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Conserved domains on  [gi|1622897827|ref|XP_014977801|]
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WD repeat-containing protein 18 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
34-319 6.95e-32

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.41  E-value: 6.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  34 VWELHSGANLLTYRGGQAGPHGLALL-NGEYLLAAQLGKNyISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA 112
Cdd:COG2319   104 LWDLATGLLLRTLTGHTGAVRSVAFSpDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 113 -ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlqadpsRIPAPRHVWSHHTLPITDLH 191
Cdd:COG2319   183 dGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL---------ATGKLLRTLTGHSGSVRSVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 192 CGFGGPlaRVATSSLDQTVKLWEVSSGELLLSVL-FDVSIMAVTMDLAEHHMFCGGSEGSifqVDLFTWPGQRERnfqpe 270
Cdd:COG2319   254 FSPDGR--LLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGT---VRLWDLATGKLL----- 323

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622897827 271 qdagKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTL 319
Cdd:COG2319   324 ----RTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
Periplasmic_Binding_Protein_type1 super family cl10011
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 224-442 8.44e-30

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: 119.07  E-value: 8.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 224 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERNFQPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 302
Cdd:cd06377     1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 303 ETVRLwdvqSKQCIRTLALKGPVTNATILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 375
Cdd:cd06377    81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897827 376 HQQGSEPSYLDrteqlqavLCSTMEKSVLGGQDQLRVRVTelEDEVRNLRKINRDLFDFSTRFITRP 442
Cdd:cd06377   151 CQPWDPTSFLL--------LWQNNSQFHLGTVLNLSVLDE--SDLQRSLQQHLESLKDPSPAIVMFG 207
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
34-319 6.95e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.41  E-value: 6.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  34 VWELHSGANLLTYRGGQAGPHGLALL-NGEYLLAAQLGKNyISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA 112
Cdd:COG2319   104 LWDLATGLLLRTLTGHTGAVRSVAFSpDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 113 -ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlqadpsRIPAPRHVWSHHTLPITDLH 191
Cdd:COG2319   183 dGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL---------ATGKLLRTLTGHSGSVRSVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 192 CGFGGPlaRVATSSLDQTVKLWEVSSGELLLSVL-FDVSIMAVTMDLAEHHMFCGGSEGSifqVDLFTWPGQRERnfqpe 270
Cdd:COG2319   254 FSPDGR--LLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGT---VRLWDLATGKLL----- 323

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622897827 271 qdagKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTL 319
Cdd:COG2319   324 ----RTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
PBP1_iGluR_NMDA_NR3 cd06377
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of ...
 224-442 8.44e-30

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: 119.07  E-value: 8.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 224 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERNFQPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 302
Cdd:cd06377     1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 303 ETVRLwdvqSKQCIRTLALKGPVTNATILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 375
Cdd:cd06377    81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897827 376 HQQGSEPSYLDrteqlqavLCSTMEKSVLGGQDQLRVRVTelEDEVRNLRKINRDLFDFSTRFITRP 442
Cdd:cd06377   151 CQPWDPTSFLL--------LWQNNSQFHLGTVLNLSVLDE--SDLQRSLQQHLESLKDPSPAIVMFG 207
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 31-309 9.67e-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: 114.35  E-value: 9.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  31 SCIVWELHSGANLLTYRGGQAGPHGLALL-NGEYLLAAQLGKnYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLA 109
Cdd:cd00200    32 TIKVWDLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDK-TIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 110 -GVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlqadpsRIPAPRHVWSHHTLPIT 188
Cdd:cd00200   111 sSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL---------RTGKCVATLTGHTGEVN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 189 dlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLftwpgqreRNF 267
Cdd:cd00200   182 --SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL--------RTG 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622897827 268 QPEQdagkVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:cd00200   252 ECVQ----TLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40_alt pfam14077
Alternative WD40 repeat motif; WD repeats are short subdomains of about 40 amino acids and ...
 395-442 1.59e-24

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: 95.23  E-value: 1.59e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622897827 395 LCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLFDFSTRFITRP 442
Cdd:pfam14077   1 MCSTTDKNVLGDQEQLKVRVSELEEEVRTLRKINKDLFDFSTRIITKP 48
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 275-309 6.82e-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: 51.16  E-value: 6.82e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622897827  275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
275-309 1.22e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.42  E-value: 1.22e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622897827 275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
34-319 6.95e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.41  E-value: 6.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  34 VWELHSGANLLTYRGGQAGPHGLALL-NGEYLLAAQLGKNyISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA 112
Cdd:COG2319   104 LWDLATGLLLRTLTGHTGAVRSVAFSpDGKTLASGSADGT-VRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSD 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 113 -ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlqadpsRIPAPRHVWSHHTLPITDLH 191
Cdd:COG2319   183 dGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL---------ATGKLLRTLTGHSGSVRSVA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 192 CGFGGPlaRVATSSLDQTVKLWEVSSGELLLSVL-FDVSIMAVTMDLAEHHMFCGGSEGSifqVDLFTWPGQRERnfqpe 270
Cdd:COG2319   254 FSPDGR--LLASGSADGTVRLWDLATGELLRTLTgHSGGVNSVAFSPDGKLLASGSDDGT---VRLWDLATGKLL----- 323

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622897827 271 qdagKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTL 319
Cdd:COG2319   324 ----RTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTL 368
WD40 COG2319
WD40 repeat [General function prediction only];
34-312 4.77e-31

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 123.10  E-value: 4.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  34 VWELHSGANLLTYRGGQAGPHGLALL-NGEYLLAAQLGKNyISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA 112
Cdd:COG2319   146 LWDLATGKLLRTLTGHSGAVTSVAFSpDGKLLASGSDDGT-VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSA 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 113 E-SIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlqadpsRIPAPRHVWSHHTLPITDLH 191
Cdd:COG2319   225 DgTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL---------ATGELLRTLTGHSGGVNSVA 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 192 CGFGGplARVATSSLDQTVKLWEVSSGELLLSVL-FDVSIMAVTMDLAEHHMFCGGSEGSifqVDLFTWPGQRERnfqpe 270
Cdd:COG2319   296 FSPDG--KLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGT---VRLWDLATGELL----- 365

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622897827 271 qdagKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQS 312
Cdd:COG2319   366 ----RTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
34-320 1.73e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 121.56  E-value: 1.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  34 VWELHSGANLLTYRGGQAGPHGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA- 112
Cdd:COG2319    62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAd 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 113 ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 192
Cdd:COG2319   142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGHTGAVRSVAF 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 193 GFGGplARVATSSLDQTVKLWEVSSGELLlsvlfdvsimavtmdlaehhmfcggsegsifqvdlftwpgqrernfqpeqd 272
Cdd:COG2319   213 SPDG--KLLASGSADGTVRLWDLATGKLL--------------------------------------------------- 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1622897827 273 agKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTLA 320
Cdd:COG2319   240 --RTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLT 285
PBP1_iGluR_NMDA_NR3 cd06377
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of ...
 224-442 8.44e-30

