|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
720-1140 |
5.26e-35 |
|
WD40 repeat [General function prediction only]; :
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 139.28 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 720 QRFYLGHDDDILCLAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIV 799
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 800 LWDWKKGEKLSVARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRRAGGGLIgrkgyvgtlgkndtmmcavygwtee 876
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSP---DgkLLASGSDdGTVRLWDLATGKLL------------------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 877 mafsgtstgdvciwrdvflvKTVKAHDGPVFSMHALEKG--FVTGGKDGVVALWDdsferclktyaikradlapgskgll 954
Cdd:COG2319 198 --------------------RTLTGHTGAVRSVAFSPDGklLASGSADGTVRLWD------------------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 955 lednpsiraislghghilvgTKNGEILEVdksgpvtllVQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCML 1034
Cdd:COG2319 233 --------------------LATGKLLRT---------LTGH-SGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1035 AVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDVISDIQFSPgSGKYLAVASHDSFVDIYNVTS 1114
Cdd:COG2319 283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKTLASGSDDGTVRLWDLAT 361
|
410 420
....*....|....*....|....*.
gi 41387501 1115 SKRVGVCKGATSYITHIDWDSRGKLL 1140
Cdd:COG2319 362 GELLRTLTGHTGAVTSVAFSPDGRTL 387
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
1.66e-32 |
|
WD40 repeat [General function prediction only]; :
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 131.96 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 58 RGHSDDIISLALHPERVLVATGQVGKEpyICVWDSYTVQTVSVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 218 GDIYVW--KGINLIRTIQGaHTAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETeqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 293 --GDHILVGTQDSEI--FEIvvhERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MDE 367
Cdd:COG2319 256 pdGRLLASGSADGTVrlWDL---ATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTG 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41387501 368 PIRCAAVNADGVHLALGMKDGSLTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 332 AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
5.73e-19 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons. :
Pssm-ID: 460922 Cd Length: 72 Bit Score: 82.60 E-value: 5.73e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 41387501 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
4.69e-17 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons. :
Pssm-ID: 460922 Cd Length: 72 Bit Score: 76.82 E-value: 4.69e-17
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 41387501 672 APGNSIRLHFIHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNR 715
Cdd:pfam03451 29 PPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
321-592 |
4.84e-17 |
|
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. The actual alignment was detected with superfamily member cd00200:
Pssm-ID: 475233 [Multi-domain] Cd Length: 289 Bit Score: 83.54 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 321 QGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIAR-CNMDEPIRCAAVNADGVHLALGMKDGSLTVLRVRDMT 399
Cdd:cd00200 6 KGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 400 EVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQrYKKVGECVGSLSFITHLDWSSDSKYLQT--NDGSGKrlL 477
Cdd:cd00200 85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGHTDWVNSVAFSPDGTFVASssQDGTIK--L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 478 YKMPGGKEVTS----KEEVKGMHW---------------------ASWTCVAGLEVNGIWpkysdindINSVDGNYVGQV 532
Cdd:cd00200 162 WDLRTGKCVATltghTGEVNSVAFspdgekllssssdgtiklwdlSTGKCLGTLRGHENG--------VNSVAFSPDGYL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 533 LVTADDYGVVKLFRypcLRKGAKFRKYIGHSAHVTNVRWSHDYQWVISiGGADHSVFQWK 592
Cdd:cd00200 234 LASGSEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIWD 289
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1363-1410 |
2.31e-14 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons. :
Pssm-ID: 460922 Cd Length: 72 Bit Score: 69.50 E-value: 2.31e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 41387501 1363 KKKRPIEDLVLELAFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1410
Cdd:pfam03451 26 KKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1407-1556 |
3.87e-13 |
|
WD40 repeat [General function prediction only]; :
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 73.41 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1407 LHNVATGTQSF-YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSVHIWDAVNKQTLSILRcSHSKGVCSVSF 1485
Cdd:COG2319 188 LWDLATGKLLRtLTGHTGAVRSVAFSPDGKLL---ASG----SAD-----GTVRLWDLATGKLLRTLT-GHSGSVRSVAF 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41387501 1486 SATGKLLLSVGLDpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTqFVSVGI-KHVKFWTLAGRALL 1556
Cdd:COG2319 255 SPDGRLLASGSAD--GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKL-LASGSDdGTVRLWDLATGKLL 323
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
720-1140 |
5.26e-35 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 139.28 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 720 QRFYLGHDDDILCLAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIV 799
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 800 LWDWKKGEKLSVARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRRAGGGLIgrkgyvgtlgkndtmmcavygwtee 876
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSP---DgkLLASGSDdGTVRLWDLATGKLL------------------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 877 mafsgtstgdvciwrdvflvKTVKAHDGPVFSMHALEKG--FVTGGKDGVVALWDdsferclktyaikradlapgskgll 954
Cdd:COG2319 198 --------------------RTLTGHTGAVRSVAFSPDGklLASGSADGTVRLWD------------------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 955 lednpsiraislghghilvgTKNGEILEVdksgpvtllVQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCML 1034
Cdd:COG2319 233 --------------------LATGKLLRT---------LTGH-SGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1035 AVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDVISDIQFSPgSGKYLAVASHDSFVDIYNVTS 1114
Cdd:COG2319 283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKTLASGSDDGTVRLWDLAT 361
|
410 420
....*....|....*....|....*.
