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Conserved domains on  [gi|38014171|gb|AAH00040|]
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WD repeat domain 18 [Homo sapiens]

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];
22-318 5.13e-33

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.49  E-value: 5.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  22 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA- 100
Cdd:COG2319  62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAd 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 101 ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 180
Cdd:COG2319 142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGHTGAVRSVAF 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 181 GFGGplARVATSSLDQTVKLWEVSSGELLLSV-LFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDL------FTWPGQRER 253
Cdd:COG2319 213 SPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLatgellRTLTGHSGG 290

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 254 ----SFHP--------------------EQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT-VA 308
Cdd:COG2319 291 vnsvAFSPdgkllasgsddgtvrlwdlaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTlTG 370

                       330
                ....*....|
gi 38014171 309 LKGPVTNAAI 318
Cdd:COG2319 371 HTGAVTSVAF 380
Periplasmic_Binding_Protein_type1 super family cl10011
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 212-430 6.36e-31

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: 122.16  E-value: 6.36e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 212 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 290
Cdd:cd06377   1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 291 ETVRLwdvqSKQCIRTVALKGPVTNAAILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 363
Cdd:cd06377  81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38014171 364 HQQGSEPSYLDrteqlqavLCSTMEKSVLGGQDQLRVRVTelEDEVRNLRKINRDLFDFSTRFITRP 430
Cdd:cd06377 151 CQPWDPTSFLL--------LWQNNSQFHLGTVLNLSVLDE--SDLQRSLQQHLESLKDPSPAIVMFG 207
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
22-318 5.13e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.49  E-value: 5.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  22 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA- 100
Cdd:COG2319  62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAd 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 101 ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 180
Cdd:COG2319 142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGHTGAVRSVAF 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 181 GFGGplARVATSSLDQTVKLWEVSSGELLLSV-LFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDL------FTWPGQRER 253
Cdd:COG2319 213 SPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLatgellRTLTGHSGG 290

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 254 ----SFHP--------------------EQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT-VA 308
Cdd:COG2319 291 vnsvAFSPdgkllasgsddgtvrlwdlaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTlTG 370

                       330
                ....*....|
gi 38014171 309 LKGPVTNAAI 318
Cdd:COG2319 371 HTGAVTSVAF 380
PBP1_iGluR_NMDA_NR3 cd06377
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of ...
 212-430 6.36e-31

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: 122.16  E-value: 6.36e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 212 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 290
Cdd:cd06377   1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 291 ETVRLwdvqSKQCIRTVALKGPVTNAAILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 363
Cdd:cd06377  81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38014171 364 HQQGSEPSYLDrteqlqavLCSTMEKSVLGGQDQLRVRVTelEDEVRNLRKINRDLFDFSTRFITRP 430
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 ...
 19-297 1.23e-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: 116.67  E-value: 1.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  19 SCIVWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAQLGKnYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLA 97
Cdd:cd00200  32 TIKVWDLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDK-TIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  98 -GVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadpsRIPAPRHVWSHHTLPIT 176
Cdd:cd00200 111 sSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL---------RTGKCVATLTGHTGEVN 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 177 dlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWpgqrersf 255
Cdd:cd00200 182 --SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-------- 251

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38014171 256 hpeqDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 297
Cdd:cd00200 252 ----ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40_alt pfam14077
Alternative WD40 repeat motif; WD repeats are short subdomains of about 40 amino acids and ...
 383-430 1.44e-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: 1.44e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 38014171   383 LCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLFDFSTRFITRP 430
Cdd:pfam14077   1 MCSTTDKNVLGDQEQLKVRVSELEEEVRTLRKINKDLFDFSTRIITKP 48
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 263-297 8.40e-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: 8.40e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 38014171    263 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 297
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
263-297 1.45e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.42  E-value: 1.45e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 38014171   263 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 297
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
22-318 5.13e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.49  E-value: 5.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  22 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA- 100
Cdd:COG2319  62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAd 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 101 ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 180
Cdd:COG2319 142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGHTGAVRSVAF 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 181 GFGGplARVATSSLDQTVKLWEVSSGELLLSV-LFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDL------FTWPGQRER 253
Cdd:COG2319 213 SPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLatgellRTLTGHSGG 290

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 254 ----SFHP--------------------EQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT-VA 308
Cdd:COG2319 291 vnsvAFSPdgkllasgsddgtvrlwdlaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTlTG 370

                       330
                ....*....|
gi 38014171 309 LKGPVTNAAI 318
Cdd:COG2319 371 HTGAVTSVAF 380
WD40 COG2319
WD40 repeat [General function prediction only];
22-300 7.69e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.41  E-value: 7.69e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  22 VWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAQLGKNyISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA 100
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSpDGKLLASGSDDGT-VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSA 224

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 101 E-SIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadpsRIPAPRHVWSHHTLPITDLH 179
Cdd:COG2319 225 DgTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL---------ATGELLRTLTGHSGGVNSVA 295

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 180 CGFGGplARVATSSLDQTVKLWEVSSGELLLSVL-FDVSIMAVTMDLAEHHMFCGGSEGSifqVDLFTWPGQRERsfhpe 258
Cdd:COG2319 296 FSPDG--KLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGT---VRLWDLATGELL----- 365

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38014171 259 qdagKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQS 300
Cdd:COG2319 366 ----RTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
PBP1_iGluR_NMDA_NR3 cd06377
N-terminal leucine-isoleucine-valine-binding protein (LIVBP)-like domain of the NR3 subunit of ...
 212-430 6.36e-31

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: 122.16  E-value: 6.36e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 212 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 290
Cdd:cd06377   1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 291 ETVRLwdvqSKQCIRTVALKGPVTNAAILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 363
Cdd:cd06377  81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 38014171 364 HQQGSEPSYLDrteqlqavLCSTMEKSVLGGQDQLRVRVTelEDEVRNLRKINRDLFDFSTRFITRP 430
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 ...
 19-297 1.23e-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: 116.67  E-value: 1.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  19 SCIVWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAQLGKnYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLA 97
Cdd:cd00200  32 TIKVWDLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDK-TIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSS 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  98 -GVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadpsRIPAPRHVWSHHTLPIT 176
Cdd:cd00200 111 sSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL---------RTGKCVATLTGHTGEVN 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 177 dlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWpgqrersf 255
Cdd:cd00200 182 --SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-------- 251

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 38014171 256 hpeqDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 297
Cdd:cd00200 252 ----ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 81-306 2.71e-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: 110.12  E-value: 2.71e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  81 GPVTCLTASPNGLYVL-AGVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadps 159
Cdd:cd00200  52 GPVRDVAASADGTYLAsGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV--------- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 160 RIPAPRHVWSHHTLPITdlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGS 238
Cdd:cd00200 123 ETGKCLTTLRGHTDWVN--SVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSDGT 200

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 38014171 239 IFQVDLftwpgqrersfhPEQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT 306
Cdd:cd00200 201 IKLWDL------------STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 80-306 6.10e-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: 106.27  E-value: 6.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  80 PGPVTCLTASPNGLYVLAGVA-ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadp 158
Cdd:cd00200   9 TGGVTCVAFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL-------- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 159 sRIPAPRHVWSHHTLPITDLHCGFGGPLarVATSSLDQTVKLWEVSSGELLLSVLF-DVSIMAVTMDLAEHHMFCGGSEG 237
Cdd:cd00200  81 -ETGECVRTLTGHTSYVSSVAFSPDGRI--LSSSSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDG 157

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 38014171 238 SIFQVDLftwpgqreRSFHPEQdagkVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT 306
Cdd:cd00200 158 TIKLWDL--------RTGKCVA----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
22-306 2.71e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.92  E-value: 2.71e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  22 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAE 101
Cdd:COG2319  20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASAD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 102 -SIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 180
Cdd:COG2319 100 gTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT---------GKLLRTLTGHSGAVTSVAF 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 181 GFGGplARVATSSLDQTVKLWEVSSGELLlsvlfdvsimavtmdlaehhmfcggsegsifqvdlftwpgqrersfhpeqd 260
Cdd:COG2319 171 SPDG--KLLASGSDDGTVRLWDLATGKLL--------------------------------------------------- 197

