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Conserved domains on  [gi|119589984|gb|EAW69578|]
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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];
34-330 4.35e-33

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.88  E-value: 4.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  34 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA- 112
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAd 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 113 ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 192
Cdd:COG2319  142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGHTGAVRSVAF 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 193 GFGGplARVATSSLDQTVKLWEVSSGELLLSV-LFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDL------FTWPGQRER 265
Cdd:COG2319  213 SPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLatgellRTLTGHSGG 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 266 ----SFHP--------------------EQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT-VA 320
Cdd:COG2319  291 vnsvAFSPdgkllasgsddgtvrlwdlaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTlTG 370

                        330
                 ....*....|
gi 119589984 321 LKGPVTNAAI 330
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 ...
 224-442 5.64e-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: 122.54  E-value: 5.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 224 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 302
Cdd:cd06377    1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 303 ETVRLwdvqSKQCIRTVALKGPVTNAAILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 375
Cdd:cd06377   81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119589984 376 HQQGSEPSYLDrteqlqavLCSTMEKSVLGGQDQLRVRVTelEDEVRNLRKINRDLFDFSTRFITRP 442
Cdd:cd06377  151 CQPWDPTSFLL--------LWQNNSQFHLGTVLNLSVLDE--SDLQRSLQQHLESLKDPSPAIVMFG 207
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
34-330 4.35e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.88  E-value: 4.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  34 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA- 112
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAd 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 113 ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 192
Cdd:COG2319  142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGHTGAVRSVAF 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 193 GFGGplARVATSSLDQTVKLWEVSSGELLLSV-LFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDL------FTWPGQRER 265
Cdd:COG2319  213 SPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLatgellRTLTGHSGG 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 266 ----SFHP--------------------EQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT-VA 320
Cdd:COG2319  291 vnsvAFSPdgkllasgsddgtvrlwdlaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTlTG 370

                        330
                 ....*....|
gi 119589984 321 LKGPVTNAAI 330
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 ...
 224-442 5.64e-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: 122.54  E-value: 5.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 224 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 302
Cdd:cd06377    1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 303 ETVRLwdvqSKQCIRTVALKGPVTNAAILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 375
Cdd:cd06377   81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119589984 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 1.04e-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: 117.05  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  31 SCIVWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAQLGKnYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLA 109
Cdd:cd00200   32 TIKVWDLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDK-TIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 110 -GVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadpsRIPAPRHVWSHHTLPIT 188
Cdd:cd00200  111 sSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL---------RTGKCVATLTGHTGEVN 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 189 dlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWpgqrersf 267
Cdd:cd00200  182 --SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-------- 251

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 119589984 268 hpeqDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:cd00200  252 ----ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 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 119589984  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 7.60e-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: 7.60e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 119589984   275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
275-309 1.33e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.42  E-value: 1.33e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 119589984  275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
WD40 COG2319
WD40 repeat [General function prediction only];
34-330 4.35e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 128.88  E-value: 4.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  34 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA- 112
Cdd:COG2319   62 LLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSAd 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 113 ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 192
Cdd:COG2319  142 GTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT---------GKLLRTLTGHTGAVRSVAF 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 193 GFGGplARVATSSLDQTVKLWEVSSGELLLSV-LFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDL------FTWPGQRER 265
Cdd:COG2319  213 SPDG--KLLASGSADGTVRLWDLATGKLLRTLtGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLatgellRTLTGHSGG 290

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 266 ----SFHP--------------------EQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT-VA 320
Cdd:COG2319  291 vnsvAFSPdgkllasgsddgtvrlwdlaTGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTlTG 370

                        330
                 ....*....|
gi 119589984 321 LKGPVTNAAI 330
Cdd:COG2319  371 HTGAVTSVAF 380
WD40 COG2319
WD40 repeat [General function prediction only];
34-312 6.48e-32

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.79  E-value: 6.48e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  34 VWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAQLGKNyISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVA 112
Cdd:COG2319  146 LWDLATGKLLRTLTGHSGAVTSVAFSpDGKLLASGSDDGT-VRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSA 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 113 E-SIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadpsRIPAPRHVWSHHTLPITDLH 191
Cdd:COG2319  225 DgTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL---------ATGELLRTLTGHSGGVNSVA 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 192 CGFGGplARVATSSLDQTVKLWEVSSGELLLSVL-FDVSIMAVTMDLAEHHMFCGGSEGSifqVDLFTWPGQRERsfhpe 270
Cdd:COG2319  296 FSPDG--KLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKTLASGSDDGT---VRLWDLATGELL----- 365

