cyclophilin 38 [Arabidopsis thaliana]
peptidylprolyl isomerase( domain architecture ID 10112474)
cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
cyclophilin_TLP40_like | cd01924 | cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ... |
250-424 | 4.82e-103 | ||||
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: 303.60 E-value: 4.82e-103
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Name | Accession | Description | Interval | E-value | ||||
cyclophilin_TLP40_like | cd01924 | cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ... |
250-424 | 4.82e-103 | ||||
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: 303.60 E-value: 4.82e-103
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PpiB | COG0652 | Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
258-424 | 1.62e-25 | ||||
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 101.79 E-value: 1.62e-25
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Pro_isomerase | pfam00160 | Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
258-423 | 2.02e-23 | ||||
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: 95.40 E-value: 2.02e-23
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PRK10903 | PRK10903 | peptidylprolyl isomerase A; |
252-420 | 4.23e-06 | ||||
peptidylprolyl isomerase A; Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 47.14 E-value: 4.23e-06
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Name | Accession | Description | Interval | E-value | ||||
cyclophilin_TLP40_like | cd01924 | cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ... |
250-424 | 4.82e-103 | ||||
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: 303.60 E-value: 4.82e-103
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cyclophilin | cd00317 | cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ... |
260-415 | 1.51e-27 | ||||
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: 106.96 E-value: 1.51e-27
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PpiB | COG0652 | Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
258-424 | 1.62e-25 | ||||
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 101.79 E-value: 1.62e-25
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Pro_isomerase | pfam00160 | Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
258-423 | 2.02e-23 | ||||
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: 95.40 E-value: 2.02e-23
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cyclophilin_EcCYP_like | cd01920 | cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ... |
258-413 | 2.23e-13 | ||||
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: 67.47 E-value: 2.23e-13
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PRK10903 | PRK10903 | peptidylprolyl isomerase A; |
252-420 | 4.23e-06 | ||||
peptidylprolyl isomerase A; Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 47.14 E-value: 4.23e-06
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cyclophilin_RRM | cd01921 | cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ... |
253-416 | 7.19e-06 | ||||
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: 46.18 E-value: 7.19e-06
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cyclophilin_RING | cd01923 | cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
265-410 | 8.08e-06 | ||||
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: 45.87 E-value: 8.08e-06
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cyclophilin_CeCYP16-like | cd01925 | cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ... |
267-431 | 1.94e-05 | ||||
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: 45.04 E-value: 1.94e-05
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Blast search parameters | ||||
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