|
Name |
Accession |
Description |
Interval |
E-value |
| PpiB |
COG0652 |
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
4-178 |
4.39e-63 |
|
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 191.54 E-value: 4.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 4 KTATATVHTNHGDIVIDLFGNHAPNTVDNFIGLAEGtkeykgqnasgtesgPFYDEAIFHRIIAGFMIQGGDPLGTGTGG 83
Cdd:COG0652 5 PNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKE---------------GFYDGTIFHRVIPGFMIQGGDPTGTGTGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 84 PGYMFDDEIHPELQFDRpYLLAMANAgkrGGRGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHWD 163
Cdd:COG0652 70 PGYTIPDEFDPGLKHKR-GTLAMARA---QGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVE--GMDVVDKIAAGPTDPGD 143
|
170
....*....|....*
gi 2785973443 164 RPLEPVVITSIDIEK 178
Cdd:COG0652 144 GPLEPVVIESVTIVE 158
|
|
| cyclophilin |
cd00317 |
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ... |
9-173 |
6.75e-53 |
|
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: 165.13 E-value: 6.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 9 TVHTNHGDIVIDLFGNHAPNTVDNFIGLAEGTkeykgqnasgtesgpFYDEAIFHRIIAGFMIQGGD--PLGTGTGGPGY 86
Cdd:cd00317 1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGG---------------FYDGTTFHRVIPGFMIQGGDptGTGGGGSGPGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 87 MFDDEIHPELQFDRPYLLAMANAGkrggRGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHWDRPL 166
Cdd:cd00317 66 KFPDENFPLKYHHRRGTLSMANAG----PNTNGSQFFITTAPTPHLDGKHTVFGKVVE--GMDVVDKIERGDTDENGRPI 139
|
....*..
gi 2785973443 167 EPVVITS 173
Cdd:cd00317 140 KPVTISD 146
|
|
| Pro_isomerase |
pfam00160 |
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
10-176 |
7.93e-45 |
|
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: 145.09 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 10 VHTN-HGDIVIDLFGNHAPNTVDNFIGLAEgtkeyKGqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGYM- 87
Cdd:pfam00160 1 IETNgLGRIVIELFGDKAPKTVENFLQLCK-----KG----------FYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFp 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 88 FDDEIHPELQFDRPYLLAMANAGKrgGRGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHwDRPLE 167
Cdd:pfam00160 66 IPDEIFPLLLKHKRGALSMANTGP--APNSNGSQFFITLGPAPHLDGKYTVFGKVVE--GMDVLEKIEKVPTDG-DRPVK 140
|
....*....
gi 2785973443 168 PVVITSIDI 176
Cdd:pfam00160 141 PVKILSCGV 149
|
|
| PTZ00060 |
PTZ00060 |
cyclophilin; Provisional |
13-172 |
1.33e-30 |
|
cyclophilin; Provisional
Pssm-ID: 240249 Cd Length: 183 Bit Score: 109.55 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 13 NHGDIVIDLFGNHAPNTVDNFIGLAEGTKeykgqnaSGTESGPF-YDEAIFHRIIAGFMIQGGDPLGTGTGGPGYM---- 87
Cdd:PTZ00060 28 PAGRIVFELFSDVTPKTAENFRALCIGDK-------VGSSGKNLhYKGSIFHRIIPQFMCQGGDITNHNGTGGESIygrk 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 88 FDDEiHPELQFDRPYLLAMANAGKrggrGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHwDRPLE 167
Cdd:PTZ00060 101 FTDE-NFKLKHDQPGLLSMANAGP----NTNGSQFFITTVPCPWLDGKHVVFGKVIE--GMEVVRAMEKEGTQS-GYPKK 172
|
....*
gi 2785973443 168 PVVIT 172
Cdd:PTZ00060 173 PVVVT 177
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PpiB |
COG0652 |
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
4-178 |
4.39e-63 |
|
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 191.54 E-value: 4.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 4 KTATATVHTNHGDIVIDLFGNHAPNTVDNFIGLAEGtkeykgqnasgtesgPFYDEAIFHRIIAGFMIQGGDPLGTGTGG 83
Cdd:COG0652 5 PNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKE---------------GFYDGTIFHRVIPGFMIQGGDPTGTGTGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 84 PGYMFDDEIHPELQFDRpYLLAMANAgkrGGRGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHWD 163
Cdd:COG0652 70 PGYTIPDEFDPGLKHKR-GTLAMARA---QGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVE--GMDVVDKIAAGPTDPGD 143
|
170
....*....|....*
gi 2785973443 164 RPLEPVVITSIDIEK 178
Cdd:COG0652 144 GPLEPVVIESVTIVE 158
|
|
| cyclophilin |
cd00317 |
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ... |
9-173 |
6.75e-53 |
|
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: 165.13 E-value: 6.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 9 TVHTNHGDIVIDLFGNHAPNTVDNFIGLAEGTkeykgqnasgtesgpFYDEAIFHRIIAGFMIQGGD--PLGTGTGGPGY 86
Cdd:cd00317 1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGG---------------FYDGTTFHRVIPGFMIQGGDptGTGGGGSGPGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 87 MFDDEIHPELQFDRPYLLAMANAGkrggRGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHWDRPL 166
Cdd:cd00317 66 KFPDENFPLKYHHRRGTLSMANAG----PNTNGSQFFITTAPTPHLDGKHTVFGKVVE--GMDVVDKIERGDTDENGRPI 139
|
....*..
gi 2785973443 167 EPVVITS 173
Cdd:cd00317 140 KPVTISD 146
|
|
| cyclophilin_WD40 |
cd01927 |
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
9-174 |
1.47e-46 |
|
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: 149.15 E-value: 1.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 9 TVHTNHGDIVIDLFGNHAPNTVDNFIGLAEGTkeykgqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGYM- 87
Cdd:cd01927 1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNG---------------YYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 88 --FDDEIHPELQFDRPYLLAMANAGKrggrGTNGSQFFITVVPTPHLNGAHTIFGEVAddASKKVVDEIARVATDHWDRP 165
Cdd:cd01927 66 keFEDEFSPSLKHDRPYTLSMANAGP----NTNGSQFFITTVATPWLDNKHTVFGRVV--KGMDVVQRIENVKTDKNDRP 139
|
....*....
gi 2785973443 166 LEPVVITSI 174
Cdd:cd01927 140 YEDIKIINI 148
|
|
| Pro_isomerase |
pfam00160 |
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
10-176 |
7.93e-45 |
|
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: 145.09 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 10 VHTN-HGDIVIDLFGNHAPNTVDNFIGLAEgtkeyKGqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGYM- 87
Cdd:pfam00160 1 IETNgLGRIVIELFGDKAPKTVENFLQLCK-----KG----------FYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFp 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 88 FDDEIHPELQFDRPYLLAMANAGKrgGRGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHwDRPLE 167
Cdd:pfam00160 66 IPDEIFPLLLKHKRGALSMANTGP--APNSNGSQFFITLGPAPHLDGKYTVFGKVVE--GMDVLEKIEKVPTDG-DRPVK 140
|
....*....
gi 2785973443 168 PVVITSIDI 176
Cdd:pfam00160 141 PVKILSCGV 149
|
|
| cyclophilin_CeCYP16-like |
cd01925 |
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ... |
5-176 |
4.42e-41 |
|
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: 135.94 E-value: 4.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 5 TATATVHTNHGDIVIDLFGNHAPNTVDNFIGLA-EGtkeykgqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGG 83
Cdd:cd01925 5 TGKVILKTTAGDIDIELWSKEAPKACRNFIQLClEG----------------YYDNTIFHRVVPGFIIQGGDPTGTGTGG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 84 PGYM---FDDEIHPELQFDRPYLLAMANAGKRggrgTNGSQFFITVVPTPHLNGAHTIFGEVADDASKKVVdEIARVATD 160
Cdd:cd01925 69 ESIYgepFKDEFHSRLRFNRRGLVGMANAGDD----SNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLL-KLAEVETD 143
|
170
....*....|....*.
gi 2785973443 161 HWDRPLEPVVITSIDI 176
Cdd:cd01925 144 KDERPVYPPKITSVEV 159
|
|
| cyclophilin_SpCYP2_like |
cd01922 |
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ... |
9-171 |
5.58e-40 |
|
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: 132.66 E-value: 5.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 9 TVHTNHGDIVIDLFGNHAPNTVDNFIGLAEgtkeyKGqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGY-- 86
Cdd:cd01922 1 TLETTMGEITLELYWNHAPKTCKNFYELAK-----RG----------YYNGTIFHRLIKDFMIQGGDPTGTGRGGASIyg 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 87 -MFDDEIHPELQFDRPYLLAMANAGKrggrGTNGSQFFITVVPTPHLNGAHTIFGEVAddASKKVVDEIARVATDHwDRP 165
Cdd:cd01922 66 kKFEDEIHPELKHTGAGILSMANAGP----NTNGSQFFITLAPTPWLDGKHTIFGRVS--KGMKVIENMVEVQTQT-DRP 138
|
....*.
gi 2785973443 166 LEPVVI 171
Cdd:cd01922 139 IDEVKI 144
|
|
| Cyclophilin_PPIL3_like |
cd01928 |
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ... |
9-176 |
5.69e-38 |
|
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: 127.55 E-value: 5.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 9 TVHTNHGDIVIDLFGNHAPNTVDNFIGLAegtkeykgqnASGtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGY-- 86
Cdd:cd01928 4 TLHTNLGDIKIELFCDDCPKACENFLALC----------ASG-----YYNGCIFHRNIKGFMVQTGDPTGTGKGGESIwg 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 87 -MFDDEIHPELQFDRPYLLAMANAGKRggrgTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHWDRP 165
Cdd:cd01928 69 kKFEDEFRETLKHDSRGVVSMANNGPN----TNGSQFFITYAKQPHLDGKYTVFGKVID--GFETLDTLEKLPVDKKYRP 142
|
170
....*....|.
gi 2785973443 166 LEPVVITSIDI 176
Cdd:cd01928 143 LEEIRIKDVTI 153
|
|
| cyclophilin_RING |
cd01923 |
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
11-176 |
1.12e-37 |
|
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having a modified RING finger domain. This group includes the nuclear proteins, Human hCyP-60 and Caenorhabditis elegans MOG-6 which, compared to the archetypal cyclophilin Human cyclophilin A exhibit reduced peptidylprolyl cis- trans isomerase activity and lack a residue important for cyclophilin binding. Human hCyP-60 has been shown to physically interact with the proteinase inhibitor peptide eglin c and; C. elegans MOG-6 to physically interact with MEP-1, a nuclear zinc finger protein. MOG-6 has been shown to function in germline sex determination.
Pssm-ID: 238904 [Multi-domain] Cd Length: 159 Bit Score: 127.15 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 11 HTNHGDIVIDLFGNHAPNTVDNFIGLAEgtkeyKGqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGYM--- 87
Cdd:cd01923 5 HTNKGDLNLELHCDKAPKACENFIKLCK-----KG----------YYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWgkp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 88 FDDEIHPELQFDRPYLLAMANAGKrggrGTNGSQFFITVVPTPHLNGAHTIFGEVADDASkkVVDEIARVATDHWDRPLE 167
Cdd:cd01923 70 FKDEFKPNLSHDGRGVLSMANSGP----NTNGSQFFITYRSCKHLDGKHTVFGRVVGGLE--TLEAMENVPDPGTDRPKE 143
|
....*....
gi 2785973443 168 PVVITSIDI 176
Cdd:cd01923 144 EIKIEDTSV 152
|
|
| cyclophilin_ABH_like |
cd01926 |
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ... |
15-172 |
5.15e-37 |
|
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: 125.45 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 15 GDIVIDLFGNHAPNTVDNFIGLAEGTKeykgqnasGTESGPF-YDEAIFHRIIAGFMIQGGDPLGTGTGGPGYM----FD 89
Cdd:cd01926 15 GRIVMELFADVVPKTAENFRALCTGEK--------GKGGKPFgYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSIygekFP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 90 DEiHPELQFDRPYLLAMANAGKrggrGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHwDRPLEPV 169
Cdd:cd01926 87 DE-NFKLKHTGPGLLSMANAGP----NTNGSQFFITTVKTPWLDGKHVVFGKVVE--GMDVVKKIENVGSGN-GKPKKKV 158
|
...
gi 2785973443 170 VIT 172
Cdd:cd01926 159 VIA 161
|
|
| PTZ00060 |
PTZ00060 |
cyclophilin; Provisional |
13-172 |
1.33e-30 |
|
cyclophilin; Provisional
Pssm-ID: 240249 Cd Length: 183 Bit Score: 109.55 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 13 NHGDIVIDLFGNHAPNTVDNFIGLAEGTKeykgqnaSGTESGPF-YDEAIFHRIIAGFMIQGGDPLGTGTGGPGYM---- 87
Cdd:PTZ00060 28 PAGRIVFELFSDVTPKTAENFRALCIGDK-------VGSSGKNLhYKGSIFHRIIPQFMCQGGDITNHNGTGGESIygrk 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 88 FDDEiHPELQFDRPYLLAMANAGKrggrGTNGSQFFITVVPTPHLNGAHTIFGEVADdaSKKVVDEIARVATDHwDRPLE 167
Cdd:PTZ00060 101 FTDE-NFKLKHDQPGLLSMANAGP----NTNGSQFFITTVPCPWLDGKHVVFGKVIE--GMEVVRAMEKEGTQS-GYPKK 172
|
....*
gi 2785973443 168 PVVIT 172
Cdd:PTZ00060 173 PVVVT 177
|
|
| cyclophilin_EcCYP_like |
cd01920 |
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ... |
9-173 |
5.37e-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: 91.74 E-value: 5.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 9 TVHTNHGDIVIDLFGNHAPNTVDNFIGLAEgtkeyKGqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGymf 88
Cdd:cd01920 1 EFQTSLGDIVVELYDDKAPITVENFLAYVR-----KG----------FYDNTIFHRVISGFVIQGGGFTPDLAQKET--- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 89 DDEIHPE----LQFDRpYLLAMAnagKRGGRGTNGSQFFITVVPTPHLN-----GAHTIFGEVadDASKKVVDEIARVAT 159
Cdd:cd01920 63 LKPIKNEagngLSNTR-GTIAMA---RTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEV--TEGMDVVDKIAGVET 136
|
170
....*....|....*...
gi 2785973443 160 ----DHWDRPLEPVVITS 173
Cdd:cd01920 137 ysfgSYQDVPVQDVIIES 154
|
|
| PLN03149 |
PLN03149 |
peptidyl-prolyl isomerase H (cyclophilin H); Provisional |
1-172 |
8.42e-22 |
|
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
Pssm-ID: 178694 Cd Length: 186 Bit Score: 87.20 E-value: 8.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 1 MTIKTATAtvhtnhGDIVIDLFGNHAPNTVDNFIGLAEGtkEYKgqnASGTESGpfYDEAIFHRIIAGFMIQGGDPLGTG 80
Cdd:PLN03149 25 VTIGGIPA------GRIKMELFADIAPKTAENFRQFCTG--EFR---KAGLPQG--YKGCQFHRVIKDFMIQGGDFLKGD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 81 TGGPGYM----FDDEiHPELQFDRPYLLAMANAGKrggrGTNGSQFFITVVPTPHLNGAHTIFGEVADDAsKKVVDEIAR 156
Cdd:PLN03149 92 GTGCVSIygskFEDE-NFIAKHTGPGLLSMANSGP----NTNGCQFFITCAKCDWLDNKHVVFGRVLGDG-LLVVRKIEN 165
|
170
....*....|....*.
gi 2785973443 157 VATDHWDRPLEPVVIT 172
Cdd:PLN03149 166 VATGPNNRPKLACVIS 181
|
|
| PRK10791 |
PRK10791 |
peptidylprolyl isomerase B; |
9-178 |
3.61e-18 |
|
peptidylprolyl isomerase B;
Pssm-ID: 182734 Cd Length: 164 Bit Score: 77.19 E-value: 3.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 9 TVHTNHGDIVIDLFGNHAPNTVDNFIGLAEGTkeykgqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGymf 88
Cdd:PRK10791 3 TFHTNHGDIVIKTFDDKAPETVKNFLDYCREG---------------FYNNTIFHRVINGFMIQGGGFEPGMKQKAT--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 89 DDEIHPElqfdrpyllamANAGKRGGRGT-----------NGSQFFITVVPTPHLN--------GAHTIFGEVADdaSKK 149
Cdd:PRK10791 65 KEPIKNE-----------ANNGLKNTRGTlamartqaphsATAQFFINVVDNDFLNfsgeslqgWGYCVFAEVVE--GMD 131
|
170 180 190
....*....|....*....|....*....|...
