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Conserved domains on  [gi|347519972|gb|EGY27118|]
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peptidyl-prolyl cis-trans isomerase cyp18 [Desulfovibrio sp. A2]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112428)

peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-160 6.52e-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: 238.88  E-value: 6.52e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTREPIENEANNGLRNEKYTV 83
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGTI 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347519972  84 AMARTMAPHSATAQFFINVKDNAFLDHrapTMQGWGYAVFGKVTEGTDVVDKIKAVRTATVGSFENVPTTAVVIKKA 160
Cdd:cd01920   82 AMARTNAPDSATSQFFINLKDNASLDY---QNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
 
Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-160 6.52e-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: 238.88  E-value: 6.52e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTREPIENEANNGLRNEKYTV 83
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGTI 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347519972  84 AMARTMAPHSATAQFFINVKDNAFLDHrapTMQGWGYAVFGKVTEGTDVVDKIKAVRTATVGSFENVPTTAVVIKKA 160
Cdd:cd01920   82 AMARTNAPDSATSQFFINLKDNASLDY---QNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-164 9.72e-76

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 223.12  E-value: 9.72e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   1 MIKLETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTRePIENEANNGLRNEK 80
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGLKHKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  81 YTVAMARTMAPHSATAQFFINVKDNAFLDHraptmqgwGYAVFGKVTEGTDVVDKIKAVRTATvgsfENVPTTAVVIKKA 160
Cdd:COG0652   87 GTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIESV 154


                 ....
gi 347519972 161 TVLS 164
Cdd:COG0652  155 TIVE 158
PRK10903 PRK10903
peptidylprolyl isomerase A;
2-163 4.37e-72

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 215.09  E-value: 4.37e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   2 IKLETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTREPIENEANNGLRNEKY 81
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  82 TVAMARTMAPHSATAQFFINVKDNAFLDHrapTMQGWGYAVFGKVTEGTDVVDKIKAVRTATVGSFENVPTTAVVIKKAT 161
Cdd:PRK10903 111 TIAMARTADKDSATSQFFINVADNAFLDH---GQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAK 187


                 ..
gi 347519972 162 VL 163
Cdd:PRK10903 188 VL 189
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-162 3.46e-55

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: 170.90  E-value: 3.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972    4 LETS-MGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTREPIENE-ANNGLRNEKY 81
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEiFPLLLKHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   82 TVAMART-MAPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAVRTAtvgsfENVPTTAVVIKKA 160
Cdd:pfam00160  81 ALSMANTgPAPNSNGSQFFITLGPAPHLDGK--------YTVFGKVVEGMDVLEKIEKVPTD-----GDRPVKPVKILSC 147


                  ..
gi 347519972  161 TV 162
Cdd:pfam00160 148 GV 149
 
Name Accession Description Interval E-value
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-160 6.52e-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: 238.88  E-value: 6.52e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTREPIENEANNGLRNEKYTV 83
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGTI 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 347519972  84 AMARTMAPHSATAQFFINVKDNAFLDHrapTMQGWGYAVFGKVTEGTDVVDKIKAVRTATVGSFENVPTTAVVIKKA 160
Cdd:cd01920   82 AMARTNAPDSATSQFFINLKDNASLDY---QNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-164 9.72e-76

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 223.12  E-value: 9.72e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   1 MIKLETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTRePIENEANNGLRNEK 80
Cdd:COG0652    8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGY-TIPDEFDPGLKHKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  81 YTVAMARTMAPHSATAQFFINVKDNAFLDHraptmqgwGYAVFGKVTEGTDVVDKIKAVRTATvgsfENVPTTAVVIKKA 160
Cdd:COG0652   87 GTLAMARAQGPNSAGSQFFIVLGDNPHLDG--------GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVVIESV 154


                 ....
gi 347519972 161 TVLS 164
Cdd:COG0652  155 TIVE 158
PRK10903 PRK10903
peptidylprolyl isomerase A;
2-163 4.37e-72

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 215.09  E-value: 4.37e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   2 IKLETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTREPIENEANNGLRNEKY 81
Cdd:PRK10903  31 VLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  82 TVAMARTMAPHSATAQFFINVKDNAFLDHrapTMQGWGYAVFGKVTEGTDVVDKIKAVRTATVGSFENVPTTAVVIKKAT 161
Cdd:PRK10903 111 TIAMARTADKDSATSQFFINVADNAFLDH---GQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAK 187


                 ..
gi 347519972 162 VL 163
Cdd:PRK10903 188 VL 189
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-162 8.09e-69

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 205.84  E-value: 8.09e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   1 MIKLETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTREPIENEANNGLRNEK 80
Cdd:PRK10791   1 MVTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  81 YTVAMARTMAPHSATAQFFINVKDNAFLDHRAPTMQGWGYAVFGKVTEGTDVVDKIKAVRTATVGSFENVPTTAVVIKKA 160
Cdd:PRK10791  81 GTLAMARTQAPHSATAQFFINVVDNDFLNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESV 160


                 ..
gi 347519972 161 TV 162
Cdd:PRK10791 161 TV 162
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 4-162 3.46e-55

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: 170.90  E-value: 3.46e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972    4 LETS-MGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTREPIENE-ANNGLRNEKY 81
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEiFPLLLKHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   82 TVAMART-MAPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAVRTAtvgsfENVPTTAVVIKKA 160
Cdd:pfam00160  81 ALSMANTgPAPNSNGSQFFITLGPAPHLDGK--------YTVFGKVVEGMDVLEKIEKVPTD-----GDRPVKPVKILSC 147


                  ..
gi 347519972  161 TV 162
Cdd:pfam00160 148 GV 149
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 4-159 1.73e-46

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: 148.57  E-value: 1.73e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMREKPTR-EPIENEANNGLR-NEKY 81
Cdd:cd00317    2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGSGPgYKFPDENFPLKYhHRRG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 347519972  82 TVAMARtMAPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAVRTATVGsfenVPTTAVVIKK 159
Cdd:cd00317   82 TLSMAN-AGPNTNGSQFFITTAPTPHLDGK--------HTVFGKVVEGMDVVDKIERGDTDENG----RPIKPVTISD 146
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 4-141 7.78e-27

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: 98.69  E-value: 7.78e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGY--DEKMREKPTREPIENEANNGLRNEK- 80
Cdd:cd01927    2 IHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPtgDGTGGESIWGKEFEDEFSPSLKHDRp 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 347519972  81 YTVAMARTmAPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAVRT 141
Cdd:cd01927   82 YTLSMANA-GPNTNGSQFFITTVATPWLDNK--------HTVFGRVVKGMDVVQRIENVKT 133
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 9-138 1.28e-25

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: 96.36  E-value: 1.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   9 GDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGG--------YD---EKMREKP-------TREPIEN 70
Cdd:cd01924    7 GTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDpqgknpgfPDpetGKSRTIPleikpegQKQPVYG 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 347519972  71 EANNG----------LRNEKYTVAMART-MAPHSATAQFFINVKDNAFLDHRAPTMQGwGYAVFGKVTEGTDVVDKIKA 138
Cdd:cd01924   87 KTLEEagrydeqpvlPFNAFGAIAMARTeFDPNSASSQFFFLLKDNELTPSRNNVLDG-RYAVFGYVTDGLDILRELKV 164
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 2-162 1.39e-22

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: 87.88  E-value: 1.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   2 IKLETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGgyDE----KMREKPTREPIENEANNGLR 77
Cdd:cd01928    3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTG--DPtgtgKGGESIWGKKFEDEFRETLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  78 -NEKYTVAMARTmAPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAVRTATvgsfENVPTTAVV 156
Cdd:cd01928   81 hDSRGVVSMANN-GPNTNGSQFFITYAKQPHLDGK--------YTVFGKVIDGFETLDTLEKLPVDK----KYRPLEEIR 147


                 ....*.
gi 347519972 157 IKKATV 162
Cdd:cd01928  148 IKDVTI 153
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 2-164 3.58e-22

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: 87.09  E-value: 3.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   2 IKLETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGgydekmreKPT----------REPIENE 71
Cdd:cd01923    2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGG--------DPTgtgrggesiwGKPFKDE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  72 ANNGLRNE-KYTVAMARTmAPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAVRTATvgsfENV 150
Cdd:cd01923   74 FKPNLSHDgRGVLSMANS-GPNTNGSQFFITYRSCKHLDGK--------HTVFGRVVGGLETLEAMENVPDPG----TDR 140

                        170
                 ....*....|....
gi 347519972 151 PTTAVVIKKATVLS 164
Cdd:cd01923  141 PKEEIKIEDTSVFV 154
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 9-157 8.14e-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: 86.16  E-value: 8.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   9 GDIVIEVDDEKAPKSAANFR-----EYVAAG---HYDGTIFHRVIDGFMIQGGGY-----------------DEKMREKP 63
Cdd:cd01926   15 GRIVMELFADVVPKTAENFRalctgEKGKGGkpfGYKGSTFHRVIPDFMIQGGDFtrgngtggksiygekfpDENFKLKH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  64 TREPIENEANNGlrnekytvamartmaPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAvrtat 143
Cdd:cd01926   95 TGPGLLSMANAG---------------PNTNGSQFFITTVKTPWLDGK--------HVVFGKVVEGMDVVKKIEN----- 146

