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Conserved domains on  [gi|564335110|ref|XP_006231949|]
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peptidylprolyl isomerase domain and WD repeat-containing protein 1 isoform X1 [Rattus norvegicus]

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 ...
 414-562 8.46e-105

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: 311.32  E-value: 8.46e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 414 IVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDR 493
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335110 494 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINI 562
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKT-DKNDRPYEDIKIINI 148
WD40 COG2319
WD40 repeat [General function prediction only];
8-238 1.07e-15

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110   8 HRDVITHVVCTK-TDFIITASHDGHVKFWKkIEEGiEFVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNFDM 86
Cdd:COG2319  119 HTGAVRSVAFSPdGKTLASGSADGTVRLWD-LATG-KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  87 INMLKlgyfpgqcewiyCPGDAISSVAASEKST--------GKIFIYDGRGdNQPLHIFdKLHVSPLTQIRLNPVYKAVV 158
Cdd:COG2319  197 LRTLT------------GHTGAVRSVAFSPDGKllasgsadGTVRLWDLAT-GKLLRTL-TGHSGSVRSVAFSPDGRLLA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 159 SSDKSGMIeywtgppheyKFpktvnWEYKTDTDLYEFAKCKAYPTSICFSPDGKKIATIGSDRKVRIFRFLTGKLMRVFD 238
Cdd:COG2319  263 SGSADGTV----------RL-----WDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT 327
 
Name Accession Description Interval E-value
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 414-562 8.46e-105

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: 311.32  E-value: 8.46e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 414 IVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDR 493
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335110 494 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINI 562
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKT-DKNDRPYEDIKIINI 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 413-565 6.85e-70

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 221.97  E-value: 6.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 413 AIVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGEsiwGGEFEDEFHSTLRHD 492
Cdd:COG0652    9 VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKHK 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335110 493 RpYTLSMANA-GSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPkTDKPYEDVSIINITVK 565
Cdd:COG0652   86 R-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP-GDGPLEPVVIESVTIV 157
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 414-564 1.48e-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: 186.69  E-value: 1.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  414 IVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIwgGEFEDEFHSTLRHDR 493
Cdd:pfam00160   1 IETNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564335110  494 PYTLSMANAGS--NTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPktDKPYEDVSIINITV 564
Cdd:pfam00160  79 RGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG--DRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 406-561 1.29e-46

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 161.55  E-value: 1.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 406 PKRVSDSAIVHTSMGDIHIKLFPVECPKTVENF---CVHSRNG------YYNGHTFHRIIKGFMIQTGDPT-GTGMGGES 475
Cdd:PTZ00060  16 PKVFFDISIDNAPAGRIVFELFSDVTPKTAENFralCIGDKVGssgknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGES 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 476 IWGGEFEDEfHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISnvKVNPKTDKPYE 555
Cdd:PTZ00060  96 IYGRKFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAME--KEGTQSGYPKK 172


                 ....*.
gi 564335110 556 DVSIIN 561
Cdd:PTZ00060 173 PVVVTD 178
WD40 COG2319
WD40 repeat [General function prediction only];
8-238 1.07e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110   8 HRDVITHVVCTK-TDFIITASHDGHVKFWKkIEEGiEFVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNFDM 86
Cdd:COG2319  119 HTGAVRSVAFSPdGKTLASGSADGTVRLWD-LATG-KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  87 INMLKlgyfpgqcewiyCPGDAISSVAASEKST--------GKIFIYDGRGdNQPLHIFdKLHVSPLTQIRLNPVYKAVV 158
Cdd:COG2319  197 LRTLT------------GHTGAVRSVAFSPDGKllasgsadGTVRLWDLAT-GKLLRTL-TGHSGSVRSVAFSPDGRLLA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 159 SSDKSGMIeywtgppheyKFpktvnWEYKTDTDLYEFAKCKAYPTSICFSPDGKKIATIGSDRKVRIFRFLTGKLMRVFD 238
Cdd:COG2319  263 SGSADGTV----------RL-----WDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT 327
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-237 3.92e-15