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: 119.07  E-value: 8.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 224 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERNFQPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 302
Cdd:cd06377     1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 303 ETVRLwdvqSKQCIRTLALKGPVTNATILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 375
Cdd:cd06377    81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622897827 376 HQQGSEPSYLDrteqlqavLCSTMEKSVLGGQDQLRVRVTelEDEVRNLRKINRDLFDFSTRFITRP 442
Cdd:cd06377   151 CQPWDPTSFLL--------LWQNNSQFHLGTVLNLSVLDE--SDLQRSLQQHLESLKDPSPAIVMFG 207
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 31-309 9.67e-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: 114.35  E-value: 9.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  31 SCIVWELHSGANLLTYRGGQAGPHGLALL-NGEYLLAAQLGKnYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLA 109
Cdd:cd00200    32 TIKVWDLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDK-TIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 110 -GVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlqadpsRIPAPRHVWSHHTLPIT 188
Cdd:cd00200   111 sSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL---------RTGKCVATLTGHTGEVN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 189 dlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLftwpgqreRNF 267
Cdd:cd00200   182 --SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL--------RTG 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622897827 268 QPEQdagkVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:cd00200   252 ECVQ----TLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 93-319 8.59e-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: 108.96  E-value: 8.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  93 GPVTCLTASPNGLYVL-AGVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlqadps 171
Cdd:cd00200    52 GPVRDVAASADGTYLAsGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV--------- 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 172 RIPAPRHVWSHHTLPITdlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGS 250
Cdd:cd00200   123 ETGKCLTTLRGHTDWVN--SVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSDGT 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622897827 251 IFQVDLftwpgqrernfqPEQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTL 319
Cdd:cd00200   201 IKLWDL------------STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTL 257
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 92-319 1.56e-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: 105.49  E-value: 1.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  92 PGPVTCLTASPNGLYVLAGVA-ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlqadp 170
Cdd:cd00200     9 TGGVTCVAFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL-------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 171 sRIPAPRHVWSHHTLPITDLHCGFGGPLarVATSSLDQTVKLWEVSSGELLLSVLF-DVSIMAVTMDLAEHHMFCGGSEG 249
Cdd:cd00200    81 -ETGECVRTLTGHTSYVSSVAFSPDGRI--LSSSSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDG 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 250 SIFQVDLftwpgqreRNFQPEQdagkVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTL 319
Cdd:cd00200   158 TIKLWDL--------RTGKCVA----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL 215
WD40 COG2319
WD40 repeat [General function prediction only];
34-319 9.52e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 105.38  E-value: 9.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  34 VWELHSGANLLTYRGGQAGPHGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAE 113
Cdd:COG2319    20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASAD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 114 -SIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 192
Cdd:COG2319   100 gTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT---------GKLLRTLTGHSGAVTSVAF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 193 GFGGplARVATSSLDQTVKLWEVSSGELLlsvlfdvsimavtmdlaehhmfcggsegsifqvdlftwpgqrernfqpeqd 272
Cdd:COG2319   171 SPDG--KLLASGSDDGTVRLWDLATGKLL--------------------------------------------------- 197

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1622897827 273 agKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTL 319
Cdd:COG2319   198 --RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTL 242
WD40_alt pfam14077
Alternative WD40 repeat motif; WD repeats are short subdomains of about 40 amino acids and ...
 395-442 1.59e-24

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: 95.23  E-value: 1.59e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1622897827 395 LCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLFDFSTRFITRP 442
Cdd:pfam14077   1 MCSTTDKNVLGDQEQLKVRVSELEEEVRTLRKINKDLFDFSTRIITKP 48
WD40 COG2319
WD40 repeat [General function prediction only];
64-319 1.63e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 1.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827  64 LLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAE-SIHLWEVSTGNLLVILSRHYQDVSCLQFT 142
Cdd:COG2319     8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDlTLLLLDAAAGALLATLLGHTAAVLSVAFS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 143 GDSSHFISGGKDCLVLAWSLCSvlqadpsriPAPRHVWSHHTLPITDLHCGFGGplARVATSSLDQTVKLWEVSSGELLl 222
Cdd:COG2319    88 PDGRLLASASADGTVRLWDLAT---------GLLLRTLTGHTGAVRSVAFSPDG--KTLASGSADGTVRLWDLATGKLL- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 223 svlfdvsimavtmdlaehhmfcggsegsifqvdlftwpgqrernfqpeqdagKVFKGHRNQVTCLSVSTDGSVLLSGSHD 302
Cdd:COG2319   156 ----------------------------------------------------RTLTGHSGAVTSVAFSPDGKLLASGSDD 183

                         250
                  ....*....|....*..
gi 1622897827 303 ETVRLWDVQSKQCIRTL 319
Cdd:COG2319   184 GTVRLWDLATGKLLRTL 200
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 275-319 1.12e-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: 59.27  E-value: 1.12e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622897827 275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTL 319
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL 47
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 275-309 6.82e-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: 51.16  E-value: 6.82e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1622897827  275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
275-309 1.22e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.42  E-value: 1.22e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1622897827 275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 176-320 3.33e-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: 51.57  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 176 PRHVWSHHTLPITDLHcgFGGPLARVATSSLDQTVKLWEVSSGELLLSvlfdvsimavtmdlaehhmfcggsegsifqvd 255
Cdd:cd00200     1 LRRTLKGHTGGVTCVA--FSPDGKLLATGSGDGTIKVWDLETGELLRT-------------------------------- 46

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622897827 256 lftwpgqrernfqpeqdagkvFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTLA 320
Cdd:cd00200    47 ---------------------LKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 280-310 4.40e-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: 48.53  E-value: 4.40e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622897827 280 HRNQVTCLSVSTDGSVLLSGSHDETVRLWDV 310
Cdd:pfam20426 123 HKDVVSCVAVTSDGSILATGSYDTTVMVWEV 153
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 135-314 9.44e-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: 44.14  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 135 DVSCLQFTGDSSHFISGGKDCLVLAWSLcsvlQADPSRI---PAPRH--------VWshhtlpITDLhcGFGGP--LARV 201
Cdd:cd22857   128 NLLCMRVDPNENYFAFGGKEVELNVWDL----EEKPGKIwraKNVPNdslglrvpVW------VTDL--TFLSKddHRKI 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 202 ATSSLDQTVKLWEVSSGEL-LLSVLF-DVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTwpGQRERNFqpeqdagKVFKG 279
Cdd:cd22857   196 VTGTGYHQVRLYDTRAQRRpVVSVDFgETPIKAVAEDPDGHTVYVGDTSGDLASIDLRT--GKLLGCF-------KGKCG 266

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622897827 280 HrnQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQ 314
Cdd:cd22857   267 G--SIRSIARHPELPLIASCGLDRYLRIWDTETRQ 299
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 122-161 2.54e-04

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: 38.45  E-value: 2.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1622897827  122 TGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWS 161
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 215-318 1.60e-03

Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous with the Nup160 of vertebrates. The nuclear core complex, or NPC, mediates macromolecular transport across the nuclear envelope. Deletion of the NUP120 gene causes clustering of NPCs at one side of the nuclear envelope, moderate nucleolar fragmentation and slower cell growth. The vertebrate NPC is estimated to contain between 30 and 60 different proteins. most of which are not known. Two important ones in creating the nucleoporin basket are Nup98 and Nup153, and Nup120, in conjunction with Nup 133, interacts with these two and itself plays a role in mRNA export. Nup160, Nup133, Nup96, and Nup107 are all targets of phosphorylation. The phosphorylation sites are clustered mainly at the N-terminal regions of these proteins, which are predicted to be natively disordered. The entire Nup107-160 sub-complex is stable throughout the cell cycle, thus it seems unlikely that phosphorylation affects interactions within the Nup107-160 sub-complex, but rather that it regulates the association of the sub-complex with the NPC and other proteins.


Pssm-ID: 432020 [Multi-domain]  Cd Length: 540  Bit Score: 40.91  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622897827 215 VSSGELLLSvLFDVSIMAVTMDLAEHHMfcggsEGSIFQVDLFTWPgqrERNFQPEQDAGKVFKGHRNQVTCLSVST--- 291
Cdd:pfam11715 159 VSPLELLVS-LADGGLLKLTRSSDGGAW-----KESTFEPASWLQS---LSGLLGWLADPTIRYSGSSVALSLSAAPavt 229

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622897827 292 ---DGSVLLSGSHDETVRLWDVQSKQCIRT 318
Cdd:pfam11715 230 tvgGQNFLFTLSLDHTLRVWDLLTGKCLAT 259
WD40 pfam00400
WD domain, G-beta repeat;
123-161 3.37e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.01  E-value: 3.37e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622897827 123 GNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLAWS 161
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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