHLDGHHVVFGQVISGQEVVREIE 155
Cdd:cd01924  112 ARTEFDPNSasSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
PRK10791 PRK10791
peptidylprolyl isomerase B;
22-159 2.76e-06

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 47.91  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564341286  22 GRVVFELFSDVCPKTCENFRCLCTGEkgtgkstqkplHYKSCLFHRVVKDFMVQGGDFSEGNGRggESIYGGFFEDESFA 101
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCREG-----------FYNNTIFHRVINGFMIQGGGFEPGMKQ--KATKEPIKNEANNG 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564341286 102 VKHNKEfLLSMAnRGKDTNG--SQFFITTKPTPHLDGH--------HVVFGQVISGQEVVREIENQKT 159
Cdd:PRK10791  76 LKNTRG-TLAMA-RTQAPHSatAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVAT 141
 
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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