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Conserved domains on  [gi|3850079|emb|CAA21906|]
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SIP/FAR complex WD repeat (scaffold) subunit, striatin Csc3 [Schizosaccharomyces pombe]

Protein Classification

Striatin and WD40 domain-containing protein( domain architecture ID 13744662)

Striatin and WD40 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Striatin pfam08232
Striatin family; Striatin is an intracellular protein which has a caveolin-binding motif, a ...
 24-138 4.48e-23

Striatin family; Striatin is an intracellular protein which has a caveolin-binding motif, a coiled-coil structure, a calmodulin-binding site, and a WD (pfam00400) repeat domain. It acts as a scaffold protein and is involved in signalling pathways.


:

Pssm-ID: 462401  Cd Length: 85  Bit Score: 93.34  E-value: 4.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079     24 LQGVIQYLQYEAFKNERDHNLWEIERAELKIRVAQLERERAKLEQSLSFQQRRAEMLEKSLRELRKDKnisvkdldefhl 103
Cdd:pfam08232   1 LPGVLHFLQTEWHRHERDRNAWEIERAEMKARIAKLEGERRGQENLKKDLKRRIKMLEYALKQESKRK------------ 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 3850079    104 ldkpaanntkadaeacllKSKNYIKKSLQEIVYLT 138
Cdd:pfam08232  69 ------------------KSRQYLKKCLQEIGYLD 85
WD40 COG2319
WD40 repeat [General function prediction only];
303-552 9.25e-21

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 94.98  E-value: 9.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  303 FASGTENGVINVWRLDEDsndnsmgiiKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLpanqtsdsiskiLT 382
Cdd:COG2319 135 LASGSADGTVRLWDLATG---------KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL------------AT 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  383 GSTI--FQGHEDCVWEL-FCHevkdNNPILLSLSSDGTVRGWK-YTGEQLFKIRCDSKQPLSMSVT--DSRIAIAYNDGN 456
Cdd:COG2319 194 GKLLrtLTGHTGAVRSVaFSP----DGKLLASGSADGTVRLWDlATGKLLRTLTGHSGSVRSVAFSpdGRLLASGSADGT 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  457 VRFYDLDTQILVSqmRIAGNSaignpavkDRINKIVWkngNPD--RLYSLHENGMVRVFDVKSEELLAEKSISKVSLTGI 534
Cdd:COG2319 270 VRLWDLATGELLR--TLTGHS--------GGVNSVAF---SPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV 336

                       250
                ....*....|....*...
gi 3850079  535 AFAVNRPEFAISASDGRV 552
Cdd:COG2319 337 AFSPDGKTLASGSDDGTV 354
 
Name Accession Description Interval E-value
Striatin pfam08232
Striatin family; Striatin is an intracellular protein which has a caveolin-binding motif, a ...
 24-138 4.48e-23

Striatin family; Striatin is an intracellular protein which has a caveolin-binding motif, a coiled-coil structure, a calmodulin-binding site, and a WD (pfam00400) repeat domain. It acts as a scaffold protein and is involved in signalling pathways.


Pssm-ID: 462401  Cd Length: 85  Bit Score: 93.34  E-value: 4.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079     24 LQGVIQYLQYEAFKNERDHNLWEIERAELKIRVAQLERERAKLEQSLSFQQRRAEMLEKSLRELRKDKnisvkdldefhl 103
Cdd:pfam08232   1 LPGVLHFLQTEWHRHERDRNAWEIERAEMKARIAKLEGERRGQENLKKDLKRRIKMLEYALKQESKRK------------ 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 3850079    104 ldkpaanntkadaeacllKSKNYIKKSLQEIVYLT 138
Cdd:pfam08232  69 ------------------KSRQYLKKCLQEIGYLD 85
WD40 COG2319
WD40 repeat [General function prediction only];
303-552 9.25e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 94.98  E-value: 9.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  303 FASGTENGVINVWRLDEDsndnsmgiiKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLpanqtsdsiskiLT 382
Cdd:COG2319 135 LASGSADGTVRLWDLATG---------KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL------------AT 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  383 GSTI--FQGHEDCVWEL-FCHevkdNNPILLSLSSDGTVRGWK-YTGEQLFKIRCDSKQPLSMSVT--DSRIAIAYNDGN 456
Cdd:COG2319 194 GKLLrtLTGHTGAVRSVaFSP----DGKLLASGSADGTVRLWDlATGKLLRTLTGHSGSVRSVAFSpdGRLLASGSADGT 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  457 VRFYDLDTQILVSqmRIAGNSaignpavkDRINKIVWkngNPD--RLYSLHENGMVRVFDVKSEELLAEKSISKVSLTGI 534
Cdd:COG2319 270 VRLWDLATGELLR--TLTGHS--------GGVNSVAF---SPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV 336

