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Conserved domains on  [gi|186515528|ref|NP_001119097|]
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Cyclophilin-like peptidyl-prolyl cis-trans isomerase family protein [Arabidopsis thaliana]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 240)

peptidylprolyl isomerase (PPIase) accelerates the folding of proteins; it 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
Pro_isomerase super family cl47509
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-64 1.04e-13

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.


The actual alignment was detected with superfamily member pfam00160:

Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 68.82  E-value: 1.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186515528    4 ADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVSVKIIRCGE 64
Cdd:pfam00160  89 PAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
 
Name Accession Description Interval E-value
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-64 1.04e-13

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: 68.82  E-value: 1.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186515528    4 ADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVSVKIIRCGE 64
Cdd:pfam00160  89 PAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-64 1.45e-11

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 63.71  E-value: 1.45e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186515528   1 MSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVSVKIIRCGE 64
Cdd:PTZ00060 118 MANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGE 181
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 10-61 1.36e-08

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 54.41  E-value: 1.36e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 186515528  10 GSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEG-KPTVSVKIIR 61
Cdd:COG0652  101 GSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEPVVIES 153
 
Name Accession Description Interval E-value
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-64 1.04e-13

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: 68.82  E-value: 1.04e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186515528    4 ADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVSVKIIRCGE 64
Cdd:pfam00160  89 PAPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-64 1.45e-11

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 63.71  E-value: 1.45e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 186515528   1 MSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVSVKIIRCGE 64
Cdd:PTZ00060 118 MANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGE 181
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 10-61 1.36e-08

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 54.41  E-value: 1.36e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 186515528  10 GSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEG-KPTVSVKIIR 61
Cdd:COG0652  101 GSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEPVVIES 153
PTZ00221 PTZ00221
cyclophilin; Provisional
 10-63 5.43e-04

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 42.16  E-value: 5.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 186515528  10 GSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVG-DEEGKPTVSVKIIRCG 63
Cdd:PTZ00221 163 GSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPlDDVGRPLLPVTVSFCG 217
 
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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