gi 41387501 1115 SKRVGVCKGATSYITHIDWDSRGKLL 1140
Cdd:COG2319 362 GELLRTLTGHTGAVTSVAFSPDGRTL 387
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
725-1063 |
7.23e-34 |
|
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: 132.84 E-value: 7.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 725 GHDDDILCLAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIVLWDWK 804
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 805 KGEKLSVARGSKDKIFVVKMNPYvpDKLITAGIKH--MKFWRRAGGGLIGRkgyvgTLGKNDTMMCAVYGWTEEMAFSGT 882
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVETGKCLTT-----LRGHTDWVNSVAFSPDGTFVASSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 883 STGDVCIW--RDVFLVKTVKAHDGPVFSMHALEKG--FVTGGKDGVVALWDDSFERCLKTYaikradlapgskgllledn 958
Cdd:cd00200 155 QDGTIKLWdlRTGKCVATLTGHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGTL------------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 959 psiraislghghilvgtkngeilevdksgpvtllvQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRK 1038
Cdd:cd00200 216 -----------------------------------RGH-ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG 259
|
330 340
....*....|....*....|....*
gi 41387501 1039 LKKGGRCCCFSPDGKALAVGLNDGS 1063
Cdd:cd00200 260 HTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
1.66e-32 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 131.96 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 58 RGHSDDIISLALHPERVLVATGQVGKEpyICVWDSYTVQTVSVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 218 GDIYVW--KGINLIRTIQGaHTAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETeqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 293 --GDHILVGTQDSEI--FEIvvhERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MDE 367
Cdd:COG2319 256 pdGRLLASGSADGTVrlWDL---ATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTG 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41387501 368 PIRCAAVNADGVHLALGMKDGSLTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 332 AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
57-353 |
4.40e-30 |
|
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: 121.67 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 57 YRGHSDDIISLALHPERVLVATGQVGKEpyICVWDSYTVQTVSVLKdVHTHGIACLAFDLDGQRLVSVGLDskNAVCVWD 136
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGT--IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSD--KTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 137 WKRGKMLSMAPGHTDRIFDISWDlyqPNK--LVSCGV-KHIKFWSLcgNALTPKRGVFGKTGDlqtILCLACARDE-LTY 212
Cdd:cd00200 80 LETGECVRTLTGHTSYVSSVAFS---PDGriLSSSSRdKTIKVWDV--ETGKCLTTLRGHTDW---VNSVAFSPDGtFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 213 SGALNGDIYVW--KGINLIRTIQGaHTAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDlreteqgYKGLSVR 287
Cdd:cd00200 152 SSSQDGTIKLWdlRTGKCVATLTG-HTGEVNSVAFSPDGekLLSSSSDGTIKLWDLsTGKCLGTLR-------GHENGVN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 288 SVCW--RGDHILVGTQDS--EIFEIVVHERNKPFlimQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:cd00200 224 SVAFspDGYLLASGSEDGtiRVWDLRTGECVQTL---SGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
5.73e-19 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 82.60 E-value: 5.73e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 41387501 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
4.69e-17 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 76.82 E-value: 4.69e-17
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 41387501 672 APGNSIRLHFIHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNR 715
Cdd:pfam03451 29 PPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
321-592 |
4.84e-17 |
|
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: 83.54 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 321 QGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIAR-CNMDEPIRCAAVNADGVHLALGMKDGSLTVLRVRDMT 399
Cdd:cd00200 6 KGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 400 EVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQrYKKVGECVGSLSFITHLDWSSDSKYLQT--NDGSGKrlL 477
Cdd:cd00200 85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGHTDWVNSVAFSPDGTFVASssQDGTIK--L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 478 YKMPGGKEVTS----KEEVKGMHW---------------------ASWTCVAGLEVNGIWpkysdindINSVDGNYVGQV 532
Cdd:cd00200 162 WDLRTGKCVATltghTGEVNSVAFspdgekllssssdgtiklwdlSTGKCLGTLRGHENG--------VNSVAFSPDGYL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 533 LVTADDYGVVKLFRypcLRKGAKFRKYIGHSAHVTNVRWSHDYQWVISiGGADHSVFQWK 592
Cdd:cd00200 234 LASGSEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIWD 289
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1363-1410 |
2.31e-14 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 69.50 E-value: 2.31e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 41387501 1363 KKKRPIEDLVLELAFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1410
Cdd:pfam03451 26 KKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1407-1556 |
3.87e-13 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 73.41 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1407 LHNVATGTQSF-YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSVHIWDAVNKQTLSILRcSHSKGVCSVSF 1485
Cdd:COG2319 188 LWDLATGKLLRtLTGHTGAVRSVAFSPDGKLL---ASG----SAD-----GTVRLWDLATGKLLRTLT-GHSGSVRSVAF 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41387501 1486 SATGKLLLSVGLDpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTqFVSVGI-KHVKFWTLAGRALL 1556
Cdd:COG2319 255 SPDGRLLASGSAD--GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKL-LASGSDdGTVRLWDLATGKLL 323
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1406-1548 |
4.31e-10 |
|
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: 62.74 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1406 ILHNVATGTQSF-YQEHNDDILCLTVNQHPKFInivatgqVGDSADMSatapsVHIWDAVNKQTLSILRcSHSKGVCSVS 1484
Cdd:cd00200 118 KVWDVETGKCLTtLRGHTDWVNSVAFSPDGTFV-------ASSSQDGT-----IKLWDLRTGKCVATLT-GHTGEVNSVA 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41387501 1485 FSATGKLLLSVGLDpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTQFVSVGIKHVKFW 1548
Cdd:cd00200 185 FSPDGEKLLSSSSD--GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
760-802 |
3.64e-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: 39.60 E-value: 3.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 41387501 760 TIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIVLWD 802
Cdd:smart00320 1 SGELLKTLKG-HTGPVTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
314-353 |
1.12e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.10 E-value: 1.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 41387501 314 NKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:pfam00400 1 GKLLKTLEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
315-353 |
1.92e-03 |
|
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: 37.29 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*....
