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Conserved domains on  [gi|490253314|ref|WP_004151319|]
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MULTISPECIES: peptidylprolyl isomerase B [Klebsiella]

Protein Classification

peptidylprolyl isomerase B( domain architecture ID 10793477)

peptidylprolyl isomerase B 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
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-164 4.52e-116

peptidylprolyl isomerase B;


:

Pssm-ID: 182734  Cd Length: 164  Bit Score: 325.26  E-value: 4.52e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKSPIQNEANNGLKNTR 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKAVATGRSGMHQDVPKDDVIIKSV 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ....
gi 490253314 161 TVSE 164
Cdd:PRK10791 161 TVSE 164
 
Name Accession Description Interval E-value
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-164 4.52e-116

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 325.26  E-value: 4.52e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKSPIQNEANNGLKNTR 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKAVATGRSGMHQDVPKDDVIIKSV 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ....
gi 490253314 161 TVSE 164
Cdd:PRK10791 161 TVSE 164
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 3-160 1.86e-97

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: 277.79  E-value: 1.86e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKSPIQNEANNGLKNTRGT 82
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490253314  83 LAMARTQAPHSATAQFFINVVDNDFLNFSGESlqgWGYCVFAEVVEGMDVVDKIKAVATGRSGMHQDVPKDDVIIKSV 160
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQ---WGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-164 2.77e-80

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 234.68  E-value: 2.77e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKsPIQNEANNGLKNTR 80
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGLKHKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFsgeslqgwGYCVFAEVVEGMDVVDKIKAVATGRsgmhQDVPKDDVIIKSV 160
Cdd:COG0652   87 GTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIESV 154


                 ....
gi 490253314 161 TVSE 164
Cdd:COG0652  155 TIVE 158
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-162 4.12e-58

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: 178.22  E-value: 4.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314    4 FHTN-HGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKSPIQNE-ANNGLKNTRG 81
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEiFPLLLKHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   82 TLAMART-QAPHSATAQFFINVVDNDFLNFsgeslqgwGYCVFAEVVEGMDVVDKIKAVATGRsgmhqDVPKDDVIIKSV 160
Cdd:pfam00160  81 ALSMANTgPAPNSNGSQFFITLGPAPHLDG--------KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSC 147


                  ..
gi 490253314  161 TV 162
Cdd:pfam00160 148 GV 149
 
Name Accession Description Interval E-value
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-164 4.52e-116

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 325.26  E-value: 4.52e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKSPIQNEANNGLKNTR 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKAVATGRSGMHQDVPKDDVIIKSV 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ....
gi 490253314 161 TVSE 164
Cdd:PRK10791 161 TVSE 164
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 3-160 1.86e-97

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: 277.79  E-value: 1.86e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKSPIQNEANNGLKNTRGT 82
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490253314  83 LAMARTQAPHSATAQFFINVVDNDFLNFSGESlqgWGYCVFAEVVEGMDVVDKIKAVATGRSGMHQDVPKDDVIIKSV 160
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQ---WGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-164 2.77e-80

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 234.68  E-value: 2.77e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKsPIQNEANNGLKNTR 80
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGLKHKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFsgeslqgwGYCVFAEVVEGMDVVDKIKAVATGRsgmhQDVPKDDVIIKSV 160
Cdd:COG0652   87 GTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIESV 154


                 ....
gi 490253314 161 TVSE 164
Cdd:COG0652  155 TIVE 158
PRK10903 PRK10903
peptidylprolyl isomerase A;
2-162 3.00e-66

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 200.07  E-value: 3.00e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKSPIQNEANNGLKNTRG 81
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  82 TLAMARTQAPHSATAQFFINVVDNDFLNfsgESLQGWGYCVFAEVVEGMDVVDKIKAVATGRSGMHQDVPKDDVIIKSVT 161
Cdd:PRK10903 111 TIAMARTADKDSATSQFFINVADNAFLD---HGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAK 187


                 .
gi 490253314 162 V 162
Cdd:PRK10903 188 V 188
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-162 4.12e-58

