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Conserved domains on  [gi|257745192|emb|CBC52202|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

peptidylprolyl isomerase( domain architecture ID 10011006)

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
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 14-199 2.18e-148

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


:

Pssm-ID: 178694  Cd Length: 186  Bit Score: 409.23  E-value: 2.18e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  14 SSGGGNVEWHVRPPNPKNPVVFFDVSIGGIPAGRIKMELFADIAPKTAENFRQFCTGELRKAGKPLGYKECQFHRVIKDF 93
Cdd:PLN03149   1 SAGAGNVEWHLRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  94 MVQSGDFLKNDGSGCMSIYGHKFEDENFTAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVM 173
Cdd:PLN03149  81 MIQGGDFLKGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVV 160

                        170       180
                 ....*....|....*....|....*.
gi 257745192 174 RKIENVAIGPNNRPKLAVVITECGEM 199
Cdd:PLN03149 161 RKIENVATGPNNRPKLACVISECGEM 186
 
Name Accession Description Interval E-value
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 14-199 2.18e-148

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 409.23  E-value: 2.18e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  14 SSGGGNVEWHVRPPNPKNPVVFFDVSIGGIPAGRIKMELFADIAPKTAENFRQFCTGELRKAGKPLGYKECQFHRVIKDF 93
Cdd:PLN03149   1 SAGAGNVEWHLRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  94 MVQSGDFLKNDGSGCMSIYGHKFEDENFTAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVM 173
Cdd:PLN03149  81 MIQGGDFLKGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVV 160

                        170       180
                 ....*....|....*....|....*.
gi 257745192 174 RKIENVAIGPNNRPKLAVVITECGEM 199
Cdd:PLN03149 161 RKIENVATGPNNRPKLACVISECGEM 186
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 32-197 2.63e-114

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: 322.28  E-value: 2.63e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  32 PVVFFDVSIGGIPAGRIKMELFADIAPKTAENFRQFCTGELRKAGKPLGYKECQFHRVIKDFMVQSGDFLKNDGSGCMSI 111
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 112 YGHKFEDENFTAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGpNNRPKLAV 191
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV-EGMDVVKKIENVGSG-NGKPKKKV 158


                 ....*.
gi 257745192 192 VITECG 197
Cdd:cd01926  159 VIADCG 164
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 45-198 5.21e-53

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: 166.66  E-value: 5.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192   45 AGRIKMELFADIAPKTAENFRQFCTGElrkagkplGYKECQFHRVIKDFMVQSGDFLKNDGSGCmSIYGhkFEDENFTAK 124
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCKKG--------FYDGTTFHRVIPGFMVQGGDPTGTGGGGK-SIFP--IPDEIFPLL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257745192  125 HT-GPGLLSMANSG--PNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGpNNRPKLAVVITECGE 198
Cdd:pfam00160  75 LKhKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVV-EGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 29-194 3.69e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 144.16  E-value: 3.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  29 PKNPVVFFDVSiggipAGRIKMELFADIAPKTAENFRQfctgeLRKAGKplgYKECQFHRVIKDFMVQSGDFlKNDGSGC 108
Cdd:COG0652    4 APNPTVTLETN-----KGDIVIELFPDKAPKTVANFVS-----LAKEGF---YDGTIFHRVIPGFMIQGGDP-TGTGTGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 109 MsiyGHKFEDENFTAKHTGPGLLSMANS-GPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGPNNRP 187
Cdd:COG0652   70 P---GYTIPDEFDPGLKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVV-EGMDVVDKIAAGPTDPGDGP 145


                 ....*..
gi 257745192 188 KLAVVIT 194
Cdd:COG0652  146 LEPVVIE 152
 
Name Accession Description Interval E-value
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 14-199 2.18e-148

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 409.23  E-value: 2.18e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  14 SSGGGNVEWHVRPPNPKNPVVFFDVSIGGIPAGRIKMELFADIAPKTAENFRQFCTGELRKAGKPLGYKECQFHRVIKDF 93
Cdd:PLN03149   1 SAGAGNVEWHLRPPNPKNPVVFFDVTIGGIPAGRIKMELFADIAPKTAENFRQFCTGEFRKAGLPQGYKGCQFHRVIKDF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  94 MVQSGDFLKNDGSGCMSIYGHKFEDENFTAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVM 173
Cdd:PLN03149  81 MIQGGDFLKGDGTGCVSIYGSKFEDENFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVV 160