gi 41387501 315 KPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:smart00320 3 ELLKTLKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
720-757 |
5.92e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.17 E-value: 5.92e-03
10 20 30
....*....|....*....|....*....|....*...
gi 41387501 720 QRFYLGHDDDILCLAIHPLKDYVATGqvGRDPSIHVWD 757
Cdd:pfam00400 4 LKTLEGHTGSVTSLAFSPDGKLLASG--SDDGTVKVWD 39
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
1080-1140 |
6.48e-03 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 41.03 E-value: 6.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41387501 1080 HRKDViSDIQFSPGSGKYLAVASHDSFVDIYNVTSSKRVGVCKGATSYITHIDWDSRGKLL 1140
Cdd:PTZ00421 124 HTKKV-GIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLL 183
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
720-1140 |
5.26e-35 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 139.28 E-value: 5.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 720 QRFYLGHDDDILCLAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIV 799
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 800 LWDWKKGEKLSVARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRRAGGGLIgrkgyvgtlgkndtmmcavygwtee 876
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSP---DgkLLASGSDdGTVRLWDLATGKLL------------------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 877 mafsgtstgdvciwrdvflvKTVKAHDGPVFSMHALEKG--FVTGGKDGVVALWDdsferclktyaikradlapgskgll 954
Cdd:COG2319 198 --------------------RTLTGHTGAVRSVAFSPDGklLASGSADGTVRLWD------------------------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 955 lednpsiraislghghilvgTKNGEILEVdksgpvtllVQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCML 1034
Cdd:COG2319 233 --------------------LATGKLLRT---------LTGH-SGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1035 AVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDVISDIQFSPgSGKYLAVASHDSFVDIYNVTS 1114
Cdd:COG2319 283 TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKTLASGSDDGTVRLWDLAT 361
|
410 420
....*....|....*....|....*.
gi 41387501 1115 SKRVGVCKGATSYITHIDWDSRGKLL 1140
Cdd:COG2319 362 GELLRTLTGHTGAVTSVAFSPDGRTL 387
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
725-1063 |
7.23e-34 |
|
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: 132.84 E-value: 7.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 725 GHDDDILCLAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIVLWDWK 804
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 805 KGEKLSVARGSKDKIFVVKMNPYvpDKLITAGIKH--MKFWRRAGGGLIGRkgyvgTLGKNDTMMCAVYGWTEEMAFSGT 882
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVETGKCLTT-----LRGHTDWVNSVAFSPDGTFVASSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 883 STGDVCIW--RDVFLVKTVKAHDGPVFSMHALEKG--FVTGGKDGVVALWDDSFERCLKTYaikradlapgskgllledn 958
Cdd:cd00200 155 QDGTIKLWdlRTGKCVATLTGHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGTL------------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 959 psiraislghghilvgtkngeilevdksgpvtllvQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRK 1038
Cdd:cd00200 216 -----------------------------------RGH-ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG 259
|
330 340
....*....|....*....|....*
gi 41387501 1039 LKKGGRCCCFSPDGKALAVGLNDGS 1063
Cdd:cd00200 260 HTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
1.66e-32 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 131.96 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 58 RGHSDDIISLALHPERVLVATGQVGKEpyICVWDSYTVQTVSVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 218 GDIYVW--KGINLIRTIQGaHTAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETeqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 293 --GDHILVGTQDSEI--FEIvvhERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MDE 367
Cdd:COG2319 256 pdGRLLASGSADGTVrlWDL---ATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTG 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41387501 368 PIRCAAVNADGVHLALGMKDGSLTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 332 AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
719-1063 |
8.02e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.95 E-value: 8.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 719 TQRFYLGHDDDILCLAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTI 798
Cdd:COG2319 112 LLRTLTGHTGAVRSVAFSPDGKTLASG--SADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDD--GTV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 799 VLWDWKKGEKLSVARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRRAGGGLIGrkgyvgTLGKNDtmmcavyGWTE 875
Cdd:COG2319 187 RLWDLATGKLLRTLTGHTGAVRSVAFSP---DgkLLASGSAdGTVRLWDLATGKLLR------TLTGHS-------GSVR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 876 EMAFS--------GTSTGDVCIWrDV---FLVKTVKAHDGPVFSMHALEKG--FVTGGKDGVVALWDDSFERCLKTYaik 942
Cdd:COG2319 251 SVAFSpdgrllasGSADGTVRLW-DLatgELLRTLTGHSGGVNSVAFSPDGklLASGSDDGTVRLWDLATGKLLRTL--- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 943 radlapgskglllednpsiraislghghilvgtkngeilevdksgpvtllvQGHmEGEVWGLATHPYLPICATVSDDKTL 1022