                       250
                ....*....|....*...
gi 3850079  535 AFAVNRPEFAISASDGRV 552
Cdd:COG2319 337 AFSPDGKTLASGSDDGTV 354
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 303-565 1.05e-20

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: 92.78  E-value: 1.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  303 FASGTENGVINVWRLDEDSndnsmgiikPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPANQTSdsiskilt 382
Cdd:cd00200  24 LATGSGDGTIKVWDLETGE---------LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECV-------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  383 gsTIFQGHEDCVWELFCHevkDNNPILLSLSSDGTVRGWKY-TGEQLFKIRCDSKQP--LSMSVTDSRIAIAYNDGNVRF 459
Cdd:cd00200  87 --RTLTGHTSYVSSVAFS---PDGRILSSSSRDKTIKVWDVeTGKCLTTLRGHTDWVnsVAFSPDGTFVASSSQDGTIKL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  460 YDLDTQILVsqMRIAGNsaignpavKDRINKIVWkNGNPDRLYSLHENGMVRVFDVKSEELLAEKSISKVSLTGIAFAVN 539
Cdd:cd00200 162 WDLRTGKCV--ATLTGH--------TGEVNSVAF-SPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230

                       250       260
                ....*....|....*....|....*....
gi 3850079  540 RpEFAISAS-DG--RVFFLRQDDKLSTLE 565
Cdd:cd00200 231 G-YLLASGSeDGtiRVWDLRTGECVQTLS 258
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 330-367 1.59e-07

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: 47.69  E-value: 1.59e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 3850079     330 KPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWS 367
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
330-367 3.24e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 3.24e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 3850079    330 KPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWS 367
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 10-92 1.60e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079   10 QDEKRADKEPNLYTLQGVIQYLQYEAFKNERDHNLWEIERAELKIRVAQLERERAKLEQSLSFQQRRAEMLEKSLRELRK 89
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                ...
gi 3850079   90 DKN 92
Cdd:COG4942  98 ELE 100
 
Name Accession Description Interval E-value
Striatin pfam08232
Striatin family; Striatin is an intracellular protein which has a caveolin-binding motif, a ...
 24-138 4.48e-23

Striatin family; Striatin is an intracellular protein which has a caveolin-binding motif, a coiled-coil structure, a calmodulin-binding site, and a WD (pfam00400) repeat domain. It acts as a scaffold protein and is involved in signalling pathways.


Pssm-ID: 462401  Cd Length: 85  Bit Score: 93.34  E-value: 4.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079     24 LQGVIQYLQYEAFKNERDHNLWEIERAELKIRVAQLERERAKLEQSLSFQQRRAEMLEKSLRELRKDKnisvkdldefhl 103
Cdd:pfam08232   1 LPGVLHFLQTEWHRHERDRNAWEIERAEMKARIAKLEGERRGQENLKKDLKRRIKMLEYALKQESKRK------------ 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 3850079    104 ldkpaanntkadaeacllKSKNYIKKSLQEIVYLT 138
Cdd:pfam08232  69 ------------------KSRQYLKKCLQEIGYLD 85
WD40 COG2319
WD40 repeat [General function prediction only];
303-552 9.25e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 94.98  E-value: 9.25e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  303 FASGTENGVINVWRLDEDsndnsmgiiKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLpanqtsdsiskiLT 382
Cdd:COG2319 135 LASGSADGTVRLWDLATG---------KLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDL------------AT 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  383 GSTI--FQGHEDCVWEL-FCHevkdNNPILLSLSSDGTVRGWK-YTGEQLFKIRCDSKQPLSMSVT--DSRIAIAYNDGN 456
Cdd:COG2319 194 GKLLrtLTGHTGAVRSVaFSP----DGKLLASGSADGTVRLWDlATGKLLRTLTGHSGSVRSVAFSpdGRLLASGSADGT 269

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  457 VRFYDLDTQILVSqmRIAGNSaignpavkDRINKIVWkngNPD--RLYSLHENGMVRVFDVKSEELLAEKSISKVSLTGI 534
Cdd:COG2319 270 VRLWDLATGELLR--TLTGHS--------GGVNSVAF---SPDgkLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSV 336

                       250
                ....*....|....*...
gi 3850079  535 AFAVNRPEFAISASDGRV 552
Cdd:COG2319 337 AFSPDGKTLASGSDDGTV 354
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 303-565 1.05e-20

