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Conserved domains on  [gi|306869131|gb|EFN00933|]
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Peptidyl-prolyl cis-trans isomerase B [Actinobacillus pleuropneumoniae serovar 12 str. 1096]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112428)

peptidylprolyl isomerase 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_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 3-166 3.98e-87

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: 251.98  E-value: 3.98e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   3 TLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKAPIQNEANNRLSNKRGT 82
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  83 LAMARTSDPHSASSQFFINVADNTFLDYRSKemfgrevvqEWGYAVFGEVVEGMDVVDKIKGVKTGNKGFHQDVPVEDVV 162
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNE---------QWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVI 151


                 ....
gi 306869131 163 IESV 166
Cdd:cd01920  152 IESA 155
 
Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 3-166 3.98e-87

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: 251.98  E-value: 3.98e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   3 TLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKAPIQNEANNRLSNKRGT 82
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  83 LAMARTSDPHSASSQFFINVADNTFLDYRSKemfgrevvqEWGYAVFGEVVEGMDVVDKIKGVKTGNKGFHQDVPVEDVV 162
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNE---------QWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVI 151


                 ....
gi 306869131 163 IESV 166
Cdd:cd01920  152 IESA 155
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-169 6.37e-85

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 246.67  E-value: 6.37e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   1 MITLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKAPIQNEANNRLSNKR 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  81 GTLAMARTSDPHSASSQFFINVADNTFLDYRSkemfgrEVVQEWGYAVFGEVVEGMDVVDKIKGVKTGNKGFHQDVPVED 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSG------ESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKED 154


                 ....*....
gi 306869131 161 VVIESVTVA 169
Cdd:PRK10791 155 VIIESVTVS 163
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-169 1.93e-81

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 237.76  E-value: 1.93e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   1 MITLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKaPIQNEANNRLSNKR 80
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGLKHKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  81 GTLAMARTSDPHSASSQFFINVADNTFLDYrskemfgrevvqewGYAVFGEVVEGMDVVDKIKGVKTGNkgfhQDVPVED 160
Cdd:COG0652   87 GTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------------GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEP 148


                 ....*....
gi 306869131 161 VVIESVTVA 169
Cdd:COG0652  149 VVIESVTIV 157
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-168 4.98e-60

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: 183.23  E-value: 4.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131    4 LHTN-FGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKAPIQNE-ANNRLSNKRG 81
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEiFPLLLKHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   82 TLAMART-SDPHSASSQFFINVADNTFLDYRskemfgrevvqewgYAVFGEVVEGMDVVDKIKGVKTGNkgfhqDVPVED 160
Cdd:pfam00160  81 ALSMANTgPAPNSNGSQFFITLGPAPHLDGK--------------YTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKP 141


                  ....*...
gi 306869131  161 VVIESVTV 168
Cdd:pfam00160 142 VKILSCGV 149
 
Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 3-166 3.98e-87

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: 251.98  E-value: 3.98e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   3 TLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKAPIQNEANNRLSNKRGT 82
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  83 LAMARTSDPHSASSQFFINVADNTFLDYRSKemfgrevvqEWGYAVFGEVVEGMDVVDKIKGVKTGNKGFHQDVPVEDVV 162
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNE---------QWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVI 151


                 ....
gi 306869131 163 IESV 166
Cdd:cd01920  152 IESA 155
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-169 6.37e-85

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 246.67  E-value: 6.37e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   1 MITLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKAPIQNEANNRLSNKR 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  81 GTLAMARTSDPHSASSQFFINVADNTFLDYRSkemfgrEVVQEWGYAVFGEVVEGMDVVDKIKGVKTGNKGFHQDVPVED 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSG------ESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKED 154


                 ....*....
gi 306869131 161 VVIESVTVA 169
Cdd:PRK10791 155 VIIESVTVS 163
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-169 1.93e-81

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 237.76  E-value: 1.93e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   1 MITLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKaPIQNEANNRLSNKR 80
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGLKHKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  81 GTLAMARTSDPHSASSQFFINVADNTFLDYrskemfgrevvqewGYAVFGEVVEGMDVVDKIKGVKTGNkgfhQDVPVED 160
Cdd:COG0652   87 GTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------------GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEP 148


                 ....*....
gi 306869131 161 VVIESVTVA 169
Cdd:COG0652  149 VVIESVTIV 157
PRK10903 PRK10903
peptidylprolyl isomerase A;
2-168 5.20e-75

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 222.80  E-value: 5.20e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   2 ITLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKAPIQNEANNRLSNKRG 81
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  82 TLAMARTSDPHSASSQFFINVADNTFLDYRSKemfgrevvqEWGYAVFGEVVEGMDVVDKIKGVKTGNKGFHQDVPVEDV 161
Cdd:PRK10903 111 TIAMARTADKDSATSQFFINVADNAFLDHGQR---------DFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPV 181


                 ....*..
gi 306869131 162 VIESVTV 168
Cdd:PRK10903 182 VILSAKV 188
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-168 4.98e-60

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: 183.23  E-value: 4.98e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131    4 LHTN-FGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLIEKATKAPIQNE-ANNRLSNKRG 81
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEiFPLLLKHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   82 TLAMART-SDPHSASSQFFINVADNTFLDYRskemfgrevvqewgYAVFGEVVEGMDVVDKIKGVKTGNkgfhqDVPVED 160
Cdd:pfam00160  81 ALSMANTgPAPNSNGSQFFITLGPAPHLDGK--------------YTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKP 141


                  ....*...
gi 306869131  161 VVIESVTV 168
Cdd:pfam00160 142 VKILSCGV 149
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 3-165 1.58e-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: 161.28  E-value: 1.58e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   3 TLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMT-SGLIEKATKAPIQNEANNRLS-NKR 80
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTgTGGGGSGPGYKFPDENFPLKYhHRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  81 GTLAMARtSDPHSASSQFFINVADNTFLDyrskemfGRevvqewgYAVFGEVVEGMDVVDKIKGVKTGNkgfhQDVPVED 160
Cdd:cd00317   81 GTLSMAN-AGPNTNGSQFFITTAPTPHLD-------GK-------HTVFGKVVEGMDVVDKIERGDTDE----NGRPIKP 141


                 ....*
gi 306869131 161 VVIES 165
Cdd:cd00317  142 VTISD 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 4-168 1.12e-35

cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.


Pssm-ID: 238904 [Multi-domain]  Cd Length: 159  Bit Score: 121.75  E-value: 1.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   4 LHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGG---GMTSGLiEKATKAPIQNEANNRLSNK- 79
Cdd:cd01923    4 LHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGdptGTGRGG-ESIWGKPFKDEFKPNLSHDg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  80 RGTLAMArTSDPHSASSQFFINVADNTFLDYRskemfgrevvqewgYAVFGEVVEGMDVVDKIKGVKTGNKgfhqDVPVE 159
Cdd:cd01923   83 RGVLSMA-NSGPNTNGSQFFITYRSCKHLDGK--------------HTVFGRVVGGLETLEAMENVPDPGT----DRPKE 143


                 ....*....
gi 306869131 160 DVVIESVTV 168
Cdd:cd01923  144 EIKIEDTSV 152
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 3-166 1.29e-35

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: 121.03  E-value: 1.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   3 TLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMTSGLI--EKATKAPIQNEANNRLSNKR 80
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTggESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  81 -GTLAMArTSDPHSASSQFFINVADNTFLDYRskemfgrevvqewgYAVFGEVVEGMDVVDKIKGVKTGnkgfHQDVPVE 159
Cdd:cd01927   81 pYTLSMA-NAGPNTNGSQFFITTVATPWLDNK--------------HTVFGRVVKGMDVVQRIENVKTD----KNDRPYE 141


                 ....*..
gi 306869131 160 DVVIESV 166
Cdd:cd01927  142 DIKIINI 148
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 2-168 2.67e-32

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: 112.91  E-value: 2.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   2 ITLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMT-SGlieKATKAPIQNEANNRLS--- 77
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTgTG---KGGESIWGKKFEDEFRetl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  78 --NKRGTLAMArTSDPHSASSQFFINVADNTFLDYRskemfgrevvqewgYAVFGEVVEGMDVVDKIKGVKTGNKgfhqD 155
Cdd:cd01928   80 khDSRGVVSMA-NNGPNTNGSQFFITYAKQPHLDGK--------------YTVFGKVIDGFETLDTLEKLPVDKK----Y 140

                        170
                 ....*....|...
gi 306869131 156 VPVEDVVIESVTV 168
Cdd:cd01928  141 RPLEEIRIKDVTI 153
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 2-157 1.60e-29

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: 106.28  E-value: 1.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   2 ITLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMT-SGL-IEKATKAPIQNEANNRLS-N 78
Cdd:cd01925    8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTgTGTgGESIYGEPFKDEFHSRLRfN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  79 KRGTLAMARTSDpHSASSQFFINVADNTFLDyRSKEMFGReVVQEWGYAVF----GEVVEGMDVVD--KIKGVKTGNKGF 152
Cdd:cd01925   88 RRGLVGMANAGD-DSNGSQFFFTLDKADELN-NKHTLFGK-VTGDTIYNLLklaeVETDKDERPVYppKITSVEVLENPF 164


                 ....*
gi 306869131 153 HQDVP 157
Cdd:cd01925  165 DDIVP 169
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 6-168 3.17e-29

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: 105.60  E-value: 3.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   6 TNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGG---GMTSGLIEKAT---------------KAP 67
Cdd:cd01924    4 TDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGdpqGKNPGFPDPETgksrtipleikpegqKQP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  68 IQNEANNR----------LSNKRGTLAMARTS-DPHSASSQFFINVADNTFLDYRSKEMFGRevvqewgYAVFGEVVEGM 136
Cdd:cd01924   84 VYGKTLEEagrydeqpvlPFNAFGAIAMARTEfDPNSASSQFFFLLKDNELTPSRNNVLDGR-------YAVFGYVTDGL 156

                        170       180       190
                 ....*....|....*....|....*....|..
gi 306869131 137 DVVDKIkgvKTGNKgfhqdvpvedvvIESVTV 168
Cdd:cd01924  157 DILREL---KVGDK------------IESARV 173
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 3-163 1.14e-26

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: 98.38  E-value: 1.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   3 TLHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQGGGMT-SGLIEKATKAP-IQNEANNRLSNK- 79
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTgTGRGGASIYGKkFEDEIHPELKHTg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  80 RGTLAMArTSDPHSASSQFFINVADNTFLDYRskemfgrevvqewgYAVFGEVVEGMDVVDKIKGVKTGNkgfhqDVPVE 159
Cdd:cd01922   81 AGILSMA-NAGPNTNGSQFFITLAPTPWLDGK--------------HTIFGRVSKGMKVIENMVEVQTQT-----DRPID 140


                 ....
gi 306869131 160 DVVI 163
Cdd:cd01922  141 EVKI 144
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 9-163 3.69e-25

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: 94.63  E-value: 3.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   9 GDIKIELNFEKAPVTAKNFEDYC-------KEGF-YNGTIFHRVIDGFMIQGGGMTSGL---IEKATKAPIQNEANNRLS 77
Cdd:cd01926   15 GRIVMELFADVVPKTAENFRALCtgekgkgGKPFgYKGSTFHRVIPDFMIQGGDFTRGNgtgGKSIYGEKFPDENFKLKH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  78 NKRGTLAMArTSDPHSASSQFFINVADNTFLDyrskemfGREVvqewgyaVFGEVVEGMDVVDKIKGVKTGNkgfhqDVP 157
Cdd:cd01926   95 TGPGLLSMA-NAGPNTNGSQFFITTVKTPWLD-------GKHV-------VFGKVVEGMDVVKKIENVGSGN-----GKP 154


                 ....*.
gi 306869131 158 VEDVVI 163
Cdd:cd01926  155 KKKVVI 160
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 4-163 6.75e-21

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: 83.93  E-value: 6.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   4 LHTNFGDIKIELNFEKAPVTAKNFEDYCKEGFYNGTIFHRVIDGFMIQ--------GGGMTSGLIEKATKAP-IQNEANN 74
Cdd:cd01921    2 LETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQtgdptgtgAGGESIYSQLYGRQARfFEPEILP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  75 RL-SNKRGTLAMArTSDPHSASSQFFINVADNT-FLDYRSkemfgrevvqewgyAVFGEVVEGMDVVDKIKGVKTGNKGf 152
Cdd:cd01921   82 LLkHSKKGTVSMV-NAGDNLNGSQFYITLGENLdYLDGKH--------------TVFGQVVEGFDVLEKINDAIVDDDG- 145

                        170
                 ....*....|.
gi 306869131 153 hqdVPVEDVVI 163
Cdd:cd01921  146 ---RPLKDIRI 153
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 9-148 1.57e-16

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 72.95  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   9 GDIKIELNFEKAPVTAKNFEDYC-----KEGF---YNGTIFHRVIDGFMIQGG----GMTSGLIE-KATKAPIQNEANNR 75
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCtgefrKAGLpqgYKGCQFHRVIKDFMIQGGdflkGDGTGCVSiYGSKFEDENFIAKH 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 306869131  76 LSNkrGTLAMArTSDPHSASSQFFINVADNTFLDYRskemfgrevvqewgYAVFGEVV-EGMDVVDKIKGVKTG 148
Cdd:PLN03149 113 TGP--GLLSMA-NSGPNTNGCQFFITCAKCDWLDNK--------------HVVFGRVLgDGLLVVRKIENVATG 169
PTZ00060 PTZ00060
cyclophilin; Provisional
 9-160 2.82e-16

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 72.18  E-value: 2.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131   9 GDIKIELNFEKAPVTAKNFEDYC---------KEGFYNGTIFHRVIDGFMIQGGGMT--SGLIEKATKAPIQNEANNRLS 77
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDITnhNGTGGESIYGRKFTDENFKLK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869131  78 NKR-GTLAMArTSDPHSASSQFFINVADNTFLDyrskemfGREVvqewgyaVFGEVVEGMDVVDKIKGVKTGNKGFHQDV 156
Cdd:PTZ00060 110 HDQpGLLSMA-NAGPNTNGSQFFITTVPCPWLD-------GKHV-------VFGKVIEGMEVVRAMEKEGTQSGYPKKPV 174


                 ....
gi 306869131 157 PVED 160
Cdd:PTZ00060 175 VVTD 178
 
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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