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Conserved domains on  [gi|2025689035|gb|QTU91089|]
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peptidylprolyl isomerase A, partial [Lasiopodomys brandtii]

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
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 2-118 2.49e-84

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.


The actual alignment was detected with superfamily member cd01926:

Pssm-ID: 469651 [Multi-domain]  Cd Length: 164  Bit Score: 242.93  E-value: 2.49e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   2 FGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGK 81
Cdd:cd01926    48 FGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGK 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2025689035  82 HVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCG 118
Cdd:cd01926   128 HVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 2-118 2.49e-84

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: 242.93  E-value: 2.49e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   2 FGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGK 81
Cdd:cd01926    48 FGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGK 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2025689035  82 HVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCG 118
Cdd:cd01926   128 HVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 4-120 6.46e-70

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 207.39  E-value: 6.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   4 YKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKHV 83
Cdd:PTZ00060   66 YKGSIFHRIIPQFMCQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHV 145

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2025689035  84 VFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCGQL 120
Cdd:PTZ00060  146 VFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 3-118 1.82e-43

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: 138.93  E-value: 1.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   3 GYKGSSFHRIIPGFMCQGGDFTrhnGTGGRSIYGEKFEDENFI--LKHtGPGILSMANAG--PNTNGSQFFICTTKTEWL 78
Cdd:pfam00160  33 FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPllLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHL 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2025689035  79 DGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCG 118
Cdd:pfam00160 109 DGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-100 4.56e-40

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 130.68  E-value: 4.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   1 GFgYKGSSFHRIIPGFMCQGGDFTRhNGTGGRsiyGEKFEDENFI-LKHTgPGILSMANA-GPNTNGSQFFICTTKTEWL 78
Cdd:COG0652    41 GF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHL 114

                          90       100
                  ....*....|....*....|..
gi 2025689035  79 DGKHVVFGKVKEGMNIVEAMER 100
Cdd:COG0652   115 DGGYTVFGKVVEGMDVVDKIAA 136
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 2-118 2.49e-84

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: 242.93  E-value: 2.49e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   2 FGYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGK 81
Cdd:cd01926    48 FGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGK 127

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2025689035  82 HVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCG 118
Cdd:cd01926   128 HVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 4-120 6.46e-70

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 207.39  E-value: 6.46e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   4 YKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKHV 83
Cdd:PTZ00060   66 YKGSIFHRIIPQFMCQGGDITNHNGTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHV 145

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2025689035  84 VFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCGQL 120
Cdd:PTZ00060  146 VFGKVIEGMEVVRAMEKEGTQSGYPKKPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 3-120 9.26e-52

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 161.54  E-value: 9.26e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   3 GYKGSSFHRIIPGFMCQGGDFTRHNGTGGRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKH 82
Cdd:PLN03149   67 GYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKH 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2025689035  83 VVFGKV-KEGMNIVEAMERFGS-RNGKTSKKITISDCGQL 120
Cdd:PLN03149  147 VVFGRVlGDGLLVVRKIENVATgPNNRPKLACVISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 3-116 7.54e-51

cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.


Pssm-ID: 238194 [Multi-domain]  Cd Length: 146  Bit Score: 157.81  E-value: 7.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   3 GYKGSSFHRIIPGFMCQGGDFTRHNGTGgrSIYGEKFEDENFILK-HTGPGILSMANAGPNTNGSQFFICTTKTEWLDGK 81
Cdd:cd00317    33 FYDGTTFHRVIPGFMIQGGDPTGTGGGG--SGPGYKFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGK 110

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2025689035  82 HVVFGKVKEGMNIVEAMERFG-SRNGKTSKKITISD 116
Cdd:cd00317   111 HTVFGKVVEGMDVVDKIERGDtDENGRPIKPVTISD 146
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 4-114 2.43e-44

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: 141.13  E-value: 2.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   4 YKGSSFHRIIPGFMCQGGDFTrHNGTGGRSIYGEKFEDE-NFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKH 82
Cdd:cd01922    34 YNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPELKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKH 112

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2025689035  83 VVFGKVKEGMNIVEAMERFGSRNGKTSKKITI 114
Cdd:cd01922   113 TIFGRVSKGMKVIENMVEVQTQTDRPIDEVKI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 3-118 1.82e-43

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: 138.93  E-value: 1.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   3 GYKGSSFHRIIPGFMCQGGDFTrhnGTGGRSIYGEKFEDENFI--LKHtGPGILSMANAG--PNTNGSQFFICTTKTEWL 78
Cdd:pfam00160  33 FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFPllLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHL 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2025689035  79 DGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITISDCG 118
Cdd:pfam00160 109 DGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 4-111 9.34e-41

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: 132.20  E-value: 9.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   4 YKGSSFHRIIPGFMCQGGDFTrHNGTGGRSIYGEKFEDE-NFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKH 82
Cdd:cd01927    34 YNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKH 112

                          90       100
                  ....*....|....*....|....*....
gi 2025689035  83 VVFGKVKEGMNIVEAMErfgsrNGKTSKK 111
Cdd:cd01927   113 TVFGRVVKGMDVVQRIE-----NVKTDKN 136
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-100 4.56e-40

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 130.68  E-value: 4.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   1 GFgYKGSSFHRIIPGFMCQGGDFTRhNGTGGRsiyGEKFEDENFI-LKHTgPGILSMANA-GPNTNGSQFFICTTKTEWL 78
Cdd:COG0652    41 GF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHL 114