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 119589984 271 qdagKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQS 312
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 ...
 224-442 5.64e-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: 122.54  E-value: 5.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 224 VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWPGQRERSFHPEQDA-GKVFKGHRNQVTCLSVSTDGSVLLSGSHD 302
Cdd:cd06377    1 VLKRIGHTVRLGALLPHPWFTRGRAGAALAVDLPTGLLPYNLSLEVVVAApWARDPASLTRSLCHSVVVQGVAALLAFPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 303 ETVRLwdvqSKQCIRTVALKGPVTNAAILLAPVSmlssdfRPSLPLPHFNKHLLGAEHGDEP-------RHGGLTLRLGL 375
Cdd:cd06377   81 SRGEL----LQLDFLSAALEIPVVSILRREFPRP------LRSQNPFHLQLDLQSSLESLEDvlvsllqANSWEDVSLLL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119589984 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 1.04e-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: 117.05  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  31 SCIVWELHSGANLLTYRGGQAGPRGLALL-NGEYLLAAQLGKnYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLA 109
Cdd:cd00200   32 TIKVWDLETGELLRTLKGHTGPVRDVAASaDGTYLASGSSDK-TIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 110 -GVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadpsRIPAPRHVWSHHTLPIT 188
Cdd:cd00200  111 sSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDL---------RTGKCVATLTGHTGEVN 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 189 dlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTWpgqrersf 267
Cdd:cd00200  182 --SVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTlRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG-------- 251

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 119589984 268 hpeqDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:cd00200  252 ----ECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 93-318 2.50e-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: 110.50  E-value: 2.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  93 GPVTCLTASPNGLYVL-AGVAESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadps 171
Cdd:cd00200   52 GPVRDVAASADGTYLAsGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDV--------- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 172 RIPAPRHVWSHHTLPITdlHCGFGGPLARVATSSLDQTVKLWEVSSGELLLS-VLFDVSIMAVTMDLAEHHMFCGGSEGS 250
Cdd:cd00200  123 ETGKCLTTLRGHTDWVN--SVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSSSDGT 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119589984 251 IFQVDLftwpgqrersfhPEQDAGKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT 318
Cdd:cd00200  201 IKLWDL------------STGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQT 256
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 92-318 5.24e-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: 106.65  E-value: 5.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  92 PGPVTCLTASPNGLYVLAGVA-ESIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlqadp 170
Cdd:cd00200    9 TGGVTCVAFSPDGKLLATGSGdGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDL-------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 171 sRIPAPRHVWSHHTLPITDLHCGFGGPLarVATSSLDQTVKLWEVSSGELLLSVLF-DVSIMAVTMDLAEHHMFCGGSEG 249
Cdd:cd00200   81 -ETGECVRTLTGHTSYVSSVAFSPDGRI--LSSSSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDGTFVASSSQDG 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119589984 250 SIFQVDLftwpgqreRSFHPEQdagkVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT 318
Cdd:cd00200  158 TIKLWDL--------RTGKCVA----TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGT 214
WD40 COG2319
WD40 repeat [General function prediction only];
34-318 2.25e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 107.30  E-value: 2.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  34 VWELHSGANLLTYRGGQAGPRGLALLNGEYLLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAE 113
Cdd:COG2319   20 LLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASAD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 114 -SIHLWEVSTGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHC 192
Cdd:COG2319  100 gTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT---------GKLLRTLTGHSGAVTSVAF 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 193 GFGGplARVATSSLDQTVKLWEVSSGELLlsvlfdvsimavtmdlaehhmfcggsegsifqvdlftwpgqrersfhpeqd 272
Cdd:COG2319  171 SPDG--KLLASGSDDGTVRLWDLATGKLL--------------------------------------------------- 197

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 119589984 273 agKVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRT 318
Cdd:COG2319  198 --RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRT 241
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 119589984  395 LCSTMEKSVLGGQDQLRVRVTELEDEVRNLRKINRDLFDFSTRFITRP 442
Cdd:pfam14077   1 MCSTTDKNVLGDQEQLKVRVSELEEEVRTLRKINKDLFDFSTRIITKP 48
WD40 COG2319
WD40 repeat [General function prediction only];
64-330 1.60e-16