                        170
                 ....*....|....
gi 347519972 144 VGSFENVPTTAVVI 157
Cdd:cd01926  147 VGSGNGKPKKKVVI 160
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-143 1.42e-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: 84.89  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGGYDEKMR--EKPTREPIENEANNGLrneKY 81
Cdd:cd01922    2 LETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRggASIYGKKFEDEIHPEL---KH 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347519972  82 TVAMARTMA---PHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAVRTAT 143
Cdd:cd01922   79 TGAGILSMAnagPNTNGSQFFITLAPTPWLDGK--------HTIFGRVSKGMKVIENMVEVQTQT 135
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 4-127 1.43e-19

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: 80.47  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQGGgydekmreKPT----------REPIENEAN 73
Cdd:cd01925   10 LKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGG--------DPTgtgtggesiyGEPFKDEFH 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 347519972  74 NGLR-NEKYTVAMARTmAPHSATAQFFINvkdnafLDhRAPTMQGwGYAVFGKVT 127
Cdd:cd01925   82 SRLRfNRRGLVGMANA-GDDSNGSQFFFT------LD-KADELNN-KHTLFGKVT 127
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 4-136 1.56e-16

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: 72.37  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDIVIEVDDEKAPKSAANFREYVAAGHYDGTIFHRVIDGFMIQ--------GGGYD--EKMREKPTREpIENEAN 73
Cdd:cd01921    2 LETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQtgdptgtgAGGESiySQLYGRQARF-FEPEIL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 347519972  74 NGLRNEKY-TVAMArTMAPHSATAQFFINVKDNA-FLDHRAptmqgwgyAVFGKVTEGTDVVDKI 136
Cdd:cd01921   81 PLLKHSKKgTVSMV-NAGDNLNGSQFYITLGENLdYLDGKH--------TVFGQVVEGFDVLEKI 136
PTZ00060 PTZ00060
cyclophilin; Provisional
 9-157 1.11e-14

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 67.95  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   9 GDIVIEVDDEKAPKSAANFREYVAAG---------HYDGTIFHRVIDGFMIQGGGY-----------------DEKMREK 62
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALCIGDkvgssgknlHYKGSIFHRIIPQFMCQGGDItnhngtggesiygrkftDENFKLK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  63 PTREPIENEANNGlrnekytvamartmaPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVTEGTDVVDKIKAvrta 142
Cdd:PTZ00060 110 HDQPGLLSMANAG---------------PNTNGSQFFITTVPCPWLDGK--------HVVFGKVIEGMEVVRAMEK---- 162

                        170
                 ....*....|....*
gi 347519972 143 tVGSFENVPTTAVVI 157
Cdd:PTZ00060 163 -EGTQSGYPKKPVVV 176
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 9-159 4.46e-13

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 63.70  E-value: 4.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   9 GDIVIEVDDEKAPKSAANFREYVAAGH--------YDGTIFHRVIDGFMIQGGGY-----------------DEKMREKP 63
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFlkgdgtgcvsiygskfeDENFIAKH 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  64 TREPIENEANNGlrnekytvamartmaPHSATAQFFINVKDNAFLDHRaptmqgwgYAVFGKVT-EGTDVVDKIKAVRTA 142
Cdd:PLN03149 113 TGPGLLSMANSG---------------PNTNGCQFFITCAKCDWLDNK--------HVVFGRVLgDGLLVVRKIENVATG 169

                        170
                 ....*....|....*..
gi 347519972 143 TvgsfENVPTTAVVIKK 159
Cdd:PLN03149 170 P----NNRPKLACVISE 182
PTZ00221 PTZ00221
cyclophilin; Provisional
 4-157 2.75e-04

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 39.85  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972   4 LETSMGDI-----VIEVDDEKAPKSAANFREYV--------AAG---HYDGTIFHRVIDGFMIQGGGYDEKMREKPTREP 67
Cdd:PTZ00221  57 LDISIGDVlagrlVFELFEDVVPETVENFRALItgscgidtNTGvklDYLYTPVHHVDRNNNIIVLGELDSFNVSSTGTP 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 347519972  68 IENEANNGLRNEKYTVAMArTMAPHSATAQFFINVKDNAFLDHRAptmqgwgyAVFGKVTEGTDVVDKIKAVRTATVGSf 147
Cdd:PTZ00221 137 IADEGYRHRHTERGLLTMI-SEGPHTSGSVFGITLGPSPSLDFKQ--------VVFGKAVDDLSLLEKLESLPLDDVGR- 206

                        170
                 ....*....|
gi 347519972 148 envPTTAVVI 157
Cdd:PTZ00221 207 ---PLLPVTV 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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