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Conserved domains on  [gi|94730675|sp|Q499N3|]
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RecName: Full=WD repeat-containing protein 18

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_type1 super family cl10011
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 212-430 1.60e-35

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


The actual alignment was detected with superfamily member cd06377:

Pssm-ID: 471960 [Multi-domain]  Cd Length: 373  Bit Score: 134.87  E-value: 1.60e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 212 VLFDMGITSVTMDLAEHYIFCGGSDGSIFQVDLCSRPGPREQSFQPEQN-TGKVFKGHRNQVTCLSVSTDGSILLSGSHD 290
Cdd:cd06377   1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAaPWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 291 ESVRLwdvkSKQCVRTVPLKGPVTNAAITLAPPSmlnpefRPSLPLPHFNKHLLGAEHGDEAQGGGLRLQLGLHlqgkEP 370
Cdd:cd06377  81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDVLVSLLQANSWE----DV 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94730675 371 SYLERLEQLQAALSGYLEKNmlgSQMLPVRVFELEEE-----VRSLRKINRDLFDFSTRIITRPS 430
Cdd:cd06377 147 SLLLCQPWDPTSFLLLWQNN---SQFHLGTVLNLSVLdesdlQRSLQQHLESLKDPSPAIVMFGC 208
WD40 COG2319
WD40 repeat [General function prediction only];
13-313 4.17e-33

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.88  E-value: 4.17e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  13 SAAPLWSCMVWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQQGKNYICAWELQRKDQLQQKIMCPGPVTCLTTAPNG 92
Cdd:COG2319  53 AGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDG 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  93 LYVLAGIA-ESIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLCSvlqadpsriLAPRHVWSQH 171
Cdd:COG2319 133 KTLASGSAdGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGH 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 172 TLPITDLHCGFGGpmARVATASLDQTMKLWAISSGDLLLSV-LFDMGITSVTMDLAEHYIFCGGSDGSIFQVDLcsrpgp 250
Cdd:COG2319 204 TGAVRSVAFSPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL------ 275

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94730675 251 reqsfqpeqNTGK---VFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRTvpLKGPV 313
Cdd:COG2319 276 ---------ATGEllrTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHT 330
 
Name Accession Description Interval E-value
PBP1_iGluR_NMDA_NR3 cd06377
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of ...
 212-430 1.60e-35

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of NMDA receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR3 subunit of NMDA receptor family. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain.


Pssm-ID: 380600 [Multi-domain]  Cd Length: 373  Bit Score: 134.87  E-value: 1.60e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 212 VLFDMGITSVTMDLAEHYIFCGGSDGSIFQVDLCSRPGPREQSFQPEQN-TGKVFKGHRNQVTCLSVSTDGSILLSGSHD 290
Cdd:cd06377   1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAaPWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 291 ESVRLwdvkSKQCVRTVPLKGPVTNAAITLAPPSmlnpefRPSLPLPHFNKHLLGAEHGDEAQGGGLRLQLGLHlqgkEP 370
Cdd:cd06377  81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDVLVSLLQANSWE----DV 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94730675 371 SYLERLEQLQAALSGYLEKNmlgSQMLPVRVFELEEE-----VRSLRKINRDLFDFSTRIITRPS 430
Cdd:cd06377 147 SLLLCQPWDPTSFLLLWQNN---SQFHLGTVLNLSVLdesdlQRSLQQHLESLKDPSPAIVMFGC 208
WD40 COG2319
WD40 repeat [General function prediction only];
13-313 4.17e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.88  E-value: 4.17e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  13 SAAPLWSCMVWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQQGKNYICAWELQRKDQLQQKIMCPGPVTCLTTAPNG 92
Cdd:COG2319  53 AGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDG 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  93 LYVLAGIA-ESIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLCSvlqadpsriLAPRHVWSQH 171
Cdd:COG2319 133 KTLASGSAdGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGH 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 172 TLPITDLHCGFGGpmARVATASLDQTMKLWAISSGDLLLSV-LFDMGITSVTMDLAEHYIFCGGSDGSIFQVDLcsrpgp 250
Cdd:COG2319 204 TGAVRSVAFSPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL------ 275