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: 92.78  E-value: 1.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  303 FASGTENGVINVWRLDEDSndnsmgiikPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPANQTSdsiskilt 382
Cdd:cd00200  24 LATGSGDGTIKVWDLETGE---------LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECV-------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  383 gsTIFQGHEDCVWELFCHevkDNNPILLSLSSDGTVRGWKY-TGEQLFKIRCDSKQP--LSMSVTDSRIAIAYNDGNVRF 459
Cdd:cd00200  87 --RTLTGHTSYVSSVAFS---PDGRILSSSSRDKTIKVWDVeTGKCLTTLRGHTDWVnsVAFSPDGTFVASSSQDGTIKL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  460 YDLDTQILVsqMRIAGNsaignpavKDRINKIVWkNGNPDRLYSLHENGMVRVFDVKSEELLAEKSISKVSLTGIAFAVN 539
Cdd:cd00200 162 WDLRTGKCV--ATLTGH--------TGEVNSVAF-SPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230

                       250       260
                ....*....|....*....|....*....
gi 3850079  540 RpEFAISAS-DG--RVFFLRQDDKLSTLE 565
Cdd:cd00200 231 G-YLLASGSeDGtiRVWDLRTGECVQTLS 258
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 331-566 2.70e-20

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: 91.63  E-value: 2.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  331 PHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPANQTsdsiskiltgSTIFQGHEDCVWELFCHevkDNNPILL 410
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGEL----------LRTLKGHTGPVRDVAAS---ADGTYLA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  411 SLSSDGTVRGWKY-TGEQLFKIRCDSKQPLSMSVTDSR--IAIAYNDGNVRFYDLDTqiLVSQMRIAGNSaignpavkDR 487
Cdd:cd00200  68 SGSSDKTIRLWDLeTGECVRTLTGHTSYVSSVAFSPDGriLSSSSRDKTIKVWDVET--GKCLTTLRGHT--------DW 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  488 INKIVWkNGNPDRLYSLHENGMVRVFDVKSEELLAEKSISKVSLTGIAFAVNRPEFAISASDG--RVFFLRQDDKLSTLE 565
Cdd:cd00200 138 VNSVAF-SPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGtiKLWDLSTGKCLGTLR 216


                .
gi 3850079  566 S 566
Cdd:cd00200 217 G 217
WD40 COG2319
WD40 repeat [General function prediction only];
304-552 1.19e-18

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 88.43  E-value: 1.19e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  304 ASGTENGVINVWRLDEDsndnsmgiiKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPANQTSdsiskiltg 383
Cdd:COG2319 178 ASGSDDGTVRLWDLATG---------KLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLL--------- 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  384 sTIFQGHEDCVWEL-FCHevkdNNPILLSLSSDGTVRGWK-YTGEQLFKIRCDSKQPLSMSVT--DSRIAIAYNDGNVRF 459
Cdd:COG2319 240 -RTLTGHSGSVRSVaFSP----DGRLLASGSADGTVRLWDlATGELLRTLTGHSGGVNSVAFSpdGKLLASGSDDGTVRL 314

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  460 YDLDTQILVSQMRiaGNSaignpavkDRINKIVWkngNPD--RLYSLHENGMVRVFDVKSEELLAEKSISKVSLTGIAFA 537
Cdd:COG2319 315 WDLATGKLLRTLT--GHT--------GAVRSVAF---SPDgkTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFS 381

                       250
                ....*....|....*
gi 3850079  538 VNRPEFAISASDGRV 552
Cdd:COG2319 382 PDGRTLASGSADGTV 396
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 300-552 4.51e-18

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: 85.08  E-value: 4.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  300 TPSFASGTENGVINVWRLDEDsndnsmgiiKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPANQTsdsisk 379
Cdd:cd00200  63 GTYLASGSSDKTIRLWDLETG---------ECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC------ 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  380 iltgSTIFQGHEDCVWELFcheVKDNNPILLSLSSDGTVRGWKYTGEQLFK--------IRCdskqpLSMSVTDSRIAIA 451
Cdd:cd00200 128 ----LTTLRGHTDWVNSVA---FSPDGTFVASSSQDGTIKLWDLRTGKCVAtltghtgeVNS-----VAFSPDGEKLLSS 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  452 YNDGNVRFYDLDTQILVSQMRiagnsaignpAVKDRINKIVWkngNPDRLY--SLHENGMVRVFDVKSEELLAEKSISKV 529
Cdd:cd00200 196 SSDGTIKLWDLSTGKCLGTLR----------GHENGVNSVAF---SPDGYLlaSGSEDGTIRVWDLRTGECVQTLSGHTN 262

                       250       260
                ....*....|....*....|...
gi 3850079  530 SLTGIAFAVNRPEFAISASDGRV 552
Cdd:cd00200 263 SVTSLAWSPDGKRLASGSADGTI 285
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 303-514 1.22e-17

