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Conserved domains on  [gi|530392757|ref|XP_005269436|]
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peptidyl-prolyl cis-trans isomerase F, mitochondrial isoform X1 [Homo sapiens]

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 ...
 46-163 8.23e-90

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: 260.27  E-value: 8.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  46 PLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI 120
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530392757 121 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDW 163
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPW 123
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 46-163 8.23e-90

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: 260.27  E-value: 8.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  46 PLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI 120
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530392757 121 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDW 163
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPW 123
PTZ00060 PTZ00060
cyclophilin; Provisional
 45-163 4.86e-73

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 218.56  E-value: 4.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  45 NPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGE------KGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGK 118
Cdd:PTZ00060  15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530392757 119 SIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDW 163
Cdd:PTZ00060  95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPW 139
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 59-163 8.92e-42

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: 138.16  E-value: 8.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757   59 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFTNHNGtGGKSIYGsrFPDENF--TLKHVg 136
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPTGTGG-GGKSIFP--IPDEIFplLLKHK- 78

                          90       100
                  ....*....|....*....|....*....
gi 530392757  137 PGVLSMANAG--PNTNGSQFFICTIKTDW 163
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPH 107
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 45-168 7.33e-40

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 133.37  E-value: 7.33e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  45 NPLVYLDVDangkpLGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKsiyGSR 124
Cdd:COG0652    6 NPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GYT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530392757 125 FPDENFT-LKHVgPGVLSMANA-GPNTNGSQFFICTIKTDWsmaLD 168
Cdd:COG0652   74 IPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPH---LD 115
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 46-163 8.23e-90

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: 260.27  E-value: 8.23e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  46 PLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKG-----FGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI 120
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530392757 121 YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDW 163
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPW 123
PTZ00060 PTZ00060
cyclophilin; Provisional
 45-163 4.86e-73

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 218.56  E-value: 4.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  45 NPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGE------KGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGK 118
Cdd:PTZ00060  15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGE 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530392757 119 SIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDW 163
Cdd:PTZ00060  95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPW 139
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 45-169 2.87e-61

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 188.89  E-value: 2.87e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  45 NPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGE---KGF--GYKGSTFHRVIPSFMCQAGDFTNHNGTGGKS 119
Cdd:PLN03149  18 NPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkAGLpqGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVS 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530392757 120 IYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWsmaLDD 169
Cdd:PLN03149  98 IYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDW---LDN 144
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 60-169 2.46e-48

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: 154.73  E-value: 2.46e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  60 GRVVLELKADVVPKTAENFRALCTGEkgfGYKGSTFHRVIPSFMCQAGDFTNHNGtgGKSIYGSRFPDENFTLK-HVGPG 138
Cdd:cd00317    7 GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFPDENFPLKyHHRRG 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 530392757 139 VLSMANAGPNTNGSQFFICTIKTDWsmaLDD 169
Cdd:cd00317   82 TLSMANAGPNTNGSQFFITTAPTPH---LDG 109
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 59-163 8.92e-42

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: 138.16  E-value: 8.92e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757   59 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFTNHNGtGGKSIYGsrFPDENF--TLKHVg 136
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPTGTGG-GGKSIFP--IPDEIFplLLKHK- 78

                          90       100
                  ....*....|....*....|....*....
gi 530392757  137 PGVLSMANAG--PNTNGSQFFICTIKTDW 163
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPH 107
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 45-168 7.33e-40

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 133.37  E-value: 7.33e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  45 NPLVYLDVDangkpLGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKsiyGSR 124
Cdd:COG0652    6 NPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GYT 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530392757 125 FPDENFT-LKHVgPGVLSMANA-GPNTNGSQFFICTIKTDWsmaLD 168
Cdd:COG0652   74 IPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPH---LD 115
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 59-163 1.47e-36

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: 124.57  E-value: 1.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  59 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE-NFTLKHVGP 137
Cdd:cd01922    6 MGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPELKHTGA 81