                        170       180
                 ....*....|....*....|....*.
gi 257745192 174 RKIENVAIGPNNRPKLAVVITECGEM 199
Cdd:PLN03149 161 RKIENVATGPNNRPKLACVISECGEM 186
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 32-197 2.63e-114

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: 322.28  E-value: 2.63e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  32 PVVFFDVSIGGIPAGRIKMELFADIAPKTAENFRQFCTGELRKAGKPLGYKECQFHRVIKDFMVQSGDFLKNDGSGCMSI 111
Cdd:cd01926    1 PKVFFDITIGGEPAGRIVMELFADVVPKTAENFRALCTGEKGKGGKPFGYKGSTFHRVIPDFMIQGGDFTRGNGTGGKSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 112 YGHKFEDENFTAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGpNNRPKLAV 191
Cdd:cd01926   81 YGEKFPDENFKLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVV-EGMDVVKKIENVGSG-NGKPKKKV 158


                 ....*.
gi 257745192 192 VITECG 197
Cdd:cd01926  159 VIADCG 164
PTZ00060 PTZ00060
cyclophilin; Provisional
 26-199 1.88e-79

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 234.74  E-value: 1.88e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  26 PPNPKNPVVFFDVSIGGIPAGRIKMELFADIAPKTAENFRQFCTGE-LRKAGKPLGYKECQFHRVIKDFMVQSGDFLKND 104
Cdd:PTZ00060  10 PEMSKRPKVFFDISIDNAPAGRIVFELFSDVTPKTAENFRALCIGDkVGSSGKNLHYKGSIFHRIIPQFMCQGGDITNHN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 105 GSGCMSIYGHKFEDENFTAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAiGPN 184
Cdd:PTZ00060  90 GTGGESIYGRKFTDENFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVI-EGMEVVRAMEKEG-TQS 167

                        170
                 ....*....|....*
gi 257745192 185 NRPKLAVVITECGEM 199
Cdd:PTZ00060 168 GYPKKPVVVTDCGEL 182
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 35-194 4.36e-57

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: 176.69  E-value: 4.36e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  35 FFDVSIGgipagRIKMELFADIAPKTAENFRQFCTGElrkagkplGYKECQFHRVIKDFMVQSGDFLKNDGSGcmSIYGH 114
Cdd:cd00317    1 TLDTTKG-----RIVIELYGDEAPKTVENFLSLARGG--------FYDGTTFHRVIPGFMIQGGDPTGTGGGG--SGPGY 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 115 KFEDENFTAK-HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGPNNRPKLAVVI 193
Cdd:cd00317   66 KFPDENFPLKyHHRRGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVV-EGMDVVDKIERGDTDENGRPIKPVTI 144


                 .
gi 257745192 194 T 194
Cdd:cd00317  145 S 145
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 45-198 5.21e-53

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: 166.66  E-value: 5.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192   45 AGRIKMELFADIAPKTAENFRQFCTGElrkagkplGYKECQFHRVIKDFMVQSGDFLKNDGSGCmSIYGhkFEDENFTAK 124
Cdd:pfam00160   6 LGRIVIELFGDKAPKTVENFLQLCKKG--------FYDGTTFHRVIPGFMVQGGDPTGTGGGGK-SIFP--IPDEIFPLL 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257745192  125 HT-GPGLLSMANSG--PNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGpNNRPKLAVVITECGE 198
Cdd:pfam00160  75 LKhKRGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVV-EGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 46-187 1.88e-49

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: 157.62  E-value: 1.88e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  46 GRIKMELFADIAPKTAENFRQFCtgelrKAGKplgYKECQFHRVIKDFMVQSGDFLkNDGSGCMSIYGHKFEDE-NFTAK 124
Cdd:cd01927    7 GDIHIRLFPEEAPKTVENFTTHA-----RNGY---YNNTIFHRVIKGFMIQTGDPT-GDGTGGESIWGKEFEDEfSPSLK 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257745192 125 HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGdGLLVMRKIENVAIGPNNRP 187
Cdd:cd01927   78 HDRPYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVK-GMDVVQRIENVKTDKNDRP 139
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 46-193 8.14e-46

