|
Name |
Accession |
Description |
Interval |
E-value |
| PpiB |
COG0652 |
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
12-197 |
4.04e-73 |
|
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 217.73 E-value: 4.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 12 QQGEIKVVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGEsiyGGAFEDEFS 91
Cdd:COG0652 3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 92 LNAFNLYGALSMANS-GPNTNGSQFFIVQmkevpqnmlsqladggwpqpivdaygekGGTPWLDQKHTVFGQIIDGETTL 170
Cdd:COG0652 80 PGLKHKRGTLAMARAqGPNSAGSQFFIVL----------------------------GDNPHLDGGYTVFGKVVEGMDVV 131
|
170 180
....*....|....*....|....*..
gi 613313570 171 EDIANTKVGPQDKPLHDVVIESIDVEE 197
Cdd:COG0652 132 DKIAAGPTDPGDGPLEPVVIESVTIVE 158
|
|
| cyclophilin_WD40 |
cd01927 |
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
19-193 |
9.65e-67 |
|
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: 201.15 E-value: 9.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 19 VMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGAFEDEFSLN-AFNL 97
Cdd:cd01927 1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSlKHDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 98 YGALSMANSGPNTNGSQFFIVQMKevpqnmlsqladggwpqpivdaygekggTPWLDQKHTVFGQIIDGETTLEDIANTK 177
Cdd:cd01927 81 PYTLSMANAGPNTNGSQFFITTVA----------------------------TPWLDNKHTVFGRVVKGMDVVQRIENVK 132
|
170
....*....|....*.
gi 613313570 178 VGPQDKPLHDVVIESI 193
Cdd:cd01927 133 TDKNDRPYEDIKIINI 148
|
|
| Pro_isomerase |
pfam00160 |
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
20-195 |
2.21e-56 |
|
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: 175.14 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 20 MHTN-KGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYggAFEDEF-SLNAFNL 97
Cdd:pfam00160 1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIfPLLLKHK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 98 YGALSMANSG--PNTNGSQFFIVqmkevpqnmlsqladggwpqpivdaygeKGGTPWLDQKHTVFGQIIDGETTLEDIAN 175
Cdd:pfam00160 79 RGALSMANTGpaPNSNGSQFFIT----------------------------LGPAPHLDGKYTVFGKVVEGMDVLEKIEK 130
|
170 180
....*....|....*....|
gi 613313570 176 TKVGPqDKPLHDVVIESIDV 195
Cdd:pfam00160 131 VPTDG-DRPVKPVKILSCGV 149
|
|
| PLN03149 |
PLN03149 |
peptidyl-prolyl isomerase H (cyclophilin H); Provisional |
25-190 |
7.16e-39 |
|
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
Pssm-ID: 178694 Cd Length: 186 Bit Score: 131.88 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 25 GDMTFKLFPNIAPKTVENFVT-----HAKNGY---YDGITFHRVINDFMIQGGD-PTATGMGGESIYGGAFEDEFSLNAF 95
Cdd:PLN03149 33 GRIKMELFADIAPKTAENFRQfctgeFRKAGLpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGCVSIYGSKFEDENFIAKH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 96 NLYGALSMANSGPNTNGSQFFIVQMKevpqnmlsqladggwpqpivdaygekggTPWLDQKHTVFGQII-DGETTLEDIA 174
Cdd:PLN03149 113 TGPGLLSMANSGPNTNGCQFFITCAK----------------------------CDWLDNKHVVFGRVLgDGLLVVRKIE 164
|
170
....*....|....*.
gi 613313570 175 NTKVGPQDKPLHDVVI 190
Cdd:PLN03149 165 NVATGPNNRPKLACVI 180
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PpiB |
COG0652 |
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ... |
12-197 |
4.04e-73 |
|
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440417 [Multi-domain] Cd Length: 159 Bit Score: 217.73 E-value: 4.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 12 QQGEIKVVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGEsiyGGAFEDEFS 91
Cdd:COG0652 3 AAPNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 92 LNAFNLYGALSMANS-GPNTNGSQFFIVQmkevpqnmlsqladggwpqpivdaygekGGTPWLDQKHTVFGQIIDGETTL 170
Cdd:COG0652 80 PGLKHKRGTLAMARAqGPNSAGSQFFIVL----------------------------GDNPHLDGGYTVFGKVVEGMDVV 131
|
170 180
....*....|....*....|....*..
