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Conserved domains on  [gi|289803023|ref|NP_001104768|]
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probable inactive peptidyl-prolyl cis-trans isomerase-like 6 isoform 2 [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 ...
 144-333 3.22e-64

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: 200.56  E-value: 3.22e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 144 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 223
Cdd:cd01926    3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 224 YGptfeelygslkrsvkrqkesrgvgkiEKYRDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQL 303
Cdd:cd01926   81 YG--------------------------EKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKV 134

                        170       180       190
                 ....*....|....*....|....*....|
gi 289803023 304 IEGTEVLKQLELVPTQNERPIHMCRITDSG 333
Cdd:cd01926  135 VEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 144-333 3.22e-64

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: 200.56  E-value: 3.22e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 144 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 223
Cdd:cd01926    3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 224 YGptfeelygslkrsvkrqkesrgvgkiEKYRDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQL 303
Cdd:cd01926   81 YG--------------------------EKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKV 134

                        170       180       190
                 ....*....|....*....|....*....|
gi 289803023 304 IEGTEVLKQLELVPTQNERPIHMCRITDSG 333
Cdd:cd01926  135 VEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 127-334 2.28e-60

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 191.60  E-value: 2.28e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 127 LTEDFSAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAgFSQRGIRLHYKNSIFHRIVQNGW 206
Cdd:PTZ00060   1 FFKLFSQSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 207 IQGGDIVYGKGDNGESIYGPTFEelygslkrsvkrqkesrgvgkiekyrDENFSVPHNKRGVLGMANKGRHSNGSQFYIT 286
Cdd:PTZ00060  80 CQGGDITNHNGTGGESIYGRKFT--------------------------DENFKLKHDQPGLLSMANAGPNTNGSQFFIT 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 289803023 287 LQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNERPIHMCRITDSGD 334
Cdd:PTZ00060 134 TVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGE 181
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 153-333 2.02e-50

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: 164.74  E-value: 2.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023  153 SPIGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVygkGDNGESIYGPTFeely 232
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPI---- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023  233 gslkrsvkrqkesrgvgkiekyRDENF-SVPHNKRGVLGMANKGR--HSNGSQFYITLQATPYLDRKFVAFGQLIEGTEV 309
Cdd:pfam00160  67 ----------------------PDEIFpLLLKHKRGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDV 124

                         170       180
                  ....*....|....*....|....
gi 289803023  310 LKQLELVPTQNERPIHMCRITDSG 333
Cdd:pfam00160 125 LEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 156-330 3.37e-33

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 120.27  E-value: 3.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIvygkgdNGESIYGPTFeelygsl 235
Cdd:COG0652   16 GDIVIELFPDKAPKTVANFVSLA--KEGF--------YDGTIFHRVIPGFMIQGGDP------TGTGTGGPGY------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 236 krsvkrqkesrgvgkieKYRDENFSVPHNKRGVLGMAN-KGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLE 314
Cdd:COG0652   73 -----------------TIPDEFDPGLKHKRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIA 135

                        170
                 ....*....|....*..
gi 289803023 315 LVPTQ-NERPIHMCRIT 330
Cdd:COG0652  136 AGPTDpGDGPLEPVVIE 152
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 144-333 3.22e-64

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: 200.56  E-value: 3.22e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 144 VFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGFSqrGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDNGESI 223
Cdd:cd01926    3 VFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 224 YGptfeelygslkrsvkrqkesrgvgkiEKYRDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQL 303
Cdd:cd01926   81 YG--------------------------EKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKV 134

                        170       180       190
                 ....*....|....*....|....*....|
gi 289803023 304 IEGTEVLKQLELVPTQNERPIHMCRITDSG 333
Cdd:cd01926  135 VEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 127-334 2.28e-60

