NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530361577|ref|XP_005270419|]
View 

peptidyl-prolyl cis-trans isomerase H isoform X1 [Homo sapiens]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 240)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cyclophilin super family cl00197
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 8-177 2.49e-116

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


The actual alignment was detected with superfamily member PLN03149:

Pssm-ID: 469651  Cd Length: 186  Bit Score: 327.18  E-value: 2.49e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577   8 PVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGV 87
Cdd:PLN03149  16 PKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  88 ASIYRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKII-DGLLVMRKIENVPTGPNNKPK 166
Cdd:PLN03149  96 VSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPK 175

                        170
                 ....*....|.
gi 530361577 167 LPVVISQCGEM 177
Cdd:PLN03149 176 LACVISECGEM 186
 
Name Accession Description Interval E-value
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 8-177 2.49e-116

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 327.18  E-value: 2.49e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577   8 PVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGV 87
Cdd:PLN03149  16 PKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  88 ASIYRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKII-DGLLVMRKIENVPTGPNNKPK 166
Cdd:PLN03149  96 VSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPK 175

                        170
                 ....*....|.
gi 530361577 167 LPVVISQCGEM 177
Cdd:PLN03149 176 LACVISECGEM 186
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 11-175 3.35e-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: 326.14  E-value: 3.35e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  11 PVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGVASI 90
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  91 YRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGpNNKPKLPVV 170
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVV 159


                 ....*
gi 530361577 171 ISQCG 175
Cdd:cd01926  160 IADCG 164
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 25-176 5.20e-59

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: 180.91  E-value: 5.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577   25 GRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDFVNGDGTGvasIYRGPFADENF--KL 102
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCKKGF--------YDGTTFHRVIPGFMVQGGDPTGTGGGG---KSIFPIPDEIFplLL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530361577  103 RHSaPGLLSMANSGPS--TNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGpNNKPKLPVVISQCGE 176
Cdd:pfam00160  76 KHK-RGALSMANTGPApnSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 10-171 4.31e-51

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 161.11  E-value: 4.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  10 NPVVFFDVSiggqeVGRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDFvNGDGTGVAS 89
Cdd:COG0652    6 NPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLAKEGF--------YDGTIFHRVIPGFMIQGGDP-TGTGTGGPG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  90 iyrGPFADENFK-LRHsAPGLLSMANS-GPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKL 167
Cdd:COG0652   72 ---YTIPDEFDPgLKH-KRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLE 147


                 ....
gi 530361577 168 PVVI 171
Cdd:COG0652  148 PVVI 151
 
Name Accession Description Interval E-value
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 8-177 2.49e-116

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 327.18  E-value: 2.49e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577   8 PVNPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGV 87
Cdd:PLN03149  16 PKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDFMIQGGDFLKGDGTGC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  88 ASIYRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKII-DGLLVMRKIENVPTGPNNKPK 166
Cdd:PLN03149  96 VSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPK 175

                        170
                 ....*....|.
gi 530361577 167 LPVVISQCGEM 177
Cdd:PLN03149 176 LACVISECGEM 186
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 11-175 3.35e-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: 326.14  E-value: 3.35e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  11 PVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGVASI 90
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  91 YRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGpNNKPKLPVV 170
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVV 159


                 ....*
gi 530361577 171 ISQCG 175
Cdd:cd01926  160 IADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 10-177 1.50e-79

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 234.35  E-value: 1.50e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  10 NPVVFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGE-FRKDGVPIGYKGSTFHRVIKDFMIQGGDFVNGDGTGVA 88
Cdd:PTZ00060  15 RPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkVGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGGE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  89 SIYRGPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGpNNKPKLP 168
Cdd:PTZ00060  95 SIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQ-SGYPKKP 173


                 ....*....
gi 530361577 169 VVISQCGEM 177
Cdd:PTZ00060 174 VVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 24-172 1.18e-63

