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Conserved domains on  [gi|1621407636|gb|THE49257|]
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peptidylprolyl isomerase A [Enterobacter bugandensis]

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 2.02e-131

peptidylprolyl isomerase A;


:

Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 366.09  E-value: 2.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636   1 MLKSTLAAVAAVFALSAVSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQ 80
Cdd:PRK10903    1 MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  81 GGGFNEQMQQKQPNPPIKNEADNGLLNKRGTISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVAD 160
Cdd:PRK10903   81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1621407636 161 KISQVQTHDVGPYQNVPSKPVVIISAKVLP 190
Cdd:PRK10903  161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
 
Name Accession Description Interval E-value
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-190 2.02e-131

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 366.09  E-value: 2.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636   1 MLKSTLAAVAAVFALSAVSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQ 80
Cdd:PRK10903    1 MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  81 GGGFNEQMQQKQPNPPIKNEADNGLLNKRGTISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVAD 160
Cdd:PRK10903   81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1621407636 161 KISQVQTHDVGPYQNVPSKPVVIISAKVLP 190
Cdd:PRK10903  161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 32-186 2.55e-82

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: 240.81  E-value: 2.55e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGFNEQMQQKQPNPPIKNEADNGLLNKRGT 111
Cdd:cd01920     1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1621407636 112 ISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVADKISQVQTHDVGPYQNVPSKPVVIISA 186
Cdd:cd01920    81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 25-189 1.68e-76

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 226.20  E-value: 1.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  25 AKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGFNEQMQQKqPNPPIKNEADNG 104
Cdd:COG0652     3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGG-PGYTIPDEFDPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636 105 LLNKRGTISMARTADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVQTHDvgpyQNVPSKPVVII 184
Cdd:COG0652    82 LKHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLDG-----GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIE 152


                  ....*
gi 1621407636 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 1.96e-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: 185.15  E-value: 1.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  34 TTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGFNEQMQQKQPNPPIKNEADNGLL-NKRGTI 112
Cdd:pfam00160   3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEIFPLLLkHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621407636 113 SMART-ADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVQTHDvgpyqNVPSKPVVIISAKV 188
Cdd:pfam00160  83 SMANTgPAPNSNGSQFFITLGPAPHLDG-----KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSCGV 149
 
Name Accession Description Interval E-value
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-190 2.02e-131

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 366.09  E-value: 2.02e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636   1 MLKSTLAAVAAVFALSAVSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQ 80
Cdd:PRK10903    1 MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  81 GGGFNEQMQQKQPNPPIKNEADNGLLNKRGTISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVAD 160
Cdd:PRK10903   81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 1621407636 161 KISQVQTHDVGPYQNVPSKPVVIISAKVLP 190
Cdd:PRK10903  161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 32-186 2.55e-82

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: 240.81  E-value: 2.55e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGFNEQMQQKQPNPPIKNEADNGLLNKRGT 111
Cdd:cd01920     1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1621407636 112 ISMARTADKDSATSQFFLNVADNAFLDHGQRDFGYAVFGKIVKGMDVADKISQVQTHDVGPYQNVPSKPVVIISA 186
Cdd:cd01920    81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 25-189 1.68e-76

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 226.20  E-value: 1.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  25 AKGDPHVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGFNEQMQQKqPNPPIKNEADNG 104
Cdd:COG0652     3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGG-PGYTIPDEFDPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636 105 LLNKRGTISMARTADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVQTHDvgpyQNVPSKPVVII 184
Cdd:COG0652    82 LKHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLDG-----GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIE 152


                  ....*
gi 1621407636 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 1.96e-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: 185.15  E-value: 1.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  34 TTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGFNEQMQQKQPNPPIKNEADNGLL-NKRGTI 112
Cdd:pfam00160   3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEIFPLLLkHKRGAL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621407636 113 SMART-ADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVQTHDvgpyqNVPSKPVVIISAKV 188
Cdd:pfam00160  83 SMANTgPAPNSNGSQFFITLGPAPHLDG-----KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSCGV 149
PRK10791 PRK10791
peptidylprolyl isomerase B;
31-188 1.98e-57

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 178.11  E-value: 1.98e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  31 VLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGFNEQMQQKQPNPPIKNEADNGLLNKRG 110
Cdd:PRK10791    2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTRG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636 111 TISMARTADKDSATSQFFLNVADNAFLD-HGQR--DFGYAVFGKIVKGMDVADKISQVQTHDVGPYQNVPSKPVVIISAK 187
Cdd:PRK10791   82 TLAMARTQAPHSATAQFFINVVDNDFLNfSGESlqGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESVT 161


                  .
gi 1621407636 188 V 188
Cdd:PRK10791  162 V 162
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 33-185 2.23e-49

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: 156.66  E-value: 2.23e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  33 LTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGF-NEQMQQKQPNPPIKNE-ADNGLLNKRG 110
Cdd:cd00317     2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPtGTGGGGSGPGYKFPDEnFPLKYHHRRG 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1621407636 111 TISMARtADKDSATSQFFLNVADNAFLDhGQrdfgYAVFGKIVKGMDVADKISQVQThdvgPYQNVPSKPVVIIS 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 6.26e-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: 97.49  E-value: 6.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  30 HVLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGG-------GfNEQMQQKqpnpPIKNEAD 102
Cdd:cd01923     1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGdptgtgrG-GESIWGK----PFKDEFK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636 103 NGLLNK-RGTISMARTAdKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVQTHDvgpyQNVPSKPV 181
Cdd:cd01923    76 PNLSHDgRGVLSMANSG-PNTNGSQFFITYRSCKHLDG-----KHTVFGRVVGGLETLEAMENVPDPG----TDRPKEEI 145


                  ....*...
gi 1621407636 182 VIISAKVL 189
Cdd:cd01923   146 KIEDTSVF 153
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 32-186 1.96e-25

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: 95.61  E-value: 1.96e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGFNEQMQQKQP--NPPIKNEADNGLLNKR 109
Cdd:cd01927     1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESiwGKEFEDEFSPSLKHDR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1621407636 110 -GTISMArTADKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIVKGMDVADKISQVQThdvgPYQNVPSKPVVIISA 186
Cdd:cd01927    81 pYTLSMA-NAGPNTNGSQFFITTVATPWLDN-----KHTVFGRVVKGMDVVQRIENVKT----DKNDRPYEDIKIINI 148
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 31-189 1.01e-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: 92.03  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  31 VLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGG-------GfNEQMQQKqpnpPIKNEADN 103
Cdd:cd01925     8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGdptgtgtG-GESIYGE----PFKDEFHS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636 104 GL-LNKRGTISMArTADKDSATSQFFLNVADNAFLDHGQRDFGyAVFGKIVKGMdvaDKISQVQTHDVGPyqnvPSKPVV 182
Cdd:cd01925    83 RLrFNRRGLVGMA-NAGDDSNGSQFFFTLDKADELNNKHTLFG-KVTGDTIYNL---LKLAEVETDKDER----PVYPPK 153


                  ....*..
gi 1621407636 183 IISAKVL 189
Cdd:cd01925   154 ITSVEVL 160
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 33-162 2.52e-22

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.


Pssm-ID: 238905  Cd Length: 176  Bit Score: 88.65  E-value: 2.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  33 LTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGGfNEQMQQKQPNP----------------- 95
Cdd:cd01924     2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGD-PQGKNPGFPDPetgksrtipleikpegq 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  96 --PIKNEADNG----------LLNKRGTISMARTA-DKDSATSQFFLNVADNAFLDHG--QRDFGYAVFGKIVKGMDVAD 160
Cdd:cd01924    81 kqPVYGKTLEEagrydeqpvlPFNAFGAIAMARTEfDPNSASSQFFFLLKDNELTPSRnnVLDGRYAVFGYVTDGLDILR 160


                  ..
gi 1621407636 161 KI 162
Cdd:cd01924   161 EL 162
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 35-183 1.66e-21

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: 86.16  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  35 TSAGNIELELNSQKAPVSVKNF---------LDYVNSGfYNNTTFHRVIPGFMIQGGGF-----------------NEQM 88
Cdd:cd01926    12 EPAGRIVMELFADVVPKTAENFralctgekgKGGKPFG-YKGSTFHRVIPDFMIQGGDFtrgngtggksiygekfpDENF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  89 QQKQPNPpikneadngllnkrGTISMArTADKDSATSQFFLNVADNAFLDhGQrdfgYAVFGKIVKGMDVADKISQVQTH 168
Cdd:cd01926    91 KLKHTGP--------------GLLSMA-NAGPNTNGSQFFITTVKTPWLD-GK----HVVFGKVVEGMDVVKKIENVGSG 150

                         170
                  ....*....|....*
gi 1621407636 169 dvgpyQNVPSKPVVI 183
Cdd:cd01926   151 -----NGKPKKKVVI 160
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 32-176 6.76e-21

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: 84.12  E-value: 6.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGGG-----------FNEQMQQkQPNPPIKNE 100
Cdd:cd01922     1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDptgtgrggasiYGKKFED-EIHPELKHT 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621407636 101 AdngllnkRGTISMArTADKDSATSQFFLNVADNAFLDhGQrdfgYAVFGKIVKGMDVADKISQVQTHDVGPYQNV 176
Cdd:cd01922    80 G-------AGILSMA-NAGPNTNGSQFFITLAPTPWLD-GK----HTIFGRVSKGMKVIENMVEVQTQTDRPIDEV 142
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 31-167 1.11e-20

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: 83.64  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  31 VLLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQGG-----GFNEQMQQkqpNPPIKNEADNGL 105
Cdd:cd01928     3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGdptgtGKGGESIW---GKKFEDEFRETL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1621407636 106 -LNKRGTISMArTADKDSATSQFFLNVADNAFLdhgqrDFGYAVFGKIVKGMDVADKISQVQT 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 4.82e-18

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: 77.00  E-value: 4.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  32 LLTTSAGNIELELNSQKAPVSVKNFLDYVNSGFYNNTTFHRVIPGFMIQ------GGGFNEQM--QQKQPNPPIKNEADN 103
Cdd:cd01921     1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQtgdptgTGAGGESIysQLYGRQARFFEPEIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636 104 GLL--NKRGTISMArTADKDSATSQFFLNVADNafLDhgQRDFGYAVFGKIVKGMDVADKISQVQTHDVG-PYQNVPSKP 180
Cdd:cd01921    81 PLLkhSKKGTVSMV-NAGDNLNGSQFYITLGEN--LD--YLDGKHTVFGQVVEGFDVLEKINDAIVDDDGrPLKDIRIKH 155


                  ....
gi 1621407636 181 VVII 184
Cdd:cd01921   156 THIL 159
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 34-183 3.05e-13

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 64.86  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  34 TTSAGNIELELNSQKAPVSVKNFL-----DYVNSGF---YNNTTFHRVIPGFMIQGGGFneqmqqkqpnppIKNE----- 100
Cdd:PLN03149   29 GIPAGRIKMELFADIAPKTAENFRqfctgEFRKAGLpqgYKGCQFHRVIKDFMIQGGDF------------LKGDgtgcv 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636 101 -------ADNGLLNKR---GTISMARTAdKDSATSQFFLNVADNAFLDHgqrdfGYAVFGKIV-KGMDVADKISQVQThd 169
Cdd:PLN03149   97 siygskfEDENFIAKHtgpGLLSMANSG-PNTNGCQFFITCAKCDWLDN-----KHVVFGRVLgDGLLVVRKIENVAT-- 168

                         170
                  ....*....|....
gi 1621407636 170 vGPyQNVPSKPVVI 183
Cdd:PLN03149  169 -GP-NNRPKLACVI 180
PTZ00060 PTZ00060
cyclophilin; Provisional
 36-183 7.29e-13

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 63.71  E-value: 7.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636  36 SAGNIELELNSQKAPVSVKNFL-----DYVNSG----FYNNTTFHRVIPGFMIQGGGF-NEQMQQKQPNPPIKNEADNGL 105
Cdd:PTZ00060   28 PAGRIVFELFSDVTPKTAENFRalcigDKVGSSgknlHYKGSIFHRIIPQFMCQGGDItNHNGTGGESIYGRKFTDENFK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621407636 106 LN--KRGTISMArTADKDSATSQFFLNVADNAFLDhGQrdfgYAVFGKIVKGMDVADKISQvqthdVGPYQNVPSKPVVI 183
Cdd:PTZ00060  108 LKhdQPGLLSMA-NAGPNTNGSQFFITTVPCPWLD-GK----HVVFGKVIEGMEVVRAMEK-----EGTQSGYPKKPVVV 176
 
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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