gi 2785973443 150 VVDEIARVATD----HWDRPLEPVVITSIDIEK 178
Cdd:PRK10791 132 VVDKIKGVATGrsgmHQDVPKEDVIIESVTVSE 164
|
|
| cyclophilin_RRM |
cd01921 |
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ... |
12-172 |
3.15e-16 |
|
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: 71.99 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 12 TNHGDIVIDLFGNHAPNTVDNFIGLAEgTKeykgqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGY----- 86
Cdd:cd01921 4 TTLGDLVIDLFTDECPLACLNFLKLCK-LK--------------YYNFCLFYNVQKDFIAQTGDPTGTGAGGESIysqly 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 87 -----MFDDEIHPELQFDRPYLLAMANAGKRggrgTNGSQFFITVVP-TPHLNGAHTIFGEVADdaSKKVVDEIARVATD 160
Cdd:cd01921 69 grqarFFEPEILPLLKHSKKGTVSMVNAGDN----LNGSQFYITLGEnLDYLDGKHTVFGQVVE--GFDVLEKINDAIVD 142
|
170
....*....|..
gi 2785973443 161 HWDRPLEPVVIT 172
Cdd:cd01921 143 DDGRPLKDIRIK 154
|
|
| PRK10903 |
PRK10903 |
peptidylprolyl isomerase A; |
12-178 |
6.40e-13 |
|
peptidylprolyl isomerase A;
Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 63.71 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 12 TNHGDIVIDLFGNHAPNTVDNFIglaegtkEYkgqnasgTESGpFYDEAIFHRIIAGFMIQGGDplgtgtggpgymFDDE 91
Cdd:PRK10903 35 TSAGNIELELNSQKAPVSVKNFV-------DY-------VNSG-FYNNTTFHRVIPGFMIQGGG------------FTEQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 92 IHPELQfdRPYLLAMANAGKRGGRGT-----------NGSQFFITVVPTPHLNG-----AHTIFGEVADdaSKKVVDEIA 155
Cdd:PRK10903 88 MQQKKP--NPPIKNEADNGLRNTRGTiamartadkdsATSQFFINVADNAFLDHgqrdfGYAVFGKVVK--GMDVADKIS 163
|
170 180
....*....|....*....|....*..
gi 2785973443 156 RVATD----HWDRPLEPVVITSIDIEK 178
Cdd:PRK10903 164 QVPTHdvgpYQNVPSKPVVILSAKVLP 190
|
|
| cyclophilin_TLP40_like |
cd01924 |
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ... |
12-144 |
4.01e-06 |
|
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: 44.74 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 12 TNHGDIVIDLFGNHAPNTVDNFIGLAEgtkeyKGqnasgtesgpFYDEAIFHRIIAGFMIQGGDPLGTGTGGPGYMFDD- 90
Cdd:cd01924 4 TDNGTITIVLDGYNAPVTAGNFVDLVE-----RG----------FYDGMEFHRVEGGFVVQTGDPQGKNPGFPDPETGKs 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 91 -----EIHPELQF---------------DRPYLL-----AMANAGKRGGRGTNGSQFFI-------TVVPTPHLNGAHTI 138
Cdd:cd01924 69 rtiplEIKPEGQKqpvygktleeagrydEQPVLPfnafgAIAMARTEFDPNSASSQFFFllkdnelTPSRNNVLDGRYAV 148
|
....*.
gi 2785973443 139 FGEVAD 144
Cdd:cd01924 149 FGYVTD 154
|
|
| PTZ00221 |
PTZ00221 |
cyclophilin; Provisional |
15-172 |
1.10e-05 |
|
cyclophilin; Provisional
Pssm-ID: 140248 Cd Length: 249 Bit Score: 44.09 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2785973443 15 GDIVIDLFGNHAPNTVDNFIGLAEGtkEYKGQNASGTESGPFYDEaiFHRI-IAGFMIQGGDPLGTGTGGPGYMFDDEIH 93
Cdd:PTZ00221 67 GRLVFELFEDVVPETVENFRALITG--SCGIDTNTGVKLDYLYTP--VHHVdRNNNIIVLGELDSFNVSSTGTPIADEGY 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2785973443 94 PELQFDRPyLLAMANAGKRggrgTNGSQFFITVVPTPHLNGAHTIFGEVADDASkkVVDEIARVATDHWDRPLEPVVIT 172
Cdd:PTZ00221 143 RHRHTERG-LLTMISEGPH----TSGSVFGITLGPSPSLDFKQVVFGKAVDDLS--LLEKLESLPLDDVGRPLLPVTVS 214
|
|
| |
