|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10903 |
PRK10903 |
peptidylprolyl isomerase A; |
1-190 |
2.12e-140 |
|
peptidylprolyl isomerase A;
Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 388.82 E-value: 2.12e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 1 MFKSTLAAMAAVFALSALSPAAMAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQ 80
Cdd:PRK10903 1 MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160
Cdd:PRK10903 81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160
|
170 180 190
....*....|....*....|....*....|
gi 15833468 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
Cdd:PRK10903 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
|
|
| cyclophilin_EcCYP_like |
cd01920 |
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ... |
32-186 |
4.03e-86 |
|
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: 250.44 E-value: 4.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 32 LLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGT 111
Cdd:cd01920 1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833468 112 IAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSA 186
Cdd:cd01920 81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
|
|
| PpiB |
COG0652 |
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
23-189 |
1.04e-80 |
|
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 236.61 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 23 MAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQkKPNPPIKNEAD 102
Cdd:COG0652 1 MKAAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTG-GPGYTIPDEFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 103 NGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHDvgpyQNVPSKPVV 182
Cdd:COG0652 80 PGLKHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLDG-----GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVV 150
|
....*..
gi 15833468 183 ILSAKVL 189
Cdd:COG0652 151 IESVTIV 157
|
|
| Pro_isomerase |
pfam00160 |
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
34-188 |
1.26e-63 |
|
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: 193.24 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 34 TTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADN-GLRNTRGTI 112
Cdd:pfam00160 3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEIFPlLLKHKRGAL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833468 113 AMART-ADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHDvgpyqNVPSKPVVILSAKV 188
Cdd:pfam00160 83 SMANTgPAPNSNGSQFFITLGPAPHLDG-----KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSCGV 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10903 |
PRK10903 |
peptidylprolyl isomerase A; |
1-190 |
2.12e-140 |
|
peptidylprolyl isomerase A;
Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 388.82 E-value: 2.12e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 1 MFKSTLAAMAAVFALSALSPAAMAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQ 80
Cdd:PRK10903 1 MFKSTLAAMAAVFALSALSPAALAAKGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160
Cdd:PRK10903 81 GGGFTEQMQQKKPNPPIKNEADNGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVAD 160
|
170 180 190
....*....|....*....|....*....|
gi 15833468 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
Cdd:PRK10903 161 KISQVPTHDVGPYQNVPSKPVVILSAKVLP 190
|
|
| cyclophilin_EcCYP_like |
cd01920 |
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ... |
32-186 |
4.03e-86 |
|
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: 250.44 E-value: 4.03e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 32 LLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRGT 111
Cdd:cd01920 1 EFQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETLKPIKNEAGNGLSNTRGT 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833468 112 IAMARTADKDSATSQFFINVADNAFLDHGQRDFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSA 186
Cdd:cd01920 81 IAMARTNAPDSATSQFFINLKDNASLDYQNEQWGYTVFGEVTEGMDVVDKIAGVETYSFGSYQDVPVQDVIIESA 155
|
|
| PpiB |
COG0652 |
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
23-189 |
1.04e-80 |
|
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 236.61 E-value: 1.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 23 MAAKGDPHVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQkKPNPPIKNEAD 102
Cdd:COG0652 1 MKAAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTG-GPGYTIPDEFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 103 NGLRNTRGTIAMARTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHDvgpyQNVPSKPVV 182
Cdd:COG0652 80 PGLKHKRGTLAMARAQGPNSAGSQFFIVLGDNPHLDG-----GYTVFGKVVEGMDVVDKIAAGPTDP----GDGPLEPVV 150
|
....*..
gi 15833468 183 ILSAKVL 189
Cdd:COG0652 151 IESVTIV 157
|
|
| Pro_isomerase |
pfam00160 |
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
34-188 |
1.26e-63 |
|
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: 193.24 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 34 TTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADN-GLRNTRGTI 112
Cdd:pfam00160 3 TNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFPIPDEIFPlLLKHKRGAL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15833468 113 AMART-ADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHDvgpyqNVPSKPVVILSAKV 188
Cdd:pfam00160 83 SMANTgPAPNSNGSQFFITLGPAPHLDG-----KYTVFGKVVEGMDVLEKIEKVPTDG-----DRPVKPVKILSCGV 149
|
|
| PRK10791 |
PRK10791 |
peptidylprolyl isomerase B; |
31-188 |
3.68e-59 |
|
peptidylprolyl isomerase B;
Pssm-ID: 182734 Cd Length: 164 Bit Score: 182.35 E-value: 3.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 31 VLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGLRNTRG 110
Cdd:PRK10791 2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKATKEPIKNEANNGLKNTRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 111 TIAMARTADKDSATSQFFINVADNAFLD-HGQR--DFGYAVFGKVVKGMDVADKISQVPTHDVGPYQNVPSKPVVILSAK 187
Cdd:PRK10791 82 TLAMARTQAPHSATAQFFINVVDNDFLNfSGESlqGWGYCVFAEVVEGMDVVDKIKGVATGRSGMHQDVPKEDVIIESVT 161
|
.
gi 15833468 188 V 188
Cdd:PRK10791 162 V 162
|
|
| cyclophilin |
cd00317 |
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ... |
33-185 |
1.49e-52 |
|
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing.
Pssm-ID: 238194 [Multi-domain] Cd Length: 146 Bit Score: 164.74 E-value: 1.49e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 33 LTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQ-MQQKKPNPPIKNE-ADNGLRNTRG 110
Cdd:cd00317 2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTgGGGSGPGYKFPDEnFPLKYHHRRG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833468 111 TIAMARtADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPThdvgPYQNVPSKPVVILS 185
Cdd:cd00317 82 TLSMAN-AGPNTNGSQFFITTAPTPHLD-GK----HTVFGKVVEGMDVVDKIERGDT----DENGRPIKPVTISD 146
|
|
| cyclophilin_RING |
cd01923 |
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
30-189 |
3.42e-29 |
|
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: 105.58 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 30 HVLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFT------EQMQQKkpnpPIKNEADN 103
Cdd:cd01923 1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTgtgrggESIWGK----PFKDEFKP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 104 GLRNT-RGTIAMARTAdKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHDvgpyQNVPSKPVV 182
Cdd:cd01923 77 NLSHDgRGVLSMANSG-PNTNGSQFFITYRSCKHLDG-----KHTVFGRVVGGLETLEAMENVPDPG----TDRPKEEIK 146
|
....*..
gi 15833468 183 ILSAKVL 189
Cdd:cd01923 147 IEDTSVF 153
|
|
| cyclophilin_WD40 |
cd01927 |
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
32-176 |
4.42e-28 |
|
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: 102.54 E-value: 4.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 32 LLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKP--NPPIKNEADNGLRNTR 109
Cdd:cd01927 1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESiwGKEFEDEFSPSLKHDR 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15833468 110 -GTIAMArTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPT-HDVGPYQNV 176
Cdd:cd01927 81 pYTLSMA-NAGPNTNGSQFFITTVATPWLDN-----KHTVFGRVVKGMDVVQRIENVKTdKNDRPYEDI 143
|
|
| cyclophilin_TLP40_like |
cd01924 |
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ... |
33-188 |
3.78e-25 |
|
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: 95.97 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 33 LTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGG-------GFTEQMQQKKPNPP--IKNEADN 103
Cdd:cd01924 2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGdpqgknpGFPDPETGKSRTIPleIKPEGQK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 104 G-------------------LRNTRGTIAMARTA-DKDSATSQFFINVADNAFLDHG--QRDFGYAVFGKVVKGMDVADK 161
Cdd:cd01924 82 QpvygktleeagrydeqpvlPFNAFGAIAMARTEfDPNSASSQFFFLLKDNELTPSRnnVLDGRYAVFGYVTDGLDILRE 161
|
170 180
....*....|....*....|....*..
gi 15833468 162 IsqvpthDVGPyqnvpskpvVILSAKV 188
Cdd:cd01924 162 L------KVGD---------KIESARV 173
|
|
| cyclophilin_CeCYP16-like |
cd01925 |
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ... |
31-189 |
8.73e-25 |
|
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: 94.73 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 31 VLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFT------EQMQQKkpnpPIKNEADNG 104
Cdd:cd01925 8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTgtgtggESIYGE----PFKDEFHSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 105 LR-NTRGTIAMArTADKDSATSQFFINVADNAFLDHGQrdfgyAVFGKVVkGMDVAD--KISQVPTHDVGPyqnvPSKPV 181
Cdd:cd01925 84 LRfNRRGLVGMA-NAGDDSNGSQFFFTLDKADELNNKH-----TLFGKVT-GDTIYNllKLAEVETDKDER----PVYPP 152
|
....*...
gi 15833468 182 VILSAKVL 189
Cdd:cd01925 153 KITSVEVL 160
|
|
| cyclophilin_ABH_like |
cd01926 |
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ... |
35-183 |
2.45e-23 |
|
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: 90.78 E-value: 2.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 35 TSAGNIELELDKQKAPVSVQNF---------VDYVNSGfYNNTTFHRVIPGFMIQGGGFT-----------------EQM 88
Cdd:cd01926 12 EPAGRIVMELFADVVPKTAENFralctgekgKGGKPFG-YKGSTFHRVIPDFMIQGGDFTrgngtggksiygekfpdENF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 89 QQKKPNPpikneadnglrntrGTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTH 168
Cdd:cd01926 91 KLKHTGP--------------GLLSMA-NAGPNTNGSQFFITTVKTPWLD-GK----HVVFGKVVEGMDVVKKIENVGSG 150
|
170
....*....|....*
gi 15833468 169 dvgpyQNVPSKPVVI 183
Cdd:cd01926 151 -----NGKPKKKVVI 160
|
|
| cyclophilin_SpCYP2_like |
cd01922 |
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ... |
32-176 |
1.43e-22 |
|
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: 88.36 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 32 LLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFT------EQMQQKKpnppIKNEADNGL 105
Cdd:cd01922 1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTgtgrggASIYGKK----FEDEIHPEL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15833468 106 RNT-RGTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHDVGPYQNV 176
Cdd:cd01922 77 KHTgAGILSMA-NAGPNTNGSQFFITLAPTPWLD-GK----HTIFGRVSKGMKVIENMVEVQTQTDRPIDEV 142
|
|
| Cyclophilin_PPIL3_like |
cd01928 |
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ... |
31-167 |
5.48e-22 |
|
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: 87.11 E-value: 5.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 31 VLLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFT------EQMQQKKpnppIKNEADNG 104
Cdd:cd01928 3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTgtgkggESIWGKK----FEDEFRET 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15833468 105 LR-NTRGTIAMArTADKDSATSQFFINVADNAFLdhgqrDFGYAVFGKVVKGMDVADKISQVPT 167
Cdd:cd01928 79 LKhDSRGVVSMA-NNGPNTNGSQFFITYAKQPHL-----DGKYTVFGKVIDGFETLDTLEKLPV 136
|
|
| cyclophilin_RRM |
cd01921 |
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ... |
32-184 |
1.63e-19 |
|
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: 80.85 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 32 LLTTSAGNIELELDKQKAPVSVQNFVDYVNSGFYNNTTFHRVIPGFMIQGGgfteqmqqkKPNPPIKNEAD----NGLRN 107
Cdd:cd01921 1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTG---------DPTGTGAGGESiysqLYGRQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 108 TR---------------GTIAMArTADKDSATSQFFINVADNafLDhgQRDFGYAVFGKVVKGMDVADKISQVPTHDVG- 171
Cdd:cd01921 72 ARffepeilpllkhskkGTVSMV-NAGDNLNGSQFYITLGEN--LD--YLDGKHTVFGQVVEGFDVLEKINDAIVDDDGr 146
|
170
....*....|...
gi 15833468 172 PYQNVPSKPVVIL 184
Cdd:cd01921 147 PLKDIRIKHTHIL 159
|
|
| PTZ00060 |
PTZ00060 |
cyclophilin; Provisional |
36-183 |
3.01e-14 |
|
cyclophilin; Provisional
Pssm-ID: 240249 Cd Length: 183 Bit Score: 67.56 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 36 SAGNIELELDKQKAPVSVQNFV-----DYVNSG----FYNNTTFHRVIPGFMIQGGGFT-------EQMQQKKpnppIKN 99
Cdd:PTZ00060 28 PAGRIVFELFSDVTPKTAENFRalcigDKVGSSgknlHYKGSIFHRIIPQFMCQGGDITnhngtggESIYGRK----FTD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 100 EADNGLRNTRGTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQvpthdVGPYQNVPSK 179
Cdd:PTZ00060 104 ENFKLKHDQPGLLSMA-NAGPNTNGSQFFITTVPCPWLD-GK----HVVFGKVIEGMEVVRAMEK-----EGTQSGYPKK 172
|
....
gi 15833468 180 PVVI 183
Cdd:PTZ00060 173 PVVV 176
|
|
| PLN03149 |
PLN03149 |
peptidyl-prolyl isomerase H (cyclophilin H); Provisional |
34-183 |
4.20e-12 |
|
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
Pssm-ID: 178694 Cd Length: 186 Bit Score: 61.78 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 34 TTSAGNIELELDKQKAPVSVQNFV-----DYVNSGF---YNNTTFHRVIPGFMIQGGGFT-----------------EQM 88
Cdd:PLN03149 29 GIPAGRIKMELFADIAPKTAENFRqfctgEFRKAGLpqgYKGCQFHRVIKDFMIQGGDFLkgdgtgcvsiygskfedENF 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 89 QQKKPNPPIKNEADNGLrNTRGtiamartadkdsatSQFFINVADNAFLDHgqrdfGYAVFGKVV-KGMDVADKISQVPT 167
Cdd:PLN03149 109 IAKHTGPGLLSMANSGP-NTNG--------------CQFFITCAKCDWLDN-----KHVVFGRVLgDGLLVVRKIENVAT 168
|
170
....*....|....*.
gi 15833468 168 hdvGPyQNVPSKPVVI 183
Cdd:PLN03149 169 ---GP-NNRPKLACVI 180
|
|
| PTZ00221 |
PTZ00221 |
cyclophilin; Provisional |
37-183 |
6.79e-04 |
|
cyclophilin; Provisional
Pssm-ID: 140248 Cd Length: 249 Bit Score: 39.08 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833468 37 AGNIELELDKQKAPVSVQNFVDYV--------NSGF---YNNTTFHRVIPGFMIQGGGFTEQMQQKKPNPPIKNEADNGL 105
Cdd:PTZ00221 66 AGRLVFELFEDVVPETVENFRALItgscgidtNTGVkldYLYTPVHHVDRNNNIIVLGELDSFNVSSTGTPIADEGYRHR 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15833468 106 RNTRGTIAMARTADKDSATSqFFINVADNAFLDhgqrdFGYAVFGKVVKGMDVADKISQVPTHDVGPyqnvPSKPVVI 183
Cdd:PTZ00221 146 HTERGLLTMISEGPHTSGSV-FGITLGPSPSLD-----FKQVVFGKAVDDLSLLEKLESLPLDDVGR----PLLPVTV 213
|
|
| |
