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Conserved domains on  [gi|489112021|ref|WP_003021875|]
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MULTISPECIES: peptidylprolyl isomerase B [Citrobacter]

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 1.90e-115

peptidylprolyl isomerase B;


:

Pssm-ID: 182734  Cd Length: 164  Bit Score: 323.71  E-value: 1.90e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEAIKNEANNGLKNTR 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  81 GTLAMARTQAPHSATAQFFINVADNDFLNFSGESMQGWGYCVFAEVVEGMDVVDKIKGVSTGRSGMHQDVPKEDVIIENV 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ....
gi 489112021 161 TVSE 164
Cdd:PRK10791 161 TVSE 164
 
Name Accession Description Interval E-value
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-164 1.90e-115

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 323.71  E-value: 1.90e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEAIKNEANNGLKNTR 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  81 GTLAMARTQAPHSATAQFFINVADNDFLNFSGESMQGWGYCVFAEVVEGMDVVDKIKGVSTGRSGMHQDVPKEDVIIENV 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ....
gi 489112021 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 4.77e-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: 276.63  E-value: 4.77e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEAIKNEANNGLKNTRGT 82
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489112021  83 LAMARTQAPHSATAQFFINVADNDFLNFSGESmqgWGYCVFAEVVEGMDVVDKIKGVSTGRSGMHQDVPKEDVIIENV 160
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQ---WGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-164 5.05e-79

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 231.21  E-value: 5.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKeAIKNEANNGLKNTR 80
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGLKHKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  81 GTLAMARTQAPHSATAQFFINVADNDFLNFsgesmqgwGYCVFAEVVEGMDVVDKIKGVSTGRsgmhQDVPKEDVIIENV 160
Cdd:COG0652   87 GTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIESV 154


                 ....
gi 489112021 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 5.30e-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: 177.83  E-value: 5.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021    4 FHTN-HGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEAIKNE-ANNGLKNTRG 81
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEiFPLLLKHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   82 TLAMART-QAPHSATAQFFINVADNDFLNFsgesmqgwGYCVFAEVVEGMDVVDKIKGVSTGRsgmhqDVPKEDVIIENV 160
Cdd:pfam00160  81 ALSMANTgPAPNSNGSQFFITLGPAPHLDG--------KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSC 147


                  ..
gi 489112021  161 TV 162
Cdd:pfam00160 148 GV 149
 
Name Accession Description Interval E-value
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-164 1.90e-115

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 323.71  E-value: 1.90e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEAIKNEANNGLKNTR 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  81 GTLAMARTQAPHSATAQFFINVADNDFLNFSGESMQGWGYCVFAEVVEGMDVVDKIKGVSTGRSGMHQDVPKEDVIIENV 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ....
gi 489112021 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 4.77e-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: 276.63  E-value: 4.77e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEAIKNEANNGLKNTRGT 82
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489112021  83 LAMARTQAPHSATAQFFINVADNDFLNFSGESmqgWGYCVFAEVVEGMDVVDKIKGVSTGRSGMHQDVPKEDVIIENV 160
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQ---WGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-164 5.05e-79

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 231.21  E-value: 5.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKeAIKNEANNGLKNTR 80
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGLKHKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  81 GTLAMARTQAPHSATAQFFINVADNDFLNFsgesmqgwGYCVFAEVVEGMDVVDKIKGVSTGRsgmhQDVPKEDVIIENV 160
Cdd:COG0652   87 GTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIESV 154


                 ....
gi 489112021 161 TVSE 164
Cdd:COG0652  155 TIVE 158
PRK10903 PRK10903
peptidylprolyl isomerase A;
2-162 3.05e-67

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 202.77  E-value: 3.05e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEAIKNEANNGLKNTRG 81
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  82 TLAMARTQAPHSATAQFFINVADNDFLNfsgESMQGWGYCVFAEVVEGMDVVDKIKGVSTGRSGMHQDVPKEDVIIENVT 161
Cdd:PRK10903 111 TIAMARTADKDSATSQFFINVADNAFLD---HGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAK 187


                 .
gi 489112021 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 5.30e-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: 177.83  E-value: 5.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021    4 FHTN-HGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEAIKNE-ANNGLKNTRG 81
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEiFPLLLKHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   82 TLAMART-QAPHSATAQFFINVADNDFLNFsgesmqgwGYCVFAEVVEGMDVVDKIKGVSTGRsgmhqDVPKEDVIIENV 160
Cdd:pfam00160  81 ALSMANTgPAPNSNGSQFFITLGPAPHLDG--------KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSC 147


