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Conserved domains on  [gi|1039745247|ref|XP_017171263|]
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peptidyl-prolyl cis-trans isomerase F, mitochondrial isoform X2 [Mus musculus]

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

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 45-104 1.59e-38

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: 127.37  E-value: 1.59e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039745247  45 PLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPAFMCQ 104
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQ 65
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 45-104 1.59e-38

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: 127.37  E-value: 1.59e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039745247  45 PLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPAFMCQ 104
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQ 65
PTZ00060 PTZ00060
cyclophilin; Provisional
 40-104 1.76e-29

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 104.93  E-value: 1.76e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039745247  40 SSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGE------KGFGYKGSTFHRVIPAFMCQ 104
Cdd:PTZ00060   11 EMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQ 81
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 58-104 4.02e-18

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: 74.60  E-value: 4.02e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039745247  58 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPAFMCQ 104
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQ 49
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 43-104 3.58e-15

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 67.12  E-value: 3.58e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039745247  43 GNPLVYLDVgadgqPLGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQ 104
Cdd:COG0652     5 PNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQ 58
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 45-104 1.59e-38

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: 127.37  E-value: 1.59e-38
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039745247  45 PLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPAFMCQ 104
Cdd:cd01926     1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQ 65
PTZ00060 PTZ00060
cyclophilin; Provisional
 40-104 1.76e-29

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 104.93  E-value: 1.76e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039745247  40 SSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGE------KGFGYKGSTFHRVIPAFMCQ 104
Cdd:PTZ00060   11 EMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQ 81
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 44-104 8.04e-24

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 90.28  E-value: 8.04e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039745247  44 NPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGE---KGF--GYKGSTFHRVIPAFMCQ 104
Cdd:PLN03149   18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQ 83
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 58-104 4.02e-18

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: 74.60  E-value: 4.02e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039745247  58 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPAFMCQ 104
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQ 49
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 43-104 3.58e-15

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 67.12  E-value: 3.58e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039745247  43 GNPLVYLDVgadgqPLGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQ 104
Cdd:COG0652     5 PNPTVTLET-----NKGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQ 58
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 58-104 4.55e-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: 53.99  E-value: 4.55e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1039745247  58 LGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQ 104
Cdd:cd01920     6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQ 49
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 58-108 2.86e-09

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: 51.67  E-value: 2.86e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039745247  58 LGRVVLELKADVVPKTAENFRALCTGekGFgYKGSTFHRVIPAFMCQVSCP 108
Cdd:cd01928     9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDP 56
PTZ00221 PTZ00221
cyclophilin; Provisional
 47-97 1.84e-08

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 50.64  E-value: 1.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039745247  47 VYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKG--------FGYKGSTFHRV 97
Cdd:PTZ00221   55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHV 113
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 58-108 1.14e-06

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: 44.76  E-value: 1.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039745247  58 LGRVVLELKADVVPKTAENFralCTGEKGFGYKGSTFHRVIPAFMCQVSCP 108
Cdd:cd01927     6 KGDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDP 53
PRK10903 PRK10903
peptidylprolyl isomerase A;
37-104 3.94e-06

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 43.68  E-value: 3.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039745247  37 GANSSSGNPLVYLDVGAdgqplGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPAFMCQ 104
Cdd:PRK10903   21 AALAAKGDPHVLLTTSA-----GNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQ 80
 
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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