NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462562885|ref|XP_054175766|]
View 

WD repeat-containing protein 88 isoform X2 [Homo sapiens]

Protein Classification

WD40 repeat domain-containing protein( domain architecture ID 11455410)

WD40 repeat domain-containing protein similar to proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly

CATH:  2.130.10.10
PubMed:  10322433|8090199
SCOP:  4002744

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
83-269 4.22e-38

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.51  E-value: 4.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  83 IWgdqDPLSKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHRPkAPVVECSITGDSSRVIA 162
Cdd:COG2319   188 LW---DLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS-GSVRSVAFSPDGRLLAS 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 163 ASYDKTVRAWDLETGKLLWKVRYDTFIV-SCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIKDHhTRSITSCCFDPD 241
Cdd:COG2319   264 GSADGTVRLWDLATGELLRTLTGHSGGVnSVAFSPDGKLLASGSD-DGTVRLWDLATGKLLRTLTGH-TGAVRSVAFSPD 341

                         170       180
                  ....*....|....*....|....*...
gi 2462562885 242 SQRVASVSLDRCIKIWDVTSQATLLTIT 269
Cdd:COG2319   342 GKTLASGSDDGTVRLWDLATGELLRTLT 369
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
83-269 4.22e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.51  E-value: 4.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  83 IWgdqDPLSKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHRPkAPVVECSITGDSSRVIA 162
Cdd:COG2319   188 LW---DLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS-GSVRSVAFSPDGRLLAS 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 163 ASYDKTVRAWDLETGKLLWKVRYDTFIV-SCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIKDHhTRSITSCCFDPD 241
Cdd:COG2319   264 GSADGTVRLWDLATGELLRTLTGHSGGVnSVAFSPDGKLLASGSD-DGTVRLWDLATGKLLRTLTGH-TGAVRSVAFSPD 341

                         170       180
                  ....*....|....*....|....*...
gi 2462562885 242 SQRVASVSLDRCIKIWDVTSQATLLTIT 269
Cdd:COG2319   342 GKTLASGSDDGTVRLWDLATGELLRTLT 369
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 94-269 6.35e-34

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: 124.75  E-value: 6.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  94 PFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFE-HrpKAPVVECSITGDSSRVIAASYDKTVRAW 172
Cdd:cd00200    43 LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTgH--TSYVSSVAFSPDGRILSSSSRDKTIKVW 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 173 DLETGKLLWKVRYDT-FIVSCKFSPDGKYVVSGfDVDHGICIMDAENITTVSVIKdHHTRSITSCCFDPDSQRVASVSLD 251
Cdd:cd00200   121 DVETGKCLTTLRGHTdWVNSVAFSPDGTFVASS-SQDGTIKLWDLRTGKCVATLT-GHTGEVNSVAFSPDGEKLLSSSSD 198

                         170
                  ....*....|....*...
gi 2462562885 252 RCIKIWDVTSQATLLTIT 269
Cdd:cd00200   199 GTIKLWDLSTGKCLGTLR 216
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 227-258 3.85e-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: 45.77  E-value: 3.85e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462562885  227 DHHTRSITSCCFDPDSQRVASVSLDRCIKIWD 258
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 94-264 7.15e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 7.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  94 PFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDF-EHRPKAPVVECSiTGDSSRVIAASYDKTVRAW 172
Cdd:PLN00181  525 PVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTEMkEHEKRVWSIDYS-SADPTLLASGSDDGSVKLW 603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 173 DLETGKLLWKVRYDTFIVSCKFSPDGKYVVSGFDVDHGICIMDAEN--ITTVSVIKDHHTRSITSCCfdpDSQRVASVSL 250
Cdd:PLN00181  604 SINQGVSIGTIKTKANICCVQFPSESGRSLAFGSADHKVYYYDLRNpkLPLCTMIGHSKTVSYVRFV---DSSTLVSSST 680

                         170
                  ....*....|....
gi 2462562885 251 DRCIKIWDVTSQAT 264
Cdd:PLN00181  681 DNTLKLWDLSMSIS 694
WD40 pfam00400
WD domain, G-beta repeat;
94-130 1.62e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 1.62e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462562885  94 PFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWD 130
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 64-210 2.92e-04