Cdd:COG2319 327 ---------------------------------------------------TGH-TGAVRSVAFSPDGKTLASGSDDGTV 354
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 41387501 1023 RIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGS 1063
Cdd:COG2319 355 RLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
52-354 |
2.16e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 125.79 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 52 HRQKFYRGHSDDIISLALHPERVLVATGQVGKEpyICVWDSYTVQTVSVLKDvHTHGIACLAFDLDGQRLVSVGLDskNA 131
Cdd:COG2319 111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT--VRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDD--GT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 132 VCVWDWKRGKMLSMAPGHTDRIFDISWDlyqPN--KLVSCGV-KHIKFWSLcgnaltpKRGVFGKT--GDLQTILCLACA 206
Cdd:COG2319 186 VRLWDLATGKLLRTLTGHTGAVRSVAFS---PDgkLLASGSAdGTVRLWDL-------ATGKLLRTltGHSGSVRSVAFS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 207 RDELT-YSGALNGDIYVW--KGINLIRTIQGaHTAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIdlreteQG 280
Cdd:COG2319 256 PDGRLlASGSADGTVRLWdlATGELLRTLTG-HSGGVNSVAFSPDGklLASGSDDGTVRLWDLaTGKLLRTL------TG 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41387501 281 YKGlSVRSVCWR--GDHILVGTQDSEI--FEIvvhERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSL 354
Cdd:COG2319 329 HTG-AVRSVAFSpdGKTLASGSDDGTVrlWDL---ATGELLRTLTGH-TGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
57-353 |
4.40e-30 |
|
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: 121.67 E-value: 4.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 57 YRGHSDDIISLALHPERVLVATGQVGKEpyICVWDSYTVQTVSVLKdVHTHGIACLAFDLDGQRLVSVGLDskNAVCVWD 136
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGT--IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSD--KTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 137 WKRGKMLSMAPGHTDRIFDISWDlyqPNK--LVSCGV-KHIKFWSLcgNALTPKRGVFGKTGDlqtILCLACARDE-LTY 212
Cdd:cd00200 80 LETGECVRTLTGHTSYVSSVAFS---PDGriLSSSSRdKTIKVWDV--ETGKCLTTLRGHTDW---VNSVAFSPDGtFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 213 SGALNGDIYVW--KGINLIRTIQGaHTAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDlreteqgYKGLSVR 287
Cdd:cd00200 152 SSSQDGTIKLWdlRTGKCVATLTG-HTGEVNSVAFSPDGekLLSSSSDGTIKLWDLsTGKCLGTLR-------GHENGVN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 288 SVCW--RGDHILVGTQDS--EIFEIVVHERNKPFlimQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:cd00200 224 SVAFspDGYLLASGSEDGtiRVWDLRTGECVQTL---SGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
260-802 |
3.87e-29 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 121.94 E-value: 3.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 260 RLWDLTFKPITVIDLRETEQGYKGLSVRSVCWRGDHILVGTQDSEIFEIVVHERNKPFLIMQGHcEGELWALAVHPTKPL 339
Cdd:COG2319 14 ADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH-TAAVLSVAFSPDGRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 340 AVTGSDDRSVRIWSLVDHALIARCNM-DEPIRCAAVNADGVHLALGMKDGSLTVLRVRDMTEVVHIKDRKEAIHELKYSP 418
Cdd:COG2319 93 LASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 419 DGTYLAVGCNDSSVDIYGVAQrykkvGECVGSL----SFITHLDWSSDSKYLQT--NDGSGKrlLYKMPGGKEVTSKEEv 492
Cdd:COG2319 173 DGKLLASGSDDGTVRLWDLAT-----GKLLRTLtghtGAVRSVAFSPDGKLLASgsADGTVR--LWDLATGKLLRTLTG- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 493 kgmHWASWTCVAglevngiWpkysdindinSVDGnyvgQVLVTADDYGVVKLFRypcLRKGAKFRKYIGHSAHVTNVRWS 572
Cdd:COG2319 245 ---HSGSVRSVA-------F----------SPDG----RLLASGSADGTVRLWD---LATGELLRTLTGHSGGVNSVAFS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 573 HDYQWVISiGGADHSVFQWkfiperklkdalhiapqesltesnsdesdsdlsdvpeldseieqetqltyhrqvykedlpq 652
Cdd:COG2319 298 PDGKLLAS-GSDDGTVRLW------------------------------------------------------------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 653 lkeqckekqksatskrrERAPGNSIRLHfihgyrgydcrsnlfytqigeivyhvaavgviynrqqntqrfyLGHDDDILC 732
Cdd:COG2319 316 -----------------DLATGKLLRTL-------------------------------------------TGHTGAVRS 335
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 733 LAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIVLWD 802
Cdd:COG2319 336 VAFSPDGKTLASG--SDDGTVRLWDLATGELLRTLTG-HTGAVTSVAFSPDGRTLASGSAD--GTVRLWD 400
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
251-591 |
5.13e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.48 E-value: 5.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 251 ATGGRDGCIRLWDLTFKPITVIDLRETEqgykglSVRSVCWR--GDHILVGTQDSEI--FEIvvhERNKPFLIMQGHcEG 326
Cdd:COG2319 94 ASASADGTVRLWDLATGLLLRTLTGHTG------AVRSVAFSpdGKTLASGSADGTVrlWDL---ATGKLLRTLTGH-SG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 327 ELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MDEPIRCAAVNADGVHLALGMKDGSLTVLRVRDMTEVVHIK 405
Cdd:COG2319 164 AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 406 DRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQrykkvGECVGSL----SFITHLDWSSDSKYLQTNDGSGKRLLYKMP 481