gi 613313570 171 EDIANTKVGPQDKPLHDVVIESIDVEE 197
Cdd:COG0652 132 DKIAAGPTDPGDGPLEPVVIESVTIVE 158
|
|
| cyclophilin_WD40 |
cd01927 |
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
19-193 |
9.65e-67 |
|
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: 201.15 E-value: 9.65e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 19 VMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGAFEDEFSLN-AFNL 97
Cdd:cd01927 1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSlKHDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 98 YGALSMANSGPNTNGSQFFIVQMKevpqnmlsqladggwpqpivdaygekggTPWLDQKHTVFGQIIDGETTLEDIANTK 177
Cdd:cd01927 81 PYTLSMANAGPNTNGSQFFITTVA----------------------------TPWLDNKHTVFGRVVKGMDVVQRIENVK 132
|
170
....*....|....*.
gi 613313570 178 VGPQDKPLHDVVIESI 193
Cdd:cd01927 133 TDKNDRPYEDIKIINI 148
|
|
| cyclophilin |
cd00317 |
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ... |
19-192 |
1.04e-62 |
|
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: 190.94 E-value: 1.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 19 VMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGeSIYGGAFEDE-FSLNAFNL 97
Cdd:cd00317 1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDEnFPLKYHHR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 98 YGALSMANSGPNTNGSQFFIVQmkevpqnmlsqladggwpqpivdaygekGGTPWLDQKHTVFGQIIDGETTLEDIANTK 177
Cdd:cd00317 80 RGTLSMANAGPNTNGSQFFITT----------------------------APTPHLDGKHTVFGKVVEGMDVVDKIERGD 131
|
170
....*....|....*
gi 613313570 178 VGPQDKPLHDVVIES 192
Cdd:cd00317 132 TDENGRPIKPVTISD 146
|
|
| cyclophilin_RING |
cd01923 |
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ... |
18-195 |
1.20e-62 |
|
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: 191.47 E-value: 1.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 18 VVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGAFEDEFslNAFNL 97
Cdd:cd01923 2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEF--KPNLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 98 Y---GALSMANSGPNTNGSQFFIVQmkevpqnmlsqladggwpqpivdaygekGGTPWLDQKHTVFGQIIDGETTLEDIA 174
Cdd:cd01923 80 HdgrGVLSMANSGPNTNGSQFFITY----------------------------RSCKHLDGKHTVFGRVVGGLETLEAME 131
|
170 180
....*....|....*....|.
gi 613313570 175 NTKVGPQDKPLHDVVIESIDV 195
Cdd:cd01923 132 NVPDPGTDRPKEEIKIEDTSV 152
|
|
| Pro_isomerase |
pfam00160 |
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ... |
20-195 |
2.21e-56 |
|
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: 175.14 E-value: 2.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 20 MHTN-KGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYggAFEDEF-SLNAFNL 97
Cdd:pfam00160 1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIF--PIPDEIfPLLLKHK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 98 YGALSMANSG--PNTNGSQFFIVqmkevpqnmlsqladggwpqpivdaygeKGGTPWLDQKHTVFGQIIDGETTLEDIAN 175
Cdd:pfam00160 79 RGALSMANTGpaPNSNGSQFFIT----------------------------LGPAPHLDGKYTVFGKVVEGMDVLEKIEK 130
|
170 180
....*....|....*....|
gi 613313570 176 TKVGPqDKPLHDVVIESIDV 195
Cdd:pfam00160 131 VPTDG-DRPVKPVKILSCGV 149
|
|
| Cyclophilin_PPIL3_like |
cd01928 |
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ... |
18-195 |
3.47e-55 |
|
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: 172.24 E-value: 3.47e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 18 VVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGAFEDEFSLN-AFN 96
Cdd:cd01928 3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETlKHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 97 LYGALSMANSGPNTNGSQFFIVQMKEvpqnmlsqladggwpqpivdaygekggtPWLDQKHTVFGQIIDGETTLEDIANT 176
Cdd:cd01928 83 SRGVVSMANNGPNTNGSQFFITYAKQ----------------------------PHLDGKYTVFGKVIDGFETLDTLEKL 134
|
170
....*....|....*....
gi 613313570 177 KVGPQDKPLHDVVIESIDV 195
Cdd:cd01928 135 PVDKKYRPLEEIRIKDVTI 153
|
|
| cyclophilin_CeCYP16-like |
cd01925 |
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ... |
17-195 |
4.64e-52 |
|
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: 164.83 E-value: 4.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 17 KVVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGAFEDEF-SLNAF 95
Cdd:cd01925 7 KVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFhSRLRF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 96 NLYGALSMANSGPNTNGSQFFIVQmkevpqnmlsqladggwpqpivdaygekGGTPWLDQKHTVFGQIIdGET--TLEDI 173
Cdd:cd01925 87 NRRGLVGMANAGDDSNGSQFFFTL----------------------------DKADELNNKHTLFGKVT-GDTiyNLLKL 137
|
170 180
....*....|....*....|..
