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Conserved domains on  [gi|1720387556|ref|XP_030105088|]
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RING-type E3 ubiquitin-protein ligase PPIL2 isoform X2 [Mus musculus]

Protein Classification

cyclophilin_RING domain-containing protein( domain architecture ID 10112469)

cyclophilin_RING domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 103-262 1.86e-106

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: 308.19  E-value: 1.86e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 103 YVRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDEFRPNLSH 182
Cdd:cd01923     1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 183 TGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVEsDPKTDRPKEEVLICTTTVFVDPYEE 262
Cdd:cd01923    81 DGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVP-DPGTDRPKEEIKIEDTSVFVDPFEE 159
 
Name Accession Description Interval E-value
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 103-262 1.86e-106

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: 308.19  E-value: 1.86e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 103 YVRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDEFRPNLSH 182
Cdd:cd01923     1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 183 TGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVEsDPKTDRPKEEVLICTTTVFVDPYEE 262
Cdd:cd01923    81 DGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVP-DPGTDRPKEEIKIEDTSVFVDPFEE 159
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 103-250 9.50e-55

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 176.51  E-value: 9.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 103 YVRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGEsfwGKPFKDEFRPNLSH 182
Cdd:COG0652     8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKH 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387556 183 TgRGVLSMANS-GPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDPkTDRPKEEVLI 250
Cdd:COG0652    85 K-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP-GDGPLEPVVI 151
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 106-255 1.00e-54

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: 175.91  E-value: 1.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 106 LHTN-KGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESfwGKPFKDEFRPNLSHTG 184
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKS--IFPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387556 185 RGVLSMANSG--PNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDPktDRPKEEVLICTTTV 255
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG--DRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 109-250 2.20e-36

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 129.58  E-value: 2.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 109 NKGDLNLELHCDLTPKTCENFIKLC---------KKQYYDGTIFHRSIRNFVIQGGDPTGTGTGG-ESFWGKPFKDE-Fr 177
Cdd:PTZ00060   28 PAGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGgESIYGRKFTDEnF- 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387556 178 pNLSHTGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESdpKTDRPKEEVLI 250
Cdd:PTZ00060  107 -KLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGT--QSGYPKKPVVV 176
 
Name Accession Description Interval E-value
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 103-262 1.86e-106

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: 308.19  E-value: 1.86e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 103 YVRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDEFRPNLSH 182
Cdd:cd01923     1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 183 TGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVEsDPKTDRPKEEVLICTTTVFVDPYEE 262
Cdd:cd01923    81 DGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVP-DPGTDRPKEEIKIEDTSVFVDPFEE 159
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 104-255 1.13e-66

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: 206.90  E-value: 1.13e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 104 VRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDEFRPNLSHT 183
Cdd:cd01928     3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387556 184 GRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDPKtDRPKEEVLICTTTV 255
Cdd:cd01928    83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKK-YRPLEEIRIKDVTI 153
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 106-250 3.83e-60

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: 189.78  E-value: 3.83e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 106 LHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGeSFWGKPFKDEFRPNLSHTGR 185
Cdd:cd00317     2 LDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHRR 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387556 186 GVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDPKtDRPKEEVLI 250
Cdd:cd00317    81 GTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDEN-GRPIKPVTI 144
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 106-250 4.73e-58

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: 184.59  E-value: 4.73e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 106 LHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDEFRPNLSHTGR 185
Cdd:cd01927     2 IHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDRP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387556 186 GVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDpKTDRPKEEVLI 250
Cdd:cd01927    82 YTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTD-KNDRPYEDIKI 145
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 103-250 9.50e-55

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 176.51  E-value: 9.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 103 YVRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGEsfwGKPFKDEFRPNLSH 182
Cdd:COG0652     8 TVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKH 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720387556 183 TgRGVLSMANS-GPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDPkTDRPKEEVLI 250
Cdd:COG0652    85 K-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP-GDGPLEPVVI 151
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 106-255 1.00e-54