Cdd:COG2319 244 GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-----GELLRTLtghsGGVNSVAFSPDGKLLASGSDDGTVRLWDLA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 482 GGKEVTSkeeVKGmHWASWTCVAglevngiwpkYSDindinsvdgnyVGQVLVTADDYGVVKLFRypcLRKGAKFRKYIG 561
Cdd:COG2319 319 TGKLLRT---LTG-HTGAVRSVA----------FSP-----------DGKTLASGSDDGTVRLWD---LATGELLRTLTG 370
|
330 340 350
....*....|....*....|....*....|
gi 41387501 562 HSAHVTNVRWSHDYQWVISiGGADHSVFQW 591
Cdd:COG2319 371 HTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
318-847 |
3.74e-27 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 116.16 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 318 LIMQGHCEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MDEPIRCAAVNADGVHLALGMKDGSLTVLRVR 396
Cdd:COG2319 29 LLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLgHTAAVLSVAFSPDGRLLASASADGTVRLWDLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 397 DMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQrykkvGECVGSLS----FITHLDWSSDSKYLQTNDGS 472
Cdd:COG2319 109 TGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-----GKLLRTLTghsgAVTSVAFSPDGKLLASGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 473 GKRLLYKMPGGKEVTSkeeVKGmHWASWTCVAglevngiWpkysdindinSVDgnyvGQVLVTADDYGVVKLFRypcLRK 552
Cdd:COG2319 184 GTVRLWDLATGKLLRT---LTG-HTGAVRSVA-------F----------SPD----GKLLASGSADGTVRLWD---LAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 553 GAKFRKYIGHSAHVTNVRWSHDYQWVISiGGADHSVFQWKfiperklkdalhiapqesltesnsdesdsdlsdvpeldse 632
Cdd:COG2319 236 GKLLRTLTGHSGSVRSVAFSPDGRLLAS-GSADGTVRLWD---------------------------------------- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 633 ieqetqltyhrqvykedlpqlkeqckekqksatskrrerapgnsirlhfihgyrgydcrsnlfyTQIGEIVyhvaavgvi 712
Cdd:COG2319 275 ----------------------------------------------------------------LATGELL--------- 281
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 713 ynrqqntqRFYLGHDDDILCLAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASVGI 792
Cdd:COG2319 282 --------RTLTGHSGGVNSVAFSPDGKLLASG--SDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKTLASGSD 350
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 41387501 793 DdsHTIVLWDWKKGEKLSVARGSKDKIFVVKmnpYVPD--KLITAGI-KHMKFWRRAG 847
Cdd:COG2319 351 D--GTVRLWDLATGELLRTLTGHTGAVTSVA---FSPDgrTLASGSAdGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
895-1266 |
3.40e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 107.30 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 895 LVKTVKAHDGPVFSMHALEKG--FVTGGKDGVVALWDdsferclktyaikradLAPGSKGLLLEDNPS-IRAISLGH-GH 970
Cdd:COG2319 70 LLATLLGHTAAVLSVAFSPDGrlLASASADGTVRLWD----------------LATGLLLRTLTGHTGaVRSVAFSPdGK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 971 ILV-GTKNGEILEVD-KSGPVTLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRC 1045
Cdd:COG2319 134 TLAsGSADGTVRLWDlATGKLLRTLTGH-SGAVTSVAFSPdgkLL---ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1046 CCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDVISDIQFSPgSGKYLAVASHDSFVDIYNVTSSKRVGVCKGAT 1125
Cdd:COG2319 210 VAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGELLRTLTGHS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1126 SYITHIDWDSRGKLLqvntgakeqlffeAPRGKKQTIpsveveKIsWATWTSVLglccegIWPIIGEVTDVTASCLTSDK 1205
Cdd:COG2319 289 GGVNSVAFSPDGKLL-------------ASGSDDGTV------RL-WDLATGKL------LRTLTGHTGAVRSVAFSPDG 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41387501 1206 MVLATGDDLGFVKLFRypaKGKFGKFKKYVAHSTHVTNVRWTYDDSMLVTlGGADMSLMVW 1266
Cdd:COG2319 343 KTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
712-929 |
2.79e-21 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 95.86 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 712 IYNRQQNTQRFYL-GHDDDILCLAIHPLKDYVATGqvGRDPSIHVWDTETIKPLSILKGyHQYGICAVDFSADGKRLASV 790
Cdd:cd00200 77 LWDLETGECVRTLtGHTSYVSSVAFSPDGRILSSS--SRDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 791 GIDdsHTIVLWDWKKGEKLSVARGSKDKIFVVKmnpYVPD--KLITAGI-KHMKFWRRAGGGLIgrkgyvGTL-GKNDTM 866
Cdd:cd00200 154 SQD--GTIKLWDLRTGKCVATLTGHTGEVNSVA---FSPDgeKLLSSSSdGTIKLWDLSTGKCL------GTLrGHENGV 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41387501 867 MCAVYGWTEEMAFSGTSTGDVCIWRDVF--LVKTVKAHDGPVFSM--HALEKGFVTGGKDGVVALWD 929
Cdd:cd00200 223 NSVAFSPDGYLLASGSEDGTIRVWDLRTgeCVQTLSGHTNSVTSLawSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
895-1140 |
2.98e-21 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 95.86 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 895 LVKTVKAHDGPVFSMHALEKG--FVTGGKDGVVALWD---DSFERCLKTYAIKRADLAPGSKGLLLednpsiraislghg 969
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGklLATGSGDGTIKVWDletGELLRTLKGHTGPVRDVAASADGTYL-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 970 hiLVGTKNGEILEVD-KSGPVTLLVQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCF 1048
Cdd:cd00200 67 --ASGSSDKTIRLWDlETGECVRTLTGH-TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1049 SPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDVISDIQFSPgSGKYLAVASHDSFVDIYNVTSSKRVGVCKGATSYI 1128
Cdd:cd00200 144 SPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222
|
250
....*....|..