                          90       100
                  ....*....|....*....|..
gi 2025689035  79 DGKHVVFGKVKEGMNIVEAMER 100
Cdd:COG0652   115 DGGYTVFGKVVEGMDVVDKIAA 136
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 4-116 2.33e-37

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: 124.07  E-value: 2.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   4 YKGSSFHRIIPGFMCQGGDFTrHNGTGGRSIYGEKFEDE-NFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKH 82
Cdd:cd01923    36 YDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPNLSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKH 114

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2025689035  83 VVFGKVKEGMNIVEAMERFGS-RNGKTSKKITISD 116
Cdd:cd01923   115 TVFGRVVGGLETLEAMENVPDpGTDRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 4-100 4.65e-35

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: 117.92  E-value: 4.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   4 YKGSSFHRIIPGFMCQGGDFTrHNGTGGRSIYGEKFEDENF-ILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKH 82
Cdd:cd01928    37 YNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFReTLKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKY 115

                          90
                  ....*....|....*...
gi 2025689035  83 VVFGKVKEGMNIVEAMER 100
Cdd:cd01928   116 TVFGKVIDGFETLDTLEK 133
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 4-88 3.46e-31

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: 108.59  E-value: 3.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   4 YKGSSFHRIIPGFMCQGGDFTrHNGTGGRSIYGEKFEDE-NFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKH 82
Cdd:cd01925    42 YDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHSRLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKH 120


                  ....*.
gi 2025689035  83 VVFGKV 88
Cdd:cd01925   121 TLFGKV 126
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 4-96 7.84e-22

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: 84.31  E-value: 7.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   4 YKGSSFHRIIPGFMCQGGDFTrHNGTGGRSIYGEK-------FEDE-NFILKHTGPGILSMANAGPNTNGSQFFICTTK- 74
Cdd:cd01921    34 YNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqarfFEPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEn 112

                          90       100
                  ....*....|....*....|..
gi 2025689035  75 TEWLDGKHVVFGKVKEGMNIVE 96
Cdd:cd01921   113 LDYLDGKHTVFGQVVEGFDVLE 134
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 1-100 1.66e-13

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: 62.85  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   1 GFgYKGSSFHRIIPGFMCQGGDFTRHngtggrsiyGEKFEDENFILKHTGPGI------LSMA-NAGPNTNGSQFFICTT 73
Cdd:cd01920    32 GF-YDNTIFHRVISGFVIQGGGFTPD---------LAQKETLKPIKNEAGNGLsntrgtIAMArTNAPDSATSQFFINLK 101

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2025689035  74 KTEWLD-----GKHVVFGKVKEGMNIVEAMER 100
Cdd:cd01920   102 DNASLDyqneqWGYTVFGEVTEGMDVVDKIAG 133
PTZ00221 PTZ00221
cyclophilin; Provisional
 31-120 2.07e-12

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 61.42  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035  31 GRSIYGEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTTKTEWLDGKHVVFGKVKEGMNIVEAMERFG-SRNGKTS 109
Cdd:PTZ00221  129 NVSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPlDDVGRPL 208

                          90
                  ....*....|.
gi 2025689035 110 KKITISDCGQL 120
Cdd:PTZ00221  209 LPVTVSFCGAL 219
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-105 2.16e-12

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 60.63  E-value: 2.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   1 GFgYKGSSFHRIIPGFMCQGGDFTrhngtggrsiygekfedENFILKHTGPGILSMANAG-PNTNG-------------- 65
Cdd:PRK10903   63 GF-YNNTTFHRVIPGFMIQGGGFT-----------------EQMQQKKPNPPIKNEADNGlRNTRGtiamartadkdsat 124

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2025689035  66 SQFFICTTKTEWLD-GK----HVVFGKVKEGMNIVEAMERFGSRN 105
Cdd:PRK10903  125 SQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHD 169
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 1-99 2.17e-08

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: 49.75  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   1 GFgYKGSSFHRIIPGFMCQGGD-FTRHNG-----TG--------------GRSIYGEKFE-----DENFILKHTGPGILS 55
Cdd:cd01924    32 GF-YDGMEFHRVEGGFVVQTGDpQGKNPGfpdpeTGksrtipleikpegqKQPVYGKTLEeagryDEQPVLPFNAFGAIA 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2025689035  56 MANA--GPNTNGSQFFI-------CTTKTEWLDGKHVVFGKVKEGMNIVEAME 99
Cdd:cd01924   111 MARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
PRK10791 PRK10791
peptidylprolyl isomerase B;
1-96 2.99e-06

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 43.67  E-value: 2.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2025689035   1 GFgYKGSSFHRIIPGFMCQGGDFtrHNGTGGRSIYGEKFEDENFILKHTgPGILSMANAG-PNTNGSQFFICTTKTEWLD 79
Cdd:PRK10791   34 GF-YNNTIFHRVINGFMIQGGGF--EPGMKQKATKEPIKNEANNGLKNT-RGTLAMARTQaPHSATAQFFINVVDNDFLN 109

                          90       100
                  ....*....|....*....|....*
gi 2025689035  80 GK--------HVVFGKVKEGMNIVE 96
Cdd:PRK10791  110 FSgeslqgwgYCVFAEVVEGMDVVD 134
 
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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