gi 613313570 174 ANTKVGPQDKPLHDVVIESIDV 195
Cdd:cd01925 138 AEVETDKDERPVYPPKITSVEV 159
|
|
| cyclophilin_SpCYP2_like |
cd01922 |
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ... |
19-190 |
7.94e-49 |
|
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: 155.77 E-value: 7.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 19 VMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGAFEDEFSLN-AFNL 97
Cdd:cd01922 1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPElKHTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 98 YGALSMANSGPNTNGSQFFIVQmkevpqnmlsqladggwpqpivdaygekGGTPWLDQKHTVFGQIIDGETTLEDIANTK 177
Cdd:cd01922 81 AGILSMANAGPNTNGSQFFITL----------------------------APTPWLDGKHTIFGRVSKGMKVIENMVEVQ 132
|
170
....*....|...
gi 613313570 178 VGpQDKPLHDVVI 190
Cdd:cd01922 133 TQ-TDRPIDEVKI 144
|
|
| cyclophilin_ABH_like |
cd01926 |
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ... |
25-190 |
1.41e-48 |
|
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: 155.88 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 25 GDMTFKLFPNIAPKTVENFVT--------HAKNGYYDGITFHRVINDFMIQGGDPTA-TGMGGESIYGGAFEDEfslnAF 95
Cdd:cd01926 15 GRIVMELFADVVPKTAENFRAlctgekgkGGKPFGYKGSTFHRVIPDFMIQGGDFTRgNGTGGKSIYGEKFPDE----NF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 96 NLY----GALSMANSGPNTNGSQFFIVQMKevpqnmlsqladggwpqpivdaygekggTPWLDQKHTVFGQIIDGETTLE 171
Cdd:cd01926 91 KLKhtgpGLLSMANAGPNTNGSQFFITTVK----------------------------TPWLDGKHVVFGKVVEGMDVVK 142
|
170
....*....|....*....
gi 613313570 172 DIANTKVGpQDKPLHDVVI 190
Cdd:cd01926 143 KIENVGSG-NGKPKKKVVI 160
|
|
| PLN03149 |
PLN03149 |
peptidyl-prolyl isomerase H (cyclophilin H); Provisional |
25-190 |
7.16e-39 |
|
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
Pssm-ID: 178694 Cd Length: 186 Bit Score: 131.88 E-value: 7.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 25 GDMTFKLFPNIAPKTVENFVT-----HAKNGY---YDGITFHRVINDFMIQGGD-PTATGMGGESIYGGAFEDEFSLNAF 95
Cdd:PLN03149 33 GRIKMELFADIAPKTAENFRQfctgeFRKAGLpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGCVSIYGSKFEDENFIAKH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 96 NLYGALSMANSGPNTNGSQFFIVQMKevpqnmlsqladggwpqpivdaygekggTPWLDQKHTVFGQII-DGETTLEDIA 174
Cdd:PLN03149 113 TGPGLLSMANSGPNTNGCQFFITCAK----------------------------CDWLDNKHVVFGRVLgDGLLVVRKIE 164
|
170
....*....|....*.
gi 613313570 175 NTKVGPQDKPLHDVVI 190
Cdd:PLN03149 165 NVATGPNNRPKLACVI 180
|
|
| PTZ00060 |
PTZ00060 |
cyclophilin; Provisional |
23-191 |
3.61e-38 |
|
cyclophilin; Provisional
Pssm-ID: 240249 Cd Length: 183 Bit Score: 129.96 E-value: 3.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 23 NKGDMTFKLFPNIAPKTVENF---------VTHAKNGYYDGITFHRVINDFMIQGGDPT-ATGMGGESIYGGAFEDE-FS 91
Cdd:PTZ00060 28 PAGRIVFELFSDVTPKTAENFralcigdkvGSSGKNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGESIYGRKFTDEnFK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 92 LNaFNLYGALSMANSGPNTNGSQFFIVQmkeVPqnmlsqladggwpqpivdaygekggTPWLDQKHTVFGQIIDGETTLE 171
Cdd:PTZ00060 108 LK-HDQPGLLSMANAGPNTNGSQFFITT---VP-------------------------CPWLDGKHVVFGKVIEGMEVVR 158
|
170 180
....*....|....*....|.
gi 613313570 172 DIanTKVGPQD-KPLHDVVIE 191
Cdd:PTZ00060 159 AM--EKEGTQSgYPKKPVVVT 177
|
|
| cyclophilin_EcCYP_like |
cd01920 |
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ... |
20-192 |
6.33e-31 |
|
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: 110.23 E-value: 6.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 20 MHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESiyGGAFEDEFSLNAFNLYG 99
Cdd:cd01920 2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKET--LKPIKNEAGNGLSNTRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 100 ALSMANSG-PNTNGSQFFIvqmkevpqnmlsQLADGGWPQPIVDAYGekggtpwldqkHTVFGQIIDGETTLEDIANTKV 178
Cdd:cd01920 80 TIAMARTNaPDSATSQFFI------------NLKDNASLDYQNEQWG-----------YTVFGEVTEGMDVVDKIAGVET 136
|
170
....*....|....*...
gi 613313570 179 GP----QDKPLHDVVIES 192
Cdd:cd01920 137 YSfgsyQDVPVQDVIIES 154
|
|
| cyclophilin_RRM |
cd01921 |
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ... |
19-190 |
3.98e-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: 103.57 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 19 VMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGG-------AFEDEF- 90
Cdd:cd01921 1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSQlygrqarFFEPEIl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 91 -SLNAfNLYGALSMANSGPNTNGSQFFIVqmkevpqnmlsqLADggwpqpivdaygekgGTPWLDQKHTVFGQIIDGETT 169
Cdd:cd01921 81 pLLKH-SKKGTVSMVNAGDNLNGSQFYIT------------LGE---------------NLDYLDGKHTVFGQVVEGFDV 132
|
170 180
....*....|....*....|.
gi 613313570 170 LEDIANTKVGPQDKPLHDVVI 190
Cdd:cd01921 133 LEKINDAIVDDDGRPLKDIRI 153
|
|
| PRK10791 |
PRK10791 |
peptidylprolyl isomerase B; |
18-197 |
3.05e-21 |
|
peptidylprolyl isomerase B;
Pssm-ID: 182734 Cd Length: 164 Bit Score: 85.66 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 18 VVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDpTATGMGGESIyGGAFEDEFSLNAFNL 97
Cdd:PRK10791 2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGG-FEPGMKQKAT-KEPIKNEANNGLKNT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 98 YGALSMANSG-PNTNGSQFFIVQMKEVPQNMLSQLADgGWpqpivdaygekggtpwldqKHTVFGQIIDGETTLEDIANT 176
Cdd:PRK10791 80 RGTLAMARTQaPHSATAQFFINVVDNDFLNFSGESLQ-GW-------------------GYCVFAEVVEGMDVVDKIKGV 139
|
170 180
....*....|....*....|....*
gi 613313570 177 KVGP----QDKPLHDVVIESIDVEE 197
Cdd:PRK10791 140 ATGRsgmhQDVPKEDVIIESVTVSE 164
|
|
| cyclophilin_TLP40_like |
cd01924 |
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ... |
20-197 |
2.23e-18 |
|
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: 78.25 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 20 MHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMG---------------------G 78
Cdd:cd01924 2 EATDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleikpegqK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 79 ESIYG------GAFEDEFSLnAFNLYGALSMANS--GPNTNGSQFFIvqmkevpqnmlsqladggwpqPIVDAYGEKGGT 150
Cdd:cd01924 82 QPVYGktleeaGRYDEQPVL-PFNAFGAIAMARTefDPNSASSQFFF---------------------LLKDNELTPSRN 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 613313570 151 PWLDQKHTVFGQIIDGETTLEDIantKVGpqDKplhdvvIESIDVEE 197
Cdd:cd01924 140 NVLDGRYAVFGYVTDGLDILREL---KVG--DK------IESARVVE 175
|
|
| PRK10903 |
PRK10903 |
peptidylprolyl isomerase A; |
13-195 |
1.44e-16 |
|
peptidylprolyl isomerase A;
Pssm-ID: 182824 [Multi-domain] Cd Length: 190 Bit Score: 74.11 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 13 QGEIKVVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMggESIYGGAFEDEFSL 92
Cdd:PRK10903 26 KGDPHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQ--QKKPNPPIKNEADN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 613313570 93 NAFNLYGALSMA-NSGPNTNGSQFFIvqmkevpqnmlsQLADggwpqpivDAYGEKGGTpwlDQKHTVFGQIIDGETTLE 171
Cdd:PRK10903 104 GLRNTRGTIAMArTADKDSATSQFFI------------NVAD--------NAFLDHGQR---DFGYAVFGKVVKGMDVAD 160
|
170 180
....*....|....*....|....*...
gi 613313570 172 DIANTK---VGP-QDKPLHDVVIESIDV 195
Cdd:PRK10903 161 KISQVPthdVGPyQNVPSKPVVILSAKV 188
|
|
| |
