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Conserved domains on  [gi|2258869608|gb|USN92723|]
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MAG: peptidylprolyl isomerase [Candidatus Nomurabacteria bacterium]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10002023)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

CATH:  2.40.100.10
EC:  5.2.1.8
Gene Ontology:  GO:0000413|GO:0003755
PubMed:  14731520|15998457
SCOP:  4000390

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 39-209 3.28e-79

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


:

Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 233.52  E-value: 3.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  39 NNDMNPIAVLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNTKtdnvltyGTGGPGYVI 118
Cdd:COG0652     2 KAAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGT-------GTGGPGYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 119 QDEHVKGklLTNERGTISMANS-GPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNANNLP 197
Cdd:COG0652    75 PDEFDPG--LKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLD-------GGYTVFGKVVEGMDVVDKIAAGPTDPGDGP 145

                         170
                  ....*....|..
gi 2258869608 198 LEDVVIESATIK 209
Cdd:COG0652   146 LEPVVIESVTIV 157
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 39-209 3.28e-79

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 233.52  E-value: 3.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  39 NNDMNPIAVLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNTKtdnvltyGTGGPGYVI 118
Cdd:COG0652     2 KAAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGT-------GTGGPGYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 119 QDEHVKGklLTNERGTISMANS-GPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNANNLP 197
Cdd:COG0652    75 PDEFDPG--LKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLD-------GGYTVFGKVVEGMDVVDKIAAGPTDPGDGP 145

                         170
                  ....*....|..
gi 2258869608 198 LEDVVIESATIK 209
Cdd:COG0652   146 LEPVVIESVTIV 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 47-205 3.06e-60

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: 185.16  E-value: 3.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  47 VLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPnTKTDNvltyGTGGPGYVIQDEHVKGK 126
Cdd:cd00317     1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDP-TGTGG----GGSGPGYKFPDENFPLK 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258869608 127 lLTNERGTISMANSGPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNANNLPLEDVVIES 205
Cdd:cd00317    76 -YHHRRGTLSMANAGPNTNGSQFFITTAPTPHLD-------GKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 51-208 2.19e-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: 180.53  E-value: 2.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  51 NLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNTKTdnvltyGTGGPGYVIQDEHvKGKLLTN 130
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTG------GGGKSIFPIPDEI-FPLLLKH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 131 ERGTISMANSG--PNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNaNNLPLEDVVIESATI 208
Cdd:pfam00160  78 KRGALSMANTGpaPNSNGSQFFITLGPAPHLD-------GKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
PRK10903 PRK10903
peptidylprolyl isomerase A;
43-208 2.75e-36

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 125.73  E-value: 2.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  43 NPIAVLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDpntKTDNVLTYGTGGPgyvIQDEH 122
Cdd:PRK10903   28 DPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGG---FTEQMQQKKPNPP---IKNEA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 123 VKGklLTNERGTISMA-NSGPNSGGSQFFINLVDNTNLDFDKQPLSskHPVFGRVISGMDVVDTIGQVETNA----NNLP 197
Cdd:PRK10903  102 DNG--LRNTRGTIAMArTADKDSATSQFFINVADNAFLDHGQRDFG--YAVFGKVVKGMDVADKISQVPTHDvgpyQNVP 177

                         170
                  ....*....|.
gi 2258869608 198 LEDVVIESATI 208
Cdd:PRK10903  178 SKPVVILSAKV 188
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 39-209 3.28e-79

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 233.52  E-value: 3.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  39 NNDMNPIAVLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNTKtdnvltyGTGGPGYVI 118
Cdd:COG0652     2 KAAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGT-------GTGGPGYTI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 119 QDEHVKGklLTNERGTISMANS-GPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNANNLP 197
Cdd:COG0652    75 PDEFDPG--LKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLD-------GGYTVFGKVVEGMDVVDKIAAGPTDPGDGP 145

                         170
                  ....*....|..
gi 2258869608 198 LEDVVIESATIK 209
Cdd:COG0652   146 LEPVVIESVTIV 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 47-205 3.06e-60