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: 148.72  E-value: 8.14e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  46 GRIKMELFADIAPKTAENFRQFCtgelrKAGKplgYKECQFHRVIKDFMVQSGDfLKNDGSGCMSIYGHKFEDE-NFTAK 124
Cdd:cd01923    9 GDLNLELHCDKAPKACENFIKLC-----KKGY---YDGTIFHRSIRNFMIQGGD-PTGTGRGGESIWGKPFKDEfKPNLS 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257745192 125 HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGdGLLVMRKIENVAIGPNNRPKLAVVI 193
Cdd:cd01923   80 HDGRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVG-GLETLEAMENVPDPGTDRPKEEIKI 147
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 46-194 5.95e-45

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: 146.04  E-value: 5.95e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  46 GRIKMELFADIAPKTAENFRQFCTGELrkagkplgYKECQFHRVIKDFMVQSGDfLKNDGSGCMSIYGHKFEDENF-TAK 124
Cdd:cd01928   10 GDIKIELFCDDCPKACENFLALCASGY--------YNGCIFHRNIKGFMVQTGD-PTGTGKGGESIWGKKFEDEFReTLK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 125 HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGPNNRPKLAVVIT 194
Cdd:cd01928   81 HDSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVI-DGFETLDTLEKLPVDKKYRPLEEIRIK 149
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 29-194 3.69e-44

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 144.16  E-value: 3.69e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  29 PKNPVVFFDVSiggipAGRIKMELFADIAPKTAENFRQfctgeLRKAGKplgYKECQFHRVIKDFMVQSGDFlKNDGSGC 108
Cdd:COG0652    4 APNPTVTLETN-----KGDIVIELFPDKAPKTVANFVS-----LAKEGF---YDGTIFHRVIPGFMIQGGDP-TGTGTGG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 109 MsiyGHKFEDENFTAKHTGPGLLSMANS-GPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGPNNRP 187
Cdd:COG0652   70 P---GYTIPDEFDPGLKHKRGTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVV-EGMDVVDKIAAGPTDPGDGP 145


                 ....*..
gi 257745192 188 KLAVVIT 194
Cdd:COG0652  146 LEPVVIE 152
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 46-193 1.33e-42

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: 139.98  E-value: 1.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  46 GRIKMELFADIAPKTAENFRQFCTGELrkagkplgYKECQFHRVIKDFMVQSGDFLKNdGSGCMSIYGHKFEDE-NFTAK 124
Cdd:cd01922    7 GEITLELYWNHAPKTCKNFYELAKRGY--------YNGTIFHRLIKDFMIQGGDPTGT-GRGGASIYGKKFEDEiHPELK 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 257745192 125 HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVlGDGLLVMRKIENVAiGPNNRPKLAVVI 193
Cdd:cd01922   78 HTGAGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRV-SKGMKVIENMVEVQ-TQTDRPIDEVKI 144
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 45-196 4.95e-40

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: 134.40  E-value: 4.95e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  45 AGRIKMELFADIAPKTAENFRQFCTGELrkagkplgYKECQFHRVIKDFMVQSGDfLKNDGSGCMSIYGHKFEDE-NFTA 123
Cdd:cd01925   14 AGDIDIELWSKEAPKACRNFIQLCLEGY--------YDNTIFHRVVPGFIIQGGD-PTGTGTGGESIYGEPFKDEfHSRL 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 257745192 124 KHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLGDGLLVMRKIENVAIGPNNRPKLAVVITEC 196
Cdd:cd01925   85 RFNRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGDTIYNLLKLAEVETDKDERPVYPPKITSV 157
PTZ00221 PTZ00221
cyclophilin; Provisional
 34-199 2.37e-31

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 114.20  E-value: 2.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  34 VFFDVSIGGIPAGRIKMELFADIAPKTAENFRQFCTGEL---RKAGKPLGYKECQFHRV-IKDFMVQSGDFLkndgSGCM 109
Cdd:PTZ00221  55 AFLDISIGDVLAGRLVFELFEDVVPETVENFRALITGSCgidTNTGVKLDYLYTPVHHVdRNNNIIVLGELD----SFNV 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 110 SIYGHKFEDENFTAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVMRKIENVAIGPNNRPKL 189
Cdd:PTZ00221 131 SSTGTPIADEGYRHRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAV-DDLSLLEKLESLPLDDVGRPLL 209