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94730675 251 reqsfqpeqNTGK---VFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRTvpLKGPV 313
Cdd:COG2319 276 ---------ATGEllrTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHT 330
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 22-297 3.56e-29

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: 115.51  E-value: 3.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  22 VWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAqqGKNY-ICAWELQRKDQLQQKIMCPGPVTCLTTAPNGLYVLAGI 99
Cdd:cd00200  35 VWDLETGELLRTLKGHTGPVRDVAASaDGTYLASG--SSDKtIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSS 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 100 A-ESIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLcsvlqadpsRILAPRHVWSQHTLPITdl 178
Cdd:cd00200 113 RdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL---------RTGKCVATLTGHTGEVN-- 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 179 HCGFGGPMARVATASLDQTMKLWAISSGDLLLS-VLFDMGITSVTMDLAEHYIFCGGSDGSIFQVDLCSRpgpreqsfqp 257
Cdd:cd00200 182 SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG---------- 251

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 94730675 258 eqNTGKVFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWD 297
Cdd:cd00200 252 --ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40_alt pfam14077
Alternative WD40 repeat motif; WD repeats are short subdomains of about 40 amino acids and ...
 383-429 2.84e-22

Alternative WD40 repeat motif; WD repeats are short subdomains of about 40 amino acids and fold into 4 antiparallel beta hairpins. This domain here has been detected on the C-terminus of WD repeat-containing protein 18 during target selection by the Joint Center for Structural Genomics.


Pssm-ID: 433698  Cd Length: 48  Bit Score: 89.07  E-value: 2.84e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 94730675   383 LSGYLEKNMLGSQ-MLPVRVFELEEEVRSLRKINRDLFDFSTRIITRP 429
Cdd:pfam14077   1 MCSTTDKNVLGDQeQLKVRVSELEEEVRTLRKINKDLFDFSTRIITKP 48
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 263-297 3.87e-09

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: 51.93  E-value: 3.87e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 94730675    263 KVFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWD 297
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 110-149 5.59e-05

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: 39.99  E-value: 5.59e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 94730675    110 TGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWS 149
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
111-149 1.05e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 94730675   111 GNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWS 149
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
PBP1_iGluR_NMDA_NR3 cd06377
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of ...
 212-430 1.60e-35

N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of NMDA receptor family; N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domain of the NR3 subunit of NMDA receptor family. The ionotropic N-methyl-D-asparate (NMDA) subtype of glutamate receptor serves critical functions in neuronal development, functioning, and degeneration in the mammalian central nervous system. The functional NMDA receptor is a heterotetramer composed of two NR1 and two NR2 (A, B, C, and D) or of NR3 (A and B) subunits. The receptor controls a cation channel that is highly permeable to monovalent ions and calcium and exhibits voltage-dependent inhibition by magnesium. Dual agonists, glutamate and glycine, are required for efficient activation of the NMDA receptor. Among NMDA receptor subtypes, the NR2B subunit containing receptors appear particularly important for pain perception; thus NR2B-selective antagonists may be useful in the treatment of chronic pain.


