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Conserved domains on  [gi|1063717061|ref|NP_001319764|]
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rotamase cyclophilin 2 [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 ...
 4-169 1.39e-112

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: 316.89  E-value: 1.39e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   4 PKVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGENGIGkaGKALHYKGSAFHRIIPGFMCQGGDFTRGNGTGGE 83
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  84 SIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPSERV 163
Cdd:cd01926    79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                  ....*.
gi 1063717061 164 VIEDCG 169
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 ...
 4-169 1.39e-112

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: 316.89  E-value: 1.39e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   4 PKVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGENGIGkaGKALHYKGSAFHRIIPGFMCQGGDFTRGNGTGGE 83
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  84 SIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPSERV 163
Cdd:cd01926    79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                  ....*.
gi 1063717061 164 VIEDCG 169
Cdd:cd01926   159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-171 1.10e-100

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 287.51  E-value: 1.10e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   1 MANPKVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGENgIGKAGKALHYKGSAFHRIIPGFMCQGGDFTRGNGT 80
Cdd:PTZ00060   13 SKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  81 GGESIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPS 160
Cdd:PTZ00060   92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171

                         170
                  ....*....|.
gi 1063717061 161 ERVVIEDCGEL 171
Cdd:PTZ00060  172 KPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 17-170 1.13e-57

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


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 177.45  E-value: 1.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  17 AGRVVMELFADVTPRTANNFRALCTGEngigkagkalHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYGskFEDENF- 95
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063717061  96 -KLKHtGPGILSMANSG--PNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPSERVVIEDCGE 170
Cdd:pfam00160  73 lLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-166 4.78e-54

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 168.42  E-value: 4.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   1 MANPKVFFDiligkMKAGRVVMELFADVTPRTANNFRALCtgengigKAGkalHYKGSAFHRIIPGFMCQGGDFTrGNGT 80
Cdd:COG0652     4 APNPTVTLE-----TNKGDIVIELFPDKAPKTVANFVSLA-------KEG---FYDGTIFHRVIPGFMIQGGDPT-GTGT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  81 GGEsiyGSKFEDENFK-LKHTgPGILSMANS-GPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGN 158
Cdd:COG0652    68 GGP---GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGD 143


                  ....*....
gi 1063717061 159 -PSERVVIE 166
Cdd:COG0652   144 gPLEPVVIE 152
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 4-169 1.39e-112

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: 316.89  E-value: 1.39e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   4 PKVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGENGIGkaGKALHYKGSAFHRIIPGFMCQGGDFTRGNGTGGE 83
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  84 SIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPSERV 163
Cdd:cd01926    79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                  ....*.
gi 1063717061 164 VIEDCG 169
Cdd:cd01926   159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-171 1.10e-100

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 287.51  E-value: 1.10e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   1 MANPKVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGENgIGKAGKALHYKGSAFHRIIPGFMCQGGDFTRGNGT 80
Cdd:PTZ00060   13 SKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  81 GGESIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPS 160
Cdd:PTZ00060   92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171

                         170
                  ....*....|.
gi 1063717061 161 ERVVIEDCGEL 171
Cdd:PTZ00060  172 KPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 3-171 5.04e-80

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 235.50  E-value: 5.04e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   3 NPKVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGEngIGKAGKALHYKGSAFHRIIPGFMCQGGDFTRGNGTGG 82
Cdd:PLN03149   18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  83 ESIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVV-DGYNVVKAMEDVGSDMGN-PS 160
Cdd:PLN03149   96 VSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNrPK 175

                         170
                  ....*....|.
gi 1063717061 161 ERVVIEDCGEL 171
Cdd:PLN03149  176 LACVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 18-167 4.01e-63

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: 191.32  E-value: 4.01e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  18 GRVVMELFADVTPRTANNFRALCTGEngigkagkalHYKGSAFHRIIPGFMCQGGDFTrgNGTGGESIYGSKFEDENFKL 97
Cdd:cd00317     7 GRIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGPGYKFPDENFPL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063717061  98 K-HTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSD-MGNPSERVVIED 167
Cdd:cd00317    75 KyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDeNGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 17-170 1.13e-57

