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Conserved domains on  [gi|17539496|ref|NP_501118|]
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Peptidyl-prolyl cis-trans isomerase [Caenorhabditis elegans]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10112468)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 13-159 1.06e-105

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: 298.68  E-value: 1.06e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  13 ILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGDKFSDEIDERLKHTG 92
Cdd:cd01922   1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539496  93 AGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTdNHDRPKIEIRILK 159
Cdd:cd01922  81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQT-QTDRPIDEVKILK 146
 
Name Accession Description Interval E-value
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 13-159 1.06e-105

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: 298.68  E-value: 1.06e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  13 ILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGDKFSDEIDERLKHTG 92
Cdd:cd01922   1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539496  93 AGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTdNHDRPKIEIRILK 159
Cdd:cd01922  81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQT-QTDRPIDEVKILK 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 7-160 3.58e-73

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 216.57  E-value: 3.58e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   7 DQAPYVILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGAsiyGDKFSDEIDE 86
Cdd:COG0652   4 APNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539496  87 RLKHTgAGILSMANA-GPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNHDRPKIEIRILKA 160
Cdd:COG0652  81 GLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESV 154
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 17-160 3.16e-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: 191.31  E-value: 3.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496    17 TMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGdkFSDEIDERLKHTGAGIL 96
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFP--IPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539496    97 SMANAG--PNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNhDRPKIEIRILKA 160
Cdd:pfam00160  83 SMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSC 147
PTZ00060 PTZ00060
cyclophilin; Provisional
 10-147 1.19e-52

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 165.79  E-value: 1.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   10 PYVILDTTM-----GKIALELYWNHAPRTCQNFSQL---------AKRNYYNGTIFHRIIADFMIQGGDPT-GTGRGGAS 74
Cdd:PTZ00060  16 PKVFFDISIdnapaGRIVFELFSDVTPKTAENFRALcigdkvgssGKNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGES 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539496   75 IYGDKFSDEiDERLKHTGAGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDN 147
Cdd:PTZ00060  96 IYGRKFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS 167
 
Name Accession Description Interval E-value
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 13-159 1.06e-105

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: 298.68  E-value: 1.06e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  13 ILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGDKFSDEIDERLKHTG 92
Cdd:cd01922   1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539496  93 AGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTdNHDRPKIEIRILK 159
Cdd:cd01922  81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQT-QTDRPIDEVKILK 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 11-160 3.86e-79

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: 231.92  E-value: 3.86e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  11 YVILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGDKFSDEIDERLKH 90
Cdd:cd01923   1 YVRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSH 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  91 TGAGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNHDRPKIEIRILKA 160
Cdd:cd01923  81 DGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDT 150
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 7-160 3.58e-73

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 216.57  E-value: 3.58e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   7 DQAPYVILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGAsiyGDKFSDEIDE 86
Cdd:COG0652   4 APNPTVTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17539496  87 RLKHTgAGILSMANA-GPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNHDRPKIEIRILKA 160
Cdd:COG0652  81 GLKHK-RGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESV 154
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 13-159 5.98e-72

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: 213.28  E-value: 5.98e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  13 ILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGaSIYGDKFSDEIDERLKHTG 92
Cdd:cd00317   1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539496  93 AGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNHDRPKIEIRILK 159
Cdd:cd00317  80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 13-158 1.12e-69

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: 207.70  E-value: 1.12e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  13 ILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGDKFSDEIDERLKHTG 92
Cdd:cd01927   1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539496  93 AGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNHDRPKIEIRIL 158
Cdd:cd01927  81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKII 146
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 12-157 2.37e-67

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: 201.90  E-value: 2.37e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  12 VILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGDKFSDEIDERLKHT 91
Cdd:cd01928   3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539496  92 GAGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNHDRPKIEIRI 157
Cdd:cd01928  83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRI 148
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 12-158 7.74e-65

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: 196.03  E-value: 7.74e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  12 VILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGDKFSDEIDERLKHT 91
Cdd:cd01925   8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRLRFN 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  92 GAGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAgmKVIANM---GRVDTDNHDRPKIEIRIL 158
Cdd:cd01925  88 RRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTG--DTIYNLlklAEVETDKDERPVYPPKIT 155
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 17-160 3.16e-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: 191.31  E-value: 3.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496    17 TMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGdkFSDEIDERLKHTGAGIL 96
Cdd:pfam00160   5 GLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSIFP--IPDEIFPLLLKHKRGAL 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17539496    97 SMANAG--PNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNhDRPKIEIRILKA 160
Cdd:pfam00160  83 SMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG-DRPVKPVKILSC 147
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 13-157 4.47e-62

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: 189.01  E-value: 4.47e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  13 ILDTTMGKIALELYWNHAPRTCQNFSQLA--------KRNYYNGTIFHRIIADFMIQGGDPT-GTGRGGASIYGDKFSDE 83
Cdd:cd01926   9 IGGEPAGRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKFPDE 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539496  84 iDERLKHTGAGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNhDRPKIEIRI 157
Cdd:cd01926  89 -NFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSGN-GKPKKKVVI 160
PTZ00060 PTZ00060
cyclophilin; Provisional
 10-147 1.19e-52