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 41.84  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  64 DREPPPHLLPEKHQVPEKLIWgdqdplSKipfKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVV--RDFE 141
Cdd:TIGR03300  24 DEPQPAELPEFQPTVKVDQVW------SA---SVGDGVGHYYLRLQPAVAGGKVYAADADGTVAALDAETGKRLwrVDLD 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462562885 142 HRPKAPVvecsiTGDSSRVIAASYDKTVRAWDLETGKLLWKVRYDTFIVSCKFSPDGKYVVS-------GFDVDHG 210
Cdd:TIGR03300  95 ERLSGGV-----GADGGLVFVGTEKGEVIALDAEDGKELWRAKLSSEVLSPPLVANGLVVVRtndgrltALDAATG 165
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
83-269 4.22e-38

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.51  E-value: 4.22e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  83 IWgdqDPLSKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHRPkAPVVECSITGDSSRVIA 162
Cdd:COG2319   188 LW---DLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHS-GSVRSVAFSPDGRLLAS 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 163 ASYDKTVRAWDLETGKLLWKVRYDTFIV-SCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIKDHhTRSITSCCFDPD 241
Cdd:COG2319   264 GSADGTVRLWDLATGELLRTLTGHSGGVnSVAFSPDGKLLASGSD-DGTVRLWDLATGKLLRTLTGH-TGAVRSVAFSPD 341

                         170       180
                  ....*....|....*....|....*...
gi 2462562885 242 SQRVASVSLDRCIKIWDVTSQATLLTIT 269
Cdd:COG2319   342 GKTLASGSDDGTVRLWDLATGELLRTLT 369
WD40 COG2319
WD40 repeat [General function prediction only];
88-269 5.37e-37

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 135.81  E-value: 5.37e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  88 DPLSKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHrPKAPVVECSITGDSSRVIAASYDK 167
Cdd:COG2319   106 DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDG 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 168 TVRAWDLETGKLLWKVR-YDTFIVSCKFSPDGKYVVSGfDVDHGICIMDAENITTVSVIKdHHTRSITSCCFDPDSQRVA 246
Cdd:COG2319   185 TVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASG-SADGTVRLWDLATGKLLRTLT-GHSGSVRSVAFSPDGRLLA 262

                         170       180
                  ....*....|....*....|...
gi 2462562885 247 SVSLDRCIKIWDVTSQATLLTIT 269
Cdd:COG2319   263 SGSADGTVRLWDLATGELLRTLT 285
WD40 COG2319
WD40 repeat [General function prediction only];
83-261 2.91e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 133.50  E-value: 2.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  83 IWgdqDPLSKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHrPKAPVVECSITGDSSRVIA 162
Cdd:COG2319   230 LW---DLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTG-HSGGVNSVAFSPDGKLLAS 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 163 ASYDKTVRAWDLETGKLLWKVR-YDTFIVSCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIKDHhTRSITSCCFDPD 241
Cdd:COG2319   306 GSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSD-DGTVRLWDLATGELLRTLTGH-TGAVTSVAFSPD 383

                         170       180
                  ....*....|....*....|
gi 2462562885 242 SQRVASVSLDRCIKIWDVTS 261
Cdd:COG2319   384 GRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
83-269 9.36e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 132.34  E-value: 9.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  83 IWgdqDPLSKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHrPKAPVVECSITGDSSRVIA 162
Cdd:COG2319   146 LW---DLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLAS 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 163 ASYDKTVRAWDLETGKLLWKVRYDTFIV-SCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIkDHHTRSITSCCFDPD 241
Cdd:COG2319   222 GSADGTVRLWDLATGKLLRTLTGHSGSVrSVAFSPDGRLLASGSA-DGTVRLWDLATGELLRTL-TGHSGGVNSVAFSPD 299