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: 83.54  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  303 FASGTENGVINVWRLDEDsndnsmgiiKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLpanqtsDSISKILT 382
Cdd:cd00200 108 LSSSSRDKTIKVWDVETG---------KCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL------RTGKCVAT 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  383 gstiFQGHEDCVWELFCHEvkDNNPILLSlSSDGTVRGWKYTGEQLFK-IRCDSKQPLSMSV-TDSRIAIAYN-DGNVRF 459
Cdd:cd00200 173 ----LTGHTGEVNSVAFSP--DGEKLLSS-SSDGTIKLWDLSTGKCLGtLRGHENGVNSVAFsPDGYLLASGSeDGTIRV 245

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3850079  460 YDLDTQILVsqMRIAGNSAignpavkdRINKIVWKNGNPdRLYSLHENGMVRVFD 514
Cdd:cd00200 246 WDLRTGECV--QTLSGHTN--------SVTSLAWSPDGK-RLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
304-517 4.06e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 74.56  E-value: 4.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  304 ASGTENGVINVWRLDEDsndnsmgiiKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPANQTSdsiskiltg 383
Cdd:COG2319 220 ASGSADGTVRLWDLATG---------KLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELL--------- 281

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  384 sTIFQGHEDCVWELFCHevkDNNPILLSLSSDGTVRGWKY-TGEQLFKIRCDSKQPLSMSVT--DSRIAIAYNDGNVRFY 460
Cdd:COG2319 282 -RTLTGHSGGVNSVAFS---PDGKLLASGSDDGTVRLWDLaTGKLLRTLTGHTGAVRSVAFSpdGKTLASGSDDGTVRLW 357

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3850079  461 DLDTQILVSqmRIAGNSaignpavkDRINKIVWkngNPD--RLYSLHENGMVRVFDVKS 517
Cdd:COG2319 358 DLATGELLR--TLTGHT--------GAVTSVAF---SPDgrTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
292-552 6.30e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 73.79  E-value: 6.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  292 THQPLPGSTPSFASGTENGVINVWRLDEDSNDNSMGIIKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPAN 371
Cdd:COG2319  31 LLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  372 QTsdsiskiltgSTIFQGHEDCVWELFCHevkDNNPILLSLSSDGTVRGWK-YTGEQLFKIRCDSKQPLSMSVT-DSR-I 448
Cdd:COG2319 111 LL----------LRTLTGHTGAVRSVAFS---PDGKTLASGSADGTVRLWDlATGKLLRTLTGHSGAVTSVAFSpDGKlL 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  449 AIAYNDGNVRFYDLDTQILVSQMRiagnsaignpAVKDRINKIVWkngNPD--RLYSLHENGMVRVFDVKSEELLAEKSI 526
Cdd:COG2319 178 ASGSDDGTVRLWDLATGKLLRTLT----------GHTGAVRSVAF---SPDgkLLASGSADGTVRLWDLATGKLLRTLTG 244

                       250       260
                ....*....|....*....|....*.
gi 3850079  527 SKVSLTGIAFAVNRPEFAISASDGRV 552
Cdd:COG2319 245 HSGSVRSVAFSPDGRLLASGSADGTV 270
WD40 COG2319
WD40 repeat [General function prediction only];
303-421 4.58e-10

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 61.85  E-value: 4.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079  303 FASGTENGVINVWRLDEDsndnsmgiiKPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWSLPANQTsdsiskilt 382
Cdd:COG2319 303 LASGSDDGTVRLWDLATG---------KLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL--------- 364

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 3850079  383 gSTIFQGHEDCVWELfchEVKDNNPILLSLSSDGTVRGW 421
Cdd:COG2319 365 -LRTLTGHTGAVTSV---AFSPDGRTLASGSADGTVRLW 399
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 330-367 1.59e-07

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: 47.69  E-value: 1.59e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 3850079     330 KPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWS 367
Cdd:smart00320   3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
330-367 3.24e-07

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 46.95  E-value: 3.24e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 3850079    330 KPHLTFYGHEGPVLCVCVPKATHHIFSGGHDGTIRCWS 367
Cdd:pfam00400   2 KLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 10-92 1.60e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3850079   10 QDEKRADKEPNLYTLQGVIQYLQYEAFKNERDHNLWEIERAELKIRVAQLERERAKLEQSLSFQQRRAEMLEKSLRELRK 89
Cdd:COG4942  18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97


                ...
gi 3850079   90 DKN 92
Cdd:COG4942  98 ELE 100
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 46-91 3.37e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.98  E-value: 3.37e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 3850079     46 EIERAELKIRVAQLERERAKLEQSLSFQQRRAEMLEKSLRELRKDK 91
Cdd:pfam20492   5 EREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEA 50
 
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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