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


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 177.45  E-value: 1.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  17 AGRVVMELFADVTPRTANNFRALCTGEngigkagkalHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYGskFEDENF- 95
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT-GTGGGGKSIFP--IPDEIFp 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063717061  96 -KLKHtGPGILSMANSG--PNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPSERVVIEDCGE 170
Cdd:pfam00160  73 lLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-166 4.78e-54

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 168.42  E-value: 4.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   1 MANPKVFFDiligkMKAGRVVMELFADVTPRTANNFRALCtgengigKAGkalHYKGSAFHRIIPGFMCQGGDFTrGNGT 80
Cdd:COG0652     4 APNPTVTLE-----TNKGDIVIELFPDKAPKTVANFVSLA-------KEG---FYDGTIFHRVIPGFMIQGGDPT-GTGT 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  81 GGEsiyGSKFEDENFK-LKHTgPGILSMANS-GPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGN 158
Cdd:COG0652    68 GGP---GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGD 143


                  ....*....
gi 1063717061 159 -PSERVVIE 166
Cdd:COG0652   144 gPLEPVVIE 152
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 18-174 1.05e-52

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: 165.28  E-value: 1.05e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  18 GRVVMELFADVTPRTANNFRALCtgENGigkagkalHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYGSKFEDE-NFK 96
Cdd:cd01923     9 GDLNLELHCDKAPKACENFIKLC--KKG--------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPN 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063717061  97 LKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGN-PSERVVIEDCGELKNP 174
Cdd:cd01923    78 LSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDrPKEEIKIEDTSVFVDP 156
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 18-165 9.55e-51

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: 159.93  E-value: 9.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  18 GRVVMELFADVTPRTANNFRALCtgENGigkagkalHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYGSKFEDE-NFK 96
Cdd:cd01927     7 GDIHIRLFPEEAPKTVENFTTHA--RNG--------YYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPS 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  97 LKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGN-PSERVVI 165
Cdd:cd01927    76 LKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDrPYEDIKI 145
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 18-165 6.79e-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: 157.70  E-value: 6.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  18 GRVVMELFADVTPRTANNFRALCtgengigkagKALHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYGSKFEDE-NFK 96
Cdd:cd01922     7 GEITLELYWNHAPKTCKNFYELA----------KRGYYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPE 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063717061  97 LKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGNPSERVVI 165
Cdd:cd01922    76 LKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 18-167 3.38e-47

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: 151.05  E-value: 3.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  18 GRVVMELFADVTPRTANNFRALCTGEngigkagkalHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYGSKFEDENFK- 96
Cdd:cd01928    10 GDIKIELFCDDCPKACENFLALCASG----------YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREt 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063717061  97 LKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSDMGN-PSERVVIED 167
Cdd:cd01928    79 LKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYrPLEEIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 17-174 1.60e-40

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: 134.79  E-value: 1.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  17 AGRVVMELFADVTPRTANNFRALCTgENgigkagkalHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYGSKFEDE-NF 95
Cdd:cd01925    14 AGDIDIELWSKEAPKACRNFIQLCL-EG---------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  96 KLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDG--YNVVKAMEDVGSDMGNPSERVVIEDCGELKN 173
Cdd:cd01925    83 RLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDtiYNLLKLAEVETDKDERPVYPPKITSVEVLEN 162


                  .
gi 1063717061 174 P 174
Cdd:cd01925   163 P 163
PTZ00221 PTZ00221
cyclophilin; Provisional
 5-174 7.00e-35

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 122.67  E-value: 7.00e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061   5 KVFFDILIGKMKAGRVVMELFADVTPRTANNFRALCTGENGIGKA-GKALHYKGSAFHRIipgfmcqggDFTRGNGTGGE 83
Cdd:PTZ00221   54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNtGVKLDYLYTPVHHV---------DRNNNIIVLGE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  84 ------SIYGSKFEDENFKLKHTGPGILSMANSGPNTNGSQFFICTEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSD-M 156
Cdd:PTZ00221  125 ldsfnvSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDdV 204