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 191.60  E-value: 2.28e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 127 LTEDFSAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAgFSQRGIRLHYKNSIFHRIVQNGW 206
Cdd:PTZ00060   1 FFKLFSQSFPEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 207 IQGGDIVYGKGDNGESIYGPTFEelygslkrsvkrqkesrgvgkiekyrDENFSVPHNKRGVLGMANKGRHSNGSQFYIT 286
Cdd:PTZ00060  80 CQGGDITNHNGTGGESIYGRKFT--------------------------DENFKLKHDQPGLLSMANAGPNTNGSQFFIT 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 289803023 287 LQATPYLDRKFVAFGQLIEGTEVLKQLELVPTQNERPIHMCRITDSGD 334
Cdd:PTZ00060 134 TVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGE 181
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 155-331 1.01e-52

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: 170.52  E-value: 1.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 155 IGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVYGKGdnGESIYGPTFEelygs 234
Cdd:cd00317    6 KGRIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPTGTGG--GGSGPGYKFP----- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 235 lkrsvkrqkesrgvgkiekyrDENFSVP-HNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQL 313
Cdd:cd00317   69 ---------------------DENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKI 127

                        170
                 ....*....|....*....
gi 289803023 314 ELVPTQ-NERPIHMCRITD 331
Cdd:cd00317  128 ERGDTDeNGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 153-333 2.02e-50

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: 164.74  E-value: 2.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023  153 SPIGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVygkGDNGESIYGPTFeely 232
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCKKG----------FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPI---- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023  233 gslkrsvkrqkesrgvgkiekyRDENF-SVPHNKRGVLGMANKGR--HSNGSQFYITLQATPYLDRKFVAFGQLIEGTEV 309
Cdd:pfam00160  67 ----------------------PDEIFpLLLKHKRGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDV 124

                         170       180
                  ....*....|....*....|....
gi 289803023  310 LKQLELVPTQNERPIHMCRITDSG 333
Cdd:pfam00160 125 LEKIEKVPTDGDRPVKPVKILSCG 148
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 140-334 2.23e-45

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 153.07  E-value: 2.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 140 KHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKagFSQRGIRLHYKNSIFHRIVQNGWIQGGDIVYGKGDN 219
Cdd:PLN03149  17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 220 GESIYGPTFEelygslkrsvkrqkesrgvgkiekyrDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVA 299
Cdd:PLN03149  95 CVSIYGSKFE--------------------------DENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVV 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 289803023 300 FGQLI-EGTEVLKQLELVPT-QNERPIHMCRITDSGD 334
Cdd:PLN03149 149 FGRVLgDGLLVVRKIENVATgPNNRPKLACVISECGE 185
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 156-331 3.70e-42

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: 143.73  E-value: 3.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFE-ELYGS 234
Cdd:cd01928   10 GDIKIELFCDDCPKACENFLALCASG----------YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEdEFRET 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 235 LKrsvkrqkesrgvgkiekyrdenfsvpHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLE 314
Cdd:cd01928   79 LK--------------------------HDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLE 132

                        170
                 ....*....|....*...
gi 289803023 315 LVPT-QNERPIHMCRITD 331
Cdd:cd01928  133 KLPVdKKYRPLEEIRIKD 150
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 156-337 4.09e-39

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: 136.01  E-value: 4.09e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFQVLCtgkagfsQRGirlHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFEELYGSl 235
Cdd:cd01923    9 GDLNLELHCDKAPKACENFIKLC-------KKG---YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEFKP- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 236 krsvkrqkesrgvgkiekyrdeNFSvpHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLEL 315
Cdd:cd01923   77 ----------------------NLS--HDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMEN 132

                        170       180
                 ....*....|....*....|....*.
gi 289803023 316 VPTQ-NERPIHMCRITDSG---DPYA 337
Cdd:cd01923  133 VPDPgTDRPKEEIKIEDTSvfvDPFE 158
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 155-329 8.84e-34

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: 121.49  E-value: 8.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 155 IGRLIFELYCDVCPKTCKNFQVLCTgkagfsqrgiRLHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFE-ELYG 233
Cdd:cd01922    6 MGEITLELYWNHAPKTCKNFYELAK----------RGYYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEdEIHP 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 234 SLKrsvkrqkesrgvgkiekyrdenfsvpHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQL 313
Cdd:cd01922   75 ELK--------------------------HTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM 128

                        170
                 ....*....|....*.
gi 289803023 314 ELVPTQNERPIHMCRI 329
Cdd:cd01922  129 VEVQTQTDRPIDEVKI 144
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 156-330 3.37e-33

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 120.27  E-value: 3.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIvygkgdNGESIYGPTFeelygsl 235
Cdd:COG0652   16 GDIVIELFPDKAPKTVANFVSLA--KEGF--------YDGTIFHRVIPGFMIQGGDP------TGTGTGGPGY------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 236 krsvkrqkesrgvgkieKYRDENFSVPHNKRGVLGMAN-KGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLE 314
Cdd:COG0652   73 -----------------TIPDEFDPGLKHKRGTLAMARaQGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIA 135

                        170
                 ....*....|....*..
gi 289803023 315 LVPTQ-NERPIHMCRIT 330
Cdd:COG0652  136 AGPTDpGDGPLEPVVIE 152
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 156-329 2.11e-31

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: 115.25  E-value: 2.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFE-ELYGS 234
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENFTTHA--RNGY--------YNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEdEFSPS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 235 LKrsvkrqkesrgvgkiekyrdenfsvpHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGTEVLKQLE 314
Cdd:cd01927   76 LK--------------------------HDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIE 129

                        170
                 ....*....|....*.
gi 289803023 315 LVPT-QNERPIHMCRI 329
Cdd:cd01927  130 NVKTdKNDRPYEDIKI 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 156-330 2.08e-30

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: 113.60  E-value: 2.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFQVLCtgkagfsqrgIRLHYKNSIFHRIVQNGWIQGGDIVyGKGDNGESIYGPTFE-ELYGS 234
Cdd:cd01925   15 GDIDIELWSKEAPKACRNFIQLC----------LEGYYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKdEFHSR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 235 LKrsvkrqkesrgvgkiekyrdenfsvpHNKRGVLGMANKGRHSNGSQFYITLQATPYLDRKFVAFGQLIEGT--EVLKQ 312
Cdd:cd01925   84 LR--------------------------FNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTiyNLLKL 137

                        170
                 ....*....|....*...
gi 289803023 313 LELVPTQNERPIHMCRIT 330
Cdd:cd01925  138 AEVETDKDERPVYPPKIT 155
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 155-330 1.48e-28

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: 108.58  E-value: 1.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 155 IGRLIFELYCDVCPKTCKNFQVLCTGKagfsqrgirlHYKNSIFHRIVQNGWIQGGDiVYGKGDNGESIYGPtfeeLYGS 234
Cdd:cd01921    6 LGDLVIDLFTDECPLACLNFLKLCKLK----------YYNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYSQ----LYGR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 235 LKRSVKRQKesrgvgkiekyrdeNFSVPHNKRGVLGMANKGRHSNGSQFYITL-QATPYLDRKFVAFGQLIEGTEVLKQL 313
Cdd:cd01921   71 QARFFEPEI--------------LPLLKHSKKGTVSMVNAGDNLNGSQFYITLgENLDYLDGKHTVFGQVVEGFDVLEKI 136

                        170
                 ....*....|....*...
gi 289803023 314 ELVPTQNE-RPIHMCRIT 330
Cdd:cd01921  137 NDAIVDDDgRPLKDIRIK 154
PTZ00221 PTZ00221
cyclophilin; Provisional
 132-324 2.55e-26

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 104.95  E-value: 2.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 132 SAKFLRDTKHDFVFLDICIDSSPIGRLIFELYCDVCPKTCKNFQVLCTGKAGF-SQRGIRLHYKNSIFHRI-VQNGWIQG 209
Cdd:PTZ00221  43 SHRMKEEQNSCRAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIdTNTGVKLDYLYTPVHHVdRNNNIIVL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 210 GDIV-YGKGDNGESIygptfeelygslkrsvkrqkesrgvgkiekyRDENFSVPHNKRGVLGMANKGRHSNGSQFYITLQ 288
Cdd:PTZ00221 123 GELDsFNVSSTGTPI-------------------------------ADEGYRHRHTERGLLTMISEGPHTSGSVFGITLG 171

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 289803023 289 ATPYLDRKFVAFGQLIEGTEVLKQLELVP-TQNERPI 324
Cdd:PTZ00221 172 PSPSLDFKQVVFGKAVDDLSLLEKLESLPlDDVGRPL 208
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 156-323 7.99e-14

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: 68.24  E-value: 7.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGdivyGKGDNGESIygPTFEELYGSL 235
Cdd:cd01920    7 GDIVVELYDDKAPITVENFLAYV--RKGF--------YDNTIFHRVISGFVIQGG----GFTPDLAQK--ETLKPIKNEA 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 236 KRSVKrqkesrgvgkiekyrdenfsvphNKRGVLGMA-NKGRHSNGSQFYITLQATPYLDRK-----FVAFGQLIEGTEV 309
Cdd:cd01920   71 GNGLS-----------------------NTRGTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDV 127

                        170
                 ....*....|....
gi 289803023 310 LKQLELVPTQNERP 323
Cdd:cd01920  128 VDKIAGVETYSFGS 141
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 168-315 4.58e-07

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: 49.36  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 168 PKTCKNFqvlctgkAGFSQRGIrlhYKNSIFHRIVQNGWIQGGDiVYGKGDN------GESIYGP-------TFEELYGS 234
Cdd:cd01924   19 PVTAGNF-------VDLVERGF---YDGMEFHRVEGGFVVQTGD-PQGKNPGfpdpetGKSRTIPleikpegQKQPVYGK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 235 LKRSVKRQkesrgvgkiekyrDENFSVPHNKRGVLGMAN--KGRHSNGSQFYITLQA-------TPYLDRKFVAFGQLIE 305
Cdd:cd01924   88 TLEEAGRY-------------DEQPVLPFNAFGAIAMARteFDPNSASSQFFFLLKDneltpsrNNVLDGRYAVFGYVTD 154

                        170
                 ....*....|
gi 289803023 306 GTEVLKQLEL 315
Cdd:cd01924  155 GLDILRELKV 164
PRK10903 PRK10903
peptidylprolyl isomerase A;
156-323 7.02e-07

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 49.07  E-value: 7.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFqvLCTGKAGFsqrgirlhYKNSIFHRIVQNGWIQGGdivygkGDNGEsiygptfeelygsl 235
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNF--VDYVNSGF--------YNNTTFHRVIPGFMIQGG------GFTEQ-------------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 236 krsvKRQKESRGVGKIEKyrDENFsvpHNKRGVLGMANKG-RHSNGSQFYITLQATPYLD---RKF--VAFGQLIEGTEV 309
Cdd:PRK10903  88 ----MQQKKPNPPIKNEA--DNGL---RNTRGTIAMARTAdKDSATSQFFINVADNAFLDhgqRDFgyAVFGKVVKGMDV 158

                        170
                 ....*....|....
gi 289803023 310 LKQLELVPTQNERP 323
Cdd:PRK10903 159 ADKISQVPTHDVGP 172
PRK10791 PRK10791
peptidylprolyl isomerase B;
156-318 4.81e-06

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 45.99  E-value: 4.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 156 GRLIFELYCDVCPKTCKNFQVLCtgKAGFsqrgirlhYKNSIFHRIVQNGWIQGGDIVYGkgdngesiygptfeelygsl 235
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYC--REGF--------YNNTIFHRVINGFMIQGGGFEPG-------------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 289803023 236 krsvKRQKESRgvgkiEKYRDENFSVPHNKRGVLGMA-NKGRHSNGSQFYITLQATPYLDRK--------FVAFGQLIEG 306
Cdd:PRK10791  59 ----MKQKATK-----EPIKNEANNGLKNTRGTLAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEG 129

                        170
                 ....*....|..
gi 289803023 307 TEVLKQLELVPT 318
Cdd:PRK10791 130 MDVVDKIKGVAT 141
 
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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