gi 41387501 1129 THIDWDSRGKLL 1140
Cdd:cd00200 223 NSVAFSPDGYLL 234
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
5.73e-19 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 82.60 E-value: 5.73e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 41387501 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
943-1552 |
7.38e-18 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 88.04 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 943 RADLAPGSKGLLLEDNPSIRAISLGHGHILVGTKNGEILEVDKSGPVTLLVQGHmEGEVWGLATHPYLPICATVSDDKTL 1022
Cdd:COG2319 24 ALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH-TAAVLSVAFSPDGRLLASASADGTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1023 RIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDVISDIQFSPgSGKYLAVAS 1102
Cdd:COG2319 103 RLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1103 HDSFVDIYNVTSSKRVGVCKGATSYITHIDWDSRGKLLqvntgakeqlffeaprgkkqtipsvevekiswatwtsvlglc 1182
Cdd:COG2319 182 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLL------------------------------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1183 cegiwpiigevtdVTAScltSDKMV----LATGDDLGFVKlfrypakgkfgkfkkyvAHSTHVTNVRWTYDDSMLVTlGG 1258
Cdd:COG2319 220 -------------ASGS---ADGTVrlwdLATGKLLRTLT-----------------GHSGSVRSVAFSPDGRLLAS-GS 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1259 ADMSLMVWtseverhrekkncdseesDTDSeedggydsdvtreneisytiralstnirpmfgvkphlqqkepsvDERQGV 1338
Cdd:COG2319 266 ADGTVRLW------------------DLAT--------------------------------------------GELLRT 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1339 VRGSRPPVsrappqpeklqsnnvgkkkrpiedlvlelafgyrgrdcrNNVHYLNDGddiiyhtasvgilhnvatgtqsfy 1418
Cdd:COG2319 284 LTGHSGGV---------------------------------------NSVAFSPDG------------------------ 300
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1419 qehnddilcltvnqhpkfiNIVATGqvgdSADmsataPSVHIWDAVNKQTLSILRcSHSKGVCSVSFSATGKLLLSVGLD 1498
Cdd:COG2319 301 -------------------KLLASG----SDD-----GTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDD 351
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 41387501 1499 peHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTqFVSVGI-KHVKFWTLAG 1552
Cdd:COG2319 352 --GTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRT-LASGSAdGTVRLWDLAT 403
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
4.69e-17 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 76.82 E-value: 4.69e-17
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 41387501 672 APGNSIRLHFIHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNR 715
Cdd:pfam03451 29 PPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
321-592 |
4.84e-17 |
|
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: 83.54 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 321 QGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIAR-CNMDEPIRCAAVNADGVHLALGMKDGSLTVLRVRDMT 399
Cdd:cd00200 6 KGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 400 EVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQrYKKVGECVGSLSFITHLDWSSDSKYLQT--NDGSGKrlL 477
Cdd:cd00200 85 CVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVET-GKCLTTLRGHTDWVNSVAFSPDGTFVASssQDGTIK--L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 478 YKMPGGKEVTS----KEEVKGMHW---------------------ASWTCVAGLEVNGIWpkysdindINSVDGNYVGQV 532
Cdd:cd00200 162 WDLRTGKCVATltghTGEVNSVAFspdgekllssssdgtiklwdlSTGKCLGTLRGHENG--------VNSVAFSPDGYL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 533 LVTADDYGVVKLFRypcLRKGAKFRKYIGHSAHVTNVRWSHDYQWVISiGGADHSVFQWK 592
Cdd:cd00200 234 LASGSEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIWD 289
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1363-1410 |
2.31e-14 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 69.50 E-value: 2.31e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 41387501 1363 KKKRPIEDLVLELAFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1410
Cdd:pfam03451 26 KKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1407-1556 |
3.87e-13 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 73.41 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1407 LHNVATGTQSF-YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSVHIWDAVNKQTLSILRcSHSKGVCSVSF 1485
Cdd:COG2319 188 LWDLATGKLLRtLTGHTGAVRSVAFSPDGKLL---ASG----SAD-----GTVRLWDLATGKLLRTLT-GHSGSVRSVAF 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41387501 1486 SATGKLLLSVGLDpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTqFVSVGI-KHVKFWTLAGRALL 1556
Cdd:COG2319 255 SPDGRLLASGSAD--GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKL-LASGSDdGTVRLWDLATGKLL 323
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
46-178 |
3.87e-12 |
|
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: 68.90 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 46 VYSPREHR-QKFYRGHSDDIISLALHPERVLVATGQVGKEpyICVWDSYTVQTVSVLKdVHTHGIACLAFDLDGQRLVSV 124
Cdd:cd00200 161 LWDLRTGKcVATLTGHTGEVNSVAFSPDGEKLLSSSSDGT--IKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASG 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 41387501 125 GLDSKnaVCVWDWKRGKMLSMAPGHTDRIFDISWDlYQPNKLVSCGV-KHIKFWS 178
Cdd:cd00200 238 SEDGT--IRVWDLRTGECVQTLSGHTNSVTSLAWS-PDGKRLASGSAdGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1457-1556 |
4.06e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.94 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1457 SVHIWDAVNKQTLSILRcSHSKGVCSVSFSATGKLLLSVGLDpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTq 1536
Cdd:COG2319 143 TVRLWDLATGKLLRTLT-GHSGAVTSVAFSPDGKLLASGSDD--GTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKL- 218
|
90 100
....*....|....*....|.
gi 41387501 1537 FVSVGI-KHVKFWTLAGRALL 1556
Cdd:COG2319 219 LASGSAdGTVRLWDLATGKLL 239
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1428-1556 |
8.53e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.17 E-value: 8.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1428 LTVNQHPKFINIVATGQVGDSADMSATAPSVHIWDAVNKQTLSILRcSHSKGVCSVSFSATGKLLLSVGLDpeHTVTIWR 1507
Cdd:COG2319 72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 41387501 1508 WQEGAKIASRGGHNQRIFVAEFRPDSdTQFVSVGI-KHVKFWTLAGRALL 1556
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSPDG-KLLASGSDdGTVRLWDLATGKLL 197
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1406-1548 |
4.31e-10 |
|
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: 62.74 E-value: 4.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1406 ILHNVATGTQSF-YQEHNDDILCLTVNQHPKFInivatgqVGDSADMSatapsVHIWDAVNKQTLSILRcSHSKGVCSVS 1484
Cdd:cd00200 118 KVWDVETGKCLTtLRGHTDWVNSVAFSPDGTFV-------ASSSQDGT-----IKLWDLRTGKCVATLT-GHTGEVNSVA 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41387501 1485 FSATGKLLLSVGLDpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTQFVSVGIKHVKFW 1548
Cdd:cd00200 185 FSPDGEKLLSSSSD--GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1418-1556 |
2.05e-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: 60.43 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1418 YQEHNDDILCLTVNQHPKFInivatgqVGDSADMSatapsVHIWDAVNKQTLSILRCsHSKGVCSVSFSATGKLLLSVGL 1497
Cdd:cd00200 89 LTGHTSYVSSVAFSPDGRIL-------SSSSRDKT-----IKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQ 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 41387501 1498 DpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTQFVSVGIKHVKFWTLAGRALL 1556
Cdd:cd00200 156 D--GTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL 212
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1418-1551 |
3.67e-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: 59.66 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1418 YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSVHIWDAVNKQTLSILrCSHSKGVCSVSFSATGKLLLSVGL 1497
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLL---ATG----SGD-----GTIKVWDLETGELLRTL-KGHTGPVRDVAASADGTYLASGSS 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 41387501 1498 DpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSdtQFVSVGIKH--VKFWTLA 1551
Cdd:cd00200 72 D--KTIRLWDLETGECVRTLTGHTSYVSSVAFSPDG--RILSSSSRDktIKVWDVE 123
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1460-1548 |
9.51e-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: 52.34 E-value: 9.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1460 IWDAVNKQTLSILRCsHSKGVCSVSFSATGKLLLSVGLDpeHTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDSDTQFVS 1539
Cdd:cd00200 77 LWDLETGECVRTLTG-HTSYVSSVAFSPDGRILSSSSRD--KTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASS 153
|
....*....
gi 41387501 1540 VGIKHVKFW 1548
Cdd:cd00200 154 SQDGTIKLW 162
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1421-1533 |
4.41e-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: 50.41 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1421 HNDDILCLTVnqHPKFINIVATGqvGDSadmsatapSVHIWDAVNKQTLSILRcSHSKGVCSVSFSATGKLLLSVGLDpe 1500
Cdd:cd00200 176 HTGEVNSVAF--SPDGEKLLSSS--SDG--------TIKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASGSED-- 240
|
90 100 110
....*....|....*....|....*....|...
