NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22329097|ref|NP_194968|]
View 

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

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 7-173 2.84e-69

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: 225.98  E-value: 2.84e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   7 PQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGprsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGTAG 86
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  87 ESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVS 166
Cdd:cd01926  78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                ....*..
gi 22329097 167 VKIIRCG 173
Cdd:cd01926 158 VVIADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 7-173 2.84e-69

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: 225.98  E-value: 2.84e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   7 PQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGprsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGTAG 86
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  87 ESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVS 166
Cdd:cd01926  78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                ....*..
gi 22329097 167 VKIIRCG 173
Cdd:cd01926 158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 5-174 2.06e-62

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 208.16  E-value: 2.06e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097    5 KNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGPrsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGT 84
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSS--GKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   85 AGESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPT 164
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171

                        170
                 ....*....|
gi 22329097  165 VSVKIIRCGE 174
Cdd:PTZ00060 172 KPVVVTDCGE 181
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 22-174 1.23e-38

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: 140.47  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097    22 TMVFELFPEVAPKTSENFRALCTgeKGigprsgkplHYKGSFFHRIMKGSSAQAGDFVNRNGTaGESIYAgkFPDES--P 99
Cdd:pfam00160   8 RIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPTGTGGG-GKSIFP--IPDEIfpL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329097   100 KLRHEEtGLLSM--SIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVSVKIIRCGE 174
Cdd:pfam00160  74 LLKHKR-GALSManTGPAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-171 2.13e-31

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 120.27  E-value: 2.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   1 MAKKKNPQVFMDVSiDGDpaetMVFELFPEVAPKTSENFRALCtgEKGigprsgkplHYKGSFFHRIMKGSSAQAGDFvN 80
Cdd:COG0652   1 MKAAPNPTVTLETN-KGD----IVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDP-T 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  81 RNGTAGESiyaGKFPDE-SPKLRHEEtGLLSMsiA---DRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV 156
Cdd:COG0652  64 GTGTGGPG---YTIPDEfDPGLKHKR-GTLAM--AraqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAG 137

                       170
                ....*....|....*.
gi 22329097 157 GDEEG-KPTVSVKIIR 171
Cdd:COG0652 138 PTDPGdGPLEPVVIES 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 ...
 7-173 2.84e-69

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: 225.98  E-value: 2.84e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   7 PQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGprsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGTAG 86
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  87 ESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVS 166
Cdd:cd01926  78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157


                ....*..
gi 22329097 167 VKIIRCG 173
Cdd:cd01926 158 VVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 5-174 2.06e-62

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 208.16  E-value: 2.06e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097    5 KNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGPrsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGT 84
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSS--GKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   85 AGESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPT 164
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171

                        170
                 ....*....|
gi 22329097  165 VSVKIIRCGE 174
Cdd:PTZ00060 172 KPVVVTDCGE 181
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 5-174 4.60e-44

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 157.30  E-value: 4.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097    5 KNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKgigPRSGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGT 84
Cdd:PLN03149  17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   85 AGESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLI-QGKEILKKIERVG-DEEGK 162
Cdd:PLN03149  94 GCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVAtGPNNR 173

                        170
                 ....*....|..
gi 22329097  163 PTVSVKIIRCGE 174
Cdd:PLN03149 174 PKLACVISECGE 185
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 22-174 1.23e-38

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: 140.47  E-value: 1.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097    22 TMVFELFPEVAPKTSENFRALCTgeKGigprsgkplHYKGSFFHRIMKGSSAQAGDFVNRNGTaGESIYAgkFPDES--P 99
Cdd:pfam00160   8 RIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPTGTGGG-GKSIFP--IPDEIfpL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329097   100 KLRHEEtGLLSM--SIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVSVKIIRCGE 174
Cdd:pfam00160  74 LLKHKR-GALSManTGPAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-171 2.13e-31

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 120.27  E-value: 2.13e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   1 MAKKKNPQVFMDVSiDGDpaetMVFELFPEVAPKTSENFRALCtgEKGigprsgkplHYKGSFFHRIMKGSSAQAGDFvN 80
Cdd:COG0652   1 MKAAPNPTVTLETN-KGD----IVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDP-T 63

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  81 RNGTAGESiyaGKFPDE-SPKLRHEEtGLLSMsiA---DRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV 156
Cdd:COG0652  64 GTGTGGPG---YTIPDEfDPGLKHKR-GTLAM--AraqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAG 137

                       170
                ....*....|....*.
gi 22329097 157 GDEEG-KPTVSVKIIR 171
Cdd:COG0652 138 PTDPGdGPLEPVVIES 153
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 26-170 2.53e-29

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: 114.10  E-value: 2.53e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  26 ELFPEVAPKTSENFRALCtgekgigpRSGkplHYKGSFFHRIMKGSSAQAGDFVNrNGTAGESIYAGKFPDE-SPKLRHE 104
Cdd:cd01927  12 RLFPEEAPKTVENFTTHA--------RNG---YYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHD 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329097 105 ETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV-GDEEGKPTVSVKII 170
Cdd:cd01927  80 RPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVkTDKNDRPYEDIKII 146
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 11-169 3.55e-28

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: 110.99  E-value: 3.55e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  11 MDVSID---GDpaetMVFELFPEVAPKTSENFRALCTgekgigprSGkplHYKGSFFHRIMKGSSAQAGDFVNrNGTAGE 87
Cdd:cd01928   1 MSVTLHtnlGD----IKIELFCDDCPKACENFLALCA--------SG---YYNGCIFHRNIKGFMVQTGDPTG-TGKGGE 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  88 SIYAGKFPDE-SPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV-GDEEGKPTV 165
Cdd:cd01928  65 SIWGKKFEDEfRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLpVDKKYRPLE 144


                ....
gi 22329097 166 SVKI 169
Cdd:cd01928 145 EIRI 148
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 26-171 3.63e-26

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: 105.19  E-value: 3.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  26 ELFPEVAPKTSENFRALCtgEKGigprsgkplHYKGSFFHRIMKGSSAQAGDFVNrNGTAGESIYAGKFPDE-SPKLRHE 104
Cdd:cd01923  14 ELHCDKAPKACENFIKLC--KKG---------YYDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHD 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329097 105 ETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEG-KPTVSVKIIR 171
Cdd:cd01923  82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTdRPKEEIKIED 149
PTZ00221 PTZ00221
cyclophilin; Provisional
 1-173 3.89e-23

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 99.56  E-value: 3.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097    1 MAKKKNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGPRSGKPLHYKGSFFHRI-MKGSSAQAGDFV 79
Cdd:PTZ00221  47 KEEQNSCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVdRNNNIIVLGELD 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097   80 NRN-GTAGESIyagkfPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVG- 157
Cdd:PTZ00221 127 SFNvSSTGTPI-----ADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPl 201

                        170
                 ....*....|....*.
gi 22329097  158 DEEGKPTVSVKIIRCG 173
Cdd:PTZ00221 202 DDVGRPLLPVTVSFCG 217
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 23-156 4.51e-10

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: 58.99  E-value: 4.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  23 MVFELFPEVAPKTSENFRALCtgekgigpRSGkplHYKGSFFHRIMKGSSAQAGDFvNRNGTAGESIYAGKfpDESPKLR 102
Cdd:cd01920   9 IVVELYDDKAPITVENFLAYV--------RKG---FYDNTIFHRVISGFVIQGGGF-TPDLAQKETLKPIK--NEAGNGL 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097 103 HEETGLLSMS-IADRDKFGSHFHITFRPNQQLDRNN-----VVFGKLIQGKEILKKIERV 156
Cdd:cd01920  75 SNTRGTIAMArTNAPDSATSQFFINLKDNASLDYQNeqwgyTVFGEVTEGMDVVDKIAGV 134
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 32-158 4.14e-05

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: 45.13  E-value: 4.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  32 APKTSENFRALCtgEKGIgprsgkplhYKGSFFHRIMKGSSAQAGDFVNRNG--------------------TAGESIY- 90
Cdd:cd01924  18 APVTAGNFVDLV--ERGF---------YDGMEFHRVEGGFVVQTGDPQGKNPgfpdpetgksrtipleikpeGQKQPVYg 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329097  91 -----AGKFPDESPKLRHEeTGLLSM--SIADRDKFGSHFHI-------TFRPNQQLDRNNVVFGKLIQGKEILKKIeRV 156
Cdd:cd01924  87 ktleeAGRYDEQPVLPFNA-FGAIAMarTEFDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILREL-KV 164


                ..
gi 22329097 157 GD 158
Cdd:cd01924 165 GD 166
 
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