                         90       100
                 ....*....|....*....|....*.
gi 530392757 138 GVLSMANAGPNTNGSQFFICTIKTDW 163
Cdd:cd01922   82 GILSMANAGPNTNGSQFFITLAPTPW 107
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 59-163 4.17e-36

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: 123.73  E-value: 4.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  59 LGRVVLELKADVVPKTAENFralCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE-NFTLKHVGP 137
Cdd:cd01927    6 KGDIHIRLFPEEAPKTVENF---TTHARNGYYNNTIFHRVIKGFMIQTGDPTG-DGTGGESIWGKEFEDEfSPSLKHDRP 81

                         90       100
                 ....*....|....*....|....*.
gi 530392757 138 GVLSMANAGPNTNGSQFFICTIKTDW 163
Cdd:cd01927   82 YTLSMANAGPNTNGSQFFITTVATPW 107
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 59-156 2.70e-35

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: 121.75  E-value: 2.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  59 LGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE-NFTLKHVGP 137
Cdd:cd01923    8 KGDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHDGR 83

                         90
                 ....*....|....*....
gi 530392757 138 GVLSMANAGPNTNGSQFFI 156
Cdd:cd01923   84 GVLSMANSGPNTNGSQFFI 102
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 59-156 1.83e-34

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: 119.46  E-value: 1.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  59 LGRVVLELKADVVPKTAENFRALCTGekGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDENF-TLKHVGP 137
Cdd:cd01928    9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFReTLKHDSR 84

                         90
                 ....*....|....*....
gi 530392757 138 GVLSMANAGPNTNGSQFFI 156
Cdd:cd01928   85 GVVSMANNGPNTNGSQFFI 103
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 59-163 1.99e-28

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: 104.36  E-value: 1.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  59 LGRVVLELKADVVPKTAENFRALCTgeKGFgYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE-NFTLKHVGP 137
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRLRFNRR 89

                         90       100
                 ....*....|....*....|....*.
gi 530392757 138 GVLSMANAGPNTNGSQFFICTIKTDW 163
Cdd:cd01925   90 GLVGMANAGDDSNGSQFFFTLDKADE 115
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 59-156 3.44e-17

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: 75.07  E-value: 3.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  59 LGRVVLELKADVVPKTAENFRALCtgeKGFGYKGSTFHRVIPSFMCQAGDFTNhNGTGGKSIYGSRFPDE--NFT----- 131
Cdd:cd01921    6 LGDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPTG-TGAGGESIYSQLYGRQarFFEpeilp 81

                         90       100
                 ....*....|....*....|....*.
gi 530392757 132 -LKHVGPGVLSMANAGPNTNGSQFFI 156
Cdd:cd01921   82 lLKHSKKGTVSMVNAGDNLNGSQFYI 107
PTZ00221 PTZ00221
cyclophilin; Provisional
 48-156 1.48e-13

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 66.82  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  48 VYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKG--------FGYKGSTFHRVIPSF-MCQAGDFTNHNgtggK 118
Cdd:PTZ00221  55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHVDRNNnIIVLGELDSFN----V 130

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 530392757 119 SIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFI 156
Cdd:PTZ00221 131 SSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGI 168
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 59-156 3.46e-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: 64.39  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392757  59 LGRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFT-------------NHNGTGGKSIYGSrf 125
Cdd:cd01920    6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTpdlaqketlkpikNEAGNGLSNTRGT-- 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 530392757 126 pdenftlkhvgpgvLSMA-NAGPNTNGSQFFI 156
Cdd:cd01920   81 --------------IAMArTNAPDSATSQFFI 98
PRK10903 PRK10903
peptidylprolyl isomerase A;
60-110 4.44e-07

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 48.30  E-value: 4.44e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530392757  60 GRVVLELKADVVPKTAENFRALCtgEKGFgYKGSTFHRVIPSFMCQAGDFT 110
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGFT 85
 
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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