                         170
                  ....*....|....*...
gi 1063717061 157 GNPSERVVIEDCGELKNP 174
Cdd:PTZ00221  205 GRPLLPVTVSFCGALTGE 222
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 18-155 2.91e-30

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


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 108.20  E-value: 2.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  18 GRVVMELFADVTPRTANNFRALCtgengigkagKALHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYG-------SKF 90
Cdd:cd01921     7 GDLVIDLFTDECPLACLNFLKLC----------KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSqlygrqaRFF 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063717061  91 EDE-NFKLKHTGPGILSMANSGPNTNGSQFFIC-TEKTSWLDGKHVVFGKVVDGYNVVKAMEDVGSD 155
Cdd:cd01921    76 EPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKINDAIVD 142
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 17-167 2.58e-20

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: 82.11  E-value: 2.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  17 AGRVVMELFADVTPRTANNFRALCtgengigKAGkalHYKGSAFHRIIPGFMCQGGDFTrGNGTGGESIYGSKFEDENfK 96
Cdd:cd01920     6 LGDIVVELYDDKAPITVENFLAYV-------RKG---FYDNTIFHRVISGFVIQGGGFT-PDLAQKETLKPIKNEAGN-G 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  97 LKHTGpGILSMANSG-PNTNGSQFFICTEKTSWLD-----GKHVVFGKVVDGYNVVKAMEDV-----GSDMGNPSERVVI 165
Cdd:cd01920    74 LSNTR-GTIAMARTNaPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVetysfGSYQDVPVQDVII 152


                  ..
gi 1063717061 166 ED 167
Cdd:cd01920   153 ES 154
PRK10903 PRK10903
peptidylprolyl isomerase A;
17-165 3.96e-14

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 66.79  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  17 AGRVVMELFADVTPRTANNFRALCtgENGigkagkalHYKGSAFHRIIPGFMCQGGDFTrgngtggesiygskfedENFK 96
Cdd:PRK10903   37 AGNIELELNSQKAPVSVKNFVDYV--NSG--------FYNNTTFHRVIPGFMIQGGGFT-----------------EQMQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  97 LKHTGPGILSMANSG-PNTNG--------------SQFFICTEKTSWLD-GK----HVVFGKVVDGYNVVKAM-----ED 151
Cdd:PRK10903   90 QKKPNPPIKNEADNGlRNTRGtiamartadkdsatSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKIsqvptHD 169

                         170
                  ....*....|....
gi 1063717061 152 VGSDMGNPSERVVI 165
Cdd:PRK10903  170 VGPYQNVPSKPVVI 183
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 30-150 1.48e-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: 57.07  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  30 PRTANNFRALCtgENGIgkagkalhYKGSAFHRIIPGFMCQGGD-FTRGNG-----TG--------------GESIYGSK 89
Cdd:cd01924    19 PVTAGNFVDLV--ERGF--------YDGMEFHRVEGGFVVQTGDpQGKNPGfpdpeTGksrtipleikpegqKQPVYGKT 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063717061  90 FE-----DENFKLKHTGPGILSMANS--GPNTNGSQFFI-------CTEKTSWLDGKHVVFGKVVDGYNVVKAME 150
Cdd:cd01924    89 LEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
PRK10791 PRK10791
peptidylprolyl isomerase B;
18-166 1.63e-09

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 54.08  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  18 GRVVMELFADVTPRTANNFRALCTGEngigkagkalHYKGSAFHRIIPGFMCQGGDFTrgNGTGGESIYGSKFEDENFKL 97
Cdd:PRK10791    9 GDIVIKTFDDKAPETVKNFLDYCREG----------FYNNTIFHRVINGFMIQGGGFE--PGMKQKATKEPIKNEANNGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063717061  98 KHTgPGILSMANSG-PNTNGSQFFICTEKTSWLDGK--------HVVFGKVVDGYNVVKAMEDV-----GSDMGNPSERV 163
Cdd:PRK10791   77 KNT-RGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVatgrsGMHQDVPKEDV 155


                  ...
gi 1063717061 164 VIE 166
Cdd:PRK10791  156 IIE 158
 
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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