gi 41387501 1501 HTVTIWRWQEGAKIASRGGHNQRIFVAEFRPDS 1533
Cdd:cd00200 241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDG 273
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
993-1507 |
2.00e-04 |
|
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: 45.02 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 993 VQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTL 1072
Cdd:cd00200 5 LKGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1073 EDLVSFHHRKDVISDIQFSPgSGKYLAVASHDSFVDIYNVTSSKRVGVCKGATSYITHIDWDSrgkllqvntgakeqlff 1152
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSP----------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1153 eaprgkkqtipsvevekiswatwtsvlglccegiwpiigevtdvtascltsDKMVLATGDDLGFVKLFRypaKGKFGKFK 1232
Cdd:cd00200 146 ---------------------------------------------------DGTFVASSSQDGTIKLWD---LRTGKCVA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1233 KYVAHSTHVTNVRWTYDDSMLVTlGGADMSLMVWtseverhrekkncdseesDTDSEEdggydsdvtreneisytirals 1312
Cdd:cd00200 172 TLTGHTGEVNSVAFSPDGEKLLS-SSSDGTIKLW------------------DLSTGK---------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1313 tnirpmfgvkpHLQQkepsvderqgvvrgsrppvsrappqpeklqsnnvgkkkrpiedlvlelafgyrgrdcrnnvhyln 1392
Cdd:cd00200 211 -----------CLGT----------------------------------------------------------------- 214
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 1393 dgddiiyhtasvgilhnvatgtqsfYQEHNDDILCLTVNQHPKFInivatgqVGDSADmsataPSVHIWDAVNKQTLSIL 1472
Cdd:cd00200 215 -------------------------LRGHENGVNSVAFSPDGYLL-------ASGSED-----GTIRVWDLRTGECVQTL 257
|
490 500 510
....*....|....*....|....*....|....*
gi 41387501 1473 RcSHSKGVCSVSFSATGKLLLSVGLDpeHTVTIWR 1507
Cdd:cd00200 258 S-GHTNSVTSLAWSPDGKRLASGSAD--GTIRIWD 289
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
760-802 |
3.64e-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: 39.60 E-value: 3.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 41387501 760 TIKPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIVLWD 802
Cdd:smart00320 1 SGELLKTLKG-HTGPVTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
314-353 |
1.12e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.10 E-value: 1.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 41387501 314 NKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:pfam00400 1 GKLLKTLEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
381-462 |
1.85e-03 |
|
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped WD40 domain.The N-terminus of Afi1 serves to stabilize the union between Apc4 and Apc5, both of which lie towards the bottom-front of the APC,
Pssm-ID: 403945 [Multi-domain] Cd Length: 91 Bit Score: 39.18 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 381 LALGMKDGSLTVLRV-RDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVaqrYKkvGECVGSLS----FIT 455
Cdd:pfam12894 10 IALATEDGELLLHRLnWQRVWTLSPDKEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDA---EN--GKIVHHFSagsdLIT 84
|
....*..
gi 41387501 456 HLDWSSD 462
Cdd:pfam12894 85 CLGWGEN 91
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
315-353 |
1.92e-03 |
|
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: 37.29 E-value: 1.92e-03
10 20 30
....*....|....*....|....*....|....*....
gi 41387501 315 KPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:smart00320 3 ELLKTLKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
250-354 |
2.21e-03 |
|
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: 42.21 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41387501 250 FATGGRDGCIRLWDLTF--KPITVIDLRETeqGYKGLSVRSvcwRGDHILVGTQDSEIFEIvvHERN-KPFLIMQGHCEG 326
Cdd:cd22857 195 IVTGTGYHQVRLYDTRAqrRPVVSVDFGET--PIKAVAEDP---DGHTVYVGDTSGDLASI--DLRTgKLLGCFKGKCGG 267
|
90 100
....*....|....*....|....*...
gi 41387501 327 ELWALAVHPTKPLAVTGSDDRSVRIWSL 354
Cdd:cd22857 268 SIRSIARHPELPLIASCGLDRYLRIWDT 295
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
994-1026 |
2.79e-03 |
|
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: 36.91 E-value: 2.79e-03
10 20 30
....*....|....*....|....*....|...
gi 41387501 994 QGHmEGEVWGLATHPYLPICATVSDDKTLRIWD 1026
Cdd:smart00320 9 KGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
720-757 |
5.92e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.17 E-value: 5.92e-03
10 20 30
....*....|....*....|....*....|....*...
gi 41387501 720 QRFYLGHDDDILCLAIHPLKDYVATGqvGRDPSIHVWD 757
Cdd:pfam00400 4 LKTLEGHTGSVTSLAFSPDGKLLASG--SDDGTVKVWD 39
|
|
| PTZ00421 |
PTZ00421 |
coronin; Provisional |
1080-1140 |
6.48e-03 |
|
coronin; Provisional
Pssm-ID: 173611 [Multi-domain] Cd Length: 493 Bit Score: 41.03 E-value: 6.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41387501 1080 HRKDViSDIQFSPGSGKYLAVASHDSFVDIYNVTSSKRVGVCKGATSYITHIDWDSRGKLL 1140
Cdd:PTZ00421 124 HTKKV-GIVSFHPSAMNVLASAGADMVVNVWDVERGKAVEVIKCHSDQITSLEWNLDGSLL 183
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
227-263 |
7.77e-03 |
|
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: 35.75 E-value: 7.77e-03
10 20 30
....*....|....*....|....*....|....*....
gi 41387501 227 NLIRTIQGaHTAGIFSMNACEEG--FATGGRDGCIRLWD 263
Cdd:smart00320 3 ELLKTLKG-HTGPVTSVAFSPDGkyLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
725-757 |
8.09e-03 |
|
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: 35.75 E-value: 8.09e-03
10 20 30
....*....|....*....|....*....|...
gi 41387501 725 GHDDDILCLAIHPLKDYVATGqvGRDPSIHVWD 757
Cdd:smart00320 10 GHTGPVTSVAFSPDGKYLASG--SDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
762-802 |
8.87e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.40 E-value: 8.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 41387501 762 KPLSILKGyHQYGICAVDFSADGKRLASVGIDdsHTIVLWD 802
Cdd:pfam00400 2 KLLKTLEG-HTGSVTSLAFSPDGKLLASGSDD--GTVKVWD 39
|
|
|