                  ..
gi 489112021  161 TV 162
Cdd:pfam00160 148 GV 149
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 3-159 4.28e-51

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: 160.12  E-value: 4.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFE-PGMKQKATKEAIKNE-ANNGLKNTR 80
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTgTGGGGSGPGYKFPDEnFPLKYHHRR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489112021  81 GTLAMARTQaPHSATAQFFINVADNDFLNFSgesmqgwgYCVFAEVVEGMDVVDKIKGVSTGRsgmhQDVPKEDVIIEN 159
Cdd:cd00317   81 GTLSMANAG-PNTNGSQFFITTAPTPHLDGK--------HTVFGKVVEGMDVVDKIERGDTDE----NGRPIKPVTISD 146
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 3-160 8.63e-33

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: 113.71  E-value: 8.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGMKQKATKEaIKNEANNGLKNT 79
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGdptGDGTGGESIWGKE-FEDEFSPSLKHD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  80 R-GTLAMARTqAPHSATAQFFINVADNDFLNFSgesmqgwgYCVFAEVVEGMDVVDKIKGVSTGRSgmhqDVPKEDVIIE 158
Cdd:cd01927   80 RpYTLSMANA-GPNTNGSQFFITTVATPWLDNK--------HTVFGRVVKGMDVVQRIENVKTDKN----DRPYEDIKII 146


                 ..
gi 489112021 159 NV 160
Cdd:cd01927  147 NI 148
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 2-164 3.98e-31

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: 109.81  E-value: 3.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGMKQKATKEaIKNEANNGLKN 78
Cdd:cd01923    2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGdptGTGRGGESIWGKP-FKDEFKPNLSH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  79 T-RGTLAMARTqAPHSATAQFFINVADNDFLNFSgesmqgwgYCVFAEVVEGMDVVDKIKGVSTGRSgmhqDVPKEDVII 157
Cdd:cd01923   81 DgRGVLSMANS-GPNTNGSQFFITYRSCKHLDGK--------HTVFGRVVGGLETLEAMENVPDPGT----DRPKEEIKI 147


                 ....*..
gi 489112021 158 ENVTVSE 164
Cdd:cd01923  148 EDTSVFV 154
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 2-162 7.00e-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: 104.06  E-value: 7.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGgfEPGMKQKAtKEAI-----KNEANNGL 76
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTG--DPTGTGKG-GESIwgkkfEDEFRETL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  77 K-NTRGTLAMArTQAPHSATAQFFINVADNDFLNFSgesmqgwgYCVFAEVVEGMDVVDKIKGVSTGRSgmhqDVPKEDV 155
Cdd:cd01928   80 KhDSRGVVSMA-NNGPNTNGSQFFITYAKQPHLDGK--------YTVFGKVIDGFETLDTLEKLPVDKK----YRPLEEI 146


                 ....*..
gi 489112021 156 IIENVTV 162
Cdd:cd01928  147 RIKDVTI 153
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 2-109 1.91e-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: 95.50  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGgfEP---GM-KQKATKEAIKNEANNGLK 77
Cdd:cd01925    8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGG--DPtgtGTgGESIYGEPFKDEFHSRLR 85

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489112021  78 -NTRGTLAMARTQaPHSATAQFFINVADNDFLN 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 7.30e-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: 91.16  E-value: 7.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   9 GDIVIKTFDDKAPETVKNFLDYC-------REGF-YNNTIFHRVINGFMIQGGGFepgMKQKAT-KEAIKNEA----NNG 75
Cdd:cd01926   15 GRIVMELFADVVPKTAENFRALCtgekgkgGKPFgYKGSTFHRVIPDFMIQGGDF---TRGNGTgGKSIYGEKfpdeNFK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  76 LKNTR-GTLAMARTqAPHSATAQFFINVADNDFLNfsGEsmqgwgYCVFAEVVEGMDVVDKIKGVSTGrsgmhQDVPKED 154
Cdd:cd01926   92 LKHTGpGLLSMANA-GPNTNGSQFFITTVKTPWLD--GK------HVVFGKVVEGMDVVKKIENVGSG-----NGKPKKK 157


