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Conserved domains on  [gi|452001633|gb|EMD94092|]
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hypothetical protein COCHEDRAFT_1201904 [Bipolaris maydis C5]

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 ...
 4-169 8.40e-116

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: 324.98  E-value: 8.40e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   4 PRVFFDVSIGGDPAGRIVMELYADKVPKTAENFRALCTGEKGTGksGKPLHYEGSVFHRVIPQFMLQGGDFTRGNGTGGE 83
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  84 SIYGEKFEDENFKLSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTGKTSKVV 163
Cdd:cd01926   79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                 ....*.
gi 452001633 164 KIEKSG 169
Cdd:cd01926  159 VIADCG 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 ...
 4-169 8.40e-116

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: 324.98  E-value: 8.40e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   4 PRVFFDVSIGGDPAGRIVMELYADKVPKTAENFRALCTGEKGTGksGKPLHYEGSVFHRVIPQFMLQGGDFTRGNGTGGE 83
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  84 SIYGEKFEDENFKLSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTGKTSKVV 163
Cdd:cd01926   79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                 ....*.
gi 452001633 164 KIEKSG 169
Cdd:cd01926  159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-171 1.05e-101

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 289.82  E-value: 1.05e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   1 MSNPRVFFDVSIGGDPAGRIVMELYADKVPKTAENFRALCTGEKgTGKSGKPLHYEGSVFHRVIPQFMLQGGDFTRGNGT 80
Cdd:PTZ00060  13 SKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  81 GGESIYGEKFEDENFKLSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTGKTS 160
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171

                        170
                 ....*....|.
gi 452001633 161 KVVKIEKSGQL 171
Cdd:PTZ00060 172 KPVVVTDCGEL 182
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 15-169 5.42e-58

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: 178.22  E-value: 5.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   15 DPAGRIVMELYADKVPKTAENFRALCTgeKGtgksgkplHYEGSVFHRVIPQFMLQGGDFTrgnGTGGESIYGEKFEDEN 94
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEI 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 452001633   95 F--KLSHtGPGVLSMANAG--PGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTGKTSKVVKIEKSG 169
Cdd:pfam00160  71 FplLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-167 3.00e-57

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 176.51  E-value: 3.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   1 MSNPRVFFDVSiggdpAGRIVMELYADKVPKTAENFRALCtgekgtgKSGkplHYEGSVFHRVIPQFMLQGGDFTrGNGT 80
Cdd:COG0652    4 APNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA-------KEG---FYDGTIFHRVIPGFMIQGGDPT-GTGT 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  81 GGEsiyGEKFEDENFK-LSHTgPGVLSMANA-GPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTG- 157
Cdd:COG0652   68 GGP---GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGd 143

                        170
                 ....*....|
gi 452001633 158 KTSKVVKIEK 167
Cdd:COG0652  144 GPLEPVVIES 153
 
Name Accession Description Interval E-value
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 4-169 8.40e-116

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: 324.98  E-value: 8.40e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   4 PRVFFDVSIGGDPAGRIVMELYADKVPKTAENFRALCTGEKGTGksGKPLHYEGSVFHRVIPQFMLQGGDFTRGNGTGGE 83
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKG--GKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  84 SIYGEKFEDENFKLSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTGKTSKVV 163
Cdd:cd01926   79 SIYGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGNGKPKKKV 158


                 ....*.
gi 452001633 164 KIEKSG 169
Cdd:cd01926  159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 1-171 1.05e-101

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 289.82  E-value: 1.05e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   1 MSNPRVFFDVSIGGDPAGRIVMELYADKVPKTAENFRALCTGEKgTGKSGKPLHYEGSVFHRVIPQFMLQGGDFTRGNGT 80
Cdd:PTZ00060  13 SKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDK-VGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  81 GGESIYGEKFEDENFKLSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTGKTS 160
Cdd:PTZ00060  92 GGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQSGYPK 171

                        170
                 ....*....|.
gi 452001633 161 KVVKIEKSGQL 171
Cdd:PTZ00060 172 KPVVVTDCGEL 182
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 2-161 5.97e-78

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 230.11  E-value: 5.97e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   2 SNPRVFFDVSIGGDPAGRIVMELYADKVPKTAENFRALCTGEkgTGKSGKPLHYEGSVFHRVIPQFMLQGGDFTRGNGTG 81
Cdd:PLN03149  17 KNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGE--FRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  82 GESIYGEKFEDENFKLSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVV-EGMDVVQAVEKVgsQTGKTS 160
Cdd:PLN03149  95 CVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENV--ATGPNN 172


                 .
gi 452001633 161 K 161
Cdd:PLN03149 173 R 173
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 7-167 1.36e-64

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: 194.79  E-value: 1.36e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   7 FFDVSIGgdpagRIVMELYADKVPKTAENFRALCTGEkgtgksgkplHYEGSVFHRVIPQFMLQGGDFTrgNGTGGESIY 86
Cdd:cd00317    1 TLDTTKG-----RIVIELYGDEAPKTVENFLSLARGG----------FYDGTTFHRVIPGFMIQGGDPT--GTGGGGSGP 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  87 GEKFEDENFKLS-HTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVG-SQTGKTSKVVK 164
Cdd:cd00317   64 GYKFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDtDENGRPIKPVT 143


                 ...
gi 452001633 165 IEK 167
Cdd:cd00317  144 ISD 146
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 15-169 5.42e-58

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: 178.22  E-value: 5.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   15 DPAGRIVMELYADKVPKTAENFRALCTgeKGtgksgkplHYEGSVFHRVIPQFMLQGGDFTrgnGTGGESIYGEKFEDEN 94
Cdd:pfam00160   4 NGLGRIVIELFGDKAPKTVENFLQLCK--KG--------FYDGTTFHRVIPGFMVQGGDPT---GTGGGGKSIFPIPDEI 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 452001633   95 F--KLSHtGPGVLSMANAG--PGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTGKTSKVVKIEKSG 169
Cdd:pfam00160  71 FplLLKH-KRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDGDRPVKPVKILSCG 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 1-167 3.00e-57

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 176.51  E-value: 3.00e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   1 MSNPRVFFDVSiggdpAGRIVMELYADKVPKTAENFRALCtgekgtgKSGkplHYEGSVFHRVIPQFMLQGGDFTrGNGT 80
Cdd:COG0652    4 APNPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLA-------KEG---FYDGTIFHRVIPGFMIQGGDPT-GTGT 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  81 GGEsiyGEKFEDENFK-LSHTgPGVLSMANA-GPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTG- 157
Cdd:COG0652   68 GGP---GYTIPDEFDPgLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGd 143

                        170
                 ....*....|
gi 452001633 158 KTSKVVKIEK 167
Cdd:COG0652  144 GPLEPVVIES 153
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 18-161 4.24e-54

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: 168.02  E-value: 4.24e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  18 GRIVMELYADKVPKTAENFRALCtgekgtgKSGkplHYEGSVFHRVIPQFMLQGGDFTrGNGTGGESIYGEKFEDE-NFK 96
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENFTTHA-------RNG---YYNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPS 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 452001633  97 LSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVgsQTGKTSK 161
Cdd:cd01927   76 LKHDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENV--KTDKNDR 138
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 18-167 3.44e-53

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: 165.79  E-value: 3.44e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  18 GRIVMELYADKVPKTAENFRALCTgeKGtgksgkplHYEGSVFHRVIPQFMLQGGDFTrGNGTGGESIYGEKFEDE-NFK 96
Cdd:cd01922    7 GEITLELYWNHAPKTCKNFYELAK--RG--------YYNGTIFHRLIKDFMIQGGDPT-GTGRGGASIYGKKFEDEiHPE 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 452001633  97 LSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQTGKTSKVVKIEK 167
Cdd:cd01922   76 LKHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQTDRPIDEVKILK 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 18-166 1.14e-52

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: 164.90  E-value: 1.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  18 GRIVMELYADKVPKTAENFRALCtgEKGtgksgkplHYEGSVFHRVIPQFMLQGGDFTrGNGTGGESIYGEKFEDE-NFK 96
Cdd:cd01923    9 GDLNLELHCDKAPKACENFIKLC--KKG--------YYDGTIFHRSIRNFMIQGGDPT-GTGRGGESIWGKPFKDEfKPN 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 452001633  97 LSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVGSQ-TGKTSKVVKIE 166
Cdd:cd01923   78 LSHDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPgTDRPKEEIKIE 148
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 18-161 1.70e-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: 146.43  E-value: 1.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  18 GRIVMELYADKVPKTAENFRALCTgekgtgkSGkplHYEGSVFHRVIPQFMLQGGDFTrGNGTGGESIYGEKFEDENFK- 96
Cdd:cd01928   10 GDIKIELFCDDCPKACENFLALCA-------SG---YYNGCIFHRNIKGFMVQTGDPT-GTGKGGESIWGKKFEDEFREt 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 452001633  97 LSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKVgsQTGKTSK 161
Cdd:cd01928   79 LKHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKL--PVDKKYR 141
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 17-140 8.18e-39