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 38014171 261 agKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT 306
Cdd:COG2319 198 --RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241
WD40_alt pfam14077
Alternative WD40 repeat motif; WD repeats are short subdomains of about 40 amino acids and ...
 383-430 1.44e-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: 1.44e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 38014171   383 LCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLFDFSTRFITRP 430
Cdd:pfam14077   1 MCSTTDKNVLGDQEQLKVRVSELEEEVRTLRKINKDLFDFSTRIITKP 48
WD40 COG2319
WD40 repeat [General function prediction only];
52-318 1.91e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 80.73  E-value: 1.91e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171  52 LLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAE-SIHLWEVSTGNLLVILSRHYQDVSCLQFT 130
Cdd:COG2319   8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDlTLLLLDAAAGALLATLLGHTAAVLSVAFS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 131 GDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHCGFGGplARVATSSLDQTVKLWEVSSGELLl 210
Cdd:COG2319  88 PDGRLLASASADGTVRLWDLAT---------GLLLRTLTGHTGAVRSVAFSPDG--KTLASGSADGTVRLWDLATGKLL- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 211 svlfdvsimavtmdlaehhmfcggsegsifqvdlftwpgqrersfhpeqdagKVFKGHRNQVTCLSVSTDGSVLLSGSHD 290
Cdd:COG2319 156 ----------------------------------------------------RTLTGHSGAVTSVAFSPDGKLLASGSDD 183

                       250       260
                ....*....|....*....|....*....
gi 38014171 291 ETVRLWDVQSKQCIRTV-ALKGPVTNAAI 318
Cdd:COG2319 184 GTVRLWDLATGKLLRTLtGHTGAVRSVAF 212
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 263-311 3.99e-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: 3.99e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 38014171 263 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTvaLKG 311
Cdd:cd00200   3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT--LKG 49
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 263-297 8.40e-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: 8.40e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 38014171    263 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 297
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
263-297 1.45e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.42  E-value: 1.45e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 38014171   263 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 297
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 164-308 1.41e-06

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: 49.64  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 164 PRHVWSHHTLPITDLHcgFGGPLARVATSSLDQTVKLWEVSSGELLLSvlfdvsimavtmdlaehhmfcggsegsifqvd 243
Cdd:cd00200   1 LRRTLKGHTGGVTCVA--FSPDGKLLATGSGDGTIKVWDLETGELLRT-------------------------------- 46

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 38014171 244 lftwpgqrersfhpeqdagkvFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTVA 308
Cdd:cd00200  47 ---------------------LKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 123-310 4.24e-06

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: 48.38  E-value: 4.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 123 DVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlQADPSRI---PAPRH--------VWshhtlpITDLhcGFGGP--LARV 189
Cdd:cd22857 128 NLLCMRVDPNENYFAFGGKEVELNVWDL----EEKPGKIwraKNVPNdslglrvpVW------VTDL--TFLSKddHRKI 195

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171 190 ATSSLDQTVKLWEVSSGEL-LLSVLF-DVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTwpGQRERSFhpeqdagKVFKG 267
Cdd:cd22857 196 VTGTGYHQVRLYDTRAQRRpVVSVDFgETPIKAVAEDPDGHTVYVGDTSGDLASIDLRT--GKLLGCF-------KGKCG 266

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 38014171 268 HrnQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTVALK 310
Cdd:cd22857 267 G--SIRSIARHPELPLIASCGLDRYLRIWDTETRQLLSKVYLK 307
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 268-298 4.60e-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: 4.60e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 38014171   268 HRNQVTCLSVSTDGSVLLSGSHDETVRLWDV 298
Cdd:pfam20426 123 HKDVVSCVAVTSDGSILATGSYDTTVMVWEV 153
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 110-149 1.98e-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: 41.53  E-value: 1.98e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 38014171    110 TGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWS 149
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
111-149 2.69e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.10  E-value: 2.69e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 38014171   111 GNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWS 149
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 203-306 2.31e-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: 40.14  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38014171   203 VSSGELLLSvLFDVSIMAVTMDLAEHHMfcggsEGSIFQVDLFTWPgqrERSFHPEQDAGKVFKGHRNQVTCLSVST--- 279
Cdd:pfam11715 159 VSPLELLVS-LADGGLLKLTRSSDGGAW-----KESTFEPASWLQS---LSGLLGWLADPTIRYSGSSVALSLSAAPavt 229

                          90       100       110
                  ....*....|....*....|....*....|
gi 38014171   280 ---DGSVLLSGSHDETVRLWDVQSKQCIRT 306
Cdd:pfam11715 230 tvgGQNFLFTLSLDHTLRVWDLLTGKCLAT 259
 
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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