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Conserved domains on  [gi|22331588|ref|NP_190046|]
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cyclophilin71 [Arabidopsis thaliana]

Protein Classification

WD40 repeat domain-containing peptidylprolyl isomerase( domain architecture ID 13235605)

WD40 repeat domain-containing cyclophilin-type peptidylprolyl isomerase catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins

CATH:  2.40.100.10|2.130.10.10
EC:  5.2.1.8
Gene Ontology:  GO:0006457|GO:0003755|GO:0000413|GO:0005515
PubMed:  14731520|15998457|15353287|10322433|8090199|30069656|29026209

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 479-626 5.03e-113

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: 334.81  E-value: 5.03e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 479 IMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHDR 558
Cdd:cd01927   1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331588 559 PFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNV 626
Cdd:cd01927  81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIINI 148
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 68-286 5.28e-12

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 66.97  E-value: 5.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  68 MHRDVVTHVAVSAAEFFISGSM-DGHLKFWKKKGVGIEFAkhFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYD 146
Cdd:cd00200  91 GHTSYVSSVAFSPDGRILSSSSrDKTIKVWDVETGKCLTT--LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 147 MMAMIRLPYipGAVEWVYKQGDvKAKLAVSDRDSlFVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMISGDTKGI 226
Cdd:cd00200 169 CVATLTGHT--GEVNSVAFSPD-GEKLLSSSSDG-TIKLWDLSTG--KCLGTLRGHENGVNSVAFSPDGYLLASGSEDGT 242

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 227 IEYWSATTlqfpeDEVNFKLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVF 286
Cdd:cd00200 243 IRVWDLRT-----GECVQTLSGHTN---------SVTSLAWSPDGKRLASGSADGTIRIW 288
 
Name Accession Description Interval E-value
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 479-626 5.03e-113

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: 334.81  E-value: 5.03e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 479 IMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHDR 558
Cdd:cd01927   1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331588 559 PFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNV 626
Cdd:cd01927  81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIINI 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 478-628 2.62e-75

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 237.76  E-value: 2.62e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 478 VIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQsiwGREFEDEFHKSLRHD 557
Cdd:COG0652   9 VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKHK 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331588 558 RpFTLSMANA-GPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNVTV 628
Cdd:COG0652  86 R-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTI 156
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 480-628 1.35e-64

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: 209.03  E-value: 1.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588   480 MHT-TLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIwgREFEDEFHKSLRHDR 558
Cdd:pfam00160   1 IETnGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331588   559 PFTLSMANAG--PNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDkNDRPYQDVKILNVTV 628
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 485-625 8.11e-50

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 171.18  E-value: 8.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  485 GDIHMKLYPEECPKTVENFTTHC---------RNGYYDNHLFHRVIRGFMIQTGD-PLGDGTGGQSIWGREFEDEFHKsL 554
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDiTNHNGTGGESIYGRKFTDENFK-L 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331588  555 RHDRPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTdKNDRPYQDVKILN 625
Cdd:PTZ00060 109 KHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGT-QSGYPKKPVVVTD 178
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 68-286 5.28e-12

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 66.97  E-value: 5.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  68 MHRDVVTHVAVSAAEFFISGSM-DGHLKFWKKKGVGIEFAkhFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYD 146
Cdd:cd00200  91 GHTSYVSSVAFSPDGRILSSSSrDKTIKVWDVETGKCLTT--LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 147 MMAMIRLPYipGAVEWVYKQGDvKAKLAVSDRDSlFVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMISGDTKGI 226
Cdd:cd00200 169 CVATLTGHT--GEVNSVAFSPD-GEKLLSSSSDG-TIKLWDLSTG--KCLGTLRGHENGVNSVAFSPDGYLLASGSEDGT 242

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 227 IEYWSATTlqfpeDEVNFKLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVF 286
Cdd:cd00200 243 IRVWDLRT-----GECVQTLSGHTN---------SVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
69-297 1.65e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.47  E-value: 1.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  69 HRDVVTHVAVSAA-EFFISGSMDGHLKFWK-KKGvgiEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYD 146
Cdd:COG2319 161 HSGAVTSVAFSPDgKLLASGSDDGTVRLWDlATG---KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 147 MMAMIRlpyipGAVEWVYK-----QGDVkakLAVSDRDSLfVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMISG 221
Cdd:COG2319 238 LLRTLT-----GHSGSVRSvafspDGRL---LASGSADGT-VRLWDLATG--ELLRTLTGHSGGVNSVAFSPDGKLLASG 306