                         170       180
                  ....*....|....*....|....*...
gi 2462562885 242 SQRVASVSLDRCIKIWDVTSQATLLTIT 269
Cdd:COG2319   300 GKLLASGSDDGTVRLWDLATGKLLRTLT 327
WD40 COG2319
WD40 repeat [General function prediction only];
82-269 8.90e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 129.65  E-value: 8.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  82 LIWGDQDPLSKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHrPKAPVVECSITGDSSRVI 161
Cdd:COG2319    58 LTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 162 AASYDKTVRAWDLETGKLLWKVR-YDTFIVSCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIKDHhTRSITSCCFDP 240
Cdd:COG2319   137 SGSADGTVRLWDLATGKLLRTLTgHSGAVTSVAFSPDGKLLASGSD-DGTVRLWDLATGKLLRTLTGH-TGAVRSVAFSP 214

                         170       180
                  ....*....|....*....|....*....
gi 2462562885 241 DSQRVASVSLDRCIKIWDVTSQATLLTIT 269
Cdd:COG2319   215 DGKLLASGSADGTVRLWDLATGKLLRTLT 243
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 94-269 6.35e-34

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: 124.75  E-value: 6.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  94 PFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFE-HrpKAPVVECSITGDSSRVIAASYDKTVRAW 172
Cdd:cd00200    43 LLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLTgH--TSYVSSVAFSPDGRILSSSSRDKTIKVW 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 173 DLETGKLLWKVRYDT-FIVSCKFSPDGKYVVSGfDVDHGICIMDAENITTVSVIKdHHTRSITSCCFDPDSQRVASVSLD 251
Cdd:cd00200   121 DVETGKCLTTLRGHTdWVNSVAFSPDGTFVASS-SQDGTIKLWDLRTGKCVATLT-GHTGEVNSVAFSPDGEKLLSSSSD 198

                         170
                  ....*....|....*...
gi 2462562885 252 RCIKIWDVTSQATLLTIT 269
Cdd:cd00200   199 GTIKLWDLSTGKCLGTLR 216
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 96-258 2.00e-33

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: 123.60  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  96 KILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHrPKAPVVECSITGDSSRVIAASYDKTVRAWDLE 175
Cdd:cd00200   129 TTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTG-HTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 176 TGKLLWKVRYDT-FIVSCKFSPDGKYVVSGfDVDHGICIMDAENITTVSVIKdHHTRSITSCCFDPDSQRVASVSLDRCI 254
Cdd:cd00200   208 TGKCLGTLRGHEnGVNSVAFSPDGYLLASG-SEDGTIRVWDLRTGECVQTLS-GHTNSVTSLAWSPDGKRLASGSADGTI 285


                  ....
gi 2462562885 255 KIWD 258
Cdd:cd00200   286 RIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 96-261 4.82e-33

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: 122.44  E-value: 4.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  96 KILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFE-HrpKAPVVECSITGDSSRVIAASYDKTVRAWDL 174
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKgH--TGPVRDVAASADGTYLASGSSDKTIRLWDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 175 ETGKLLWKVRYDT-FIVSCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIKDhHTRSITSCCFDPDSQRVASVSLDRC 253
Cdd:cd00200    81 ETGECVRTLTGHTsYVSSVAFSPDGRILSSSSR-DKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQDGT 158


                  ....*...
gi 2462562885 254 IKIWDVTS 261
Cdd:cd00200   159 IKLWDLRT 166
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 97-269 1.73e-27

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: 107.81  E-value: 1.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  97 ILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFE-HrpKAPVVECSITGDSSRVIAASYDKTVRAWDLE 175
Cdd:cd00200    88 TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRgH--TDWVNSVAFSPDGTFVASSSQDGTIKLWDLR 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 176 TGKLLWK-VRYDTFIVSCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIKDHhTRSITSCCFDPDSQRVASVSLDRCI 254
Cdd:cd00200   166 TGKCVATlTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDLSTGKCLGTLRGH-ENGVNSVAFSPDGYLLASGSEDGTI 243

                         170
                  ....*....|....*
gi 2462562885 255 KIWDVTSQATLLTIT 269
Cdd:cd00200   244 RVWDLRTGECVQTLS 258
WD40 COG2319
WD40 repeat [General function prediction only];
112-269 2.52e-13