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: 185.16  E-value: 3.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  47 VLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPnTKTDNvltyGTGGPGYVIQDEHVKGK 126
Cdd:cd00317     1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDP-TGTGG----GGSGPGYKFPDENFPLK 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258869608 127 lLTNERGTISMANSGPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNANNLPLEDVVIES 205
Cdd:cd00317    76 -YHHRRGTLSMANAGPNTNGSQFFITTAPTPHLD-------GKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 51-208 2.19e-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: 180.53  E-value: 2.19e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  51 NLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNTKTdnvltyGTGGPGYVIQDEHvKGKLLTN 130
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTG------GGGKSIFPIPDEI-FPLLLKH 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 131 ERGTISMANSG--PNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNaNNLPLEDVVIESATI 208
Cdd:pfam00160  78 KRGALSMANTGpaPNSNGSQFFITLGPAPHLD-------GKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 48-208 1.31e-46

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: 151.03  E-value: 1.31e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  48 LNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPnTKTdnvltyGTGGP---GYVIQDEhVK 124
Cdd:cd01923     4 LHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDP-TGT------GRGGEsiwGKPFKDE-FK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 125 GKLLTNERGTISMANSGPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNANNLPLEDVVIE 204
Cdd:cd01923    76 PNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLD-------GKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIE 148


                  ....
gi 2258869608 205 SATI 208
Cdd:cd01923   149 DTSV 152
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 47-208 1.39e-45

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: 148.35  E-value: 1.39e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  47 VLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNtktdnvltyGTGGPGYVIQ----DEH 122
Cdd:cd01928     4 TLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPT---------GTGKGGESIWgkkfEDE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 123 VKGKLLTNERGTISMANSGPNSGGSQFFINlvdntnldFDKQP-LSSKHPVFGRVISGMDVVDTIGQVETNANNLPLEDV 201
Cdd:cd01928    75 FRETLKHDSRGVVSMANNGPNTNGSQFFIT--------YAKQPhLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEI 146


                  ....*..
gi 2258869608 202 VIESATI 208
Cdd:cd01928   147 RIKDVTI 153
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 48-206 1.10e-44

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: 146.05  E-value: 1.10e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  48 LNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNTKTDNVltyGTGGPgyvIQDEHVKGkl 127
Cdd:cd01920     2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQK---ETLKP---IKNEAGNG-- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 128 LTNERGTISMANSG-PNSGGSQFFINLVDNTNLDFDKQplSSKHPVFGRVISGMDVVDTIGQVETNAN----NLPLEDVV 202
Cdd:cd01920    74 LSNTRGTIAMARTNaPDSATSQFFINLKDNASLDYQNE--QWGYTVFGEVTEGMDVVDKIAGVETYSFgsyqDVPVQDVI 151


                  ....
gi 2258869608 203 IESA 206
Cdd:cd01920   152 IESA 155
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 47-206 1.68e-42

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: 140.29  E-value: 1.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  47 VLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPntktdnvLTYGTGGP---GYVIQDEHV 123
Cdd:cd01927     1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDP-------TGDGTGGEsiwGKEFEDEFS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 124 KgKLLTNERGTISMANSGPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNANNLPLEDVVI 203
Cdd:cd01927    74 P-SLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLD-------NKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKI 145


                  ...
gi 2258869608 204 ESA 206
Cdd:cd01927   146 INI 148
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 47-203 2.52e-38

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: 129.58  E-value: 2.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  47 VLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNtktdnvltyGTGGPGYVIQDEHVKGK 126
Cdd:cd01922     1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPT---------GTGRGGASIYGKKFEDE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 127 LLTNER----GTISMANSGPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNaNNLPLEDVV 202
Cdd:cd01922    72 IHPELKhtgaGILSMANAGPNTNGSQFFITLAPTPWLD-------GKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVK 143


                  .
gi 2258869608 203 I 203
Cdd:cd01922   144 I 144
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 45-203 9.94e-37

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: 125.83  E-value: 9.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  45 IAVLNTNLGVIEIELYQDDMPITAGNFVKL--------VKEGYYDGIKFHRVIDGFMIQGGDpNTKTDnvltyGTGGP-- 114
Cdd:cd01926     7 ITIGGEPAGRIVMELFADVVPKTAENFRALctgekgkgGKPFGYKGSTFHRVIPDFMIQGGD-FTRGN-----GTGGKsi 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 115 -GYVIQDEHVKGKllTNERGTISMANSGPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETNa 193
Cdd:cd01926    81 yGEKFPDENFKLK--HTGPGLLSMANAGPNTNGSQFFITTVKTPWLD-------GKHVVFGKVVEGMDVVKKIENVGSG- 150

                         170
                  ....*....|
gi 2258869608 194 NNLPLEDVVI 203
Cdd:cd01926   151 NGKPKKKVVI 160
PRK10903 PRK10903
peptidylprolyl isomerase A;
43-208 2.75e-36

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 125.73  E-value: 2.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  43 NPIAVLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDpntKTDNVLTYGTGGPgyvIQDEH 122
Cdd:PRK10903   28 DPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGG---FTEQMQQKKPNPP---IKNEA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 123 VKGklLTNERGTISMA-NSGPNSGGSQFFINLVDNTNLDFDKQPLSskHPVFGRVISGMDVVDTIGQVETNA----NNLP 197
Cdd:PRK10903  102 DNG--LRNTRGTIAMArTADKDSATSQFFINVADNAFLDHGQRDFG--YAVFGKVVKGMDVADKISQVPTHDvgpyQNVP 177

                         170
                  ....*....|.
gi 2258869608 198 LEDVVIESATI 208
Cdd:PRK10903  178 SKPVVILSAKV 188
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 46-208 1.45e-32

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: 115.53  E-value: 1.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  46 AVLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPnTKTdnvltyGTGGP---GYVIQDEh 122
Cdd:cd01925     8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDP-TGT------GTGGEsiyGEPFKDE- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 123 VKGKLLTNERGTISMANSGPNSGGSQFFINLvdntnldfDKQP-LSSKHPVFGRVISgmdvvDTI------GQVETNANN 195
Cdd:cd01925    80 FHSRLRFNRRGLVGMANAGDDSNGSQFFFTL--------DKADeLNNKHTLFGKVTG-----DTIynllklAEVETDKDE 146

                         170
                  ....*....|...
gi 2258869608 196 LPLEDVVIESATI 208
Cdd:cd01925   147 RPVYPPKITSVEV 159
PRK10791 PRK10791
peptidylprolyl isomerase B;
48-208 4.84e-30

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 108.77  E-value: 4.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  48 LNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNTKTDNVLTYGTggpgyvIQDEHVKGkl 127
Cdd:PRK10791    4 FHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEP------IKNEANNG-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 128 LTNERGTISMANSG-PNSGGSQFFINLVDNTNLDF-DKQPLSSKHPVFGRVISGMDVVDTIGQVETNAN----NLPLEDV 201
Cdd:PRK10791   76 LKNTRGTLAMARTQaPHSATAQFFINVVDNDFLNFsGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSgmhqDVPKEDV 155


                  ....*..
gi 2258869608 202 VIESATI 208
Cdd:PRK10791  156 IIESVTV 162
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 47-208 5.23e-30

cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a C-terminal RNA recognition motif domain (RRM). This subfamily of the cyclophilin domain family contains a number of eukaryotic cyclophilins having the RRM domain including the nuclear proteins: human hCyP-57, Arabidopsis thaliana AtCYP59, Caenorhabditis elegans CeCyP-44 and Paramecium tetrurelia Kin241. The Kin241 protein has been shown to have a role in cell morphogenesis.


