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Conserved domains on  [gi|41055110|ref|NP_957499|]
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peptidyl-prolyl cis-trans isomerase H isoform 2 [Danio rerio]

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 ...
 11-175 6.89e-107

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: 302.64  E-value: 6.89e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  11 PIVFFDVSIGGQEVGRMKIELFADIVPKTAENFRQFCTGEFKKDGVPVGYKGCTFHRVIKDFMIQGGDFVNGDGTGICSI 90
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  91 YRGPFADENFRMKHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAVvfinfiGTAQNKI 170
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENV------GSGNGKP 154


                ....*
gi 41055110 171 SSTIT 175
Cdd:cd01926 155 KKKVV 159
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 11-175 6.89e-107

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: 302.64  E-value: 6.89e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  11 PIVFFDVSIGGQEVGRMKIELFADIVPKTAENFRQFCTGEFKKDGVPVGYKGCTFHRVIKDFMIQGGDFVNGDGTGICSI 90
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  91 YRGPFADENFRMKHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAVvfinfiGTAQNKI 170
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENV------GSGNGKP 154


                ....*
gi 41055110 171 SSTIT 175
Cdd:cd01926 155 KKKVV 159
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 2-157 1.06e-103

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 295.59  E-value: 1.06e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110    2 NVQPSNPNNPIVFFDVSIGGQEVGRMKIELFADIVPKTAENFRQFCTGEFKKDGVPVGYKGCTFHRVIKDFMIQGGDFVN 81
Cdd:PLN03149  10 HLRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDFMIQGGDFLK 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055110   82 GDGTGICSIYRGPFADENFRMKHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVV-DGLLVMRKIEAV 157
Cdd:PLN03149  90 GDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENV 166
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 25-173 9.37e-54

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: 167.82  E-value: 9.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110    25 GRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDFVNGDGTGIcSIYrgPFADENF--RM 102
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCKKGF--------YDGTTFHRVIPGFMVQGGDPTGTGGGGK-SIF--PIPDEIFplLL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055110   103 KHsGPGLLSMANSG--PGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAVVFINFIGTAQNKISST 173
Cdd:pfam00160  76 KH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSC 147
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 8-157 8.07e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 142.62  E-value: 8.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110   8 PNNPIVFFDVSiggqeVGRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDFvNGDGTGi 87
Cdd:COG0652   4 APNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLAKEGF--------YDGTIFHRVIPGFMIQGGDP-TGTGTG- 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055110  88 csiyrGP---FADENF-RMKHsGPGLLSMANS-GPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAV 157
Cdd:COG0652  69 -----GPgytIPDEFDpGLKH-KRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAG 137
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 11-175 6.89e-107

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: 302.64  E-value: 6.89e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  11 PIVFFDVSIGGQEVGRMKIELFADIVPKTAENFRQFCTGEFKKDGVPVGYKGCTFHRVIKDFMIQGGDFVNGDGTGICSI 90
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  91 YRGPFADENFRMKHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAVvfinfiGTAQNKI 170
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENV------GSGNGKP 154


                ....*
gi 41055110 171 SSTIT 175
Cdd:cd01926 155 KKKVV 159
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 2-157 1.06e-103

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 295.59  E-value: 1.06e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110    2 NVQPSNPNNPIVFFDVSIGGQEVGRMKIELFADIVPKTAENFRQFCTGEFKKDGVPVGYKGCTFHRVIKDFMIQGGDFVN 81
Cdd:PLN03149  10 HLRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDFMIQGGDFLK 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41055110   82 GDGTGICSIYRGPFADENFRMKHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVV-DGLLVMRKIEAV 157
Cdd:PLN03149  90 GDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENV 166
PTZ00060 PTZ00060
cyclophilin; Provisional
 5-178 1.65e-74

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 221.64  E-value: 1.65e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110    5 PSNPNNPIVFFDVSIGGQEVGRMKIELFADIVPKTAENFRQFCTGEFK-KDGVPVGYKGCTFHRVIKDFMIQGGDFVNGD 83
Cdd:PTZ00060  10 PEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDKVgSSGKNLHYKGSIFHRIIPQFMCQGGDITNHN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110   84 GTGICSIYRGPFADENFRMKHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAVvfinfi 163
Cdd:PTZ00060  90 GTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKE------ 163