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: 192.48  E-value: 1.18e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  24 VGRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDFVNGDGTGvaSIYRGPFADENFK-L 102
Cdd:cd00317    6 KGRIVIELYGDEAPKTVENFLSLARGGF--------YDGTTFHRVIPGFMIQGGDPTGTGGGG--SGPGYKFPDENFPlK 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577 103 RHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVIS 172
Cdd:cd00317   76 YHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTIS 145
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 25-176 5.20e-59

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: 180.91  E-value: 5.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577   25 GRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDFVNGDGTGvasIYRGPFADENF--KL 102
Cdd:pfam00160   7 GRIVIELFGDKAPKTVENFLQLCKKGF--------YDGTTFHRVIPGFMVQGGDPTGTGGGG---KSIFPIPDEIFplLL 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530361577  103 RHSaPGLLSMANSGPS--TNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGpNNKPKLPVVISQCGE 176
Cdd:pfam00160  76 KHK-RGALSMANTGPApnSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 25-171 1.40e-51

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: 161.86  E-value: 1.40e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  25 GRMKIELFADVVPKTAENFRQFCtgefrKDGVpigYKGSTFHRVIKDFMIQGGDFVnGDGTGVASIYRGPFADE-NFKLR 103
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENFTTHA-----RNGY---YNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLK 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361577 104 HSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVI 171
Cdd:cd01927   78 HDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKI 145
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 10-171 4.31e-51

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 161.11  E-value: 4.31e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  10 NPVVFFDVSiggqeVGRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDFvNGDGTGVAS 89
Cdd:COG0652    6 NPTVTLETN-----KGDIVIELFPDKAPKTVANFVSLAKEGF--------YDGTIFHRVIPGFMIQGGDP-TGTGTGGPG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  90 iyrGPFADENFK-LRHsAPGLLSMANS-GPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKL 167
Cdd:COG0652   72 ---YTIPDEFDPgLKH-KRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLE 147


                 ....
gi 530361577 168 PVVI 171
Cdd:COG0652  148 PVVI 151
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 25-171 2.57e-50

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: 159.12  E-value: 2.57e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  25 GRMKIELFADVVPKTAENFRQFCtgefrKDGVpigYKGSTFHRVIKDFMIQGGDfVNGDGTGVASIYRGPFADE-NFKLR 103
Cdd:cd01923    9 GDLNLELHCDKAPKACENFIKLC-----KKGY---YDGTIFHRSIRNFMIQGGD-PTGTGRGGESIWGKPFKDEfKPNLS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361577 104 HSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVI 171
Cdd:cd01923   80 HDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKI 147
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 24-171 1.20e-49

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: 157.21  E-value: 1.20e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  24 VGRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDfVNGDGTGVASIYRGPFADENFK-L 102
Cdd:cd01928    9 LGDIKIELFCDDCPKACENFLALCASGY--------YNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDEFREtL 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530361577 103 RHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLPVVI 171
Cdd:cd01928   80 KHDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRI 148
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 24-171 6.38e-43

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: 139.98  E-value: 6.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  24 VGRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDfVNGDGTGVASIYRGPFADE-NFKL 102
Cdd:cd01922    6 MGEITLELYWNHAPKTCKNFYELAKRGY--------YNGTIFHRLIKDFMIQGGD-PTGTGRGGASIYGKKFEDEiHPEL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530361577 103 RHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGpNNKPKLPVVI 171
Cdd:cd01922   77 KHTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKI 144
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 24-174 1.58e-42

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: 139.79  E-value: 1.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  24 VGRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDfVNGDGTGVASIYRGPFADE-NFKL 102
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCLEGY--------YDNTIFHRVVPGFIIQGGD-PTGTGTGGESIYGEPFKDEfHSRL 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530361577 103 RHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKII-DGLLVMRKIENVPTGPNNKPKLPVVISQC 174
Cdd:cd01925   85 RFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTgDTIYNLLKLAEVETDKDERPVYPPKITSV 157
PTZ00221 PTZ00221
cyclophilin; Provisional
 13-177 6.56e-38