Pssm-ID: 238902 [Multi-domain]  Cd Length: 166  Bit Score: 108.58  E-value: 5.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  47 VLNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPN--TKTDNVL---TYGTGGPGYviQDE 121
Cdd:cd01921     1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTgtGAGGESIysqLYGRQARFF--EPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 122 HVKgKLLTNERGTISMANSGPNSGGSQFFINLVDNTNldfdkqPLSSKHPVFGRVISGMDVVDTIGQVETNANNLPLEDV 201
Cdd:cd01921    79 ILP-LLKHSKKGTVSMVNAGDNLNGSQFYITLGENLD------YLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDI 151


                  ....*..
gi 2258869608 202 VIESATI 208
Cdd:cd01921   152 RIKHTHI 158
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 48-186 3.55e-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: 106.76  E-value: 3.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  48 LNTNLGVIEIELYQDDMPITAGNFVKLVKEGYYDGIKFHRVIDGFMIQGGDPNTKTDN---------------VLTYGTG 112
Cdd:cd01924     2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleIKPEGQK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 113 GPGYVIQDEHVKG-----KLLTNERGTISMANS--GPNSGGSQFFINLVDNTNLDFDKQPLSSKHPVFGRVISGMDVVDT 185
Cdd:cd01924    82 QPVYGKTLEEAGRydeqpVLPFNAFGAIAMARTefDPNSASSQFFFLLKDNELTPSRNNVLDGRYAVFGYVTDGLDILRE 161


                  .
gi 2258869608 186 I 186
Cdd:cd01924   162 L 162
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 40-203 7.59e-28

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 103.76  E-value: 7.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  40 NDMNPIAVLNTNLGV-----IEIELYQDDMPITAGNFVKLV-----KEGY---YDGIKFHRVIDGFMIQGGD--PNTKTD 104
Cdd:PLN03149   15 NPKNPVVFFDVTIGGipagrIKMELFADIAPKTAENFRQFCtgefrKAGLpqgYKGCQFHRVIKDFMIQGGDflKGDGTG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 105 NVLTYGTGgpgyvIQDEHVKGKllTNERGTISMANSGPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVI-SGMDVV 183
Cdd:PLN03149   95 CVSIYGSK-----FEDENFIAK--HTGPGLLSMANSGPNTNGCQFFITCAKCDWLD-------NKHVVFGRVLgDGLLVV 160

                         170       180
                  ....*....|....*....|
gi 2258869608 184 DTIGQVETNANNLPLEDVVI 203
Cdd:PLN03149  161 RKIENVATGPNNRPKLACVI 180
PTZ00060 PTZ00060
cyclophilin; Provisional
 45-204 3.82e-27

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 101.84  E-value: 3.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  45 IAVLNTNLGVIEIELYQDDMPITAGNFVKLV---------KEGYYDGIKFHRVIDGFMIQGGDPNTKTdnvltyGTGGP- 114
Cdd:PTZ00060   22 ISIDNAPAGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHN------GTGGEs 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 115 --GYVIQDEHVKGKllTNERGTISMANSGPNSGGSQFFINLVDNTNLDfdkqplsSKHPVFGRVISGMDVVDTIGQVETN 192
Cdd:PTZ00060   96 iyGRKFTDENFKLK--HDQPGLLSMANAGPNTNGSQFFITTVPCPWLD-------GKHVVFGKVIEGMEVVRAMEKEGTQ 166

                         170
                  ....*....|..
gi 2258869608 193 aNNLPLEDVVIE 204
Cdd:PTZ00060  167 -SGYPKKPVVVT 177
PTZ00221 PTZ00221
cyclophilin; Provisional
 53-203 1.09e-08

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 53.33  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608  53 GVIEIELYQDDMPITAGNFVKLV--KEGYYD--GIKF-------HRV--IDGFMIQGgdpntktdNVLTYGTGGPGYVIQ 119
Cdd:PTZ00221   67 GRLVFELFEDVVPETVENFRALItgSCGIDTntGVKLdylytpvHHVdrNNNIIVLG--------ELDSFNVSSTGTPIA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258869608 120 DEHVKGKllTNERGTISMANSGPNSGGSQFFINLVDNTNLDFdkqplssKHPVFGRVISGMDVVDTIGQVETNANNLPLE 199
Cdd:PTZ00221  139 DEGYRHR--HTERGLLTMISEGPHTSGSVFGITLGPSPSLDF-------KQVVFGKAVDDLSLLEKLESLPLDDVGRPLL 209


                  ....
gi 2258869608 200 DVVI 203
Cdd:PTZ00221  210 PVTV 213
 
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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