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 69.55  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 112 VDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHRPkAPVVECSITGDSSRVIAASYDKTVRAWDLETGKLLWKVRYDT-FIV 190
Cdd:COG2319     4 ADGAALAAASADLALALLAAALGALLLLLLGLA-AAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTaAVL 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462562885 191 SCKFSPDGKYVVSGFDvDHGICIMDAENITTVSVIKdHHTRSITSCCFDPDSQRVASVSLDRCIKIWDVTSQATLLTIT 269
Cdd:COG2319    83 SVAFSPDGRLLASASA-DGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLT 159
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 83-173 4.73e-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: 59.27  E-value: 4.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  83 IWgdqDPLSKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDFEHrPKAPVVECSITGDSSRVIA 162
Cdd:cd00200   203 LW---DLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG-HTNSVTSLAWSPDGKRLAS 278

                          90
                  ....*....|.
gi 2462562885 163 ASYDKTVRAWD 173
Cdd:cd00200   279 GSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 227-258 3.85e-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: 45.77  E-value: 3.85e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 2462562885  227 DHHTRSITSCCFDPDSQRVASVSLDRCIKIWD 258
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PLN00181 PLN00181
protein SPA1-RELATED; Provisional
 94-264 7.15e-07

protein SPA1-RELATED; Provisional


Pssm-ID: 177776 [Multi-domain]  Cd Length: 793  Bit Score: 50.47  E-value: 7.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  94 PFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVVRDF-EHRPKAPVVECSiTGDSSRVIAASYDKTVRAW 172
Cdd:PLN00181  525 PVVELASRSKLSGICWNSYIKSQVASSNFEGVVQVWDVARSQLVTEMkEHEKRVWSIDYS-SADPTLLASGSDDGSVKLW 603

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 173 DLETGKLLWKVRYDTFIVSCKFSPDGKYVVSGFDVDHGICIMDAEN--ITTVSVIKDHHTRSITSCCfdpDSQRVASVSL 250
Cdd:PLN00181  604 SINQGVSIGTIKTKANICCVQFPSESGRSLAFGSADHKVYYYDLRNpkLPLCTMIGHSKTVSYVRFV---DSSTLVSSST 680

                         170
                  ....*....|....
gi 2462562885 251 DRCIKIWDVTSQAT 264
Cdd:PLN00181  681 DNTLKLWDLSMSIS 694
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 91-130 1.27e-06

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: 44.23  E-value: 1.27e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2462562885   91 SKIPFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWD 130
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
94-130 1.62e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 43.87  E-value: 1.62e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2462562885  94 PFKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWD 130
Cdd:pfam00400   3 LLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
227-258 4.83e-06

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 42.72  E-value: 4.83e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462562885 227 DHHTRSITSCCFDPDSQRVASVSLDRCIKIWD 258
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 229-270 1.03e-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: 46.17  E-value: 1.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2462562885 229 HTRSITSCCFDPDSQRVASVSLDRCIKIWDVTSQATLLTITN 270
Cdd:cd00200     8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKG 49
PQQ_ADH_I cd10277
Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); ...
 126-208 1.12e-04

Ethanol dehydrogenase, a bacterial quinoprotein (PQQ-dependent type I alcohol dehydrogenase); This bacterial family of homodimeric ethanol dehydrogenases utilize pyrroloquinoline quinone (PQQ) as a cofactor. It represents proteins whose expression may be induced by ethanol, and which are similar to quinoprotein methanol dehydrogenases, but have higher specificities for ethanol and other primary and secondary alcohols. Dehydrogenases with PQQ cofactors, such as ethanol, methanol, and membrane-bound glucose dehydrogenases, form an 8-bladed beta-propeller.


Pssm-ID: 199835 [Multi-domain]  Cd Length: 529  Bit Score: 43.44  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 126 VKLWDPVDGSVVrdFEHRPKAPVVECSITGDSSRVIAASYDKTVRAWDLETGKLLWKVRYDTFIVSC--KFSPDGK-YV- 201
Cdd:cd10277   418 LQAIDPTTGKKV--WEHKTPLPLWGGVLTTAGGLVFTGTPDGYFRAFDAKTGKELWEFQTGSGIIGPpvTWEVDGKqYVa 495


                  ....*...
gi 2462562885 202 -VSGFDVD 208
Cdd:cd10277   496 vLSGWGGA 503
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 112-181 1.40e-04

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 42.39  E-value: 1.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 112 VDDTKLLSGSYDCTVKLWDPVDGSVVrdFEHRPKAPVVEcSITGDSSRVIAASYDKTVRAWDLETGKLLW 181
Cdd:pfam13360  31 VDGGRLFVATGGGQLVALDAATGKLL--WRQTLSGEVLG-APLVAGGRVFVVAGDGSLIALDAADGRRLW 97
PQQ pfam01011
PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller ...
 159-191 2.11e-04

PQQ enzyme repeat; The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilize pyrrolo-quinoline quinone as a prosthetic group.


Pssm-ID: 395799 [Multi-domain]  Cd Length: 36  Bit Score: 37.94  E-value: 2.11e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462562885 159 RVIAASYDKTVRAWDLETGKLLWKVRYDTFIVS 191
Cdd:pfam01011   2 TVYLGSDDGYLYALDAETGKVLWSFKTGGAVLS 34
assembly_YfgL TIGR03300
outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a ...
 64-210 2.92e-04

outer membrane assembly lipoprotein YfgL; Members of this protein family are YfgL, a lipoprotein component of a complex that acts protein insertion into the bacterial outer membrane. Other members of this complex are NlpB, YfiO, and YaeT. This protein contains multiple copies of a repeat that, in other contexts, are associated with binding of the coenzyme PQQ. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274511 [Multi-domain]  Cd Length: 377  Bit Score: 41.84  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885  64 DREPPPHLLPEKHQVPEKLIWgdqdplSKipfKILSGHEHAVSTCHFCVDDTKLLSGSYDCTVKLWDPVDGSVV--RDFE 141
Cdd:TIGR03300  24 DEPQPAELPEFQPTVKVDQVW------SA---SVGDGVGHYYLRLQPAVAGGKVYAADADGTVAALDAETGKRLwrVDLD 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462562885 142 HRPKAPVvecsiTGDSSRVIAASYDKTVRAWDLETGKLLWKVRYDTFIVSCKFSPDGKYVVS-------GFDVDHG 210
Cdd:TIGR03300  95 ERLSGGV-----GADGGLVFVGTEKGEVIALDAEDGKELWRAKLSSEVLSPPLVANGLVVVRtndgrltALDAATG 165
PQQ COG1520
Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell ...
 127-189 1.02e-03

Outer membrane protein assembly factor BamB, contains PQQ-like beta-propeller repeat [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441129 [Multi-domain]  Cd Length: 370  Bit Score: 40.18  E-value: 1.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462562885 127 KLWDPVDGSVVRDFEHRPkAPVVecsiTGDssRVIAASYDKTVRAWDLETGKLLWKVRYDTFI 189
Cdd:COG1520    34 QLWSASVGDGVGKGYSRL-APAV----AGD--RVYAADADGRVAALDAATGKELWRVDLGEPL 89
PQQ_mGDH cd10280
Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes ...
 161-184 1.18e-03

Membrane-bound PQQ-dependent glucose dehydrogenase; This bacterial subfamily of enzymes belongs to the dehydrogenase family with pyrroloquinoline quinone (PQQ) as cofactor, and is the only subfamily that is bound to the membrane. Glucose dehydrogenase converts D-glucose to D-glucono-1,5-lactone in a reaction that is coupled with the respiratory chain in the periplasmic oxidation of sugars and alcohols in gram-negative bacteria. Ubiquinone functions as the electron acceptor. The alignment model contains an 8-bladed beta-propeller.


Pssm-ID: 199838 [Multi-domain]  Cd Length: 616  Bit Score: 40.25  E-value: 1.18e-03
                          10        20
                  ....*....|....*....|....
gi 2462562885 161 IAASYDKTVRAWDLETGKLLWKVR 184
Cdd:cd10280   550 IAATQDNYLRAFDKATGKELWEAR 573
PQQ_2 pfam13360
PQQ-like domain; This domain contains several repeats of the PQQ repeat.
 125-218 1.63e-03

PQQ-like domain; This domain contains several repeats of the PQQ repeat.