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: 178.22  E-value: 4.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314    4 FHTN-HGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFEPGMKQKATKSPIQNE-ANNGLKNTRG 81
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEiFPLLLKHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   82 TLAMART-QAPHSATAQFFINVVDNDFLNFsgeslqgwGYCVFAEVVEGMDVVDKIKAVATGRsgmhqDVPKDDVIIKSV 160
Cdd:pfam00160  81 ALSMANTgPAPNSNGSQFFITLGPAPHLDG--------KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSC 147


                  ..
gi 490253314  161 TV 162
Cdd:pfam00160 148 GV 149
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 3-159 1.30e-50

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: 158.97  E-value: 1.30e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGGFE-PGMKQKATKSPIQNE-ANNGLKNTR 80
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTgTGGGGSGPGYKFPDEnFPLKYHHRR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490253314  81 GTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKAVATGRsgmhQDVPKDDVIIKS 159
Cdd:cd00317   81 GTLSMANAG-PNTNGSQFFITTAPTPHLDGK--------HTVFGKVVEGMDVVDKIERGDTDE----NGRPIKPVTISD 146
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 3-160 3.14e-32

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: 112.17  E-value: 3.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGG-FEPGMKQKAT-KSPIQNEANNGLKNTR 80
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDpTGDGTGGESIwGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  81 -GTLAMARTqAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKAVATGRSgmhqDVPKDDVIIKS 159
Cdd:cd01927   81 pYTLSMANA-GPNTNGSQFFITTVATPWLDNK--------HTVFGRVVKGMDVVQRIENVKTDKN----DRPYEDIKIIN 147


                 .
gi 490253314 160 V 160
Cdd:cd01927  148 I 148
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 2-164 4.09e-32

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: 112.51  E-value: 4.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGgfEPGMKQKATKS----PIQNEANNGLK 77
Cdd:cd01923    2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGG--DPTGTGRGGESiwgkPFKDEFKPNLS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  78 NT-RGTLAMARTqAPHSATAQFFInvvdndflNFSGESLQGWGYCVFAEVVEGMDVVDKIKAVATGRSgmhqDVPKDDVI 156
Cdd:cd01923   80 HDgRGVLSMANS-GPNTNGSQFFI--------TYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGT----DRPKEEIK 146


                 ....*...
gi 490253314 157 IKSVTVSE 164
Cdd:cd01923  147 IEDTSVFV 154
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 2-162 3.90e-29

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: 104.44  E-value: 3.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGgfEPGMKQKATKS----PIQNEANNGLK 77
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTG--DPTGTGKGGESiwgkKFEDEFRETLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  78 -NTRGTLAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKAVATGRSgmhqDVPKDDVI 156
Cdd:cd01928   81 hDSRGVVSMA-NNGPNTNGSQFFITYAKQPHLDGK--------YTVFGKVIDGFETLDTLEKLPVDKK----YRPLEEIR 147


                 ....*.
gi 490253314 157 IKSVTV 162
Cdd:cd01928  148 IKDVTI 153
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 2-109 1.03e-25

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: 96.27  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGgfEP---GM-KQKATKSPIQNEANNGLK 77
Cdd:cd01925    8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGG--DPtgtGTgGESIYGEPFKDEFHSRLR 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 490253314  78 -NTRGTLAMARTQaPHSATAQFFINVVDNDFLN 109
Cdd:cd01925   86 fNRRGLVGMANAG-DDSNGSQFFFTLDKADELN 117
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 9-157 3.71e-24

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: 91.93  E-value: 3.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   9 GDIVIKTFDDKAPETVKNFLDYC-------REGF-YDNTIFHRVINGFMIQGGGFepgMKQKAT--KS----PIQNEaNN 74
Cdd:cd01926   15 GRIVMELFADVVPKTAENFRALCtgekgkgGKPFgYKGSTFHRVIPDFMIQGGDF---TRGNGTggKSiygeKFPDE-NF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  75 GLKNTR-GTLAMARTqAPHSATAQFFINVVDNDFLNfsGEslqgwgYCVFAEVVEGMDVVDKIKAVATGrsgmhQDVPKD 153
Cdd:cd01926   91 KLKHTGpGLLSMANA-GPNTNGSQFFITTVKTPWLD--GK------HVVFGKVVEGMDVVKKIENVGSG-----NGKPKK 156


                 ....
gi 490253314 154 DVII 157
Cdd:cd01926  157 KVVI 160
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 3-158 1.09e-23