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: 76.22  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110   8 HRDVITHV-VCTKTDFIITASHDGHVKFWKKieEGIEFVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNFDM 86
Cdd:cd00200    8 HTGGVTCVaFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGEC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  87 INMLKlgyfpGQCEWIYCPgdAIS---SVAASEKSTGKIFIYDGRgDNQPLHIFdKLHVSPLTQIRLNPVYKAVVSSDKS 163
Cdd:cd00200   86 VRTLT-----GHTSYVSSV--AFSpdgRILSSSSRDKTIKVWDVE-TGKCLTTL-RGHTDWVNSVAFSPDGTFVASSSQD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335110 164 GMIeywtgppheyKFpktvnWEYKTDTDLYEFAKCKAYPTSICFSPDGKKIATIGSDRKVRIFRFLTGKLMRVF 237
Cdd:cd00200  157 GTI----------KL-----WDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 203-226 2.29e-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: 36.14  E-value: 2.29e-03
                           10        20
                   ....*....|....*....|....
gi 564335110   203 TSICFSPDGKKIATIGSDRKVRIF 226
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLW 39
 
Name Accession Description Interval E-value
cyclophilin_WD40 cd01927
cyclophilin_WD40: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 414-562 8.46e-105

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: 311.32  E-value: 8.46e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 414 IVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDR 493
Cdd:cd01927    1 IIHTTKGDIHIRLFPEEAPKTVENFTTHARNGYYNNTIFHRVIKGFMIQTGDPTGDGTGGESIWGKEFEDEFSPSLKHDR 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335110 494 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINI 562
Cdd:cd01927   81 PYTLSMANAGPNTNGSQFFITTVATPWLDNKHTVFGRVVKGMDVVQRIENVKT-DKNDRPYEDIKIINI 148
PpiB COG0652
Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational ...
 413-565 6.85e-70

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


Pssm-ID: 440417 [Multi-domain]  Cd Length: 159  Bit Score: 221.97  E-value: 6.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 413 AIVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGEsiwGGEFEDEFHSTLRHD 492
Cdd:COG0652    9 VTLETNKGDIVIELFPDKAPKTVANFVSLAKEGFYDGTIFHRVIPGFMIQGGDPTGTGTGGP---GYTIPDEFDPGLKHK 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335110 493 RpYTLSMANA-GSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPkTDKPYEDVSIINITVK 565
Cdd:COG0652   86 R-GTLAMARAqGPNSAGSQFFIVLGDNPHLDGGYTVFGKVVEGMDVVDKIAAGPTDP-GDGPLEPVVIESVTIV 157
cyclophilin cd00317
cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains ...
 414-561 1.08e-66

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: 212.89  E-value: 1.08e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 414 IVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGeSIWGGEFEDEFHSTLRHDR 493
Cdd:cd00317    1 TLDTTKGRIVIELYGDEAPKTVENFLSLARGGFYDGTTFHRVIPGFMIQGGDPTGTGGGG-SGPGYKFPDENFPLKYHHR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564335110 494 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPKtDKPYEDVSIIN 561
Cdd:cd00317   80 RGTLSMANAGPNTNGSQFFITTAPTPHLDGKHTVFGKVVEGMDVVDKIERGDTDEN-GRPIKPVTISD 146
cyclophilin_RING cd01923
cyclophilin_RING: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) having ...
 416-564 7.55e-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: 206.11  E-value: 7.55e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 416 HTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDRPY 495
Cdd:cd01923    5 HTNKGDLNLELHCDKAPKACENFIKLCKKGYYDGTIFHRSIRNFMIQGGDPTGTGRGGESIWGKPFKDEFKPNLSHDGRG 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335110 496 TLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINITV 564
Cdd:cd01923   85 VLSMANSGPNTNGSQFFITYRSCKHLDGKHTVFGRVVGGLETLEAMENVPD-PGTDRPKEEIKIEDTSV 152
Cyclophilin_PPIL3_like cd01928
Cyclophilin_PPIL3_like. Proteins similar to Human cyclophilin-like peptidylprolyl cis- trans ...
 412-564 1.38e-63

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: 205.36  E-value: 1.38e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 412 SAIVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRH 491
Cdd:cd01928    2 SVTLHTNLGDIKIELFCDDCPKACENFLALCASGYYNGCIFHRNIKGFMVQTGDPTGTGKGGESIWGKKFEDEFRETLKH 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564335110 492 DRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnPKTDKPYEDVSIINITV 564
Cdd:cd01928   82 DSRGVVSMANNGPNTNGSQFFITYAKQPHLDGKYTVFGKVIDGFETLDTLEKLPV-DKKYRPLEEIRIKDVTI 153
cyclophilin_SpCYP2_like cd01922
cyclophilin_SpCYP2_like: cyclophilin 2-like peptidylprolyl cis- trans isomerase (PPIase) ...
 414-560 1.60e-62

