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Conserved domains on  [gi|21357783|ref|NP_648697|]
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uncharacterized protein Dmel_CG7768, isoform B [Drosophila melanogaster]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112519)

cyclophilin-type peptidylprolyl isomerase 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:0003755|GO:0006457
PubMed:  14731520|15998457|15353287

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 4-162 1.29e-114

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: 321.51  E-value: 1.29e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   4 PRVYFDIAAGGEKLGRIVMELRSDVVPKTAENFRALCTGEKG-----YGYKGSPFHRVIPNFMCQGGDFTNQNGTGGRSI 78
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  79 YGNKFPDENFELKHTGAGVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDGKTSKKVII 158
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 21357783 159 EDCG 162
Cdd:cd01926 161 ADCG 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 ...
 4-162 1.29e-114

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: 321.51  E-value: 1.29e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   4 PRVYFDIAAGGEKLGRIVMELRSDVVPKTAENFRALCTGEKG-----YGYKGSPFHRVIPNFMCQGGDFTNQNGTGGRSI 78
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  79 YGNKFPDENFELKHTGAGVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDGKTSKKVII 158
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 21357783 159 EDCG 162
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-164 1.21e-91

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 264.40  E-value: 1.21e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783    1 MSLPRVYFDIAAGGEKLGRIVMELRSDVVPKTAENFRALCTGE------KGYGYKGSPFHRVIPNFMCQGGDFTNQNGTG 74
Cdd:PTZ00060  13 SKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   75 GRSIYGNKFPDENFELKHTGAGVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDGKTSK 154
Cdd:PTZ00060  93 GESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKK 172

                        170
                 ....*....|
gi 21357783  155 KVIIEDCGAL 164
Cdd:PTZ00060 173 PVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 17-162 3.03e-60

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: 183.61  E-value: 3.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783    17 LGRIVMELRSDVVPKTAENFRALCTgeKGYgYKGSPFHRVIPNFMCQGGDFTnqnGTGGRSIYGNKFPDENF--ELKHtG 94
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFplLLKH-K 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783    95 AGVLSMANAGA--NTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDGKTSKKVIIEDCG 162
Cdd:pfam00160  79 RGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 17-159 1.06e-53

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 167.27  E-value: 1.06e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCtgEKGYgYKGSPFHRVIPNFMCQGGDFTNqNGTGGRsiyGNKFPDENF-ELKHTgA 95
Cdd:COG0652  15 KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GYTIPDEFDpGLKHK-R 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21357783  96 GVLSMANA-GANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDG-KTSKKVIIE 159
Cdd:COG0652  87 GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEPVVIE 152
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 4-162 1.29e-114

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: 321.51  E-value: 1.29e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   4 PRVYFDIAAGGEKLGRIVMELRSDVVPKTAENFRALCTGEKG-----YGYKGSPFHRVIPNFMCQGGDFTNQNGTGGRSI 78
Cdd:cd01926   1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGkggkpFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  79 YGNKFPDENFELKHTGAGVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDGKTSKKVII 158
Cdd:cd01926  81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKVVI 160


                ....
gi 21357783 159 EDCG 162
Cdd:cd01926 161 ADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-164 1.21e-91

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 264.40  E-value: 1.21e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783    1 MSLPRVYFDIAAGGEKLGRIVMELRSDVVPKTAENFRALCTGE------KGYGYKGSPFHRVIPNFMCQGGDFTNQNGTG 74
Cdd:PTZ00060  13 SKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   75 GRSIYGNKFPDENFELKHTGAGVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDGKTSK 154
Cdd:PTZ00060  93 GESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPKK 172

                        170
                 ....*....|
gi 21357783  155 KVIIEDCGAL 164
Cdd:PTZ00060 173 PVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 4-164 1.23e-70

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 211.23  E-value: 1.23e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783    4 PRVYFDIAAGGEKLGRIVMELRSDVVPKTAENFRALCTGE-----KGYGYKGSPFHRVIPNFMCQGGDFTNQNGTGGRSI 78
Cdd:PLN03149  19 PVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEfrkagLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGCVSI 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   79 YGNKFPDENFELKHTGAGVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVV-EGMDIVQKVESYGS-QDGKTSKKV 156
Cdd:PLN03149  99 YGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATgPNNRPKLAC 178