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 81.11  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  64 LLAAQLGKNYISAWELQRKDQLQQKIMCPGPVTCLTASPNGLYVLAGVAE-SIHLWEVSTGNLLVILSRHYQDVSCLQFT 142
Cdd:COG2319    8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDlTLLLLDAAAGALLATLLGHTAAVLSVAFS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 143 GDSSHFISGGKDCLVLVWSLCSvlqadpsriPAPRHVWSHHTLPITDLHCGFGGplARVATSSLDQTVKLWEVSSGELLl 222
Cdd:COG2319   88 PDGRLLASASADGTVRLWDLAT---------GLLLRTLTGHTGAVRSVAFSPDG--KTLASGSADGTVRLWDLATGKLL- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 223 svlfdvsimavtmdlaehhmfcggsegsifqvdlftwpgqrersfhpeqdagKVFKGHRNQVTCLSVSTDGSVLLSGSHD 302
Cdd:COG2319  156 ----------------------------------------------------RTLTGHSGAVTSVAFSPDGKLLASGSDD 183

                        250       260
                 ....*....|....*....|....*....
gi 119589984 303 ETVRLWDVQSKQCIRTV-ALKGPVTNAAI 330
Cdd:COG2319  184 GTVRLWDLATGKLLRTLtGHTGAVRSVAF 212
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 275-323 3.78e-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: 57.73  E-value: 3.78e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 119589984 275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTvaLKG 323
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT--LKG 49
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 275-309 7.60e-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: 7.60e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 119589984   275 KVFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWD 309
Cdd:smart00320   6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
275-309 1.33e-08

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 50.42  E-value: 1.33e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 119589984  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 1.27e-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: 50.03  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 176 PRHVWSHHTLPITDLHcgFGGPLARVATSSLDQTVKLWEVSSGELLLSvlfdvsimavtmdlaehhmfcggsegsifqvd 255
Cdd:cd00200    1 LRRTLKGHTGGVTCVA--FSPDGKLLATGSGDGTIKVWDLETGELLRT-------------------------------- 46

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119589984 256 lftwpgqrersfhpeqdagkvFKGHRNQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTVA 320
Cdd:cd00200   47 ---------------------LKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90
WDR74 cd22857
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ...
 135-322 4.35e-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: 4.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 135 DVSCLQFTGDSSHFISGGKDCLVLVWSLcsvlQADPSRI---PAPRH--------VWshhtlpITDLhcGFGGP--LARV 201
Cdd:cd22857  128 NLLCMRVDPNENYFAFGGKEVELNVWDL----EEKPGKIwraKNVPNdslglrvpVW------VTDL--TFLSKddHRKI 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984 202 ATSSLDQTVKLWEVSSGEL-LLSVLF-DVSIMAVTMDLAEHHMFCGGSEGSIFQVDLFTwpGQRERSFhpeqdagKVFKG 279
Cdd:cd22857  196 VTGTGYHQVRLYDTRAQRRpVVSVDFgETPIKAVAEDPDGHTVYVGDTSGDLASIDLRT--GKLLGCF-------KGKCG 266

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 119589984 280 HrnQVTCLSVSTDGSVLLSGSHDETVRLWDVQSKQCIRTVALK 322
Cdd:cd22857  267 G--SIRSIARHPELPLIASCGLDRYLRIWDTETRQLLSKVYLK 307
NBCH_WD40 pfam20426
Neurobeachin beta propeller domain; This entry represents the beta propeller domain found at ...
 280-310 4.68e-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: 4.68e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 119589984  280 HRNQVTCLSVSTDGSVLLSGSHDETVRLWDV 310
Cdd:pfam20426 123 HKDVVSCVAVTSDGSILATGSYDTTVMVWEV 153
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 122-161 1.86e-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: 1.86e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 119589984   122 TGNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWS 161
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
123-161 2.60e-04

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 38.48  E-value: 2.60e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 119589984  123 GNLLVILSRHYQDVSCLQFTGDSSHFISGGKDCLVLVWS 161
Cdd:pfam00400   1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
Nup160 pfam11715
Nucleoporin Nup120/160; Nup120 is conserved from fungi to plants to humans, and is homologous ...
 215-318 1.67e-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: 40.52  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119589984  215 VSSGELLLSvLFDVSIMAVTMDLAEHHMfcggsEGSIFQVDLFTWPgqrERSFHPEQDAGKVFKGHRNQVTCLSVST--- 291
Cdd:pfam11715 159 VSPLELLVS-LADGGLLKLTRSSDGGAW-----KESTFEPASWLQS---LSGLLGWLADPTIRYSGSSVALSLSAAPavt 229

                          90       100       110
                  ....*....|....*....|....*....|
gi 119589984  292 ---DGSVLLSGSHDETVRLWDVQSKQCIRT 318
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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