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331588 222 DTKGIIEYWSATTLQFPedevnFKLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRVY 297
Cdd:COG2319 307 SDDGTVRLWDLATGKLL-----RTLTGHTG---------AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 69-97 3.27e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.75  E-value: 3.27e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 22331588     69 HRDVVTHVAVSA-AEFFISGSMDGHLKFWK 97
Cdd:smart00320  11 HTGPVTSVAFSPdGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 479-626 5.03e-113

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: 334.81  E-value: 5.03e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 479 IMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHDR 558
Cdd:cd01927   1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331588 559 PFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNV 626
Cdd:cd01927  81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKTDKNDRPYEDIKIINI 148
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 479-625 1.81e-76

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: 240.24  E-value: 1.81e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 479 IMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGqSIWGREFEDEFHKSLRHDR 558
Cdd:cd00317   1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHR 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22331588 559 PFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILN 625
Cdd:cd00317  80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDENGRPIKPVTISD 146
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 478-628 2.62e-75

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 237.76  E-value: 2.62e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 478 VIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQsiwGREFEDEFHKSLRHD 557
Cdd:COG0652   9 VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKHK 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331588 558 RpFTLSMANA-GPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNVTV 628
Cdd:COG0652  86 R-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDPGDGPLEPVVIESVTI 156
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 478-628 4.01e-70

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: 224.22  E-value: 4.01e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 478 VIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHD 557
Cdd:cd01923   2 VRLHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHD 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331588 558 RPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNVTV 628
Cdd:cd01923  82 GRGVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPDPGTDRPKEEIKIEDTSV 152
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 478-628 6.06e-68

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: 218.07  E-value: 6.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 478 VIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHD 557
Cdd:cd01928   3 VTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKHD 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331588 558 RPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKILNVTV 628
Cdd:cd01928  83 SRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPVDKKYRPLEEIRIKDVTI 153
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 480-628 1.35e-64

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: 209.03  E-value: 1.35e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588   480 MHT-TLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIwgREFEDEFHKSLRHDR 558
Cdd:pfam00160   1 IETnGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22331588   559 PFTLSMANAG--PNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDkNDRPYQDVKILNVTV 628
Cdd:pfam00160  79 RGALSMANTGpaPNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTD-GDRPVKPVKILSCGV 149
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 484-623 1.23e-63

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: 207.11  E-value: 1.23e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 484 LGDIHMKLYPEECPKTVENFTTHC--------RNGYYDNHLFHRVIRGFMIQTGDPL-GDGTGGQSIWGREFEDE-FHks 553
Cdd:cd01926  14 AGRIVMELFADVVPKTAENFRALCtgekgkggKPFGYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKFPDEnFK-- 91

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 554 LRHDRPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDkNDRPYQDVKI 623
Cdd:cd01926  92 LKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGSG-NGKPKKKVVI 160
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 479-624 1.37e-63

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: 206.62  E-value: 1.37e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 479 IMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHDR 558
Cdd:cd01922   1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331588 559 PFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDkNDRPYQDVKIL 624
Cdd:cd01922  81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENMVEVQTQ-TDRPIDEVKIL 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 478-628 5.44e-61

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: 200.66  E-value: 5.44e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 478 VIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWGREFEDEFHKSLRHD 557
Cdd:cd01925   8 VILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRLRFN 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331588 558 RPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKgmDVVQG---IEKVKTDKNDRPYQDVKILNVTV 628
Cdd:cd01925  88 RRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTG--DTIYNllkLAEVETDKDERPVYPPKITSVEV 159
PTZ00060 PTZ00060
cyclophilin; Provisional
 485-625 8.11e-50

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 171.18  E-value: 8.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  485 GDIHMKLYPEECPKTVENFTTHC---------RNGYYDNHLFHRVIRGFMIQTGD-PLGDGTGGQSIWGREFEDEFHKsL 554
Cdd:PTZ00060  30 GRIVFELFSDVTPKTAENFRALCigdkvgssgKNLHYKGSIFHRIIPQFMCQGGDiTNHNGTGGESIYGRKFTDENFK-L 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331588  555 RHDRPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTdKNDRPYQDVKILN 625
Cdd:PTZ00060 109 KHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAMEKEGT-QSGYPKKPVVVTD 178
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 482-623 3.50e-47

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: 163.28  E-value: 3.50e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 482 TTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTGGQSIWG-------REFEDEFHKSL 554
Cdd:cd01921   4 TTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSqlygrqaRFFEPEILPLL 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 555 RHDRPFTLSMANAGPNTNGSQFFIT-TVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKI 623
Cdd:cd01921  84 KHSKKGTVSMVNAGDNLNGSQFYITlGENLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDDGRPLKDIRI 153
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 485-623 1.33e-45

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 160.00  E-value: 1.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  485 GDIHMKLYPEECPKTVENFTTHC-----RNGY---YDNHLFHRVIRGFMIQTGDPL-GDGTGGQSIWGREFEDEFHKSlR 555
Cdd:PLN03149  33 GRIKMELFADIAPKTAENFRQFCtgefrKAGLpqgYKGCQFHRVIKDFMIQGGDFLkGDGTGCVSIYGSKFEDENFIA-K 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331588  556 HDRPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVV-KGMDVVQGIEKVKTDKNDRPYQDVKI 623
Cdd:PLN03149 112 HTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGPNNRPKLACVI 180
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 480-628 3.32e-33

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: 124.48  E-value: 3.32e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 480 MHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTggQSIWGREFEDEFHKSLRHDRp 559
Cdd:cd01920   2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGGGFTPDLA--QKETLKPIKNEAGNGLSNTR- 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331588 560 FTLSMA-NAGPNTNGSQFFITTVATPWLDNK-----HTVFGRVVKGMDVVQGIEKVKTdKNDRPYQDVKILNVTV 628
Cdd:cd01920  79 GTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVET-YSFGSYQDVPVQDVII 152
PRK10903 PRK10903
peptidylprolyl isomerase A;
456-628 1.96e-26

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 106.47  E-value: 1.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  456 AADELMSVSDIGNSATTSLPE-NVIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGD 534
Cdd:PRK10903   8 AMAAVFALSALSPAALAAKGDpHVLLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  535 GTggQSIWGREFEDEFHKSLRHDRPfTLSMA-NAGPNTNGSQFFITTVATPWLDN-----KHTVFGRVVKGMDVVQGIEK 608
Cdd:PRK10903  88 MQ--QKKPNPPIKNEADNGLRNTRG-TIAMArTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQ 164

                        170       180
                 ....*....|....*....|
gi 22331588  609 VKTdKNDRPYQDVKILNVTV 628
Cdd:PRK10903 165 VPT-HDVGPYQNVPSKPVVI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
478-630 2.44e-26

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 105.69  E-value: 2.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  478 VIMHTTLGDIHMKLYPEECPKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGdplGDGTG-GQSIWGREFEDEFHKSLRH 556
Cdd:PRK10791   2 VTFHTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGG---GFEPGmKQKATKEPIKNEANNGLKN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  557 DRPfTLSMANAG-PNTNGSQFFITTVATPWLDNK--------HTVFGRVVKGMDVVQGIEKVKTDKN----DRPYQDVKI 623
Cdd:PRK10791  79 TRG-TLAMARTQaPHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSgmhqDVPKEDVII 157


                 ....*..
gi 22331588  624 LNVTVPK 630
Cdd:PRK10791 158 ESVTVSE 164
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 68-286 5.28e-12

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 66.97  E-value: 5.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  68 MHRDVVTHVAVSAAEFFISGSM-DGHLKFWKKKGVGIEFAkhFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYD 146
Cdd:cd00200  91 GHTSYVSSVAFSPDGRILSSSSrDKTIKVWDVETGKCLTT--LRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 147 MMAMIRLPYipGAVEWVYKQGDvKAKLAVSDRDSlFVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMISGDTKGI 226
Cdd:cd00200 169 CVATLTGHT--GEVNSVAFSPD-GEKLLSSSSDG-TIKLWDLSTG--KCLGTLRGHENGVNSVAFSPDGYLLASGSEDGT 242

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 227 IEYWSATTlqfpeDEVNFKLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVF 286
Cdd:cd00200 243 IRVWDLRT-----GECVQTLSGHTN---------SVTSLAWSPDGKRLASGSADGTIRIW 288
WD40 COG2319
WD40 repeat [General function prediction only];
69-297 1.65e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.47  E-value: 1.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  69 HRDVVTHVAVSAA-EFFISGSMDGHLKFWK-KKGvgiEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYD 146
Cdd:COG2319 161 HSGAVTSVAFSPDgKLLASGSDDGTVRLWDlATG---KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGK 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 147 MMAMIRlpyipGAVEWVYK-----QGDVkakLAVSDRDSLfVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMISG 221
Cdd:COG2319 238 LLRTLT-----GHSGSVRSvafspDGRL---LASGSADGT-VRLWDLATG--ELLRTLTGHSGGVNSVAFSPDGKLLASG 306

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331588 222 DTKGIIEYWSATTLQFPedevnFKLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRVY 297
Cdd:COG2319 307 SDDGTVRLWDLATGKLL-----RTLTGHTG---------AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 69-297 2.00e-11

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 65.05  E-value: 2.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  69 HRDVVTHVAVSAA-EFFISGSMDGHLKFWKKKGVgiEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNydm 147
Cdd:cd00200   8 HTGGVTCVAFSPDgKLLATGSGDGTIKVWDLETG--ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET--- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 148 mamirlpyipGAVEWVYK--QGDVKA-------KLAVSDRDSLFVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTM 218
Cdd:cd00200  83 ----------GECVRTLTghTSYVSSvafspdgRILSSSSRDKTIKVWDVETG--KCLTTLRGHTDWVNSVAFSPDGTFV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 219 ISGDTKGIIEYWSATTLqfpedevnfklksdtnlfeiiKCKTT-------ISAIEVSPDGKQFSITAPDRRIRVFWFRTG 291
Cdd:cd00200 151 ASSSQDGTIKLWDLRTG---------------------KCVATltghtgeVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG 209


                ....*.
gi 22331588 292 KLRRVY 297
Cdd:cd00200 210 KCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
69-298 2.52e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 66.09  E-value: 2.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  69 HRDVVTHVAVSA-AEFFISGSMDGHLKFWK-KKGvgiEFAKHFRSHLGPIEGLAVSIDG--LLccTISNDHAVKIYDVVN 144
Cdd:COG2319 119 HTGAVRSVAFSPdGKTLASGSADGTVRLWDlATG---KLLRTLTGHSGAVTSVAFSPDGklLA--SGSDDGTVRLWDLAT 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 145 YDmmamiRLPYIPGAVEWVYK-----QGDVkakLAVSDRDSLfVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMI 219
Cdd:COG2319 194 GK-----LLRTLTGHTGAVRSvafspDGKL---LASGSADGT-VRLWDLATG--KLLRTLTGHSGSVRSVAFSPDGRLLA 262

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22331588 220 SGDTKGIIEYWSATTlqfpeDEVNFKLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRVYD 298
Cdd:COG2319 263 SGSADGTVRLWDLAT-----GELLRTLTGHSG---------GVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT 327
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 497-607 2.89e-11

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: 62.46  E-value: 2.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 497 PKTVENFTTHCRNGYYDNHLFHRVIRGFMIQTGDPLGDGTG---------------------GQSIWGREFE-----DEF 550
Cdd:cd01924  19 PVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGfpdpetgksrtipleikpegqKQPVYGKTLEeagryDEQ 98

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22331588 551 HKSLRHDrPFTLSMANA--GPNTNGSQFFI-------TTVATPWLDNKHTVFGRVVKGMDVVQGIE 607
Cdd:cd01924  99 PVLPFNA-FGAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILRELK 163
WD40 COG2319
WD40 repeat [General function prediction only];
69-287 4.00e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.32  E-value: 4.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  69 HRDVVTHVAVSAA-EFFISGSMDGHLKFWKKKGVgiEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYDm 147
Cdd:COG2319 203 HTGAVRSVAFSPDgKLLASGSADGTVRLWDLATG--KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGE- 279

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 148 mamiRLPYIPGAVEWVY-----KQGDVkakLAVSDRDSLfVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMISGD 222
Cdd:COG2319 280 ----LLRTLTGHSGGVNsvafsPDGKL---LASGSDDGT-VRLWDLATG--KLLRTLTGHTGAVRSVAFSPDGKTLASGS 349

