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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26387325 230 KGAISSVALHPSEvrTLVAAGAKYGQIGLWDLTQQSEdaMYVFYAHSRYVSCLSFSPTNpAHLLSLSYDGTLRCGDFSS 308
Cdd:cd00200 135 TDWVNSVAFSPDG--TFVASSSQDGTIKLWDLRTGKC--VATLTGHTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLST 208

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26387325 230 KGAISSVALHPSEvrTLVAAGAKYGQIGLWDLTQQSEdaMYVFYAHSRYVSCLSFSPTNpAHLLSLSYDGTLRCGDFSS 308
Cdd:cd00200 135 TDWVNSVAFSPDG--TFVASSSQDGTIKLWDLRTGKC--VATLTGHTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLST 208

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

                           10        20        30
                   ....*....|....*....|....*....|....
gi 26387325    270 YVFYAHSRYVSCLSFSPTNPaHLLSLSYDGTLRC 303
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGK-YLASGSDDGTIKL 38

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26387325 230 KGAISSVALHPSEvrTLVAAGAKYGQIGLWDLTQQSEdaMYVFYAHSRYVSCLSFSPTNpAHLLSLSYDGTLRCGDFSS 308
Cdd:cd00200 135 TDWVNSVAFSPDG--TFVASSSQDGTIKLWDLRTGKC--VATLTGHTGEVNSVAFSPDG-EKLLSSSSDGTIKLWDLST 208

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26387325 230 KGAISSVALHPSevRTLVAAGAKYGQIGLWDLTqqSEDAMYVFYAHSRYVSCLSFSPTNPaHLLSLSYDGTLR 302
Cdd:cd00200  93 TSYVSSVAFSPD--GRILSSSSRDKTIKVWDVE--TGKCLTTLRGHTDWVNSVAFSPDGT-FVASSSQDGTIK 160

WD40 repeat [General function prediction only];

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26387325 230 KGAISSVALHPSevRTLVAAGAKYGQIGLWDLTQQSEdaMYVFYAHSRYVSCLSFSPTNpAHLLSLSYDGTLR 302
Cdd:COG2319 120 TGAVRSVAFSPD--GKTLASGSADGTVRLWDLATGKL--LRTLTGHSGAVTSVAFSPDG-KLLASGSDDGTVR 187

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.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26387325 230 KGAISSVALHPSEvRTLVAAGAKyGQIGLWDLtqQSEDAMYVFYAHSRYVSCLSFSPtNPAHLLSLSYDGTLRC 303
Cdd:cd00200 177 TGEVNSVAFSPDG-EKLLSSSSD-GTIKLWDL--STGKCLGTLRGHENGVNSVAFSP-DGYLLASGSEDGTIRV 245

WD40 repeat [General function prediction only];

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26387325 231 GAISSVALHPSevRTLVAAGAKYGQIGLWDLtqQSEDAMYVFYAHSRYVSCLSFSPtNPAHLLSLSYDGTLR 302
Cdd:COG2319 247 GSVRSVAFSPD--GRLLASGSADGTVRLWDL--ATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGTVR 313

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26387325 230 KGAISSVALHPSevRTLVAAGAKYGQIGLWDLTQQSEDamYVFYAHSRYVSCLSFSPTNPAhLLSLSYDGTLRCGDFSSA 309
Cdd:cd00200  51 TGPVRDVAASAD--GTYLASGSSDKTIRLWDLETGECV--RTLTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVETG 125

                ..
gi 26387325 310 VF 311
Cdd:cd00200 126 KC 127

WD40 repeat [General function prediction only];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26387325 222 EATVRKVTKGAISSVALHPSevRTLVAAGAKYGQIGLWDLTQQSEDAmyVFYAHSRYVSCLSFSPtNPAHLLSLSYDGTL 301
Cdd:COG2319  70 LLATLLGHTAAVLSVAFSPD--GRLLASASADGTVRLWDLATGLLLR--TLTGHTGAVRSVAFSP-DGKTLASGSADGTV 144

                .
gi 26387325 302 R 302
Cdd:COG2319 145 R 145