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Conserved domains on  [gi|872565101|ref|WP_048530868|]
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MULTISPECIES: peptidylprolyl isomerase [Bacillus]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10002023)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 15-137 3.88e-57

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


:

Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 174.97  E-value: 3.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  15 IDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGYSIPCETDgNPHRHLVGSLSMAHA-G 93
Cdd:COG0652   18 IVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGYTIPDEFD-PGLKHKRGTLAMARAqG 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 872565101  94 RNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDVM 137
Cdd:COG0652   97 PNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTD 140
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 15-137 3.88e-57

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 174.97  E-value: 3.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  15 IDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGYSIPCETDgNPHRHLVGSLSMAHA-G 93
Cdd:COG0652   18 IVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGYTIPDEFD-PGLKHKRGTLAMARAqG 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 872565101  94 RNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDVM 137
Cdd:COG0652   97 PNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTD 140
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 6-142 3.37e-52

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: 162.05  E-value: 3.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101   6 YILMENGeKIDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGYS--IPCETDGNPHRHL 83
Cdd:cd00317    1 TLDTTKG-RIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGSGPGykFPDENFPLKYHHR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872565101  84 VGSLSMAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDV------MKEVKV 142
Cdd:cd00317   80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTdengrpIKPVTI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 14-136 7.86e-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: 138.54  E-value: 7.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101   14 KIDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGP-GYSIPCETDGNPHRHLVGSLSMAHA 92
Cdd:pfam00160   8 RIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKsIFPIPDEIFPLLLKHKRGALSMANT 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 872565101   93 GR--NTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDV 136
Cdd:pfam00160  88 GPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPT 133
PTZ00060 PTZ00060
cyclophilin; Provisional
 14-142 1.40e-22

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 87.98  E-value: 1.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  14 KIDLEFFPEEAPKTVENFKKL------AEQG---FYDGVTFHRVIPGFVSQGGDPTGTGAG--GPGYSIPCETDGNPHRH 82
Cdd:PTZ00060  31 RIVFELFSDVTPKTAENFRALcigdkvGSSGknlHYKGSIFHRIIPQFMCQGGDITNHNGTggESIYGRKFTDENFKLKH 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872565101  83 LV-GSLSMAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNM-----RQGDVMKEVKV 142
Cdd:PTZ00060 111 DQpGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMekegtQSGYPKKPVVV 176
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 15-137 3.88e-57

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 174.97  E-value: 3.88e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  15 IDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGYSIPCETDgNPHRHLVGSLSMAHA-G 93
Cdd:COG0652   18 IVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGYTIPDEFD-PGLKHKRGTLAMARAqG 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 872565101  94 RNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDVM 137
Cdd:COG0652   97 PNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTD 140
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 6-142 3.37e-52

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: 162.05  E-value: 3.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101   6 YILMENGeKIDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGYS--IPCETDGNPHRHL 83
Cdd:cd00317    1 TLDTTKG-RIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGGSGPGykFPDENFPLKYHHR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 872565101  84 VGSLSMAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDV------MKEVKV 142
Cdd:cd00317   80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTdengrpIKPVTI 144
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 14-136 7.86e-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: 138.54  E-value: 7.86e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101   14 KIDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGP-GYSIPCETDGNPHRHLVGSLSMAHA 92
Cdd:pfam00160   8 RIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKsIFPIPDEIFPLLLKHKRGALSMANT 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 872565101   93 GR--NTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDV 136
Cdd:pfam00160  88 GPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPT 133
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 15-145 1.04e-33

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: 115.25  E-value: 1.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  15 IDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPgySI---PCETDGNPH-RH-LVGSLSM 89
Cdd:cd01927    9 IHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGE--SIwgkEFEDEFSPSlKHdRPYTLSM 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 872565101  90 AHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDVMKEVKVWEE 145
Cdd:cd01927   87 ANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYED 142
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 6-138 1.53e-33

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: 115.21  E-value: 1.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101   6 YILME-NGEKIDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGY-SIPCETD-GNPHRH 82
Cdd:cd01923    1 YVRLHtNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIwGKPFKDEfKPNLSH 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 872565101  83 LV-GSLSMAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDVMK 138
Cdd:cd01923   81 DGrGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPG 137
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 14-131 3.18e-31

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: 108.78  E-value: 3.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  14 KIDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPG-YSIPCETDGNPHRHLVGS--LSMA 90
Cdd:cd01922    8 EITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASiYGKKFEDEIHPELKHTGAgiLSMA 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 872565101  91 HAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNM 131
Cdd:cd01922   88 NAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM 128
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 15-145 1.06e-30

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: 107.91  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  15 IDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPG-YSIPCETDGNPH-RHLV-GSLSMAH 91
Cdd:cd01928   12 IKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESiWGKKFEDEFRETlKHDSrGVVSMAN 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 872565101  92 AGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDVMKEVKVWEE 145
Cdd:cd01928   92 NGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEE 145
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 14-128 7.16e-28

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: 100.79  E-value: 7.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  14 KIDLEFFPEEAPKTVENFKKLA--EQGF------YDGVTFHRVIPGFVSQGGDPTGTGAGGPGySIPCET--DGN-PHRH 82
Cdd:cd01926   16 RIVMELFADVVPKTAENFRALCtgEKGKggkpfgYKGSTFHRVIPDFMIQGGDFTRGNGTGGK-SIYGEKfpDENfKLKH 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 872565101  83 L-VGSLSMAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAV 128
Cdd:cd01926   95 TgPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVV 141
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 15-139 2.73e-27

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: 99.73  E-value: 2.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  15 IDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGT-GAGGPGYSIPCETDGNP-----HRHLVGsls 88
Cdd:cd01925   17 IDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTgTGGESIYGEPFKDEFHSrlrfnRRGLVG--- 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 872565101  89 MAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKAT-SGIEAVLNMRQGDVMKE 139
Cdd:cd01925   94 MANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIYNLLKLAEVETDKD 145
PTZ00060 PTZ00060
cyclophilin; Provisional
 14-142 1.40e-22

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 87.98  E-value: 1.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  14 KIDLEFFPEEAPKTVENFKKL------AEQG---FYDGVTFHRVIPGFVSQGGDPTGTGAG--GPGYSIPCETDGNPHRH 82
Cdd:PTZ00060  31 RIVFELFSDVTPKTAENFRALcigdkvGSSGknlHYKGSIFHRIIPQFMCQGGDITNHNGTggESIYGRKFTDENFKLKH 110

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872565101  83 LV-GSLSMAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGIEAVLNM-----RQGDVMKEVKV 142
Cdd:PTZ00060 111 DQpGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMekegtQSGYPKKPVVV 176
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 14-142 3.09e-22

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: 86.34  E-value: 3.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  14 KIDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGYSIPCETDGNPHRHLVGSLSMAH-A 92
Cdd:cd01920    8 DIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGTIAMARtN 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 872565101  93 GRNTGGSQFFIVHEPQPHLD-----GVHTVFGKATSGIEAVlnmrqgDVMKEVKV 142
Cdd:cd01920   88 APDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVV------DKIAGVET 136
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 24-142 1.43e-19

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: 79.80  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  24 APKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGD------PTGTGAGGPGYSIPCE----TDGNP-------------- 79
Cdd:cd01924   18 APVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDpqgknpGFPDPETGKSRTIPLEikpeGQKQPvygktleeagryde 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 872565101  80 ----HRHLVGSLSMAHA--GRNTGGSQFFI-------VHEPQPHLDGVHTVFGKATSGIEAVLNMRQGDVMKEVKV 142
Cdd:cd01924   98 qpvlPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELKVGDKIESARV 173
PRK10903 PRK10903
peptidylprolyl isomerase A;
7-133 6.22e-18

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 76.03  E-value: 6.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101   7 ILMENGEKIDLEFFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGYS-IPCETDgNPHRHLVG 85
Cdd:PRK10903  32 LLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPpIKNEAD-NGLRNTRG 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 872565101  86 SLSMAH-AGRNTGGSQFFIVHEPQPHLD------GvHTVFGKATSGIEAVLNMRQ 133
Cdd:PRK10903 111 TIAMARtADKDSATSQFFINVADNAFLDhgqrdfG-YAVFGKVVKGMDVADKISQ 164
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 15-126 8.90e-17

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: 8.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  15 IDLefFPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPgySIPCETDGNPHRHL----------- 83
Cdd:cd01921   11 IDL--FTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGE--SIYSQLYGRQARFFepeilpllkhs 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 872565101  84 -VGSLSMAHAGRNTGGSQFFI-VHEPQPHLDGVHTVFGKATSGIE 126
Cdd:cd01921   87 kKGTVSMVNAGDNLNGSQFYItLGENLDYLDGKHTVFGQVVEGFD 131
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 14-120 1.61e-16

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 72.18  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  14 KIDLEFFPEEAPKTVENFKKLAEQGF--------YDGVTFHRVIPGFVSQGGDPTGTGAG--GPGYSIPCETDGNPHRHL 83
Cdd:PLN03149  34 RIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFLKGDGTgcVSIYGSKFEDENFIAKHT 113

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 872565101  84 -VGSLSMAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGK 120
Cdd:PLN03149 114 gPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGR 151
PRK10791 PRK10791
peptidylprolyl isomerase B;
20-103 2.60e-09

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 52.53  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  20 FPEEAPKTVENFKKLAEQGFYDGVTFHRVIPGFVSQGGDPTGTGAGGPGYSIPCETDGNPHRHLVGSLSMAHAGR-NTGG 98
Cdd:PRK10791  16 FDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTRGTLAMARTQApHSAT 95


                 ....*
gi 872565101  99 SQFFI 103
Cdd:PRK10791  96 AQFFI 100
PTZ00221 PTZ00221
cyclophilin; Provisional
 17-125 7.39e-05

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 41.01  E-value: 7.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 872565101  17 LEFFPEEAPKTVENFKKL--AEQGFYD---------GVTFHRV--IPGFVSQGgdpTGTGAGGPGYSIPCETDGNPHRHL 83
Cdd:PTZ00221  71 FELFEDVVPETVENFRALitGSCGIDTntgvkldylYTPVHHVdrNNNIIVLG---ELDSFNVSSTGTPIADEGYRHRHT 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 872565101  84 V-GSLSMAHAGRNTGGSQFFIVHEPQPHLDGVHTVFGKATSGI 125
Cdd:PTZ00221 148 ErGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDL 190
 
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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