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331588 223 TKGIIEYWSATTLQFPEdevnfKLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVfW 287
Cdd:COG2319 350 DDGTVRLWDLATGELLR-----TLTGHTG---------AVTSVAFSPDGRTLASGSADGTVRL-W 399
WD40 COG2319
WD40 repeat [General function prediction only];
69-298 4.25e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.32  E-value: 4.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  69 HRDVVTHVAVSA-AEFFISGSMDGHLKFWKKKGVgiEFAKHFRSHLGPIEGLAVSIDG--LLccTISNDHAVKIYDVVNY 145
Cdd:COG2319  77 HTAAVLSVAFSPdGRLLASASADGTVRLWDLATG--LLLRTLTGHTGAVRSVAFSPDGktLA--SGSADGTVRLWDLATG 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 146 DmmamiRLPYIPGAVEWVY-----KQGDVkakLAVSDRDSLfVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMIS 220
Cdd:COG2319 153 K-----LLRTLTGHSGAVTsvafsPDGKL---LASGSDDGT-VRLWDLATG--KLLRTLTGHTGAVRSVAFSPDGKLLAS 221

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22331588 221 GDTKGIIEYWSATTLQFPedevnFKLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRVYD 298
Cdd:COG2319 222 GSADGTVRLWDLATGKLL-----RTLTGHSG---------SVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLT 285
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 69-296 7.12e-10

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 60.43  E-value: 7.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  69 HRDVVTHVAVSA-AEFFISGSMDGHLKFWKKKGVgiEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYDM 147
Cdd:cd00200  50 HTGPVRDVAASAdGTYLASGSSDKTIRLWDLETG--ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 148 MAMIRlpyipGAVEWVY-----KQGDVkakLAVSDRDSlFVHIYDPRSGSnePIASKEIHMNPIKVMKYNPVSDTMISGD 222
Cdd:cd00200 128 LTTLR-----GHTDWVNsvafsPDGTF---VASSSQDG-TIKLWDLRTGK--CVATLTGHTGEVNSVAFSPDGEKLLSSS 196

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22331588 223 TKGIIEYWSATTLQFPEDevnfkLKSDTNlfeiikcktTISAIEVSPDGKQFSITAPDRRIRVFWFRTGKLRRV 296
Cdd:cd00200 197 SDGTIKLWDLSTGKCLGT-----LRGHEN---------GVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256
PTZ00221 PTZ00221
cyclophilin; Provisional
 485-623 7.42e-10

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 59.88  E-value: 7.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  485 GDIHMKLYPEECPKTVENFT--------THCRNGYYDNHLF---HRVIRGF-MIQTGDPLGDGTggqSIWGREFEDEFHK 552
Cdd:PTZ00221  67 GRLVFELFEDVVPETVENFRalitgscgIDTNTGVKLDYLYtpvHHVDRNNnIIVLGELDSFNV---SSTGTPIADEGYR 143

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22331588  553 sLRHDRPFTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQGIEKVKTDKNDRPYQDVKI 623
Cdd:PTZ00221 144 -HRHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESLPLDDVGRPLLPVTV 213
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 69-231 1.66e-08

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 56.19  E-value: 1.66e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588  69 HRDVVTHVAVSAAEFFI-SGSMDGHLKFWKkkGVGIEFAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDVVNYDM 147
Cdd:cd00200 134 HTDWVNSVAFSPDGTFVaSSSQDGTIKLWD--LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKC 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22331588 148 MAMIRlpyipGAVEWVY-----KQGDVkakLAVSDRDSLfVHIYDPRSGsnEPIASKEIHMNPIKVMKYNPVSDTMISGD 222
Cdd:cd00200 212 LGTLR-----GHENGVNsvafsPDGYL---LASGSEDGT-IRVWDLRTG--ECVQTLSGHTNSVTSLAWSPDGKRLASGS 280


                ....*....
gi 22331588 223 TKGIIEYWS 231
Cdd:cd00200 281 ADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
69-142 2.43e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.29  E-value: 2.43e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 22331588  69 HRDVVTHVAVSAA-EFFISGSMDGHLKFWKKKGVGIefAKHFRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYDV 142
Cdd:COG2319 329 HTGAVRSVAFSPDgKTLASGSDDGTVRLWDLATGEL--LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 69-97 3.27e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.75  E-value: 3.27e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 22331588     69 HRDVVTHVAVSA-AEFFISGSMDGHLKFWK 97
Cdd:smart00320  11 HTGPVTSVAFSPdGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 109-141 7.64e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 34.60  E-value: 7.64e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 22331588    109 FRSHLGPIEGLAVSIDGLLCCTISNDHAVKIYD 141
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
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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