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: 202.38  E-value: 1.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 414 IVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRHDR 493
Cdd:cd01922    1 TLETTMGEITLELYWNHAPKTCKNFYELAKRGYYNGTIFHRLIKDFMIQGGDPTGTGRGGASIYGKKFEDEIHPELKHTG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335110 494 PYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRIsnVKVNPKTDKPYEDVSII 560
Cdd:cd01922   81 AGILSMANAGPNTNGSQFFITLAPTPWLDGKHTIFGRVSKGMKVIENM--VEVQTQTDRPIDEVKIL 145
cyclophilin_CeCYP16-like cd01925
cyclophilin_CeCYP16-like: cyclophilin-type peptidylprolyl cis- trans isomerase) (PPIase) ...
 412-564 4.77e-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: 196.80  E-value: 4.77e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 412 SAIVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGEFEDEFHSTLRH 491
Cdd:cd01925    7 KVILKTTAGDIDIELWSKEAPKACRNFIQLCLEGYYDNTIFHRVVPGFIIQGGDPTGTGTGGESIYGEPFKDEFHSRLRF 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335110 492 DRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTK-GMEVVQRISNVKVNpKTDKPYEDVSIINITV 564
Cdd:cd01925   87 NRRGLVGMANAGDDSNGSQFFFTLDKADELNNKHTLFGKVTGdTIYNLLKLAEVETD-KDERPVYPPKITSVEV 159
cyclophilin_ABH_like cd01926
cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans ...
 411-559 1.40e-56

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: 1.40e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 411 DSAIVHTSMGDIHIKLFPVECPKTVENF---C-----VHSRNGYYNGHTFHRIIKGFMIQTGDPT-GTGMGGESIWGGEF 481
Cdd:cd01926    6 DITIGGEPAGRIVMELFADVVPKTAENFralCtgekgKGGKPFGYKGSTFHRVIPDFMIQGGDFTrGNGTGGKSIYGEKF 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564335110 482 EDE-FhsTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVnpKTDKPYEDVSI 559
Cdd:cd01926   86 PDEnF--KLKHTGPGLLSMANAGPNTNGSQFFITTVKTPWLDGKHVVFGKVVEGMDVVKKIENVGS--GNGKPKKKVVI 160
Pro_isomerase pfam00160
Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD; The peptidyl-prolyl cis-trans ...
 414-564 1.48e-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: 186.69  E-value: 1.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  414 IVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIwgGEFEDEFHSTLRHDR 493
Cdd:pfam00160   1 IETNGLGRIVIELFGDKAPKTVENFLQLCKKGFYDGTTFHRVIPGFMVQGGDPTGTGGGGKSI--FPIPDEIFPLLLKHK 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564335110  494 PYTLSMANAGS--NTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNVKVNPktDKPYEDVSIINITV 564
Cdd:pfam00160  79 RGALSMANTGPapNSNGSQFFITLGPAPHLDGKYTVFGKVVEGMDVLEKIEKVPTDG--DRPVKPVKILSCGV 149
PTZ00060 PTZ00060
cyclophilin; Provisional
 406-561 1.29e-46

cyclophilin; Provisional


Pssm-ID: 240249  Cd Length: 183  Bit Score: 161.55  E-value: 1.29e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 406 PKRVSDSAIVHTSMGDIHIKLFPVECPKTVENF---CVHSRNG------YYNGHTFHRIIKGFMIQTGDPT-GTGMGGES 475
Cdd:PTZ00060  16 PKVFFDISIDNAPAGRIVFELFSDVTPKTAENFralCIGDKVGssgknlHYKGSIFHRIIPQFMCQGGDITnHNGTGGES 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 476 IWGGEFEDEfHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISnvKVNPKTDKPYE 555
Cdd:PTZ00060  96 IYGRKFTDE-NFKLKHDQPGLLSMANAGPNTNGSQFFITTVPCPWLDGKHVVFGKVIEGMEVVRAME--KEGTQSGYPKK 172


                 ....*.
gi 564335110 556 DVSIIN 561
Cdd:PTZ00060 173 PVVVTD 178
cyclophilin_RRM cd01921
cyclophilin_RRM: cyclophilin-type peptidylprolyl cis- trans isomerase domain occuring with a ...
 417-559 8.11e-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: 147.87  E-value: 8.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 417 TSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGGESIWGGE-------FEDEFHSTL 489
Cdd:cd01921    4 TTLGDLVIDLFTDECPLACLNFLKLCKLKYYNFCLFYNVQKDFIAQTGDPTGTGAGGESIYSQLygrqarfFEPEILPLL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335110 490 RHDRPYTLSMANAGSNTNGSQFFITVVP-TPWLDNKHTVFGRVTKGMEVVQRISNVKVNPKtDKPYEDVSI 559
Cdd:cd01921   84 KHSKKGTVSMVNAGDNLNGSQFYITLGEnLDYLDGKHTVFGQVVEGFDVLEKINDAIVDDD-GRPLKDIRI 153
PLN03149 PLN03149
peptidyl-prolyl isomerase H (cyclophilin H); Provisional
 411-553 3.61e-40

peptidyl-prolyl isomerase H (cyclophilin H); Provisional


Pssm-ID: 178694  Cd Length: 186  Bit Score: 144.21  E-value: 3.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 411 DSAIVHTSMGDIHIKLFPVECPKTVENF---CV--HSRNGY---YNGHTFHRIIKGFMIQTGD-PTGTGMGGESIWGGEF 481
Cdd:PLN03149  24 DVTIGGIPAGRIKMELFADIAPKTAENFrqfCTgeFRKAGLpqgYKGCQFHRVIKDFMIQGGDfLKGDGTGCVSIYGSKF 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564335110 482 EDEfHSTLRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVT-KGMEVVQRISNVKVNPkTDKP 553
Cdd:PLN03149 104 EDE-NFIAKHTGPGLLSMANSGPNTNGCQFFITCAKCDWLDNKHVVFGRVLgDGLLVVRKIENVATGP-NNRP 174
cyclophilin_EcCYP_like cd01920
cyclophilin_EcCYP_like: cyclophilin-type A-like peptidylprolyl cis- trans isomerase (PPIase) ...
 416-559 2.25e-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: 113.31  E-value: 2.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 416 HTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGdptGTGMGGESIWGGE-FEDEFHSTLRHDRp 494
Cdd:cd01920    3 QTSLGDIVVELYDDKAPITVENFLAYVRKGFYDNTIFHRVISGFVIQGG---GFTPDLAQKETLKpIKNEAGNGLSNTR- 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335110 495 YTLSMA-NAGSNTNGSQFFITVVPTPWLDNK-----HTVFGRVTKGMEVVQRISNVKV---NPKTDKPYEDVSI 559
Cdd:cd01920   79 GTIAMArTNAPDSATSQFFINLKDNASLDYQneqwgYTVFGEVTEGMDVVDKIAGVETysfGSYQDVPVQDVII 152
PRK10903 PRK10903
peptidylprolyl isomerase A;
399-564 2.50e-23

peptidylprolyl isomerase A;


Pssm-ID: 182824 [Multi-domain]  Cd Length: 190  Bit Score: 97.61  E-value: 2.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 399 AATQAEGPKRVsdsaIVHTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTgMGGESIwG 478
Cdd:PRK10903  21 AALAAKGDPHV----LLTTSAGNIELELNSQKAPVSVKNFVDYVNSGFYNNTTFHRVIPGFMIQGGGFTEQ-MQQKKP-N 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 479 GEFEDEFHSTLRHDRPyTLSMA-NAGSNTNGSQFFITVVPTPWLDN-----KHTVFGRVTKGMEVVQRISNVKVnpKTDK 552
Cdd:PRK10903  95 PPIKNEADNGLRNTRG-TIAMArTADKDSATSQFFINVADNAFLDHgqrdfGYAVFGKVVKGMDVADKISQVPT--HDVG 171

                        170
                 ....*....|..
gi 564335110 553 PYEDVSIINITV 564
Cdd:PRK10903 172 PYQNVPSKPVVI 183
PRK10791 PRK10791
peptidylprolyl isomerase B;
416-564 9.87e-21

peptidylprolyl isomerase B;


Pssm-ID: 182734  Cd Length: 164  Bit Score: 89.13  E-value: 9.87e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 416 HTSMGDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTG--DPtgtGMGGESIwGGEFEDEFHSTLRHDR 493
Cdd:PRK10791   5 HTNHGDIVIKTFDDKAPETVKNFLDYCREGFYNNTIFHRVINGFMIQGGgfEP---GMKQKAT-KEPIKNEANNGLKNTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 494 PyTLSMANAGS-NTNGSQFFITVVPTPWLDNK--------HTVFGRVTKGMEVVQRISNVKVNPK---TDKPYEDVSIIN 561
Cdd:PRK10791  81 G-TLAMARTQApHSATAQFFINVVDNDFLNFSgeslqgwgYCVFAEVVEGMDVVDKIKGVATGRSgmhQDVPKEDVIIES 159


                 ...
gi 564335110 562 ITV 564
Cdd:PRK10791 160 VTV 162
WD40 COG2319
WD40 repeat [General function prediction only];
8-238 1.07e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 79.18  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110   8 HRDVITHVVCTK-TDFIITASHDGHVKFWKkIEEGiEFVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNFDM 86
Cdd:COG2319  119 HTGAVRSVAFSPdGKTLASGSADGTVRLWD-LATG-KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  87 INMLKlgyfpgqcewiyCPGDAISSVAASEKST--------GKIFIYDGRGdNQPLHIFdKLHVSPLTQIRLNPVYKAVV 158
Cdd:COG2319  197 LRTLT------------GHTGAVRSVAFSPDGKllasgsadGTVRLWDLAT-GKLLRTL-TGHSGSVRSVAFSPDGRLLA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 159 SSDKSGMIeywtgppheyKFpktvnWEYKTDTDLYEFAKCKAYPTSICFSPDGKKIATIGSDRKVRIFRFLTGKLMRVFD 238
Cdd:COG2319  263 SGSADGTV----------RL-----WDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT 327
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 8-237 3.92e-15

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: 76.22  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110   8 HRDVITHV-VCTKTDFIITASHDGHVKFWKKieEGIEFVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNFDM 86
Cdd:cd00200    8 HTGGVTCVaFSPDGKLLATGSGDGTIKVWDL--ETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGEC 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  87 INMLKlgyfpGQCEWIYCPgdAIS---SVAASEKSTGKIFIYDGRgDNQPLHIFdKLHVSPLTQIRLNPVYKAVVSSDKS 163
Cdd:cd00200   86 VRTLT-----GHTSYVSSV--AFSpdgRILSSSSRDKTIKVWDVE-TGKCLTTL-RGHTDWVNSVAFSPDGTFVASSSQD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335110 164 GMIeywtgppheyKFpktvnWEYKTDTDLYEFAKCKAYPTSICFSPDGKKIATIGSDRKVRIFRFLTGKLMRVF 237
Cdd:cd00200  157 GTI----------KL-----WDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
8-237 9.86e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.10  E-value: 9.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110   8 HRDVITHVVCTKT-DFIITASHDGHVKFWKkIEEGiEFVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNFDM 86
Cdd:COG2319  161 HSGAVTSVAFSPDgKLLASGSDDGTVRLWD-LATG-KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKL 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  87 INMLKlgyfpGQCEWIYCPgdAISS-----VAASEksTGKIFIYDgRGDNQPLHIFDKlHVSPLTQIRLNPVYKAVVSSD 161
Cdd:COG2319  239 LRTLT-----GHSGSVRSV--AFSPdgrllASGSA--DGTVRLWD-LATGELLRTLTG-HSGGVNSVAFSPDGKLLASGS 307

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335110 162 KSGMIeywtgppheyKFpktvnWEYKTDTDLYEFAKCKAYPTSICFSPDGKKIATIGSDRKVRIFRFLTGKLMRVF 237
Cdd:COG2319  308 DDGTV----------RL-----WDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
WD40 COG2319
WD40 repeat [General function prediction only];
23-238 2.89e-11

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 65.32  E-value: 2.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  23 IITASHDGHVKFWKkIEEGIEfVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNfdminmlklgyfpGQCEW- 101
Cdd:COG2319   93 LASASADGTVRLWD-LATGLL-LRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-------------GKLLRt 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 102 IYCPGDAISSVAASekSTGKIFI---YDGR------GDNQPLHIFDKlHVSPLTQIRLNP----VykAVVSSDksgmiey 168
Cdd:COG2319  158 LTGHSGAVTSVAFS--PDGKLLAsgsDDGTvrlwdlATGKLLRTLTG-HTGAVRSVAFSPdgklL--ASGSAD------- 225