                        170
                 ....*....|....*
gi 41055110  164 GTAQNKISSTITLPN 178
Cdd:PTZ00060 164 GTQSGYPKKPVVVTD 178
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 24-157 3.92e-56

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: 173.60  E-value: 3.92e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  24 VGRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDFVNGDGTGICSIYrgPFADENFRMK 103
Cdd:cd00317   6 KGRIVIELYGDEAPKTVENFLSLARGGF--------YDGTTFHRVIPGFMIQGGDPTGTGGGGSGPGY--KFPDENFPLK 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055110 104 -HSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAV 157
Cdd:cd00317  76 yHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERG 130
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 25-173 9.37e-54

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: 167.82  E-value: 9.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110    25 GRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDFVNGDGTGIcSIYrgPFADENF--RM 102
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCKKGF--------YDGTTFHRVIPGFMVQGGDPTGTGGGGK-SIF--PIPDEIFplLL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41055110   103 KHsGPGLLSMANSG--PGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAVVFINFIGTAQNKISST 173
Cdd:pfam00160  76 KH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSC 147
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 25-157 4.00e-46

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: 148.38  E-value: 4.00e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  25 GRMKIELFADIVPKTAENFRQFCtgefkKDGVpvgYKGCTFHRVIKDFMIQGGDFVnGDGTGICSIYRGPFADE-NFRMK 103
Cdd:cd01927   7 GDIHIRLFPEEAPKTVENFTTHA-----RNGY---YNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLK 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 41055110 104 HSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAV 157
Cdd:cd01927  78 HDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENV 131
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 25-157 3.50e-44

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.


Pssm-ID: 238904 [Multi-domain]  Cd Length: 159  Bit Score: 143.71  E-value: 3.50e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  25 GRMKIELFADIVPKTAENFRQFCtgefkKDGVpvgYKGCTFHRVIKDFMIQGGDfVNGDGTGICSIYRGPFADE-NFRMK 103
Cdd:cd01923   9 GDLNLELHCDKAPKACENFIKLC-----KKGY---YDGTIFHRSIRNFMIQGGD-PTGTGRGGESIWGKPFKDEfKPNLS 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 41055110 104 HSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAV 157
Cdd:cd01923  80 HDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENV 133
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 8-157 8.07e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 142.62  E-value: 8.07e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110   8 PNNPIVFFDVSiggqeVGRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDFvNGDGTGi 87
Cdd:COG0652   4 APNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLAKEGF--------YDGTIFHRVIPGFMIQGGDP-TGTGTG- 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41055110  88 csiyrGP---FADENF-RMKHsGPGLLSMANS-GPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAV 157
Cdd:COG0652  69 -----GPgytIPDEFDpGLKH-KRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAG 137
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 24-156 5.88e-43

Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans isomerase (PPIL3). Members of this family lack a key residue important for cyclosporin binding: the tryptophan residue corresponding to W121 in human hCyP-18a; most members have a histidine at this position. The exact function of the protein is not known.


Pssm-ID: 238909 [Multi-domain]  Cd Length: 153  Bit Score: 140.26  E-value: 5.88e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  24 VGRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDfVNGDGTGICSIYRGPFADEnFR-- 101
Cdd:cd01928   9 LGDIKIELFCDDCPKACENFLALCASGY--------YNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDE-FRet 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055110 102 MKHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEA 156
Cdd:cd01928  79 LKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEK 133
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 24-157 1.02e-40

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: 134.58  E-value: 1.02e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  24 VGRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDfVNGDGTGICSIYRGPFADE-NFRM 102
Cdd:cd01922   6 MGEITLELYWNHAPKTCKNFYELAKRGY--------YNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEiHPEL 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41055110 103 KHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAV 157
Cdd:cd01922  77 KHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEV 131
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 24-158 2.01e-38

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: 129.39  E-value: 2.01e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  24 VGRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDfVNGDGTGICSIYRGPFADE-NFRM 102
Cdd:cd01925  14 AGDIDIELWSKEAPKACRNFIQLCLEGY--------YDNTIFHRVVPGFIIQGGD-PTGTGTGGESIYGEPFKDEfHSRL 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41055110 103 KHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVV-DGLLVMRKIEAVV 158
Cdd:cd01925  85 RFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIYNLLKLAEVE 141
PTZ00221 PTZ00221
cyclophilin; Provisional
 13-157 5.68e-30

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 109.96  E-value: 5.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110   13 VFFDVSIGGQEVGRMKIELFADIVPKTAENFRQFCTGEFKKD---GVPVGYKGCTFHRV-IKDFMIQGGDFvngDGTGIc 88
Cdd:PTZ00221  55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDtntGVKLDYLYTPVHHVdRNNNIIVLGEL---DSFNV- 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41055110   89 SIYRGPFADENFRMKHSGPGLLSMANSGPGTNGCQFFITCTKCDWLDGKHVVFGKVVDGLLVMRKIEAV 157
Cdd:PTZ00221 131 SSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESL 199
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 24-176 6.25e-27

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


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 99.72  E-value: 6.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  24 VGRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDfVNGDGTGICSIY-----RGP--FA 96
Cdd:cd01921   6 LGDLVIDLFTDECPLACLNFLKLCKLKY--------YNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYsqlygRQArfFE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  97 DE-NFRMKHSGPGLLSMANSGPGTNGCQFFITCTK-CDWLDGKHVVFGKVVDGLLVMRKI-EAVVFINFIGTAQNKISST 173
Cdd:cd01921  77 PEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKInDAIVDDDGRPLKDIRIKHT 156


                ...
gi 41055110 174 ITL 176
Cdd:cd01921 157 HIL 159
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 25-162 7.26e-16

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


Pssm-ID: 238901 [Multi-domain]  Cd Length: 155  Bit Score: 70.93  E-value: 7.26e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  25 GRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDFvNGDGTGICSIyrGPFADENFRMKH 104
Cdd:cd01920   7 GDIVVELYDDKAPITVENFLAYVRKGF--------YDNTIFHRVISGFVIQGGGF-TPDLAQKETL--KPIKNEAGNGLS 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41055110 105 SGPGLLSMANSG-PGTNGCQFFITCTKCDWLD-----GKHVVFGKVVDGLLVMRKIEAVVFINF 162
Cdd:cd01920  76 NTRGTIAMARTNaPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYSF 139
PRK10791 PRK10791
peptidylprolyl isomerase B;
25-157 1.29e-12

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 62.55  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110   25 GRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDFVNGDGTgicSIYRGPFADENFRMKH 104
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCREGF--------YNNTIFHRVINGFMIQGGGFEPGMKQ---KATKEPIKNEANNGLK 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41055110  105 SGPGLLSMANSG-PGTNGCQFFITCTKCDWLDGK--------HVVFGKVVDGLLVMRKIEAV 157
Cdd:PRK10791  78 NTRGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGV 139
PRK10903 PRK10903
peptidylprolyl isomerase A;
24-179 2.94e-11

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 59.47  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110   24 VGRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGDFvNGDGTGICSiyRGPFADENFRMK 103
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYVNSGF--------YNNTTFHRVIPGFMIQGGGF-TEQMQQKKP--NPPIKNEADNGL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  104 HSGPGLLSMANSGPGTNG-CQFFITCTKCDWLD-GK----HVVFGKVVDGLLVMRKIEAVVFINfIGTAQNKISSTITLP 177
Cdd:PRK10903 106 RNTRGTIAMARTADKDSAtSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHD-VGPYQNVPSKPVVIL 184


                 ..
gi 41055110  178 NA 179
Cdd:PRK10903 185 SA 186
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 25-156 1.51e-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: 51.68  E-value: 1.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  25 GRMKIELFADIVPKTAENFRQFCTGEFkkdgvpvgYKGCTFHRVIKDFMIQGGD-----------------------FVN 81
Cdd:cd01924   7 GTITIVLDGYNAPVTAGNFVDLVERGF--------YDGMEFHRVEGGFVVQTGDpqgknpgfpdpetgksrtipleiKPE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41055110  82 GDGTgicSIYRGPFA-----DENFRMKHSGPGLLSMA------NSGPGtngcQFFI-------TCTKCDWLDGKHVVFGK 143
Cdd:cd01924  79 GQKQ---PVYGKTLEeagryDEQPVLPFNAFGAIAMArtefdpNSASS----QFFFllkdnelTPSRNNVLDGRYAVFGY 151

                       170
                ....*....|...
gi 41055110 144 VVDGLLVMRKIEA 156
Cdd:cd01924 152 VTDGLDILRELKV 164
 
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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