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: 175.91  E-value: 1.00e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 106 LHTN-KGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESfwGKPFKDEFRPNLSHTG 184
Cdd:pfam00160   1 IETNgLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKS--IFPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387556 185 RGVLSMANSG--PNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDPktDRPKEEVLICTTTV 255
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG--DRPVKPVKILSCGV 149
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 106-250 3.30e-51

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: 166.94  E-value: 3.30e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 106 LHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDEFRPNLSHTGR 185
Cdd:cd01922     2 LETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTGA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720387556 186 GVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMenVESDPKTDRPKEEVLI 250
Cdd:cd01922    82 GILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM--VEVQTQTDRPIDEVKI 144
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 101-262 4.65e-48

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: 159.44  E-value: 4.65e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 101 KGYVRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKPFKDEFRPNL 180
Cdd:cd01925     5 TGKVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 181 SHTGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGgfDTLTAM---ENVESDpKTDRPKEEVLICTTTVFV 257
Cdd:cd01925    85 RFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTG--DTIYNLlklAEVETD-KDERPVYPPKITSVEVLE 161


                  ....*
gi 1720387556 258 DPYEE 262
Cdd:cd01925   162 NPFDD 166
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 111-250 3.50e-42

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: 144.32  E-value: 3.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 111 GDLNLELHCDLTPKTCENFIKLC--------KKQYYDGTIFHRSIRNFVIQGGDPTGTGTG-GESFWGKPFKDE-FrpNL 180
Cdd:cd01926    15 GRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTgGKSIYGEKFPDEnF--KL 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 181 SHTGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESDpkTDRPKEEVLI 250
Cdd:cd01926    93 KHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG--NGKPKKKVVI 160
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 106-262 3.24e-38

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: 134.01  E-value: 3.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 106 LHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFWGKP-------FKDEFRP 178
Cdd:cd01921     2 LETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSQLygrqarfFEPEILP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 179 NLSHTGRGVLSMANSGPNTNKSQFFITFRSCA-YLDKKHTIFGRVVGGFDTLTAMENVESDPKtDRPKEEVLICTTTVFV 257
Cdd:cd01921    82 LLKHSKKGTVSMVNAGDNLNGSQFYITLGENLdYLDGKHTVFGQVVEGFDVLEKINDAIVDDD-GRPLKDIRIKHTHILD 160


                  ....*
gi 1720387556 258 DPYEE 262
Cdd:cd01921   161 DPFPD 165
PTZ00060 PTZ00060
cyclophilin; Provisional
 109-250 2.20e-36

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 129.58  E-value: 2.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 109 NKGDLNLELHCDLTPKTCENFIKLC---------KKQYYDGTIFHRSIRNFVIQGGDPTGTGTGG-ESFWGKPFKDE-Fr 177
Cdd:PTZ00060   28 PAGRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDITNHNGTGgESIYGRKFTDEnF- 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720387556 178 pNLSHTGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVGGFDTLTAMENVESdpKTDRPKEEVLI 250
Cdd:PTZ00060  107 -KLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGT--QSGYPKKPVVV 176
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 111-250 7.43e-35

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 125.72  E-value: 7.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 111 GDLNLELHCDLTPKTCENFIKLCKKQY--------YDGTIFHRSIRNFVIQGGDPTGTGTGG-ESFWGKPFKDEfrpNL- 180
Cdd:PLN03149   33 GRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDFLKGDGTGcVSIYGSKFEDE---NFi 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720387556 181 -SHTGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVG-GFDTLTAMENVESDPkTDRPKEEVLI 250
Cdd:PLN03149  110 aKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGdGLLVVRKIENVATGP-NNRPKLACVI 180
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 106-250 1.34e-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: 116.39  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 106 LHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESFwgKPFKDEFRPNLSHTgR 185
Cdd:cd01920     2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKETL--KPIKNEAGNGLSNT-R 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387556 186 GVLSMANSG-PNTNKSQFFITFRSCAYLDKK-----HTIFGRVVGGFDTLTAMENVE---SDPKTDRPKEEVLI 250
Cdd:cd01920    79 GTIAMARTNaPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVEtysFGSYQDVPVQDVII 152
PRK10791 PRK10791
peptidylprolyl isomerase B;
104-255 1.05e-17