                 ...
gi 489112021 155 VII 157
Cdd:cd01926  158 VVI 160
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 3-157 1.14e-22

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: 87.59  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGgfEPGMKQKATK----EAIKNEANNGLKN 78
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGG--DPTGTGRGGAsiygKKFEDEIHPELKH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  79 T-RGTLAMARTqAPHSATAQFFINVADNDFLNfsGEsmqgwgYCVFAEVVEGMDVVDKIKGVSTgrsgmHQDVPKEDVII 157
Cdd:cd01922   79 TgAGILSMANA-GPNTNGSQFFITLAPTPWLD--GK------HTIFGRVSKGMKVIENMVEVQT-----QTDRPIDEVKI 144
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 11-137 7.45e-21

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: 83.65  E-value: 7.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  11 IVIKTFDdkAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGMKQKATKEA------IKNEANNG------ 75
Cdd:cd01924   11 IVLDGYN--APVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGdpqGKNPGFPDPETGKSrtipleIKPEGQKQpvygkt 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489112021  76 -------------LKNTRGTLAMARTQ-APHSATAQFFINVADNDFLNFSGESMQGwGYCVFAEVVEGMDVVDKIK 137
Cdd:cd01924   89 leeagrydeqpvlPFNAFGAIAMARTEfDPNSASSQFFFLLKDNELTPSRNNVLDG-RYAVFGYVTDGLDILRELK 163
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 6-136 1.30e-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: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   6 TNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQ---------GGGFEPGMKQKATKEAIKNEANNGL 76
Cdd:cd01921    4 TTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQtgdptgtgaGGESIYSQLYGRQARFFEPEILPLL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489112021  77 KNTR-GTLAMArTQAPHSATAQFFINVADN-DFLNfsGESmqgwgyCVFAEVVEGMDVVDKI 136
Cdd:cd01921   84 KHSKkGTVSMV-NAGDNLNGSQFYITLGENlDYLD--GKH------TVFGQVVEGFDVLEKI 136
PTZ00060 PTZ00060
cyclophilin; Provisional
 7-159 3.31e-16

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 71.80  E-value: 3.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   7 NHGDIVIKTFDDKAPETVKNFLDYC---------REGFYNNTIFHRVINGFMIQGGGF--EPGMKQKATKEAIKNEANNG 75
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDItnHNGTGGESIYGRKFTDENFK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  76 LKNTR-GTLAMARTqAPHSATAQFFINVADNDFLNfsGEsmqgwgYCVFAEVVEGMDVVDKIKGVstgrsGMHQDVPKED 154
Cdd:PTZ00060 108 LKHDQpGLLSMANA-GPNTNGSQFFITTVPCPWLD--GK------HVVFGKVIEGMEVVRAMEKE-----GTQSGYPKKP 173


                 ....*
gi 489112021 155 VIIEN 159
Cdd:PTZ00060 174 VVVTD 178
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 9-142 1.77e-14

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 67.55  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   9 GDIVIKTFDDKAPETVKNFLDYC-----REGF---YNNTIFHRVINGFMIQGGGFEPGMKQKATK---EAIKNEANNGLK 77
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCtgefrKAGLpqgYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSiygSKFEDENFIAKH 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489112021  78 NTRGTLAMARTqAPHSATAQFFINVADNDFLNFSgesmqgwgYCVFAEVV-EGMDVVDKIKGVSTG 142
Cdd:PLN03149 113 TGPGLLSMANS-GPNTNGCQFFITCAKCDWLDNK--------HVVFGRVLgDGLLVVRKIENVATG 169
PTZ00221 PTZ00221
cyclophilin; Provisional
 9-139 1.05e-03

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 38.31  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021   9 GDIVIKTFDDKAPETVKNF-----------------LDYCregfynNTIFHRV--INGFMIQGGGFEPGMkqKATKEAIK 69
Cdd:PTZ00221  67 GRLVFELFEDVVPETVENFralitgscgidtntgvkLDYL------YTPVHHVdrNNNIIVLGELDSFNV--SSTGTPIA 138

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489112021  70 NEANNGLKNTRGTLAMArTQAPHSATAQFFINVADNDFLNFSgesmqgwgYCVFAEVVEGMDVVDKIKGV 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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