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 130.37  E-value: 6.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  13 VFFDVSIGGQEVGRMKIELFADVVPKTAENFRQFCTGEFRKD---GVPIGYKGSTFHRV-IKDFMIQGGDFvngDGTGVA 88
Cdd:PTZ00221  55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCGIDtntGVKLDYLYTPVHHVdRNNNIIVLGEL---DSFNVS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  89 SIYRgPFADENFKLRHSAPGLLSMANSGPSTNGCQFFITCSKCDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKPKLP 168
Cdd:PTZ00221 132 STGT-PIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLLP 210


                 ....*....
gi 530361577 169 VVISQCGEM 177
Cdd:PTZ00221 211 VTVSFCGAL 219
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 24-165 2.73e-28

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: 103.19  E-value: 2.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  24 VGRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDfVNGDGTGVASIY-----RGP--FA 96
Cdd:cd01921    6 LGDLVIDLFTDECPLACLNFLKLCKLKY--------YNFCLFYNVQKDFIAQTGD-PTGTGAGGESIYsqlygRQArfFE 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530361577  97 DE-NFKLRHSAPGLLSMANSGPSTNGCQFFITCSK-CDWLDGKHVVFGKIIDGLLVMRKIENVPTGPNNKP 165
Cdd:cd01921   77 PEiLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRP 147
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 25-171 7.54e-23

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: 89.04  E-value: 7.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  25 GRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDFvNGDGTGVASIyrGPFADE-NFKLR 103
Cdd:cd01920    7 GDIVVELYDDKAPITVENFLAYVRKGF--------YDNTIFHRVISGFVIQGGGF-TPDLAQKETL--KPIKNEaGNGLS 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361577 104 HSApGLLSMANSG-PSTNGCQFFITCSKCDWLD-----GKHVVFGKIIDGLLVMRKIENVPTGPNNK----PKLPVVI 171
Cdd:cd01920   76 NTR-GTIAMARTNaPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYSFGSyqdvPVQDVII 152
PRK10903 PRK10903
peptidylprolyl isomerase A;
24-171 2.41e-15

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 70.26  E-value: 2.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  24 VGRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDFvNGDGTGVASiyRGPFADENFKLR 103
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYVNSGF--------YNNTTFHRVIPGFMIQGGGF-TEQMQQKKP--NPPIKNEADNGL 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530361577 104 HSAPGLLSMANSGPSTNG-CQFFITCSKCDWLD-GK----HVVFGKIIDGLLVMRKIENVPT---GP-NNKPKLPVVI 171
Cdd:PRK10903 106 RNTRGTIAMARTADKDSAtSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPThdvGPyQNVPSKPVVI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
25-173 1.50e-14

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 67.56  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  25 GRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGDFVNGDGTGVAsiyRGPFADENFKLRH 104
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCREGF--------YNNTIFHRVINGFMIQGGGFEPGMKQKAT---KEPIKNEANNGLK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577 105 SAPGLLSMANSG-PSTNGCQFFITCSKCDWLDGK--------HVVFGKIIDGLLVMRKIENVPTGPN----NKPKLPVVI 171
Cdd:PRK10791  78 NTRGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSgmhqDVPKEDVII 157


                 ..
gi 530361577 172 SQ 173
Cdd:PRK10791 158 ES 159
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 25-155 2.31e-12

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: 62.08  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  25 GRMKIELFADVVPKTAENFRQFCTGEFrkdgvpigYKGSTFHRVIKDFMIQGGD--FVNGDG----TGVAS--------- 89
Cdd:cd01924    7 GTITIVLDGYNAPVTAGNFVDLVERGF--------YDGMEFHRVEGGFVVQTGDpqGKNPGFpdpeTGKSRtipleikpe 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530361577  90 -----IYRGPFA-----DENFKLRHSAPGLLSMA------NSGPStngcQFFI-------TCSKCDWLDGKHVVFGKIID 146
Cdd:cd01924   79 gqkqpVYGKTLEeagryDEQPVLPFNAFGAIAMArtefdpNSASS----QFFFllkdnelTPSRNNVLDGRYAVFGYVTD 154


                 ....*....
gi 530361577 147 GLLVMRKIE 155
Cdd:cd01924  155 GLDILRELK 163
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH