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Conserved domains on  [gi|779804344|ref|WP_045330487|]
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MULTISPECIES: peptidylprolyl isomerase A [Enterobacter]

Protein Classification

peptidylprolyl isomerase A( domain architecture ID 10793496)

peptidylprolyl isomerase A 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
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-190 9.47e-132

peptidylprolyl isomerase A;


:

Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 366.86  E-value: 9.47e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344   1 MLKSTLAAVAAVFALSAVSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQ 80
Cdd:PRK10903   1 MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  81 GGGFNEQMQQKQPNPPIKNEADNGLLNKRGTISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVAD 160
Cdd:PRK10903  81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 779804344 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
Cdd:PRK10903 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
 
Name Accession Description Interval E-value
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-190 9.47e-132

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 366.86  E-value: 9.47e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344   1 MLKSTLAAVAAVFALSAVSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQ 80
Cdd:PRK10903   1 MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  81 GGGFNEQMQQKQPNPPIKNEADNGLLNKRGTISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVAD 160
Cdd:PRK10903  81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 779804344 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
Cdd:PRK10903 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 32-186 8.26e-83

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: 241.96  E-value: 8.26e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGFNEQMQQKQPNPPIKNEADNGLLNKRGT 111
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779804344 112 ISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSA 186
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 25-189 6.70e-77

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 226.98  E-value: 6.70e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  25 AKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGFNEQMQQKqPNPPIKNEADNG 104
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGG-PGYTIPDEFDPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344 105 LLNKRGTISMARTADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVPTHDvgpyQNVPSKPVVIL 184
Cdd:COG0652   82 LKHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLDG-----GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIE 152


                 ....*
gi 779804344 185 SAKVL 189
Cdd:COG0652  153 SVTIV 157
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 34-188 3.68e-61

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: 186.69  E-value: 3.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344   34 TTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGFNEQMQQKQPNPPIKNEADNGLL-NKRGTI 112
Cdd:pfam00160   3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEIFPLLLkHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779804344  113 SMART-ADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVPTHDvgpyqNVPSKPVVILSAKV 188
Cdd:pfam00160  83 SMANTgPAPNSNGSQFFITLGPAPHLDG-----KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSCGV 149
 
Name Accession Description Interval E-value
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-190 9.47e-132

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 366.86  E-value: 9.47e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344   1 MLKSTLAAVAAVFALSAVSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQ 80
Cdd:PRK10903   1 MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  81 GGGFNEQMQQKQPNPPIKNEADNGLLNKRGTISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVAD 160
Cdd:PRK10903  81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 779804344 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
Cdd:PRK10903 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 32-186 8.26e-83

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: 241.96  E-value: 8.26e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGFNEQMQQKQPNPPIKNEADNGLLNKRGT 111
Cdd:cd01920    1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779804344 112 ISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSA 186
Cdd:cd01920   81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 25-189 6.70e-77

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 226.98  E-value: 6.70e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  25 AKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGFNEQMQQKqPNPPIKNEADNG 104
Cdd:COG0652    3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGG-PGYTIPDEFDPG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344 105 LLNKRGTISMARTADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVPTHDvgpyQNVPSKPVVIL 184
Cdd:COG0652   82 LKHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLDG-----GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIE 152


                 ....*
gi 779804344 185 SAKVL 189
Cdd:COG0652  153 SVTIV 157
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 34-188 3.68e-61

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: 186.69  E-value: 3.68e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344   34 TTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGFNEQMQQKQPNPPIKNEADNGLL-NKRGTI 112
Cdd:pfam00160   3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEIFPLLLkHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779804344  113 SMART-ADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVPTHDvgpyqNVPSKPVVILSAKV 188
Cdd:pfam00160  83 SMANTgPAPNSNGSQFFITLGPAPHLDG-----KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSCGV 149
PRK10791 PRK10791
peptidylprolyl isomerase B;
31-188 3.13e-56

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 175.03  E-value: 3.13e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  31 VLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGFNEQMQQKQPNPPIKNEADNGLLNKRG 110
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTRG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344 111 TISMARTADKDSATSQFFLNVADNAFLD-HGQR--DFGYAVFGKIVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAK 187
Cdd:PRK10791  82 TLAMARTQAPHSATAQFFINVVDNDFLNfSGESlqGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESVT 161


                 .
gi 779804344 188 V 188
Cdd:PRK10791 162 V 162
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 33-185 9.23e-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: 157.81  E-value: 9.23e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  33 LTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGF-NEQMQQKQPNPPIKNE-ADNGLLNKRG 110
Cdd:cd00317    2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPtGTGGGGSGPGYKFPDEnFPLKYHHRRG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 779804344 111 TISMARtADKDSATSQFFLNVADNAFLDhGQrdfgYAVFGKIVKGMDVADKISQVPThdvgPYQNVPSKPVVILS 185
Cdd:cd00317   82 TLSMAN-AGPNTNGSQFFITTAPTPHLD-GK----HTVFGKVVEGMDVVDKIERGDT----DENGRPIKPVTISD 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 30-189 4.16e-26

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: 97.87  E-value: 4.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  30 HVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGG-------GfNEQMQQKqpnpPIKNEAD 102
Cdd:cd01923    1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGdptgtgrG-GESIWGK----PFKDEFK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344 103 NGLLNK-RGTISMARTAdKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVPTHDvgpyQNVPSKPV 181
Cdd:cd01923   76 PNLSHDgRGVLSMANSG-PNTNGSQFFITYRSCKHLDG-----KHTVFGRVVGGLETLEAMENVPDPG----TDRPKEEI 145


                 ....*...
gi 779804344 182 VILSAKVL 189
Cdd:cd01923  146 KIEDTSVF 153
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 32-176 3.55e-24

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: 92.52  E-value: 3.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGFNEQMQQKQP--NPPIKNEADNGLLNKR 109
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESiwGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 779804344 110 -GTISMArTADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVPT-HDVGPYQNV 176
Cdd:cd01927   81 pYTLSMA-NAGPNTNGSQFFITTVATPWLDN-----KHTVFGRVVKGMDVVQRIENVKTdKNDRPYEDI 143
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 33-188 7.30e-24

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: 92.51  E-value: 7.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  33 LTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGGfNEQMQQKQPNP----------------- 95
Cdd:cd01924    2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGD-PQGKNPGFPDPetgksrtipleikpegq 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  96 --PIKNEADNG----------LLNKRGTISMARTA-DKDSATSQFFLNVADNAFLDHG--QRDFGYAVFGKIVKGMDVAD 160
Cdd:cd01924   81 kqPVYGKTLEEagrydeqpvlPFNAFGAIAMARTEfDPNSASSQFFFLLKDNELTPSRnnVLDGRYAVFGYVTDGLDILR 160

                        170       180
                 ....*....|....*....|....*...
gi 779804344 161 KIsqvpthDVGPyqnvpskpvVILSAKV 188
Cdd:cd01924  161 EL------KVGD---------KIESARV 173
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 31-189 3.80e-23

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: 90.49  E-value: 3.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  31 VLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGG-------GfNEQMQQKqpnpPIKNEADN 103
Cdd:cd01925    8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGdptgtgtG-GESIYGE----PFKDEFHS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344 104 GL-LNKRGTISMArTADKDSATSQFFLNVADNAFLDHGQRDFGyAVFGKIVKGMdvaDKISQVPTHDVGPyqnvPSKPVV 182
Cdd:cd01925   83 RLrFNRRGLVGMA-NAGDDSNGSQFFFTLDKADELNNKHTLFG-KVTGDTIYNL---LKLAEVETDKDER----PVYPPK 153


                 ....*..
gi 779804344 183 ILSAKVL 189
Cdd:cd01925  154 ITSVEVL 160
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 35-183 1.93e-22

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: 88.47  E-value: 1.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  35 TSAGNIELELNSQKAPVSVKNF---------LDYVNSGfYNGTTFHRVIPGFMVQGGGF-----------------NEQM 88
Cdd:cd01926   12 EPAGRIVMELFADVVPKTAENFralctgekgKGGKPFG-YKGSTFHRVIPDFMIQGGDFtrgngtggksiygekfpDENF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  89 QQKQPNPpikneadngllnkrGTISMArTADKDSATSQFFLNVADNAFLDhGQrdfgYAVFGKIVKGMDVADKISQVPTH 168
Cdd:cd01926   91 KLKHTGP--------------GLLSMA-NAGPNTNGSQFFITTVKTPWLD-GK----HVVFGKVVEGMDVVKKIENVGSG 150

                        170
                 ....*....|....*
gi 779804344 169 dvgpyQNVPSKPVVI 183
Cdd:cd01926  151 -----NGKPKKKVVI 160
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 31-167 1.05e-21

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: 86.34  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  31 VLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGG-----GFNEQMQQkqpNPPIKNEADNGL 105
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGdptgtGKGGESIW---GKKFEDEFRETL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 779804344 106 -LNKRGTISMArTADKDSATSQFFLNVADNAFLdhgqrDFGYAVFGKIVKGMDVADKISQVPT 167
Cdd:cd01928   80 kHDSRGVVSMA-NNGPNTNGSQFFITYAKQPHL-----DGKYTVFGKVIDGFETLDTLEKLPV 136
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 32-184 2.38e-20

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: 83.16  E-value: 2.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQ------GGGFNEQM--QQKQPNPPIKNEADN 103
Cdd:cd01921    1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQtgdptgTGAGGESIysQLYGRQARFFEPEIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344 104 GLL--NKRGTISMArTADKDSATSQFFLNVADNafLDhgQRDFGYAVFGKIVKGMDVADKISQVPTHDVG-PYQNVPSKP 180
Cdd:cd01921   81 PLLkhSKKGTVSMV-NAGDNLNGSQFYITLGEN--LD--YLDGKHTVFGQVVEGFDVLEKINDAIVDDDGrPLKDIRIKH 155


                 ....
gi 779804344 181 VVIL 184
Cdd:cd01921  156 THIL 159
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 32-176 1.73e-19

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: 80.27  E-value: 1.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNGTTFHRVIPGFMVQGGG-----------FNEQMQQkQPNPPIKNE 100
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDptgtgrggasiYGKKFED-EIHPELKHT 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 779804344 101 AdngllnkRGTISMArTADKDSATSQFFLNVADNAFLDhGQrdfgYAVFGKIVKGMDVADKISQVPTHDVGPYQNV 176
Cdd:cd01922   80 G-------AGILSMA-NAGPNTNGSQFFITLAPTPWLD-GK----HTIFGRVSKGMKVIENMVEVQTQTDRPIDEV 142
PTZ00060 PTZ00060
cyclophilin; Provisional
 36-183 2.73e-13

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 64.87  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  36 SAGNIELELNSQKAPVSVKNFL-----DYVNSG----FYNGTTFHRVIPGFMVQGGGF-NEQMQQKQPNPPIKNEADNGL 105
Cdd:PTZ00060  28 PAGRIVFELFSDVTPKTAENFRalcigDKVGSSgknlHYKGSIFHRIIPQFMCQGGDItNHNGTGGESIYGRKFTDENFK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344 106 LN--KRGTISMArTADKDSATSQFFLNVADNAFLDhGQrdfgYAVFGKIVKGMDVADKISQvpthdVGPYQNVPSKPVVI 183
Cdd:PTZ00060 108 LKhdQPGLLSMA-NAGPNTNGSQFFITTVPCPWLD-GK----HVVFGKVIEGMEVVRAMEK-----EGTQSGYPKKPVVV 176
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 34-183 2.68e-12

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 62.16  E-value: 2.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344  34 TTSAGNIELELNSQKAPVSVKNFL-----DYVNSGF---YNGTTFHRVIPGFMVQGGGFneqmqqkqpnppIKNE----- 100
Cdd:PLN03149  29 GIPAGRIKMELFADIAPKTAENFRqfctgEFRKAGLpqgYKGCQFHRVIKDFMIQGGDF------------LKGDgtgcv 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779804344 101 -------ADNGLLNKR---GTISMARTAdKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIV-KGMDVADKISQVPThd 169
Cdd:PLN03149  97 siygskfEDENFIAKHtgpGLLSMANSG-PNTNGCQFFITCAKCDWLDN-----KHVVFGRVLgDGLLVVRKIENVAT-- 168

                        170
                 ....*....|....
gi 779804344 170 vGPyQNVPSKPVVI 183
Cdd:PLN03149 169 -GP-NNRPKLACVI 180
 
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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