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: 130.16  E-value: 8.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  17 AGRIVMELYADKVPKTAENFRALCTGEkgtgksgkplHYEGSVFHRVIPQFMLQGGDFTrGNGTGGESIYGEKFEDE-NF 95
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCLEG----------YYDNTIFHRVVPGFIIQGGDPT-GTGTGGESIYGEPFKDEfHS 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 452001633  96 KLSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVV 140
Cdd:cd01925   83 RLRFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVT 127
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 18-147 9.75e-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: 111.66  E-value: 9.75e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  18 GRIVMELYADKVPKTAENFRALCtgekgtgksgKPLHYEGSVFHRVIPQFMLQGGDFTrGNGTGGESIYGEK-------F 90
Cdd:cd01921    7 GDLVIDLFTDECPLACLNFLKLC----------KLKYYNFCLFYNVQKDFIAQTGDPT-GTGAGGESIYSQLygrqarfF 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 452001633  91 EDE-NFKLSHTGPGVLSMANAGPGTNGSQFFICTVK-TSWLDGKHVVFGQVVEGMDVVQ 147
Cdd:cd01921   76 EPEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLE 134
PTZ00221 PTZ00221
cyclophilin; Provisional
 5-152 1.95e-28

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 105.72  E-value: 1.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633   5 RVFFDVSIGGDPAGRIVMELYADKVPKTAENFRALCTGEKGTGK-SGKPLHYEGSVFHRVipqfmlqggDFTRGNGTGGE 83
Cdd:PTZ00221  54 RAFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDTnTGVKLDYLYTPVHHV---------DRNNNIIVLGE 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 452001633  84 ------SIYGEKFEDENFKLSHTGPGVLSMANAGPGTNGSQFFICTVKTSWLDGKHVVFGQVVEGMDVVQAVEKV 152
Cdd:PTZ00221 125 ldsfnvSSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESL 199
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 17-152 1.30e-24

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: 93.28  E-value: 1.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  17 AGRIVMELYADKVPKTAENFRALCtgEKGtgksgkplHYEGSVFHRVIPQFMLQGGDFTrGNGTGGESIYGEKFEDENfK 96
Cdd:cd01920    6 LGDIVVELYDDKAPITVENFLAYV--RKG--------FYDNTIFHRVISGFVIQGGGFT-PDLAQKETLKPIKNEAGN-G 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 452001633  97 LSHTGpGVLSMA-NAGPGTNGSQFFICTVKTSWLD-----GKHVVFGQVVEGMDVVQAVEKV 152
Cdd:cd01920   74 LSNTR-GTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGV 134
PRK10903 PRK10903
peptidylprolyl isomerase A;
17-156 2.63e-15

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 69.87  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  17 AGRIVMELYADKVPKTAENFRALCTgekgtgkSGkplHYEGSVFHRVIPQFMLQGGDFTRG--NGTGGESIygeKFEDEN 94
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYVN-------SG---FYNNTTFHRVIPGFMIQGGGFTEQmqQKKPNPPI---KNEADN 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 452001633  95 fKLSHTgPGVLSMA-NAGPGTNGSQFFICTVKTSWLD-GK----HVVFGQVVEGMDVVQAVEKVGSQT 156
Cdd:PRK10903 104 -GLRNT-RGTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHD 169
PRK10791 PRK10791
peptidylprolyl isomerase B;
18-159 6.44e-14

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 65.63  E-value: 6.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  18 GRIVMELYADKVPKTAENFRALCtgekgtgKSGkplHYEGSVFHRVIPQFMLQGGDFTRG--NGTGGESIYGEKfedeNF 95
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYC-------REG---FYNNTIFHRVINGFMIQGGGFEPGmkQKATKEPIKNEA----NN 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 452001633  96 KLSHTgPGVLSMANAG-PGTNGSQFFICTVKTSWLDGK--------HVVFGQVVEGMDVVQAVEKVgsQTGKT 159
Cdd:PRK10791  75 GLKNT-RGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGV--ATGRS 144
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 18-153 2.37e-10

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: 56.30  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  18 GRIVMELYADKVPKTAENFRALCtgEKGTgksgkplhYEGSVFHRVIPQFMLQGGD-FTRGNG-----TG---------- 81
Cdd:cd01924    7 GTITIVLDGYNAPVTAGNFVDLV--ERGF--------YDGMEFHRVEGGFVVQTGDpQGKNPGfpdpeTGksrtipleik 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 452001633  82 ----GESIYGEKFE-----DENFKLSHTGPGVLSMANA--GPGTNGSQFFI-------CTVKTSWLDGKHVVFGQVVEGM 143
Cdd:cd01924   77 pegqKQPVYGKTLEeagryDEQPVLPFNAFGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGL 156

                        170
                 ....*....|
gi 452001633 144 DVVQAVeKVG 153
Cdd:cd01924  157 DILREL-KVG 165
 
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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