                        170
                 ....*....|
gi 257745192 190 AVVITECGEM 199
Cdd:PTZ00221 210 PVTVSFCGAL 219
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 46-194 9.82e-25

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: 94.72  E-value: 9.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  46 GRIKMELFADIAPKTAENFRQFCtgelrkagKPLGYKECQFHRVIKDFMVQSGDFL--KNDGSGCMSIYGHK----FEDE 119
Cdd:cd01921    7 GDLVIDLFTDECPLACLNFLKLC--------KLKYYNFCLFYNVQKDFIAQTGDPTgtGAGGESIYSQLYGRqarfFEPE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 257745192 120 -NFTAKHTGPGLLSMANSGPNTNGCQFFITCAK-CDWLDNKHVVFGRVLgDGLLVMRKIENVAIGPNNRPKLAVVIT 194
Cdd:cd01921   79 iLPLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVV-EGFDVLEKINDAIVDDDGRPLKDIRIK 154
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 45-193 1.43e-15

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: 70.55  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  45 AGRIKMELFADIAPKTAENFRQFCtgelrKAGKplgYKECQFHRVIKDFMVQSGDFlkndgsgcmsiyghkfeDENFTAK 124
Cdd:cd01920    6 LGDIVVELYDDKAPITVENFLAYV-----RKGF---YDNTIFHRVISGFVIQGGGF-----------------TPDLAQK 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 125 HTGP--------------GLLSMANSG-PNTNGCQFFITCAKCDWLDNK-----HVVFGRVLgDGLLVMRKIENVAIGPN 184
Cdd:cd01920   61 ETLKpikneagnglsntrGTIAMARTNaPDSATSQFFINLKDNASLDYQneqwgYTVFGEVT-EGMDVVDKIAGVETYSF 139

                        170
                 ....*....|...
gi 257745192 185 NR----PKLAVVI 193
Cdd:cd01920  140 GSyqdvPVQDVII 152
PRK10791 PRK10791
peptidylprolyl isomerase B;
46-194 7.62e-10

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 55.23  E-value: 7.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  46 GRIKMELFADIAPKTAENFRQFCTGELrkagkplgYKECQFHRVIKDFMVQSGDFLKndgsgcmsiyGHKFEDENFTAKH 125
Cdd:PRK10791   9 GDIVIKTFDDKAPETVKNFLDYCREGF--------YNNTIFHRVINGFMIQGGGFEP----------GMKQKATKEPIKN 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 126 TGP-------GLLSMANSG-PNTNGCQFFITCAKCDWLDNK--------HVVFGRVLgDGLLVMRKIENVAIGPN----N 185
Cdd:PRK10791  71 EANnglkntrGTLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVV-EGMDVVDKIKGVATGRSgmhqD 149


                 ....*....
gi 257745192 186 RPKLAVVIT 194
Cdd:PRK10791 150 VPKEDVIIE 158
PRK10903 PRK10903
peptidylprolyl isomerase A;
45-193 5.44e-09

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 53.31  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192  45 AGRIKMELFADIAPKTAENFRQFCTGELrkagkplgYKECQFHRVIKDFMVQSGDFlkndgsgcmsiyghkfeDENFTAK 124
Cdd:PRK10903  37 AGNIELELNSQKAPVSVKNFVDYVNSGF--------YNNTTFHRVIPGFMIQGGGF-----------------TEQMQQK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 257745192 125 HTGPGLLSMANSG-PNTNGC--------------QFFITCAKCDWLDN-----KHVVFGRVLgDGLLVMRKIENVA---I 181
Cdd:PRK10903  92 KPNPPIKNEADNGlRNTRGTiamartadkdsatsQFFINVADNAFLDHgqrdfGYAVFGKVV-KGMDVADKISQVPthdV 170

                        170
                 ....*....|...
gi 257745192 182 GP-NNRPKLAVVI 193
Cdd:PRK10903 171 GPyQNVPSKPVVI 183
 
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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