Pssm-ID: 380600 [Multi-domain]  Cd Length: 373  Bit Score: 134.87  E-value: 1.60e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 212 VLFDMGITSVTMDLAEHYIFCGGSDGSIFQVDLCSRPGPREQSFQPEQN-TGKVFKGHRNQVTCLSVSTDGSILLSGSHD 290
Cdd:cd06377   1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAaPWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 291 ESVRLwdvkSKQCVRTVPLKGPVTNAAITLAPPSmlnpefRPSLPLPHFNKHLLGAEHGDEAQGGGLRLQLGLHlqgkEP 370
Cdd:cd06377  81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDVLVSLLQANSWE----DV 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94730675 371 SYLERLEQLQAALSGYLEKNmlgSQMLPVRVFELEEE-----VRSLRKINRDLFDFSTRIITRPS 430
Cdd:cd06377 147 SLLLCQPWDPTSFLLLWQNN---SQFHLGTVLNLSVLdesdlQRSLQQHLESLKDPSPAIVMFGC 208
WD40 COG2319
WD40 repeat [General function prediction only];
13-313 4.17e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.88  E-value: 4.17e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  13 SAAPLWSCMVWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQQGKNYICAWELQRKDQLQQKIMCPGPVTCLTTAPNG 92
Cdd:COG2319  53 AGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDG 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  93 LYVLAGIA-ESIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLCSvlqadpsriLAPRHVWSQH 171
Cdd:COG2319 133 KTLASGSAdGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGH 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 172 TLPITDLHCGFGGpmARVATASLDQTMKLWAISSGDLLLSV-LFDMGITSVTMDLAEHYIFCGGSDGSIFQVDLcsrpgp 250
Cdd:COG2319 204 TGAVRSVAFSPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL------ 275

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94730675 251 reqsfqpeqNTGK---VFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRTvpLKGPV 313
Cdd:COG2319 276 ---------ATGEllrTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT--LTGHT 330
WD40 COG2319
WD40 repeat [General function prediction only];
22-319 4.47e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.49  E-value: 4.47e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  22 VWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAQQGKNyICAWELQRKDQLQQKIMCPGPVTCLTTAPNGLYVL-AGI 99
Cdd:COG2319 104 LWDLATGLLLRTLTGHTGAVRSVAFSpDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLAsGSD 182

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 100 AESIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLcsvlqADPSRIlaprHVWSQHTLPITDLH 179
Cdd:COG2319 183 DGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL-----ATGKLL----RTLTGHSGSVRSVA 253

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 180 CGFGGPmaRVATASLDQTMKLWAISSGDLLLSVLFDMG-ITSVTMDLAEHYIFCGGSDGSIFQVDLcsrpgpreqsfqpe 258
Cdd:COG2319 254 FSPDGR--LLASGSADGTVRLWDLATGELLRTLTGHSGgVNSVAFSPDGKLLASGSDDGTVRLWDL-------------- 317

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94730675 259 qNTGKV---FKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRTVP-LKGPVTNAAIT 319
Cdd:COG2319 318 -ATGKLlrtLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTgHTGAVTSVAFS 381
WD40 COG2319
WD40 repeat [General function prediction only];
22-300 3.08e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.48  E-value: 3.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  22 VWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAQQGKNyICAWELQRKDQLQQKIMCPGPVTCLTTAPNGLYVLAGIA 100
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSpDGKLLASGSDDGT-VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSA 224

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 101 E-SIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLcsvlqaDPSRILaprHVWSQHTLPITDLH 179
Cdd:COG2319 225 DgTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL------ATGELL---RTLTGHSGGVNSVA 295

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 180 CGFGGpmARVATASLDQTMKLWAISSGDLLLSVL-FDMGITSVTMDLAEHYIFCGGSDGSifqVDLCSRPGPREqsfqpe 258
Cdd:COG2319 296 FSPDG--KLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGT---VRLWDLATGEL------ 364

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 94730675 259 qntGKVFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKS 300
Cdd:COG2319 365 ---LRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
22-319 1.05e-29

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 119.25  E-value: 1.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  22 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQQGKNYICAWELQRKDQLQQKIMCPGPVTCLTTAPNGLYVLAGIAE 101
Cdd:COG2319  20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASAD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 102 -SIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLCSvlqadpsriLAPRHVWSQHTLPITDLHc 180
Cdd:COG2319 100 gTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT---------GKLLRTLTGHSGAVTSVA- 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 181 gF---GgpmARVATASLDQTMKLWAISSGDLLLSVLFDMG-ITSVTMDLAEHYIFCGGSDGSIFQVDLcsrpgpreqsfq 256
Cdd:COG2319 170 -FspdG---KLLASGSDDGTVRLWDLATGKLLRTLTGHTGaVRSVAFSPDGKLLASGSADGTVRLWDL------------ 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94730675 257 peqNTGK---VFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRTVP-LKGPVTNAAIT 319
Cdd:COG2319 234 ---ATGKllrTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFS 297
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 22-297 3.56e-29

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: 115.51  E-value: 3.56e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  22 VWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAqqGKNY-ICAWELQRKDQLQQKIMCPGPVTCLTTAPNGLYVLAGI 99
Cdd:cd00200  35 VWDLETGELLRTLKGHTGPVRDVAASaDGTYLASG--SSDKtIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSS 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 100 A-ESIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLcsvlqadpsRILAPRHVWSQHTLPITdl 178
Cdd:cd00200 113 RdKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL---------RTGKCVATLTGHTGEVN-- 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 179 HCGFGGPMARVATASLDQTMKLWAISSGDLLLS-VLFDMGITSVTMDLAEHYIFCGGSDGSIFQVDLCSRpgpreqsfqp 257
Cdd:cd00200 182 SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG---------- 251

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 94730675 258 eqNTGKVFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWD 297
Cdd:cd00200 252 --ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 81-321 3.22e-26

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: 107.04  E-value: 3.22e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  81 GPVTCLTTAPNGLYVL-AGIAESIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLcsvlqadps 159
Cdd:cd00200  52 GPVRDVAASADGTYLAsGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV--------- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 160 RILAPRHVWSQHTLPITdlHCGFGGPMARVATASLDQTMKLWAISSGDLLLS-VLFDMGITSVTMDLAEHYIFCGGSDGS 238
Cdd:cd00200 123 ETGKCLTTLRGHTDWVN--SVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSDGT 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 239 IFQVDLcsrpgpreqsfqPEQNTGKVFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRTvpLKGPvTNAAI 318
Cdd:cd00200 201 IKLWDL------------STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT--LSGH-TNSVT 265


                ...
gi 94730675 319 TLA 321
Cdd:cd00200 266 SLA 268
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 80-306 4.35e-25

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: 103.95  E-value: 4.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  80 PGPVTCLTTAPNGLYVLAGIA-ESIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLcsvlqadp 158
Cdd:cd00200   9 TGGVTCVAFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL-------- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 159 sRILAPRHVWSQHTLPITDLHCGFGGPMarVATASLDQTMKLWAISSGDLLLSVLF-DMGITSVTMDLAEHYIFCGGSDG 237
Cdd:cd00200  81 -ETGECVRTLTGHTSYVSSVAFSPDGRI--LSSSSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94730675 238 SIFQVDLcsrpgpreqsfqpeqNTGK---VFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRT 306
Cdd:cd00200 158 TIKLWDL---------------RTGKcvaTLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT 214
WD40_alt pfam14077
Alternative WD40 repeat motif; WD repeats are short subdomains of about 40 amino acids and ...
 383-429 2.84e-22

Alternative WD40 repeat motif; WD repeats are short subdomains of about 40 amino acids and fold into 4 antiparallel beta hairpins. This domain here has been detected on the C-terminus of WD repeat-containing protein 18 during target selection by the Joint Center for Structural Genomics.