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564335110 169 wtgppheykfpKTVN-WEYKTDTDLYEFAKCKAYPTSICFSPDGKKIATIGSDRKVRIFRFLTGKLMRVFD 238
Cdd:COG2319  226 -----------GTVRlWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLT 285
cyclophilin_TLP40_like cd01924
cyclophilin_TLP40_like: cyclophilin-type peptidylprolyl cis- trans isomerases (cyclophilins) ...
 420-541 3.33e-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: 3.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 420 GDIHIKLFPVECPKTVENFCVHSRNGYYNGHTFHRIIKGFMIQTGDPTGTGMGG-------------ESIWGGEFEDEFH 486
Cdd:cd01924    7 GTITIVLDGYNAPVTAGNFVDLVERGFYDGMEFHRVEGGFVVQTGDPQGKNPGFpdpetgksrtiplEIKPEGQKQPVYG 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564335110 487 STLRHDRPY------------TLSMANA--GSNTNGSQFFI-------TVVPTPWLDNKHTVFGRVTKGMEVVQRI 541
Cdd:cd01924   87 KTLEEAGRYdeqpvlpfnafgAIAMARTefDPNSASSQFFFllkdnelTPSRNNVLDGRYAVFGYVTDGLDILREL 162
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 7-227 3.06e-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: 61.20  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110   7 MHRDVITHVVCTKTDFIITASH-DGHVKFWKkIEEGiEFVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNfd 85
Cdd:cd00200   91 GHTSYVSSVAFSPDGRILSSSSrDKTIKVWD-VETG-KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRT-- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  86 minmlklgyfpGQCEWIYcPG--DAISSVAASEK--------STGKIFIYDGRGDnQPLHIFDKlHVSPLTQIRLNPVYK 155
Cdd:cd00200  167 -----------GKCVATL-TGhtGEVNSVAFSPDgekllsssSDGTIKLWDLSTG-KCLGTLRG-HENGVNSVAFSPDGY 232

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564335110 156 AVVSSDKSGMIEYWtgppheykfpktvnwEYKTDTDLYEFAKCKAYPTSICFSPDGKKIATIGSDRKVRIFR 227
Cdd:cd00200  233 LLASGSEDGTIRVW---------------DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
PTZ00221 PTZ00221
cyclophilin; Provisional
 420-544 1.66e-06

cyclophilin; Provisional


Pssm-ID: 140248  Cd Length: 249  Bit Score: 49.48  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 420 GDIHIKLFPVECPKTVENF-------C-VHSRNGY---YNGHTFHRIIKGF-MIQTGDPTGTGMggeSIWGGEFEDEFHS 487
Cdd:PTZ00221  67 GRLVFELFEDVVPETVENFralitgsCgIDTNTGVkldYLYTPVHHVDRNNnIIVLGELDSFNV---SSTGTPIADEGYR 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564335110 488 TlRHDRPYTLSMANAGSNTNGSQFFITVVPTPWLDNKHTVFGRVTKGMEVVQRISNV 544
Cdd:PTZ00221 144 H-RHTERGLLTMISEGPHTSGSVFGITLGPSPSLDFKQVVFGKAVDDLSLLEKLESL 199
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 45-311 3.54e-06

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: 48.87  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110  45 VKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDVVNFDMINMLKLgyfpgqcewiycPGDAISSVAASekstgkifi 124
Cdd:cd00200    2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG------------HTGPVRDVAAS--------- 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 125 ydgrGDNQPLhifdklhvspltqirlnpvykAVVSSDKsgmieywtgppheykfpkTVN-WEYKTDTDLYEFAKCKAYPT 203
Cdd:cd00200   61 ----ADGTYL---------------------ASGSSDK------------------TIRlWDLETGECVRTLTGHTSYVS 97

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335110 204 SICFSPDGKKIATIGSDRKVRIFRFLTGKLMRVFDeslsmftelqqmrqqlpdmefgrrmaverelEKVDAVRliNIVFD 283
Cdd:cd00200   98 SVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLR-------------------------------GHTDWVN--SVAFS 144

                        250       260
                 ....*....|....*....|....*....
gi 564335110 284 ETGHFVLYGTMLG-IKVINVETNRCVRIL 311
Cdd:cd00200  145 PDGTFVASSSQDGtIKLWDLRTGKCVATL 173
WD40 COG2319
WD40 repeat [General function prediction only];
8-81 3.59e-05

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 46.44  E-value: 3.59e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564335110   8 HRDVITHVVCTKTD-FIITASHDGHVKFWKKieEGIEFVKHFRSHLGIIESIAVSSEGALFCSVGDDKAMKVFDV 81
Cdd:COG2319  329 HTGAVRSVAFSPDGkTLASGSDDGTVRLWDL--ATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 203-226 2.29e-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: 36.14  E-value: 2.29e-03
                           10        20
                   ....*....|....*....|....
gi 564335110   203 TSICFSPDGKKIATIGSDRKVRIF 226
Cdd:smart00320  16 TSVAFSPDGKYLASGSDDGTIKLW 39
 
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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