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 79.11  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 104 VRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESfwGKPFKDEFRPNLSHT 183
Cdd:PRK10791    2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGGFEPGMKQKAT--KEPIKNEANNGLKNT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 184 gRGVLSMANSG-PNTNKSQFFI--------TFRSCAYLDKKHTIFGRVVGGFDTLTAMENVE---SDPKTDRPKEEVLIC 251
Cdd:PRK10791   80 -RGTLAMARTQaPHSATAQFFInvvdndflNFSGESLQGWGYCVFAEVVEGMDVVDKIKGVAtgrSGMHQDVPKEDVIIE 158


                  ....
gi 1720387556 252 TTTV 255
Cdd:PRK10791  159 SVTV 162
PRK10903 PRK10903
peptidylprolyl isomerase A;
103-255 2.11e-15

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 73.34  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 103 YVRLHTNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGTGGESfwGKPFKDEFRPNLSH 182
Cdd:PRK10903   30 HVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKP--NPPIKNEADNGLRN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 183 TgRGVLSMA-NSGPNTNKSQFFITFRSCAYLDK-----KHTIFGRVVGGFDTLTAMENVESD---PKTDRPKEEVLICTT 253
Cdd:PRK10903  108 T-RGTIAMArTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPTHdvgPYQNVPSKPVVILSA 186


                  ..
gi 1720387556 254 TV 255
Cdd:PRK10903  187 KV 188
PTZ00221 PTZ00221
cyclophilin; Provisional
 111-250 1.34e-10

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 60.65  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 111 GDLNLELHCDLTPKTCENFIKLCK-----------KQYYDGTIFHRSIRNFVIQGGDPTGTGTGgeSFWGKPFKDE-FRp 178
Cdd:PTZ00221   67 GRLVFELFEDVVPETVENFRALITgscgidtntgvKLDYLYTPVHHVDRNNNIIVLGELDSFNV--SSTGTPIADEgYR- 143

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720387556 179 nLSHTGRGVLSMANSGPNTNKSQFFITFRSCAYLDKKHTIFGRVVggfDTLTAMENVESDPKTD--RPKEEVLI 250
Cdd:PTZ00221  144 -HRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAV---DDLSLLEKLESLPLDDvgRPLLPVTV 213
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 108-233 5.48e-10

cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) similar ot the Spinach thylakoid lumen protein TLP40. Compared to the archetypal cyclophilin Human cyclophilin A, these proteins have similar peptidylprolyl cis- trans isomerase activity and reduced affinity for cyclosporin A. Spinach TLP40 has been shown to have a dual function as a folding catalyst and regulator of dephosphorylation.


Pssm-ID: 238905  Cd Length: 176  Bit Score: 57.84  E-value: 5.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 108 TNKGDLNLELHCDLTPKTCENFIKLCKKQYYDGTIFHRSIRNFVIQGGDPTGTGT---------------------GGES 166
Cdd:cd01924     4 TDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPgfpdpetgksrtipleikpegQKQP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720387556 167 FWGKPFKDEFRPN-----LSHTgRGVLSMANS--GPNTNKSQFFITFRSCA-------YLDKKHTIFGRVVGGFDTLTAM 232
Cdd:cd01924    84 VYGKTLEEAGRYDeqpvlPFNA-FGAIAMARTefDPNSASSQFFFLLKDNEltpsrnnVLDGRYAVFGYVTDGLDILREL 162


                  .
gi 1720387556 233 E 233
Cdd:cd01924   163 K 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.
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