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 165.79  E-value: 1.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   10 PYVILDTTM-----GKIALELYWNHAPRTCQNFSQL---------AKRNYYNGTIFHRIIADFMIQGGDPT-GTGRGGAS 74
Cdd:PTZ00060  16 PKVFFDISIdnapaGRIVFELFSDVTPKTAENFRALcigdkvgssGKNLHYKGSIFHRIIPQFMCQGGDITnHNGTGGES 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17539496   75 IYGDKFSDEiDERLKHTGAGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDN 147
Cdd:PTZ00060  96 IYGRKFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGTQS 167
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 4-157 3.78e-52

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 164.62  E-value: 3.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496    4 PINDQAPYVILDTTMG-----KIALELYWNHAPRTCQNFSQLAKRNY--------YNGTIFHRIIADFMIQGGD-PTGTG 69
Cdd:PLN03149  13 PPNPKNPVVFFDVTIGgipagRIKMELFADIAPKTAENFRQFCTGEFrkaglpqgYKGCQFHRVIKDFMIQGGDfLKGDG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   70 RGGASIYGDKFSDEiDERLKHTGAGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAA-GMKVIANMGRVDTDNH 148
Cdd:PLN03149  93 TGCVSIYGSKFEDE-NFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGdGLLVVRKIENVATGPN 171


                 ....*....
gi 17539496  149 DRPKIEIRI 157
Cdd:PLN03149 172 NRPKLACVI 180
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 13-161 5.38e-50

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: 158.27  E-value: 5.38e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  13 ILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASIYGDK-------FSDEID 85
Cdd:cd01921   1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSQLygrqarfFEPEIL 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17539496  86 ERLKHTGAGILSMANAGPNTNGSQFFITLAP-TQHLDGKHTIFGRVAAGMKVIANMGRVDTDNHDRPKIEIRILKAY 161
Cdd:cd01921  81 PLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRIKHTH 157
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 14-147 4.15e-28

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: 102.14  E-value: 4.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  14 LDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASiyGDKFSDEIDERLKHTgA 93
Cdd:cd01920   2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLAQKET--LKPIKNEAGNGLSNT-R 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  94 GILSMA-NAGPNTNGSQFFITLAPTQHLD-----GKHTIFGRVAAGMKVIANMGRVDTDN 147
Cdd:cd01920  79 GTIAMArTNAPDSATSQFFINLKDNASLDyqneqWGYTVFGEVTEGMDVVDKIAGVETYS 138
PRK10903 PRK10903
peptidylprolyl isomerase A;
10-147 3.85e-24

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 92.98  E-value: 3.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   10 PYVILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRGGASiyGDKFSDEIDERLK 89
Cdd:PRK10903  29 PHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQMQQKKP--NPPIKNEADNGLR 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17539496   90 HTgAGILSMA-NAGPNTNGSQFFITLAPTQHLD-GK----HTIFGRVAAGMKVIANMGRVDTDN 147
Cdd:PRK10903 107 NT-RGTIAMArTADKDSATSQFFINVADNAFLDhGQrdfgYAVFGKVVKGMDVADKISQVPTHD 169
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 16-138 1.70e-16

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: 72.48  E-value: 1.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496  16 TTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGGDPTGTGRG---------------------GAS 74
Cdd:cd01924   4 TDNGTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleikpegqKQP 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17539496  75 IYGDKFS-----DEIDERLKHTgAGILSMANA--GPNTNGSQFFITL-------APTQHLDGKHTIFGRVAAGMKVIA 138
Cdd:cd01924  84 VYGKTLEeagryDEQPVLPFNA-FGAIAMARTefDPNSASSQFFFLLkdneltpSRNNVLDGRYAVFGYVTDGLDILR 160
PRK10791 PRK10791
peptidylprolyl isomerase B;
12-164 1.26e-13

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 64.86  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   12 VILDTTMGKIALELYWNHAPRTCQNFSQLAKRNYYNGTIFHRIIADFMIQGG--DPTGTGRGGAsiygDKFSDEIDERLK 89
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGgfEPGMKQKATK----EPIKNEANNGLK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   90 HTgAGILSMANAG-PNTNGSQFFITLAPTQHLDGK--------HTIFGRVAAGMKVIANMGRVDTD----NHDRPKIEIR 156
Cdd:PRK10791  78 NT-RGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGrsgmHQDVPKEDVI 156


                 ....*...
gi 17539496  157 ILKAYPSE 164
Cdd:PRK10791 157 IESVTVSE 164
PTZ00221 PTZ00221
cyclophilin; Provisional
 13-151 1.53e-13

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 66.05  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17539496   13 ILDTTMGKIALELYWNHAPRTCQNFSQLAK-----------RNYYNGTIFHRI-IADFMIQGGDPTGTGrggASIYGDKF 80
Cdd:PTZ00221  61 IGDVLAGRLVFELFEDVVPETVENFRALITgscgidtntgvKLDYLYTPVHHVdRNNNIIVLGELDSFN---VSSTGTPI 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17539496   81 SDEiDERLKHTGAGILSMANAGPNTNGSQFFITLAPTQHLDGKHTIFGRVAAGMKVIANMGRVDTDNHDRP 151
Cdd:PTZ00221 138 ADE-GYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRP 207
 
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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