NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|334187084|ref|NP_001190888|]
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 ...
 7-166 8.43e-66

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: 216.35  E-value: 8.43e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   7 PQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGprsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGTAG 86
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  87 ESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEDKKKSD 166
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 7-166 8.43e-66

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: 216.35  E-value: 8.43e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   7 PQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGprsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGTAG 86
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  87 ESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEDKKKSD 166
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157
PTZ00060 PTZ00060
cyclophilin; Provisional
 5-165 5.80e-57

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 193.14  E-value: 5.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   5 KNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGPrsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGT 84
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSS--GKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  85 AGESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEDKKK 164
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171


                 .
gi 334187084 165 S 165
Cdd:PTZ00060 172 K 172
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 22-168 1.11e-33

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: 126.22  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   22 TMVFELFPEVAPKTSENFRALCTgeKGigprsgkplHYKGSFFHRIMKGSSAQAGDFVNRNGTaGESIYAgkFPDES--P 99
Cdd:pfam00160   8 RIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPTGTGGG-GKSIFP--IPDEIfpL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187084  100 KLRHEEtGLLSM--SIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEDKKKSDGK 168
Cdd:pfam00160  74 LLKHKR-GALSManTGPAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVK 143
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-161 3.99e-29

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 113.73  E-value: 3.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   1 MAKKKNPQVFMDVSiDGDpaetMVFELFPEVAPKTSENFRALCtgEKGigprsgkplHYKGSFFHRIMKGSSAQAGDFvN 80
Cdd:COG0652    1 MKAAPNPTVTLETN-KGD----IVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDP-T 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  81 RNGTAGESiyaGKFPDE-SPKLRHEEtGLLSMsiA---DRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV 156
Cdd:COG0652   64 GTGTGGPG---YTIPDEfDPGLKHKR-GTLAM--AraqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAG 137


                 ....*
gi 334187084 157 GDEED 161
Cdd:COG0652  138 PTDPG 142
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 7-166 8.43e-66

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: 216.35  E-value: 8.43e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   7 PQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGprsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGTAG 86
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG---GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  87 ESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEDKKKSD 166
Cdd:cd01926   78 KSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKK 157
PTZ00060 PTZ00060
cyclophilin; Provisional
 5-165 5.80e-57

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 193.14  E-value: 5.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   5 KNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGPrsGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGT 84
Cdd:PTZ00060  14 KRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVGSS--GKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  85 AGESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEDKKK 164
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171


                 .
gi 334187084 165 S 165
Cdd:PTZ00060 172 K 172
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 5-157 2.82e-40

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 146.52  E-value: 2.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   5 KNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKgigPRSGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGT 84
Cdd:PLN03149  17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEF---RKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGT 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334187084  85 AGESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLI-QGKEILKKIERVG 157
Cdd:PLN03149  94 GCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVA 167
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 22-168 1.11e-33

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: 126.22  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   22 TMVFELFPEVAPKTSENFRALCTgeKGigprsgkplHYKGSFFHRIMKGSSAQAGDFVNRNGTaGESIYAgkFPDES--P 99
Cdd:pfam00160   8 RIVIELFGDKAPKTVENFLQLCK--KG---------FYDGTTFHRVIPGFMVQGGDPTGTGGG-GKSIFP--IPDEIfpL 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187084  100 KLRHEEtGLLSM--SIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEDKKKSDGK 168
Cdd:pfam00160  74 LLKHKR-GALSManTGPAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVK 143
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-161 3.99e-29

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 113.73  E-value: 3.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   1 MAKKKNPQVFMDVSiDGDpaetMVFELFPEVAPKTSENFRALCtgEKGigprsgkplHYKGSFFHRIMKGSSAQAGDFvN 80
Cdd:COG0652    1 MKAAPNPTVTLETN-KGD----IVIELFPDKAPKTVANFVSLA--KEG---------FYDGTIFHRVIPGFMIQGGDP-T 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  81 RNGTAGESiyaGKFPDE-SPKLRHEEtGLLSMsiA---DRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV 156
Cdd:COG0652   64 GTGTGGPG---YTIPDEfDPGLKHKR-GTLAM--AraqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAG 137


                 ....*
gi 334187084 157 GDEED 161
Cdd:COG0652  138 PTDPG 142
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 26-168 8.56e-28

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: 109.47  E-value: 8.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  26 ELFPEVAPKTSENFRALCtgekgigpRSGkplHYKGSFFHRIMKGSSAQAGDFVNrNGTAGESIYAGKFPDE-SPKLRHE 104
Cdd:cd01927   12 RLFPEEAPKTVENFTTHA--------RNG---YYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187084 105 ETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV-GDEEDKKKSDGK 168
Cdd:cd01927   80 RPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVkTDKNDRPYEDIK 144
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 11-172 2.45e-27

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: 108.29  E-value: 2.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  11 MDVSID---GDpaetMVFELFPEVAPKTSENFRALCTgekgigprSGkplHYKGSFFHRIMKGSSAQAGDFVNrNGTAGE 87
Cdd:cd01928    1 MSVTLHtnlGD----IKIELFCDDCPKACENFLALCA--------SG---YYNGCIFHRNIKGFMVQTGDPTG-TGKGGE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  88 SIYAGKFPDE-SPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV-GDEEDKKKS 165
Cdd:cd01928   65 SIWGKKFEDEfRETLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLpVDKKYRPLE 144


                 ....*..
gi 334187084 166 DGKKNGK 172
Cdd:cd01928  145 EIRIKDV 151
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 26-166 6.08e-25

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: 101.72  E-value: 6.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  26 ELFPEVAPKTSENFRALCtgEKGigprsgkplHYKGSFFHRIMKGSSAQAGDFVNrNGTAGESIYAGKFPDE-SPKLRHE 104
Cdd:cd01923   14 ELHCDKAPKACENFIKLC--KKG---------YYDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187084 105 ETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEE-DKKKSD 166
Cdd:cd01923   82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGtDRPKEE 144
PTZ00221 PTZ00221
cyclophilin; Provisional
 1-156 2.79e-20

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 91.08  E-value: 2.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084   1 MAKKKNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGPRSGKPLHYKGSFFHRI-MKGSSAQAGDFV 79
Cdd:PTZ00221  47 KEEQNSCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTNTGVKLDYLYTPVHHVdRNNNIIVLGELD 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334187084  80 NRN-GTAGESIyagkfPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERV 156
Cdd:PTZ00221 127 SFNvSSTGTPI-----ADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESL 199
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 23-156 4.41e-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: 4.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  23 MVFELFPEVAPKTSENFRALCtgekgigpRSGkplHYKGSFFHRIMKGSSAQAGDFvNRNGTAGESIYAGKfpDESPKLR 102
Cdd:cd01920    9 IVVELYDDKAPITVENFLAYV--------RKG---FYDNTIFHRVISGFVIQGGGF-TPDLAQKETLKPIK--NEAGNGL 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084 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 4.04e-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: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  32 APKTSENFRALCtgEKGIgprsgkplhYKGSFFHRIMKGSSAQAGDFVNRNG--------------------TAGESIY- 90
Cdd:cd01924   18 APVTAGNFVDLV--ERGF---------YDGMEFHRVEGGFVVQTGDPQGKNPgfpdpetgksrtipleikpeGQKQPVYg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187084  91 -----AGKFPDESPKLRHEeTGLLSM--SIADRDKFGSHFHI-------TFRPNQQLDRNNVVFGKLIQGKEILKKIeRV 156
Cdd:cd01924   87 ktleeAGRYDEQPVLPFNA-FGAIAMarTEFDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILREL-KV 164


                 ..
gi 334187084 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