Pssm-ID: 433698  Cd Length: 48  Bit Score: 89.07  E-value: 2.84e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 94730675   383 LSGYLEKNMLGSQ-MLPVRVFELEEEVRSLRKINRDLFDFSTRIITRP 429
Cdd:pfam14077   1 MCSTTDKNVLGDQeQLKVRVSELEEEVRTLRKINKDLFDFSTRIITKP 48
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 113-306 3.06e-22

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: 95.86  E-value: 3.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 113 LLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWSLCSVlqaDPSRILaprhvwSQHTLPITDLHCGFGGPmaRVATA 192
Cdd:cd00200   1 LRRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETG---ELLRTL------KGHTGPVRDVAASADGT--YLASG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 193 SLDQTMKLWAISSGDlLLSVL--FDMGITSVTMDLAEHYIFCGGSDGSIFQVDLcsrpgpreQSFQPEQntgkVFKGHRN 270
Cdd:cd00200  70 SSDKTIRLWDLETGE-CVRTLtgHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV--------ETGKCLT----TLRGHTD 136

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 94730675 271 QVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRT 306
Cdd:cd00200 137 WVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVAT 172
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 263-297 3.87e-09

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: 51.93  E-value: 3.87e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 94730675    263 KVFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWD 297
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 263-311 4.09e-09

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: 57.34  E-value: 4.09e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 94730675 263 KVFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWDVKSKQCVRTvpLKG 311
Cdd:cd00200   3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT--LKG 49
WD40 pfam00400
WD domain, G-beta repeat;
263-297 7.06e-09

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 51.19  E-value: 7.06e-09
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 94730675   263 KVFKGHRNQVTCLSVSTDGSILLSGSHDESVRLWD 297
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 19-149 4.25e-07

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: 51.18  E-value: 4.25e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675  19 SCMVWELHSGANLLTYRGgqagprglallngeyllaaqqgknyicawelqrkdqlqqkimCPGPVTCLTTAPNGLYVLAG 98
Cdd:cd00200 200 TIKLWDLSTGKCLGTLRG------------------------------------------HENGVNSVAFSPDGYLLASG 237

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 94730675  99 IAE-SIYLWEVSTGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWS 149
Cdd:cd00200 238 SEDgTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 252-298 4.96e-06

Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at the C-terminus of neurobeachin-like proteins.


Pssm-ID: 466575 [Multi-domain]  Cd Length: 350  Bit Score: 48.14  E-value: 4.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 94730675   252 EQSFQP-EQNTGKVFKG---HRNQVTCLSVSTDGSILLSGSHDESVRLWDV 298
Cdd:pfam20426 103 ENSFQViSLNDGRMVQSirqHKDVVSCVAVTSDGSILATGSYDTTVMVWEV 153
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 123-302 2.53e-05

WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.


Pssm-ID: 439303 [Multi-domain]  Cd Length: 325  Bit Score: 46.07  E-value: 2.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 123 DVSCLKFTGDGSHFVSAGKDCLVLAWSLcsvlQADPSRIL---APRH--------VWsqhtlpITDLhcGFGGPMA--RV 189
Cdd:cd22857 128 NLLCMRVDPNENYFAFGGKEVELNVWDL----EEKPGKIWrakNVPNdslglrvpVW------VTDL--TFLSKDDhrKI 195

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94730675 190 ATASLDQTMKLWAISSGDL-LLSVLF-DMGITSVTMDLAEHYIFCGGSDGSIFQVDLcsrpgpreqsfqpeqNTGKV--- 264
Cdd:cd22857 196 VTGTGYHQVRLYDTRAQRRpVVSVDFgETPIKAVAEDPDGHTVYVGDTSGDLASIDL---------------RTGKLlgc 260

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 94730675 265 FKGHRN-QVTCLSVSTDGSILLSGSHDESVRLWDVKSKQ 302
Cdd:cd22857 261 FKGKCGgSIRSIARHPELPLIASCGLDRYLRIWDTETRQ 299
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 110-149 5.59e-05

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: 39.99  E-value: 5.59e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 94730675    110 TGNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWS 149
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
111-149 1.05e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 1.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 94730675   111 GNLLVILSRHYQDVSCLKFTGDGSHFVSAGKDCLVLAWS 149
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 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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