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Conserved domains on  [gi|2258828840|gb|USN53041|]
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MAG: peptidylprolyl isomerase [Candidatus Nomurabacteria bacterium]

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 ...
 1-145 1.44e-61

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


:

Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 186.14  E-value: 1.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGYKFDNDPTSEPVYKKGFIA 80
Cdd:COG0652    11 LETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGYTIPDEFDPGLKHKRGTLA 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258828840  81 MANA-GRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVKMIEVTVE 145
Cdd:COG0652    91 MARAqGPNSAGSQFFIVLGDNPhLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTIV 157
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-145 1.44e-61

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 186.14  E-value: 1.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGYKFDNDPTSEPVYKKGFIA 80
Cdd:COG0652    11 LETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGYTIPDEFDPGLKHKRGTLA 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258828840  81 MANA-GRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVKMIEVTVE 145
Cdd:COG0652    91 MARAqGPNSAGSQFFIVLGDNPhLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTIV 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 1-138 4.46e-48

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: 151.65  E-value: 4.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGD--PTGTGMGGPGYKFDNDPTSEP-VYKKG 77
Cdd:cd00317     2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDptGTGGGGSGPGYKFPDENFPLKyHHRRG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258828840  78 FIAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVK 138
Cdd:cd00317    82 TLSMANAGPNTNGSQFFITTAPTPhLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVT 143
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 1-144 3.21e-44

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: 142.01  E-value: 3.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTN-LGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGP-GYKFDNDPT-SEPVYKKG 77
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKsIFPIPDEIFpLLLKHKRG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840  78 FIAMANAGR--NTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGsDRPYQEVKMIEVTV 144
Cdd:pfam00160  81 ALSMANTGPapNSNGSQFFITLGPAPhLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCGV 149
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-144 3.91e-28

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 102.23  E-value: 3.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGtgmggpgyKFDNDPTSEPVY------ 74
Cdd:PRK10903   33 LTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTE--------QMQQKKPNPPIKneadng 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840  75 ---KKGFIAMA-NAGRNTNGSQFFIMVADYPLPPD------YSIFGKVIEGQDIADKISGVdRSGSDRPYQEVKMIEVTV 144
Cdd:PRK10903  105 lrnTRGTIAMArTADKDSATSQFFINVADNAFLDHgqrdfgYAVFGKVVKGMDVADKISQV-PTHDVGPYQNVPSKPVVI 183
 
Name Accession Description Interval E-value
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-145 1.44e-61

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 186.14  E-value: 1.44e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGYKFDNDPTSEPVYKKGFIA 80
Cdd:COG0652    11 LETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGPGYTIPDEFDPGLKHKRGTLA 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258828840  81 MANA-GRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVKMIEVTVE 145
Cdd:COG0652    91 MARAqGPNSAGSQFFIVLGDNPhLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTIV 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 1-138 4.46e-48

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: 151.65  E-value: 4.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGD--PTGTGMGGPGYKFDNDPTSEP-VYKKG 77
Cdd:cd00317     2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDptGTGGGGSGPGYKFPDENFPLKyHHRRG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258828840  78 FIAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVK 138
Cdd:cd00317    82 TLSMANAGPNTNGSQFFITTAPTPhLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVT 143
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 1-144 3.21e-44

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: 142.01  E-value: 3.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTN-LGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGP-GYKFDNDPT-SEPVYKKG 77
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKsIFPIPDEIFpLLLKHKRG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840  78 FIAMANAGR--NTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGsDRPYQEVKMIEVTV 144
Cdd:pfam00160  81 ALSMANTGPapNSNGSQFFITLGPAPhLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSCGV 149
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 1-144 6.86e-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: 123.68  E-value: 6.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGY---KFDNDPTSEPVYK-K 76
Cdd:cd01923     4 LHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIwgkPFKDEFKPNLSHDgR 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258828840  77 GFIAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVKMIEVTV 144
Cdd:cd01923    84 GVLSMANSGPNTNGSQFFITYRSCKhLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSV 152
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 1-142 3.74e-36

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: 121.41  E-value: 3.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGY---KFDNDPTSEPVYKKG 77
Cdd:cd01927     2 IHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIwgkEFEDEFSPSLKHDRP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258828840  78 F-IAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVKMIEV 142
Cdd:cd01927    82 YtLSMANAGPNTNGSQFFITTVATPwLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIINI 148
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 3-144 1.02e-34

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: 1.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   3 TNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGY---KFDNDPTSEPVY-KKGF 78
Cdd:cd01928     7 TNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIwgkKFEDEFRETLKHdSRGV 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258828840  79 IAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVKMIEVTV 144
Cdd:cd01928    87 VSMANNGPNTNGSQFFITYAKQPhLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKDVTI 153
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 1-140 1.43e-32

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: 112.24  E-value: 1.43e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGY---KFDNDPTSEPVYK-K 76
Cdd:cd01922     2 LETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIygkKFEDEIHPELKHTgA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258828840  77 GFIAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDrSGSDRPYQEVKMI 140
Cdd:cd01922    82 GILSMANAGPNTNGSQFFITLAPTPwLDGKHTIFGRVSKGMKVIENMVEVQ-TQTDRPIDEVKIL 145
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 1-145 1.07e-31

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: 110.23  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGYK-FDNDPTSEPVYKKGFI 79
Cdd:cd01920     2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKpIKNEAGNGLSNTRGTI 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258828840  80 AMA-NAGRNTNGSQFFIMVAD--YPLPPD----YSIFGKVIEGQDIADKISGVdRSGSDRPYQEVKMIEVTVE 145
Cdd:cd01920    82 AMArTNAPDSATSQFFINLKDnaSLDYQNeqwgYTVFGEVTEGMDVVDKIAGV-ETYSFGSYQDVPVQDVIIE 153
PRK10903 PRK10903
peptidylprolyl isomerase A;
1-144 3.91e-28

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 102.23  E-value: 3.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGtgmggpgyKFDNDPTSEPVY------ 74
Cdd:PRK10903   33 LTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTE--------QMQQKKPNPPIKneadng 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840  75 ---KKGFIAMA-NAGRNTNGSQFFIMVADYPLPPD------YSIFGKVIEGQDIADKISGVdRSGSDRPYQEVKMIEVTV 144
Cdd:PRK10903  105 lrnTRGTIAMArTADKDSATSQFFINVADNAFLDHgqrdfgYAVFGKVVKGMDVADKISQV-PTHDVGPYQNVPSKPVVI 183
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 1-144 4.25e-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: 98.96  E-value: 4.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGY---KFDNDPTSEPVY-KK 76
Cdd:cd01925    10 LKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIygePFKDEFHSRLRFnRR 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258828840  77 GFIAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKViEGQDIAD--KISGVDRSGSDRPYQEVKMIEVTV 144
Cdd:cd01925    90 GLVGMANAGDDSNGSQFFFTLDKADeLNNKHTLFGKV-TGDTIYNllKLAEVETDKDERPVYPPKITSVEV 159
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 3-141 9.50e-27

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: 98.10  E-value: 9.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   3 TNLGDIVVQTDVDMGPRAASNFVYLA-------KEGF-YNGTIFHRVIPGFMIQGGDPTGT--GMGGPGY--KFDNDPTS 70
Cdd:cd01926    12 EPAGRIVMELFADVVPKTAENFRALCtgekgkgGKPFgYKGSTFHRVIPDFMIQGGDFTRGngTGGKSIYgeKFPDENFK 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258828840  71 EPVYKKGFIAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVdRSGSDRPYQEVKMIE 141
Cdd:cd01926    92 LKHTGPGLLSMANAGPNTNGSQFFITTVKTPwLDGKHVVFGKVVEGMDVVKKIENV-GSGNGKPKKKVVIAD 162
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 3-138 4.67e-26

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: 96.26  E-value: 4.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   3 TNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGD----PTGTGMGGPGYKFDNDPTSEPVY---- 74
Cdd:cd01921     4 TTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDptgtGAGGESIYSQLYGRQARFFEPEIlpll 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258828840  75 ---KKGFIAMANAGRNTNGSQFFIMVADY--PLPPDYSIFGKVIEGQDIADKISGVDRSGSDRPYQEVK 138
Cdd:cd01921    84 khsKKGTVSMVNAGDNLNGSQFYITLGENldYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIR 152
PRK10791 PRK10791
peptidylprolyl isomerase B;
3-144 3.74e-22

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 86.05  E-value: 3.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   3 TNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPT-GTGMGGPGYKFDNDPTSEPVYKKGFIAM 81
Cdd:PRK10791    6 TNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEpGMKQKATKEPIKNEANNGLKNTRGTLAM 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258828840  82 ANAGR-NTNGSQFFIMVADYPL------PPD---YSIFGKVIEGQDIADKISGVD--RSG--SDRPYQEVKMIEVTV 144
Cdd:PRK10791   86 ARTQApHSATAQFFINVVDNDFlnfsgeSLQgwgYCVFAEVVEGMDVVDKIKGVAtgRSGmhQDVPKEDVIIESVTV 162
PTZ00060 PTZ00060
cyclophilin; Provisional
 6-137 2.23e-20

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 82.20  E-value: 2.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   6 GDIVVQTDVDMGPRAASNFVYL---------AKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGYKFDNDPTSEPVYKK 76
Cdd:PTZ00060   30 GRIVFELFSDVTPKTAENFRALcigdkvgssGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGESIYGRKFTDENFKLK 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258828840  77 ----GFIAMANAGRNTNGSQFFIMVADYP-LPPDYSIFGKVIEGQDIADKISGVDRSgSDRPYQEV 137
Cdd:PTZ00060  110 hdqpGLLSMANAGPNTNGSQFFITTVPCPwLDGKHVVFGKVIEGMEVVRAMEKEGTQ-SGYPKKPV 174
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 1-127 2.56e-17

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: 74.02  E-value: 2.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   1 MKTNLGDIVVQTDVDMGPRAASNFVYLAKEGFYNGTIFHRVIPGFMIQGGDPTGTGMGGPGYKFDN----------DPTS 70
Cdd:cd01924     2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGFPDPETGKsrtipleikpEGQK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840  71 EPVYKK-------------------GFIAMANA--GRNTNGSQFFIMVADYPLPPD--------YSIFGKVIEGQDIADK 121
Cdd:cd01924    82 QPVYGKtleeagrydeqpvlpfnafGAIAMARTefDPNSASSQFFFLLKDNELTPSrnnvldgrYAVFGYVTDGLDILRE 161


                  ....*.
gi 2258828840 122 ISGVDR 127
Cdd:cd01924   162 LKVGDK 167
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 6-133 9.58e-17

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 72.56  E-value: 9.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258828840   6 GDIVVQTDVDMGPRAASNFVYLA-----KEGF---YNGTIFHRVIPGFMIQGGDPTGTG----MGGPGYKFDNDPTSEPV 73
Cdd:PLN03149   33 GRIKMELFADIAPKTAENFRQFCtgefrKAGLpqgYKGCQFHRVIKDFMIQGGDFLKGDgtgcVSIYGSKFEDENFIAKH 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258828840  74 YKKGFIAMANAGRNTNGSQFFIMVA--DYpLPPDYSIFGKVI-EGQDIADKISGVDRSGSDRP 133
Cdd:PLN03149  113 TGPGLLSMANSGPNTNGCQFFITCAkcDW-LDNKHVVFGRVLgDGLLVVRKIENVATGPNNRP 174
 
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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