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Conserved domains on  [gi|523967098|ref|NP_001265856|]
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peptidylprolyl isomerase domain and WD repeat-containing protein 1 isoform 3 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing peptidylprolyl isomerase( domain architecture ID 11455539)

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 ...
 355-503 2.79e-106

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: 313.24  E-value: 2.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 355 IIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDR 434
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523967098 435 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINI 503
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKT-DKNDRPYEDIKIINI 148
WD40 COG2319
WD40 repeat [General function prediction only];
46-179 1.63e-07

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.38  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  46 PGDAISSVAASEKST--------GKIFIYDGRGdNQPLHIFdKLHTSPLTQIRLNPVYKAVVSSDKSGMIeywtgpphey 117
Cdd:COG2319  203 HTGAVRSVAFSPDGKllasgsadGTVRLWDLAT-GKLLRTL-TGHSGSVRSVAFSPDGRLLASGSADGTV---------- 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523967098 118 KFpknvnWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVFD 179
Cdd:COG2319  271 RL-----WDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT 327
 
Name Accession Description Interval E-value
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 355-503 2.79e-106

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: 313.24  E-value: 2.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 355 IIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDR 434
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523967098 435 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINI 503
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKT-DKNDRPYEDIKIINI 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 354-506 4.11e-70

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 220.81  E-value: 4.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 354 AIIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGEsiwGGEFEDEFHSTLRHD 433
Cdd:COG0652    9 VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKHK 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523967098 434 RpYTLSMANA-GSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPkTDKPYEDVSIINITVK 506
Cdd:COG0652   86 R-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP-GDGPLEPVVIESVTIV 157
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 355-505 1.07e-56

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 185.54  E-value: 1.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  355 IIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIwgGEFEDEFHSTLRHDR 434
Cdd:pfam00160   1 IETNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523967098  435 PYTLSMANAGS--NTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPktDKPYEDVSIINITV 505
Cdd:pfam00160  79 RGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG--DRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 347-502 4.99e-47

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 161.55  E-value: 4.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 347 PKRVSDSAIIHTSMGDIHTKLFPVECPKTVENF---CVHSRNG------YYNGHTFHRIIKGFMIQTGDPT-GTGMGGES 416
Cdd:PTZ00060  16 PKVFFDISIDNAPAGRIVFELFSDVTPKTAENFralCIGDKVGssgknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGES 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 417 IWGGEFEDEfHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISnvKVNPKTDKPYE 496
Cdd:PTZ00060  96 IYGRKFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAME--KEGTQSGYPKK 172


                 ....*.
gi 523967098 497 DVSIIN 502
Cdd:PTZ00060 173 PVVVTD 178
WD40 COG2319
WD40 repeat [General function prediction only];
46-179 1.63e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.38  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  46 PGDAISSVAASEKST--------GKIFIYDGRGdNQPLHIFdKLHTSPLTQIRLNPVYKAVVSSDKSGMIeywtgpphey 117
Cdd:COG2319  203 HTGAVRSVAFSPDGKllasgsadGTVRLWDLAT-GKLLRTL-TGHSGSVRSVAFSPDGRLLASGSADGTV---------- 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523967098 118 KFpknvnWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVFD 179
Cdd:COG2319  271 RL-----WDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT 327
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 53-178 1.46e-05

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: 46.94  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  53 VAASEKSTGKIFIYDgrgDNQPLHIFdKLHTSPLTQIRLNPVYKAVVSS--DKSGMIeywtgppheykfpknvnWEYKTD 130
Cdd:cd00200   67 ASGSSDKTIRLWDLE---TGECVRTL-TGHTSYVSSVAFSPDGRILSSSsrDKTIKV-----------------WDVETG 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 523967098 131 TDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVF 178
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL 173
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 144-167 8.21e-04

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: 36.91  E-value: 8.21e-04
                           10        20
                   ....*....|....*....|....
gi 523967098   144 TSVCFSPDGKKIATIGSDRKVRIF 167
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLW 39
 
Name Accession Description Interval E-value
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 355-503 2.79e-106

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: 313.24  E-value: 2.79e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 355 IIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDR 434
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523967098 435 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINI 503
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKT-DKNDRPYEDIKIINI 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 354-506 4.11e-70

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 220.81  E-value: 4.11e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 354 AIIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGEsiwGGEFEDEFHSTLRHD 433
Cdd:COG0652    9 VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKHK 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523967098 434 RpYTLSMANA-GSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPkTDKPYEDVSIINITVK 506
Cdd:COG0652   86 R-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP-GDGPLEPVVIESVTIV 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 355-502 5.42e-67

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: 212.12  E-value: 5.42e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 355 IIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGeSIWGGEFEDEFHSTLRHDR 434
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 523967098 435 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPKtDKPYEDVSIIN 502
Cdd:cd00317   80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDEN-GRPIKPVTISD 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 356-505 1.72e-64

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: 206.50  E-value: 1.72e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 356 IHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDRP 435
Cdd:cd01923    4 LHTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHDGR 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 436 YTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINITV 505
Cdd:cd01923   84 GVLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPD-PGTDRPKEEIKIEDTSV 152
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 353-505 4.52e-64

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: 204.98  E-value: 4.52e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 353 SAIIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRH 432
Cdd:cd01928    2 SVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKH 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523967098 433 DRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINITV 505
Cdd:cd01928   82 DSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYRPLEEIRIKDVTI 153
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 355-501 5.50e-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: 201.99  E-value: 5.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 355 IIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDR 434
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 523967098 435 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRIsnVKVNPKTDKPYEDVSII 501
Cdd:cd01922   81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM--VEVQTQTDRPIDEVKIL 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 353-505 6.10e-60

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: 194.88  E-value: 6.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 353 SAIIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRH 432
Cdd:cd01925    7 KVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRLRF 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523967098 433 DRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTK-GMEVVQRISNVKVNpKTDKPYEDVSIINITV 505
Cdd:cd01925   87 NRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGdTIYNLLKLAEVETD-KDERPVYPPKITSVEV 159
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 352-500 4.32e-57

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: 187.08  E-value: 4.32e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 352 DSAIIHTSMGDIHTKLFPVECPKTVENF---C-----VHSRNGYYNGHTFHRIIKGFMIQTGDPT-GTGMGGESIWGGEF 422
Cdd:cd01926    6 DITIGGEPAGRIVMELFADVVPKTAENFralCtgekgKGGKPFGYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKF 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 523967098 423 EDE-FhsTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnpKTDKPYEDVSI 500
Cdd:cd01926   86 PDEnF--KLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS--GNGKPKKKVVI 160
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 355-505 1.07e-56

Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans isomerases, also known as cyclophilins, share this domain of about 109 amino acids. Cyclophilins have been found in all organizms studied so far and catalyze peptidyl-prolyl isomerization during which the peptide bond preceding proline (the peptidyl-prolyl bond) is stabilized in the cis conformation. Mammalian cyclophilin A (CypA) is a major cellular target for the immunosuppressive drug cyclosporin A (CsA). Other roles for cyclophilins may include chaperone and cell signalling function.


Pssm-ID: 459694 [Multi-domain]  Cd Length: 149  Bit Score: 185.54  E-value: 1.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  355 IIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIwgGEFEDEFHSTLRHDR 434
Cdd:pfam00160   1 IETNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523967098  435 PYTLSMANAGS--NTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPktDKPYEDVSIINITV 505
Cdd:pfam00160  79 RGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG--DRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 347-502 4.99e-47

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 161.55  E-value: 4.99e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 347 PKRVSDSAIIHTSMGDIHTKLFPVECPKTVENF---CVHSRNG------YYNGHTFHRIIKGFMIQTGDPT-GTGMGGES 416
Cdd:PTZ00060  16 PKVFFDISIDNAPAGRIVFELFSDVTPKTAENFralCIGDKVGssgknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGES 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 417 IWGGEFEDEfHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISnvKVNPKTDKPYE 496
Cdd:PTZ00060  96 IYGRKFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAME--KEGTQSGYPKK 172


                 ....*.
gi 523967098 497 DVSIIN 502
Cdd:PTZ00060 173 PVVVTD 178
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 355-500 7.52e-42

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: 147.10  E-value: 7.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 355 IIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGE-------FEDEFH 427
Cdd:cd01921    1 LLETTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSQLygrqarfFEPEIL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523967098 428 STLRHDRPYTLSMANAGSNTNGSQFFITVVP-TPWLDNKHTVFGRVTKGMEVVQRISNVKVNPKtDKPYEDVSI 500
Cdd:cd01921   81 PLLKHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDD-GRPLKDIRI 153
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 352-494 3.94e-40

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 143.05  E-value: 3.94e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 352 DSAIIHTSMGDIHTKLFPVECPKTVENF---CV--HSRNGY---YNGHTFHRIIKGFMIQTGD-PTGTGMGGESIWGGEF 422
Cdd:PLN03149  24 DVTIGGIPAGRIKMELFADIAPKTAENFrqfCTgeFRKAGLpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGCVSIYGSKF 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 523967098 423 EDEfHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVT-KGMEVVQRISNVKVNPkTDKP 494
Cdd:PLN03149 104 EDE-NFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGP-NNRP 174
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 356-500 3.26e-29

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: 112.54  E-value: 3.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 356 IHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGdptGTGMGGESIWGGE-FEDEFHSTLRHDR 434
Cdd:cd01920    2 FQTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGG---GFTPDLAQKETLKpIKNEAGNGLSNTR 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 523967098 435 pYTLSMA-NAGSNTNGSQFFITVVPTPWLDNK-----HTVFGRVTKGMEVVQRISNVKV---NPKTDKPYEDVSI 500
Cdd:cd01920   79 -GTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETysfGSYQDVPVQDVII 152
PRK10903 PRK10903
peptidylprolyl isomerase A;
340-505 4.04e-23

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 96.45  E-value: 4.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 340 AATQAEGPKRVsdsaIIHTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTgMGGESIwG 419
Cdd:PRK10903  21 AALAAKGDPHV----LLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQ-MQQKKP-N 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 420 GEFEDEFHSTLRHDRPyTLSMA-NAGSNTNGSQFFITVVPTPWLDN-----KHTVFGRVTKGMEVVQRISNVKVnpKTDK 493
Cdd:PRK10903  95 PPIKNEADNGLRNTRG-TIAMArTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPT--HDVG 171

                        170
                 ....*....|..
gi 523967098 494 PYEDVSIINITV 505
Cdd:PRK10903 172 PYQNVPSKPVVI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
357-505 2.58e-20

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 87.97  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 357 HTSMGDIHTKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTG--DPtgtGMGGESIwGGEFEDEFHSTLRHDR 434
Cdd:PRK10791   5 HTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGgfEP---GMKQKAT-KEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 435 PyTLSMANAGS-NTNGSQFFITVVPTPWLDNK--------HTVFGRVTKGMEVVQRISNVKVNPK---TDKPYEDVSIIN 502
Cdd:PRK10791  81 G-TLAMARTQApHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSgmhQDVPKEDVIIES 159


                 ...
gi 523967098 503 ITV 505
Cdd:PRK10791 160 VTV 162
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 373-482 3.65e-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: 62.08  E-value: 3.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 373 PKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGG-------------ESIWGGEFEDEFHSTLRHDRPY--- 436
Cdd:cd01924   19 PVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGFpdpetgksrtiplEIKPEGQKQPVYGKTLEEAGRYdeq 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 523967098 437 ---------TLSMANA--GSNTNGSQFFI-------TVVPTPWLDNKHTVFGRVTKGMEVVQRI 482
Cdd:cd01924   99 pvlpfnafgAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILREL 162
WD40 COG2319
WD40 repeat [General function prediction only];
46-179 1.63e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 53.38  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  46 PGDAISSVAASEKST--------GKIFIYDGRGdNQPLHIFdKLHTSPLTQIRLNPVYKAVVSSDKSGMIeywtgpphey 117
Cdd:COG2319  203 HTGAVRSVAFSPDGKllasgsadGTVRLWDLAT-GKLLRTL-TGHSGSVRSVAFSPDGRLLASGSADGTV---------- 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523967098 118 KFpknvnWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVFD 179
Cdd:COG2319  271 RL-----WDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT 327
WD40 COG2319
WD40 repeat [General function prediction only];
47-179 7.04e-07

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 51.45  E-value: 7.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  47 GDAISSVAASekSTGKIFI---YDGR------GDNQPLHIFdKLHTSPLTQIRLNPVYKAVVSSDKSGMIeywtgpphey 117
Cdd:COG2319  120 TGAVRSVAFS--PDGKTLAsgsADGTvrlwdlATGKLLRTL-TGHSGAVTSVAFSPDGKLLASGSDDGTV---------- 186

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523967098 118 KFpknvnWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVFD 179
Cdd:COG2319  187 RL-----WDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT 243
WD40 COG2319
WD40 repeat [General function prediction only];
125-178 1.50e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.29  E-value: 1.50e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 523967098 125 WEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVF 178
Cdd:COG2319  105 WDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTL 158
WD40 COG2319
WD40 repeat [General function prediction only];
46-178 1.51e-06

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 50.29  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  46 PGDAISSVAASEKST--------GKIFIYDgRGDNQPLHIFDKlHTSPLTQIRLNPVYKAVVSSDKSGMIeywtgpphey 117
Cdd:COG2319  245 HSGSVRSVAFSPDGRllasgsadGTVRLWD-LATGELLRTLTG-HSGGVNSVAFSPDGKLLASGSDDGTV---------- 312

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523967098 118 KFpknvnWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVF 178
Cdd:COG2319  313 RL-----WDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
PTZ00221 PTZ00221
cyclophilin; Provisional
 351-485 1.80e-06

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 49.48  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 351 SDSAIIHTSMGDIHT-----KLFPVECPKTVENF-------C-VHSRNGY---YNGHTFHRIIKGF-MIQTGDPTGTGMg 413
Cdd:PTZ00221  52 SCRAFLDISIGDVLAgrlvfELFEDVVPETVENFralitgsCgIDTNTGVkldYLYTPVHHVDRNNnIIVLGELDSFNV- 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 523967098 414 geSIWGGEFEDEFHSTlRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNV 485
Cdd:PTZ00221 131 --SSTGTPIADEGYRH-RHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESL 199
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 53-178 1.46e-05

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: 46.94  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  53 VAASEKSTGKIFIYDgrgDNQPLHIFdKLHTSPLTQIRLNPVYKAVVSS--DKSGMIeywtgppheykfpknvnWEYKTD 130
Cdd:cd00200   67 ASGSSDKTIRLWDLE---TGECVRTL-TGHTSYVSSVAFSPDGRILSSSsrDKTIKV-----------------WDVETG 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 523967098 131 TDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVF 178
Cdd:cd00200  126 KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATL 173
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-178 3.58e-05

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: 45.79  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  48 DAISSVAASEKST--------GKIFIYDGRGdNQPLHIFdKLHTSPLTQIRLNPVYKAVV--SSDKSGMIeywtgpphey 117
Cdd:cd00200  136 DWVNSVAFSPDGTfvasssqdGTIKLWDLRT-GKCVATL-TGHTGEVNSVAFSPDGEKLLssSSDGTIKL---------- 203

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 523967098 118 kfpknvnWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVF 178
Cdd:cd00200  204 -------WDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL 257
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-178 9.48e-05

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: 44.25  E-value: 9.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  48 DAISSVAASEKST--------GKIFIYDGRgDNQPLHIFdKLHTSPLTQIRLNPVYKAVVSSDKSGMIeywtgppheyKF 119
Cdd:cd00200   94 SYVSSVAFSPDGRilssssrdKTIKVWDVE-TGKCLTTL-RGHTDWVNSVAFSPDGTFVASSSQDGTI----------KL 161

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 523967098 120 pknvnWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVF 178
Cdd:cd00200  162 -----WDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 144-178 2.38e-04

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: 43.09  E-value: 2.38e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 523967098 144 TSVCFSPDGKKIATIGSDRKVRIFRFVTGKLMRVF 178
Cdd:cd00200   13 TCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL 47
WD40 COG2319
WD40 repeat [General function prediction only];
46-171 3.13e-04

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 42.98  E-value: 3.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  46 PGDAISSVAASekSTGKIFI---YDGR------GDNQPLHIFdKLHTSPLTQIRLNPVYKAVVSSDKSGMIEYWtgpphe 116
Cdd:COG2319  287 HSGGVNSVAFS--PDGKLLAsgsDDGTvrlwdlATGKLLRTL-TGHTGAVRSVAFSPDGKTLASGSDDGTVRLW------ 357

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 523967098 117 ykfpkNVNweykTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFRFVT 171
Cdd:COG2319  358 -----DLA----TGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 80-252 3.95e-04

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: 42.32  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  80 KLHTSPLTQIRLNPVYK--AVVSSDKSGMIeywtgppheykfpknvnWEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIAT 157
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKllATGSGDGTIKV-----------------WDLETGELLRTLKGHTGPVRDVAASADGTYLAS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098 158 IGSDRKVRIFRFVTGKLMRVFDESLSMFTELqqmrQQLPDmefgRRMAV--------------ERELEKV-----DAVRl 218
Cdd:cd00200   69 GSSDKTIRLWDLETGECVRTLTGHTSYVSSV----AFSPD----GRILSsssrdktikvwdveTGKCLTTlrghtDWVN- 139

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 523967098 219 iNIVFDETGHFVLYGTMLG-IKVINVETNRCVRIL 252
Cdd:cd00200  140 -SVAFSPDGTFVASSSQDGtIKLWDLRTGKCVATL 173
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 144-167 8.21e-04

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: 36.91  E-value: 8.21e-04
                           10        20
                   ....*....|....*....|....
gi 523967098   144 TSVCFSPDGKKIATIGSDRKVRIF 167
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLW 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 48-168 4.39e-03

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: 39.24  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 523967098  48 DAISSVAASEK--------STGKIFIYDGRGDnQPLHIFDKlHTSPLTQIRLNPVYKAVVSSDKSGMIEYWtgppheykf 119
Cdd:cd00200  178 GEVNSVAFSPDgekllsssSDGTIKLWDLSTG-KCLGTLRG-HENGVNSVAFSPDGYLLASGSEDGTIRVW--------- 246

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 523967098 120 pknvnwEYKTDTDLYEFAKCKAYPTSVCFSPDGKKIATIGSDRKVRIFR 168
Cdd:cd00200  247 ------DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
 
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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