                 ....*...
gi 21357783  157 IIEDCGAL 164
Cdd:PLN03149 179 VISECGEM 186
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 18-160 4.24e-65

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: 195.56  E-value: 4.24e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  18 GRIVMELRSDVVPKTAENFRALCTGEkgyGYKGSPFHRVIPNFMCQGGDFTNqnGTGGRSIYGNKFPDENFELK-HTGAG 96
Cdd:cd00317   7 GRIVIELYGDEAPKTVENFLSLARGG---FYDGTTFHRVIPGFMIQGGDPTG--TGGGGSGPGYKFPDENFPLKyHHRRG 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21357783  97 VLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVES-YGSQDGKTSKKVIIED 160
Cdd:cd00317  82 TLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERgDTDENGRPIKPVTISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 17-162 3.03e-60

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: 183.61  E-value: 3.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783    17 LGRIVMELRSDVVPKTAENFRALCTgeKGYgYKGSPFHRVIPNFMCQGGDFTnqnGTGGRSIYGNKFPDENF--ELKHtG 94
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCK--KGF-YDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEIFplLLKH-K 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783    95 AGVLSMANAGA--NTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDGKTSKKVIIEDCG 162
Cdd:pfam00160  79 RGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 17-159 1.06e-53

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 167.27  E-value: 1.06e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCtgEKGYgYKGSPFHRVIPNFMCQGGDFTNqNGTGGRsiyGNKFPDENF-ELKHTgA 95
Cdd:COG0652  15 KGDIVIELFPDKAPKTVANFVSLA--KEGF-YDGTIFHRVIPGFMIQGGDPTG-TGTGGP---GYTIPDEFDpGLKHK-R 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21357783  96 GVLSMANA-GANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDG-KTSKKVIIE 159
Cdd:COG0652  87 GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGdGPLEPVVIE 152
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 17-151 5.50e-50

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: 157.31  E-value: 5.50e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCTgeKGYgYKGSPFHRVIPNFMCQGGDFTNqNGTGGRSIYGNKFPDE-NFELKHTGA 95
Cdd:cd01922   6 MGEITLELYWNHAPKTCKNFYELAK--RGY-YNGTIFHRLIKDFMIQGGDPTG-TGRGGASIYGKKFEDEiHPELKHTGA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21357783  96 GVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDGK 151
Cdd:cd01922  82 GILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDR 137
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 17-155 4.35e-49

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: 155.31  E-value: 4.35e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCtgEKGYgYKGSPFHRVIPNFMCQGGDFTNQnGTGGRSIYGNKFPDE-NFELKHTGA 95
Cdd:cd01927   6 KGDIHIRLFPEEAPKTVENFTTHA--RNGY-YNNTIFHRVIKGFMIQTGDPTGD-GTGGESIWGKEFEDEfSPSLKHDRP 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  96 GVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVEsygsqDGKTSKK 155
Cdd:cd01927  82 YTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIE-----NVKTDKN 136
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 17-160 1.23e-48

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: 154.50  E-value: 1.23e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCtgEKGYgYKGSPFHRVIPNFMCQGGDFTNqNGTGGRSIYGNKFPDE-NFELKHTGA 95
Cdd:cd01923   8 KGDLNLELHCDKAPKACENFIKLC--KKGY-YDGTIFHRSIRNFMIQGGDPTG-TGRGGESIWGKPFKDEfKPNLSHDGR 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21357783  96 GVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQDG-KTSKKVIIED 160
Cdd:cd01923  84 GVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTdRPKEEIKIED 149
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 17-160 2.87e-45

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: 145.66  E-value: 2.87e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCTGekGYgYKGSPFHRVIPNFMCQGGDFTNqNGTGGRSIYGNKFPDENFE-LKHTGA 95
Cdd:cd01928   9 LGDIKIELFCDDCPKACENFLALCAS--GY-YNGCIFHRNIKGFMVQTGDPTG-TGKGGESIWGKKFEDEFREtLKHDSR 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21357783  96 GVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESygSQDGKTSKK---VIIED 160
Cdd:cd01928  85 GVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEK--LPVDKKYRPleeIRIKD 150
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 17-133 1.14e-38

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: 129.39  E-value: 1.14e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCTgeKGYgYKGSPFHRVIPNFMCQGGDFTNqNGTGGRSIYGNKFPDE-NFELKHTGA 95
Cdd:cd01925  14 AGDIDIELWSKEAPKACRNFIQLCL--EGY-YDNTIFHRVVPGFIIQGGDPTG-TGTGGESIYGEPFKDEfHSRLRFNRR 89

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 21357783  96 GVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVV 133
Cdd:cd01925  90 GLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVT 127
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 17-142 6.78e-32

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: 112.05  E-value: 6.78e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCtgeKGYGYKGSPFHRVIPNFMCQGGDFTNqNGTGGRSIYGNKFPDE--NFE----- 89
Cdd:cd01921   6 LGDLVIDLFTDECPLACLNFLKLC---KLKYYNFCLFYNVQKDFIAQTGDPTG-TGAGGESIYSQLYGRQarFFEpeilp 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21357783  90 -LKHTGAGVLSMANAGANTNGSQFFICTGK-TTWLDNKHVVFGKVVEGMDIVQKV 142
Cdd:cd01921  82 lLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKI 136
PTZ00221 PTZ00221
cyclophilin; Provisional
 5-164 1.47e-28

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 105.72  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783    5 RVYFDIAAGGEKLGRIVMELRSDVVPKTAENFRALCTGEKG--------YGYKGSPFHRVIPNF-MCQGGDFTNQNgtgg 75
Cdd:PTZ00221  54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGidtntgvkLDYLYTPVHHVDRNNnIIVLGELDSFN---- 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   76 RSIYGNKFPDENFELKHTGAGVLSMANAGANTNGSQFFICTGKTTWLDNKHVVFGKVVEGMDIVQKVESYGSQD-GKTSK 154
Cdd:PTZ00221 130 VSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDvGRPLL 209

                        170
                 ....*....|
gi 21357783  155 KVIIEDCGAL 164
Cdd:PTZ00221 210 PVTVSFCGAL 219
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 17-144 1.82e-21

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: 84.80  E-value: 1.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783  17 LGRIVMELRSDVVPKTAENFRALCtgEKGYgYKGSPFHRVIPNFMCQGGDFTNQngtGGRSIYGNKFPDE-NFELKHTgA 95
Cdd:cd01920   6 LGDIVVELYDDKAPITVENFLAYV--RKGF-YDNTIFHRVISGFVIQGGGFTPD---LAQKETLKPIKNEaGNGLSNT-R 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21357783  96 GVLSMANAGANTNG-SQFFICTGKTTWLDNK-----HVVFGKVVEGMDIVQKVES 144
Cdd:cd01920  79 GTIAMARTNAPDSAtSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAG 133
PRK10903 PRK10903
peptidylprolyl isomerase A;
18-149 9.06e-16

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 71.03  E-value: 9.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   18 GRIVMELRSDVVPKTAENFRALCtgEKGYgYKGSPFHRVIPNFMCQGGDFTnqngtggrsiygnkfpdENFELKHTGA-- 95
Cdd:PRK10903  38 GNIELELNSQKAPVSVKNFVDYV--NSGF-YNNTTFHRVIPGFMIQGGGFT-----------------EQMQQKKPNPpi 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21357783   96 ------------GVLSMA-NAGANTNGSQFFICTGKTTWLDN-----KHVVFGKVVEGMDIVQKVESYGSQD 149
Cdd:PRK10903  98 kneadnglrntrGTIAMArTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHD 169
PRK10791 PRK10791
peptidylprolyl isomerase B;
18-160 2.04e-10

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 56.00  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357783   18 GRIVMELRSDVVPKTAENFRALCTgeKGYgYKGSPFHRVIPNFMCQGGDFtnQNGTGGRSIYGNKFPDENFELKHTgAGV 97
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCR--EGF-YNNTIFHRVINGFMIQGGGF--EPGMKQKATKEPIKNEANNGLKNT-RGT 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21357783   98 LSMANAGA-NTNGSQFFICTGKTTWLDNK--------HVVFGKVVEGMDIVQKVESYGSQDGKTSKKVIIED 160
Cdd:PRK10791  83 LAMARTQApHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKED 154
 
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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