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: 90.29  E-value: 1.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGGgfEPGMKQKATKS----PIQNEANNGLKN 78
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGG--DPTGTGRGGASiygkKFEDEIHPELKH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  79 T-RGTLAMARTqAPHSATAQFFINVVDNDFLNfsGEslqgwgYCVFAEVVEGMDVVDKIKAVATgrsgmHQDVPKDDV-I 156
Cdd:cd01922   79 TgAGILSMANA-GPNTNGSQFFITLAPTPWLD--GK------HTIFGRVSKGMKVIENMVEVQT-----QTDRPIDEVkI 144


                 ..
gi 490253314 157 IK 158
Cdd:cd01922  145 LK 146
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 11-138 1.87e-22

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: 87.88  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  11 IVIKTFDdkAPETVKNFLDYCREGFYDNTIFHRVINGFMIQGG---GFEPGMKQKAT---------------KSPIQNEA 72
Cdd:cd01924   11 IVLDGYN--APVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGdpqGKNPGFPDPETgksrtipleikpegqKQPVYGKT 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490253314  73 NNG----------LKNTRGTLAMARTQ-APHSATAQFFINVVDNDFLNFSGESLQGwGYCVFAEVVEGMDVVDKIKA 138
Cdd:cd01924   89 LEEagrydeqpvlPFNAFGAIAMARTEfDPNSASSQFFFLLKDNELTPSRNNVLDG-RYAVFGYVTDGLDILRELKV 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 7-141 1.27e-16

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 72.96  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   7 NHGDIVIKTFDDKAPETVKNFLDYC---------REGFYDNTIFHRVINGFMIQGGGF--EPGMKQKATKSPIQNEANNG 75
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDItnHNGTGGESIYGRKFTDENFK 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490253314  76 LKNTR-GTLAMARTqAPHSATAQFFINVVDNDFLNfsGEslqgwgYCVFAEVVEGMDVVDKIKAVAT 141
Cdd:PTZ00060 108 LKHDQpGLLSMANA-GPNTNGSQFFITTVPCPWLD--GK------HVVFGKVIEGMEVVRAMEKEGT 165
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 6-136 3.98e-16

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: 71.22  E-value: 3.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   6 TNHGDIVIKTFDDKAPETVKNFLDYCREGFYDNTIFHRVINGFMIQ-------GGGFEPGMKQKATKSP--IQNEANNGL 76
Cdd:cd01921    4 TTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQtgdptgtGAGGESIYSQLYGRQArfFEPEILPLL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490253314  77 K-NTRGTLAMArTQAPHSATAQFFINVVDNdflnfsGESLQGwGYCVFAEVVEGMDVVDKI 136
Cdd:cd01921   84 KhSKKGTVSMV-NAGDNLNGSQFYITLGEN------LDYLDG-KHTVFGQVVEGFDVLEKI 136
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 9-142 4.63e-15

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 69.09  E-value: 4.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   9 GDIVIKTFDDKAPETVKNFLDYC-----REGF---YDNTIFHRVINGFMIQGGGFEPGMKQKATK---SPIQNEANNGLK 77
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCtgefrKAGLpqgYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSiygSKFEDENFIAKH 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490253314  78 NTRGTLAMARTqAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVV-EGMDVVDKIKAVATG 142
Cdd:PLN03149 113 TGPGLLSMANS-GPNTNGCQFFITCAKCDWLDNK--------HVVFGRVLgDGLLVVRKIENVATG 169
PTZ00221 PTZ00221
cyclophilin; Provisional
 9-139 1.13e-04

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 41.01  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314   9 GDIVIKTFDDKAPETVKNF-----------------LDYCregfydNTIFHRV--INGFMIQGGGFEPGMkqKATKSPIQ 69
Cdd:PTZ00221  67 GRLVFELFEDVVPETVENFralitgscgidtntgvkLDYL------YTPVHHVdrNNNIIVLGELDSFNV--SSTGTPIA 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490253314  70 NEANNGLKNTRGTLAMArTQAPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKAV 139
Cdd:PTZ00221 139 DEGYRHRHTERGLLTMI-SEGPHTSGSVFGITLGPSPSLDFK--------QVVFGKAVDDLSLLEKLESL 199
 
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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