Pssm-ID: 433144 [Multi-domain]  Cd Length: 233  Bit Score: 38.92  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 125 TVKLWDPVDGSVVrdFEHRPKAPVVeCSITGDSSRVIAASYDKTVRAWDLETGKLLWKVRYDTFIVSCKFSPDGKYVVsg 204
Cdd:pfam13360   4 VVTALDAATGAEL--WRVDLETGLG-GGVAVDGGRLFVATGGGQLVALDAATGKLLWRQTLSGEVLGAPLVAGGRVFV-- 78

                          90
                  ....*....|....
gi 2462562885 205 FDVDHGICIMDAEN 218
Cdd:pfam13360  79 VAGDGSLIALDAAD 92
YncE COG3391
DNA-binding beta-propeller fold protein YncE [General function prediction only];
125-269 1.74e-03

DNA-binding beta-propeller fold protein YncE [General function prediction only];


Pssm-ID: 442618 [Multi-domain]  Cd Length: 237  Bit Score: 38.91  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 125 TVKLWDPVDGSVVRDFEHRPKAPVVECSITGDSSRV-IAASYDKTVRAWDLETGKLLWKVRYDTFIVSCKFSPDGKYV-V 202
Cdd:COG3391    47 AAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLyVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLyV 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462562885 203 SGFDvDHGICIMDAENITTVSVIKDHhtRSITSCCFDPDSQR--VASVSLDRCIKI---WDVTSQATLLTIT 269
Cdd:COG3391   127 ADSG-NGRVSVIDTATGKVVATIPVG--AGPHGIAVDPDGKRlyVANSGSNTVSVIvsvIDTATGKVVATIP 195
Gcd COG4993
Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];
125-202 2.87e-03

Glucose dehydrogenase, PQQ-dependent [Carbohydrate transport and metabolism];


Pssm-ID: 444017 [Multi-domain]  Cd Length: 515  Bit Score: 38.99  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462562885 125 TVKLWDPVDGSVVrdFEHRPKAPVVECSITGDSSRVIAASYDKTVRAWDLETGKLLWKVRYDTFIVS--CKFSPDGK-YV 201
Cdd:COG4993   410 TLTAIDLNTGKIV--WQVPLGFPNWGGPLATAGGLVFIGTLDGYLRAFDAKTGKELWKFRLPSGGQAtpMTYEVDGKqYV 487


                  .
gi 2462562885 202 V 202
Cdd:COG4993   488 A 488
PQQ smart00564
beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline ...
 152-184 3.71e-03

beta-propeller repeat; Beta-propeller repeat occurring in enzymes with pyrrolo-quinoline quinone (PQQ) as cofactor, in Ire1p-like Ser/Thr kinases, and in prokaryotic dehydrogenases.


Pssm-ID: 128836 [Multi-domain]  Cd Length: 33  Bit Score: 34.43  E-value: 3.71e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 2462562885  152 SITGDSSrVIAASYDKTVRAWDLETGKLLWKVR 184
Cdd:smart00564   2 VVLSDGT-VYVGSTDGTLYALDAKTGEILWTYK 33
8prop_heme_binding_protein cd20718
eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; ...
 173-226 8.09e-03

eight-bladed beta-propeller heme-binding domain in cytochrome cd1 and similar proteins; Members here contain an 8-bladed beta-propeller heme-binding domain in cytochrome cd1 (nitrite reductase) and similar proteins including NirN and NirF. During denitrification, nitrate (Nar), nitrite (Nir), nitric oxide (Nor), and nitrous oxide (Nos) reductases catalyze the reaction cascade of NO(3-)-> NO(2-)-> NO -> N2O -> N2. The integral membrane proteins NorC, NorB, and NosR form the core assembly platform that binds the nitrate reductase NarGHI and the periplasmic nitrite reductase NirS via its maturation factor NirF. NirN and NirF form a stable complex with the nitrite reductase NirS during enzyme maturation. NirF is involved in heme d1 insertion.


Pssm-ID: 467720 [Multi-domain]  Cd Length: 380  Bit Score: 37.32  E-value: 8.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462562885 173 DLETGKLLWKVRYDTFIVSCKFSPDGKYVVSGFDVDHGICIMDAENITTVSVIK 226
Cdd:cd20718    86 DLYTLRPVASIRIGVNSRGIALSDDGKYVIAGNYEPGHVVILDADTLEPLKVIP 139
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH