|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
57-438 |
1.38e-41 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 158.92 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 57 FLGHNDDIISLALHPDKTLIATGQVGKEpyICIWNSYNVHTVSILKDvHTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:COG2319 74 LLGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 137 WRKGKLLASATGHSDRIFDISWDPyqpnrmvscgvkhikfwtlcgnaltakrgifgkTGDLqtilcLAcakeditySGAL 216
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSP---------------------------------DGKL-----LA--------SGSD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 217 NGDIYVWKGLT--LVRTIQGaHSAGIFSLYACEEG--FATGGRDGCIRLWDTDfkpiTKiDLRETEQGYKGlSIRSVCWK 292
Cdd:COG2319 183 DGTVRLWDLATgkLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLA----TG-KLLRTLTGHSG-SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 293 AD--RLLAGTQDSEIfEVIVRERDKPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWSLADHALIARCNMEEA-V 369
Cdd:COG2319 256 PDgrLLASGSADGTV-RLWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGaV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081602 370 RSVSFSPDGSQLALGMKDGSFIVLRVRDMTEVVHIKDRKEVIHEMKFSPDGSYLAVGSNDGPVDVYAVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
707-1111 |
4.17e-35 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 140.05 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 707 AVAVVYNRQQHAQRLYLGHDDDILSLTIHPVKDYVATGqvGRDAAVHVWDTQTLKCLSLLKGHhQRGVCALDFSADGKCL 786
Cdd:COG2319 59 TLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTGH-TGAVRSVAFSPDGKTL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 787 VSVGLDdfHSVVFWDWKKGEKIATTRGHKDKIFVVkcnpqhadklvtvgikhikfwqqagggftskrgSFGSAGKLetmm 866
Cdd:COG2319 136 ASGSAD--GTVRLWDLATGKLLRTLTGHSGAVTSV---------------------------------AFSPDGKL---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 867 cvsygrmedlVFSGAATGDIFIWkDVL---LLKTVKAHDGPVFAM-YALD-KGFVTGGKDGIVELWDdmfercLKTYAIK 941
Cdd:COG2319 177 ----------LASGSDDGTVRLW-DLAtgkLLRTLTGHTGAVRSVaFSPDgKLLASGSADGTVRLWD------LATGKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 942 RTalstsskglLLEDNPSIRAITLGH-GHILV-GTKNGEILEIDKSGPMTLLVQGHMEGEVWGLAAHPLLPICATVSDDK 1019
Cdd:COG2319 240 RT---------LTGHSGSVRSVAFSPdGRLLAsGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1020 TLRIWELSSQHRMLAVRKLKKGGRCCAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAV 1099
Cdd:COG2319 311 TVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPD-GRTLAS 389
|
410
....*....|..
gi 1907081602 1100 ASHDNFVDIYNV 1111
Cdd:COG2319 390 GSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1427-1807 |
2.14e-31 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.88 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1427 LTVNQHPKYRNVVATSQIGTT-------PSIHIWDAMTKHTLSMLRcFHTKGVNYINFSATGKLLVSVGVDpeHTITVWR 1499
Cdd:COG2319 72 ATLLGHTAAVLSVAFSPDGRLlasasadGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1500 WQEGTKVASRGGHLERIFVVEFRPDSdTQFVSVGV-KHMKFWTLAGSALLYKkgVIGSMEAAkmqtmLSVAFGANNLTF- 1577
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSPDG-KLLASGSDdGTVRLWDLATGKLLRT--LTGHTGAV-----RSVAFSPDGKLLa 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1578 TGAINGDVYVWK-EHFLIRLVAKAHTGPVFTMyTTLRDG-LIVTGGkerptkEGGAVKLWDqemkrcrafqLETGQLVEc 1655
Cdd:COG2319 221 SGSADGTVRLWDlATGKLLRTLTGHSGSVRSV-AFSPDGrLLASGS------ADGTVRLWD----------LATGELLR- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1656 vrsvcrgkgkilvgtkdgeiievgeksaasniLIDGHmEGEIWGLATHPSKDMFISASNDGTARIWDLADKKLLNKVNlG 1735
Cdd:COG2319 283 --------------------------------TLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-G 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081602 1736 HAA--RCAAYSPDGEMVAIGMKNGEFVILLVNTLKVWGKKRDRKSAIQDIRISPDNRFLAVGSSEQTVDFYDLT 1807
Cdd:COG2319 329 HTGavRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-48 |
5.49e-20 |
|
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: 85.68 E-value: 5.49e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907081602 2 ADRTAPRCQLRLEWVYGYRGHQCRNNLYYTAGKEVVYFVAGVGVVYN 48
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
667-714 |
5.70e-20 |
|
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: 85.68 E-value: 5.70e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907081602 667 KREKAPEDSLKLQFIHGYRGYDCRNNLFYTQAGEVVYHIAAVAVVYNR 714
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1689-1963 |
2.01e-19 |
|
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: 90.86 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1689 IDGHmEGEIWGLATHPSKDMFISASNDGTARIWDLADKKLLnKVNLGHAA--RCAAYSPDGEMVAIGMKNgefvillvNT 1766
Cdd:cd00200 5 LKGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-RTLKGHTGpvRDVAASADGTYLASGSSD--------KT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1767 LKVW----GKKRDR----KSAIQDIRISPDNRFLAVGSSEQTVDFYDLTQGTSLNRIGYCKDipsFVIQMDFSADSKYiq 1838
Cdd:cd00200 75 IRLWdletGECVRTltghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD---WVNSVAFSPDGTF-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1839 VSTGAYKRQVH--EVPLGKqvteamVVEKITwaswtsvlgdevigiwprnADKADVNCACVTHAGLNIVTGDDFGLLKLF 1916
Cdd:cd00200 150 VASSSQDGTIKlwDLRTGK------CVATLT-------------------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907081602 1917 DFpctEKFAKHKRYFGHSAHVTNIRFSSDDKYVVStGGDDCSVFVWR 1963
Cdd:cd00200 205 DL---STGKCLGTLRGHENGVNSVAFSPDGYLLAS-GSEDGTIRVWD 247
|
|
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1039-1265 |
3.78e-13 |
|
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: 71.98 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1039 KKGGRCCAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAVASHDNFVDIYNVLTSKRVG 1118
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASAD-GTYLASGSSDKTIRLWDLETGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1119 ICKGASSYITHIDWDSRGKLLqvnSGAkeqlffeaprGRKHTIRpseaekiEWDTWTcvlgPTCEGIWPAHSDvtDVNAA 1198
Cdd:cd00200 88 TLTGHTSYVSSVAFSPDGRIL---SSS----------SRDKTIK-------VWDVET----GKCLTTLRGHTD--WVNSV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081602 1199 NLTKDGSLLATGDDFGFVKLFSyPVKGQhaRFKKYVGHSAHVTNVRWlHNDSVLLTVGGADTALMIW 1265
Cdd:cd00200 142 AFSPDGTFVASSSQDGTIKLWD-LRTGK--CVATLTGHTGEVNSVAF-SPDGEKLLSSSSDGTIKLW 204
|
|
| HELP super family |
cl04081 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1357-1408 |
7.91e-13 |
|
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.
The actual alignment was detected with superfamily member pfam03451:
Pssm-ID: 460922 Cd Length: 72 Bit Score: 65.27 E-value: 7.91e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907081602 1357 KNNITKKKKLVEE-LALDHVFGYRGFDCRNNLHYLNDGaDIIFHTAAAGIVQN 1408
Cdd:pfam03451 20 KDDLDQKKEPPDKkLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYD 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
57-438 |
1.38e-41 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 158.92 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 57 FLGHNDDIISLALHPDKTLIATGQVGKEpyICIWNSYNVHTVSILKDvHTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:COG2319 74 LLGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 137 WRKGKLLASATGHSDRIFDISWDPyqpnrmvscgvkhikfwtlcgnaltakrgifgkTGDLqtilcLAcakeditySGAL 216
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSP---------------------------------DGKL-----LA--------SGSD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 217 NGDIYVWKGLT--LVRTIQGaHSAGIFSLYACEEG--FATGGRDGCIRLWDTDfkpiTKiDLRETEQGYKGlSIRSVCWK 292
Cdd:COG2319 183 DGTVRLWDLATgkLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLA----TG-KLLRTLTGHSG-SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 293 AD--RLLAGTQDSEIfEVIVRERDKPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWSLADHALIARCNMEEA-V 369
Cdd:COG2319 256 PDgrLLASGSADGTV-RLWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGaV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081602 370 RSVSFSPDGSQLALGMKDGSFIVLRVRDMTEVVHIKDRKEVIHEMKFSPDGSYLAVGSNDGPVDVYAVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
707-1111 |
4.17e-35 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 140.05 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 707 AVAVVYNRQQHAQRLYLGHDDDILSLTIHPVKDYVATGqvGRDAAVHVWDTQTLKCLSLLKGHhQRGVCALDFSADGKCL 786
Cdd:COG2319 59 TLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTGH-TGAVRSVAFSPDGKTL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 787 VSVGLDdfHSVVFWDWKKGEKIATTRGHKDKIFVVkcnpqhadklvtvgikhikfwqqagggftskrgSFGSAGKLetmm 866
Cdd:COG2319 136 ASGSAD--GTVRLWDLATGKLLRTLTGHSGAVTSV---------------------------------AFSPDGKL---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 867 cvsygrmedlVFSGAATGDIFIWkDVL---LLKTVKAHDGPVFAM-YALD-KGFVTGGKDGIVELWDdmfercLKTYAIK 941
Cdd:COG2319 177 ----------LASGSDDGTVRLW-DLAtgkLLRTLTGHTGAVRSVaFSPDgKLLASGSADGTVRLWD------LATGKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 942 RTalstsskglLLEDNPSIRAITLGH-GHILV-GTKNGEILEIDKSGPMTLLVQGHMEGEVWGLAAHPLLPICATVSDDK 1019
Cdd:COG2319 240 RT---------LTGHSGSVRSVAFSPdGRLLAsGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1020 TLRIWELSSQHRMLAVRKLKKGGRCCAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAV 1099
Cdd:COG2319 311 TVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPD-GRTLAS 389
|
410
....*....|..
gi 1907081602 1100 ASHDNFVDIYNV 1111
Cdd:COG2319 390 GSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
57-353 |
9.20e-35 |
|
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: 135.54 E-value: 9.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 57 FLGHNDDIISLALHPDKTLIATGQVGKEpyICIWNSYNVHTVSILKdVHTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGT--IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSD--KTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 137 WRKGKLLASATGHSDRIFDISWDPYqpNRMVSCGVKH--IKFWTL-CGNALTAKRGIFGktgdlqTILCLA-CAKEDITY 212
Cdd:cd00200 80 LETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WVNSVAfSPDGTFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 213 SGALNGDIYVW--KGLTLVRTIQGaHSAGIFSLYACEEG--FATGGRDGCIRLWDTDFKPITKIdLRETEQGykglsIRS 288
Cdd:cd00200 152 SSSQDGTIKLWdlRTGKCVATLTG-HTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGT-LRGHENG-----VNS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081602 289 VCWKADRLL--AGTQDS--EIFEVivrERDKPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWS 353
Cdd:cd00200 225 VAFSPDGYLlaSGSEDGtiRVWDL---RTGECVQTLSGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
724-1025 |
1.06e-33 |
|
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: 132.46 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 724 GHDDDILSLTIHPVKDYVATGqvGRDAAVHVWDTQTLKCLSLLKGhHQRGVCALDFSADGKCLVSVGLDdfHSVVFWDWK 803
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 804 KGEKIATTRGHKDKIFVVKCNPQHadKLVTVGIKH--IKFWQQAGGGFTSkrgSFGsaGKLETMMCVSYGRMEDLVFSGA 881
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDG--RILSSSSRDktIKVWDVETGKCLT---TLR--GHTDWVNSVAFSPDGTFVASSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 882 ATGDIFIWkDV---LLLKTVKAHDGPVFAMYALDKG--FVTGGKDGIVELWDDMFERCLKTYAIKR---TALSTSSKGLL 953
Cdd:cd00200 155 QDGTIKLW-DLrtgKCVATLTGHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGTLRGHEngvNSVAFSPDGYL 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081602 954 LednpsiraitlghghiLVGTKNGEILEID-KSGPMTLLVQGHmEGEVWGLAAHPLLPICATVSDDKTLRIWE 1025
Cdd:cd00200 234 L----------------ASGSEDGTIRVWDlRTGECVQTLSGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1427-1807 |
2.14e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.88 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1427 LTVNQHPKYRNVVATSQIGTT-------PSIHIWDAMTKHTLSMLRcFHTKGVNYINFSATGKLLVSVGVDpeHTITVWR 1499
Cdd:COG2319 72 ATLLGHTAAVLSVAFSPDGRLlasasadGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1500 WQEGTKVASRGGHLERIFVVEFRPDSdTQFVSVGV-KHMKFWTLAGSALLYKkgVIGSMEAAkmqtmLSVAFGANNLTF- 1577
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSPDG-KLLASGSDdGTVRLWDLATGKLLRT--LTGHTGAV-----RSVAFSPDGKLLa 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1578 TGAINGDVYVWK-EHFLIRLVAKAHTGPVFTMyTTLRDG-LIVTGGkerptkEGGAVKLWDqemkrcrafqLETGQLVEc 1655
Cdd:COG2319 221 SGSADGTVRLWDlATGKLLRTLTGHSGSVRSV-AFSPDGrLLASGS------ADGTVRLWD----------LATGELLR- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1656 vrsvcrgkgkilvgtkdgeiievgeksaasniLIDGHmEGEIWGLATHPSKDMFISASNDGTARIWDLADKKLLNKVNlG 1735
Cdd:COG2319 283 --------------------------------TLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-G 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081602 1736 HAA--RCAAYSPDGEMVAIGMKNGEFVILLVNTLKVWGKKRDRKSAIQDIRISPDNRFLAVGSSEQTVDFYDLT 1807
Cdd:COG2319 329 HTGavRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1468-1770 |
2.53e-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: 96.25 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1468 HTKGVNYINFSATGKLLVSVGVDpeHTITVWRWQEGTKVASRGGHLERIFVVEFRPDSdTQFVSVGVKHM-KFWTLAGSA 1546
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGD--GTIKVWDLETGELLRTLKGHTGPVRDVAASADG-TYLASGSSDKTiRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1547 LLYkkgvigSMEAAKmQTMLSVAFGANNLTFTGAI-NGDVYVWK-EHFLIRLVAKAHTGPVFTMyTTLRDGLIVTGGker 1624
Cdd:cd00200 85 CVR------TLTGHT-SYVSSVAFSPDGRILSSSSrDKTIKVWDvETGKCLTTLRGHTDWVNSV-AFSPDGTFVASS--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1625 ptKEGGAVKLWD-QEMKRCRAFQLETGQlvecVRSVC--RGKGKILVGTKDGEIIeVGEKSAASNI-LIDGHmEGEIWGL 1700
Cdd:cd00200 154 --SQDGTIKLWDlRTGKCVATLTGHTGE----VNSVAfsPDGEKLLSSSSDGTIK-LWDLSTGKCLgTLRGH-ENGVNSV 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081602 1701 ATHPSKDMFISASNDGTARIWDLADKKLLNKVNlGHAAR--CAAYSPDGEMVAIGMKNgefvillvNTLKVW 1770
Cdd:cd00200 226 AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSvtSLAWSPDGKRLASGSAD--------GTIRIW 288
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-48 |
5.49e-20 |
|
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: 85.68 E-value: 5.49e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907081602 2 ADRTAPRCQLRLEWVYGYRGHQCRNNLYYTAGKEVVYFVAGVGVVYN 48
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
667-714 |
5.70e-20 |
|
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: 85.68 E-value: 5.70e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907081602 667 KREKAPEDSLKLQFIHGYRGYDCRNNLFYTQAGEVVYHIAAVAVVYNR 714
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1689-1963 |
2.01e-19 |
|
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: 90.86 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1689 IDGHmEGEIWGLATHPSKDMFISASNDGTARIWDLADKKLLnKVNLGHAA--RCAAYSPDGEMVAIGMKNgefvillvNT 1766
Cdd:cd00200 5 LKGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-RTLKGHTGpvRDVAASADGTYLASGSSD--------KT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1767 LKVW----GKKRDR----KSAIQDIRISPDNRFLAVGSSEQTVDFYDLTQGTSLNRIGYCKDipsFVIQMDFSADSKYiq 1838
Cdd:cd00200 75 IRLWdletGECVRTltghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD---WVNSVAFSPDGTF-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1839 VSTGAYKRQVH--EVPLGKqvteamVVEKITwaswtsvlgdevigiwprnADKADVNCACVTHAGLNIVTGDDFGLLKLF 1916
Cdd:cd00200 150 VASSSQDGTIKlwDLRTGK------CVATLT-------------------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907081602 1917 DFpctEKFAKHKRYFGHSAHVTNIRFSSDDKYVVStGGDDCSVFVWR 1963
Cdd:cd00200 205 DL---STGKCLGTLRGHENGVNSVAFSPDGYLLAS-GSEDGTIRVWD 247
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1039-1265 |
3.78e-13 |
|
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: 71.98 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1039 KKGGRCCAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAVASHDNFVDIYNVLTSKRVG 1118
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASAD-GTYLASGSSDKTIRLWDLETGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1119 ICKGASSYITHIDWDSRGKLLqvnSGAkeqlffeaprGRKHTIRpseaekiEWDTWTcvlgPTCEGIWPAHSDvtDVNAA 1198
Cdd:cd00200 88 TLTGHTSYVSSVAFSPDGRIL---SSS----------SRDKTIK-------VWDVET----GKCLTTLRGHTD--WVNSV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081602 1199 NLTKDGSLLATGDDFGFVKLFSyPVKGQhaRFKKYVGHSAHVTNVRWlHNDSVLLTVGGADTALMIW 1265
Cdd:cd00200 142 AFSPDGTFVASSSQDGTIKLWD-LRTGK--CVATLTGHTGEVNSVAF-SPDGEKLLSSSSDGTIKLW 204
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1357-1408 |
7.91e-13 |
|
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: 65.27 E-value: 7.91e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907081602 1357 KNNITKKKKLVEE-LALDHVFGYRGFDCRNNLHYLNDGaDIIFHTAAAGIVQN 1408
Cdd:pfam03451 20 KDDLDQKKEPPDKkLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYD 71
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
105-136 |
2.33e-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: 40.37 E-value: 2.33e-04
10 20 30
....*....|....*....|....*....|..
gi 1907081602 105 HTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:smart00320 11 HTGPVTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1689-1722 |
2.78e-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: 39.99 E-value: 2.78e-04
10 20 30
....*....|....*....|....*....|....
gi 1907081602 1689 IDGHmEGEIWGLATHPSKDMFISASNDGTARIWD 1722
Cdd:smart00320 8 LKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1689-1722 |
5.60e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 5.60e-04
10 20 30
....*....|....*....|....*....|....
gi 1907081602 1689 IDGHmEGEIWGLATHPSKDMFISASNDGTARIWD 1722
Cdd:pfam00400 7 LEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
315-353 |
7.53e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 7.53e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1907081602 315 KPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWS 353
Cdd:pfam00400 2 KLLKTLEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
759-801 |
1.42e-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: 38.06 E-value: 1.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1907081602 759 TLKCLSLLKGHhQRGVCALDFSADGKCLVSVGLDdfHSVVFWD 801
Cdd:smart00320 1 SGELLKTLKGH-TGPVTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1923-1962 |
1.42e-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: 38.06 E-value: 1.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907081602 1923 KFAKHKRYFGHSAHVTNIRFSSDDKYVVStGGDDCSVFVW 1962
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLAS-GSDDGTIKLW 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1928-1962 |
1.61e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|....*
gi 1907081602 1928 KRYFGHSAHVTNIRFSSDDKYVVStGGDDCSVFVW 1962
Cdd:pfam00400 5 KTLEGHTGSVTSLAFSPDGKLLAS-GSDDGTVKVW 38
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
57-438 |
1.38e-41 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 158.92 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 57 FLGHNDDIISLALHPDKTLIATGQVGKEpyICIWNSYNVHTVSILKDvHTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:COG2319 74 LLGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 137 WRKGKLLASATGHSDRIFDISWDPyqpnrmvscgvkhikfwtlcgnaltakrgifgkTGDLqtilcLAcakeditySGAL 216
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSP---------------------------------DGKL-----LA--------SGSD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 217 NGDIYVWKGLT--LVRTIQGaHSAGIFSLYACEEG--FATGGRDGCIRLWDTDfkpiTKiDLRETEQGYKGlSIRSVCWK 292
Cdd:COG2319 183 DGTVRLWDLATgkLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLA----TG-KLLRTLTGHSG-SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 293 AD--RLLAGTQDSEIfEVIVRERDKPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWSLADHALIARCNMEEA-V 369
Cdd:COG2319 256 PDgrLLASGSADGTV-RLWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGaV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081602 370 RSVSFSPDGSQLALGMKDGSFIVLRVRDMTEVVHIKDRKEVIHEMKFSPDGSYLAVGSNDGPVDVYAVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
57-397 |
6.11e-39 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 151.22 E-value: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 57 FLGHNDDIISLALHPDKTLIATGQVGKEpyICIWNSYNVHTVSILKDvHTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:COG2319 116 LTGHTGAVRSVAFSPDGKTLASGSADGT--VRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDD--GTVRLWD 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 137 WRKGKLLASATGHSDRIFDISWDPyqpnrmvscgvkhikfwtlcgnaltakrgifgktgDLQTILclacakeditySGAL 216
Cdd:COG2319 191 LATGKLLRTLTGHTGAVRSVAFSP-----------------------------------DGKLLA-----------SGSA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 217 NGDIYVW--KGLTLVRTIQGaHSAGIFSLYACEEG--FATGGRDGCIRLWDTDFKpitkiDLRETEQGYKGlSIRSVCWK 292
Cdd:COG2319 225 DGTVRLWdlATGKLLRTLTG-HSGSVRSVAFSPDGrlLASGSADGTVRLWDLATG-----ELLRTLTGHSG-GVNSVAFS 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 293 AD--RLLAGTQDSEI--FEVivrERDKPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWSLADHALIARCNM-EE 367
Cdd:COG2319 298 PDgkLLASGSDDGTVrlWDL---ATGKLLRTLTGH-TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGhTG 373
|
330 340 350
....*....|....*....|....*....|
gi 1907081602 368 AVRSVSFSPDGSQLALGMKDGSFIVLRVRD 397
Cdd:COG2319 374 AVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
707-1111 |
4.17e-35 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 140.05 E-value: 4.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 707 AVAVVYNRQQHAQRLYLGHDDDILSLTIHPVKDYVATGqvGRDAAVHVWDTQTLKCLSLLKGHhQRGVCALDFSADGKCL 786
Cdd:COG2319 59 TLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTGH-TGAVRSVAFSPDGKTL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 787 VSVGLDdfHSVVFWDWKKGEKIATTRGHKDKIFVVkcnpqhadklvtvgikhikfwqqagggftskrgSFGSAGKLetmm 866
Cdd:COG2319 136 ASGSAD--GTVRLWDLATGKLLRTLTGHSGAVTSV---------------------------------AFSPDGKL---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 867 cvsygrmedlVFSGAATGDIFIWkDVL---LLKTVKAHDGPVFAM-YALD-KGFVTGGKDGIVELWDdmfercLKTYAIK 941
Cdd:COG2319 177 ----------LASGSDDGTVRLW-DLAtgkLLRTLTGHTGAVRSVaFSPDgKLLASGSADGTVRLWD------LATGKLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 942 RTalstsskglLLEDNPSIRAITLGH-GHILV-GTKNGEILEIDKSGPMTLLVQGHMEGEVWGLAAHPLLPICATVSDDK 1019
Cdd:COG2319 240 RT---------LTGHSGSVRSVAFSPdGRLLAsGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1020 TLRIWELSSQHRMLAVRKLKKGGRCCAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAV 1099
Cdd:COG2319 311 TVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPD-GRTLAS 389
|
410
....*....|..
gi 1907081602 1100 ASHDNFVDIYNV 1111
Cdd:COG2319 390 GSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
57-353 |
9.20e-35 |
|
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: 135.54 E-value: 9.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 57 FLGHNDDIISLALHPDKTLIATGQVGKEpyICIWNSYNVHTVSILKdVHTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGT--IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSD--KTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 137 WRKGKLLASATGHSDRIFDISWDPYqpNRMVSCGVKH--IKFWTL-CGNALTAKRGIFGktgdlqTILCLA-CAKEDITY 212
Cdd:cd00200 80 LETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WVNSVAfSPDGTFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 213 SGALNGDIYVW--KGLTLVRTIQGaHSAGIFSLYACEEG--FATGGRDGCIRLWDTDFKPITKIdLRETEQGykglsIRS 288
Cdd:cd00200 152 SSSQDGTIKLWdlRTGKCVATLTG-HTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGT-LRGHENG-----VNS 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907081602 289 VCWKADRLL--AGTQDS--EIFEVivrERDKPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWS 353
Cdd:cd00200 225 VAFSPDGYLlaSGSEDGtiRVWDL---RTGECVQTLSGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
724-1025 |
1.06e-33 |
|
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: 132.46 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 724 GHDDDILSLTIHPVKDYVATGqvGRDAAVHVWDTQTLKCLSLLKGhHQRGVCALDFSADGKCLVSVGLDdfHSVVFWDWK 803
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKG-HTGPVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 804 KGEKIATTRGHKDKIFVVKCNPQHadKLVTVGIKH--IKFWQQAGGGFTSkrgSFGsaGKLETMMCVSYGRMEDLVFSGA 881
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPDG--RILSSSSRDktIKVWDVETGKCLT---TLR--GHTDWVNSVAFSPDGTFVASSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 882 ATGDIFIWkDV---LLLKTVKAHDGPVFAMYALDKG--FVTGGKDGIVELWDDMFERCLKTYAIKR---TALSTSSKGLL 953
Cdd:cd00200 155 QDGTIKLW-DLrtgKCVATLTGHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGTLRGHEngvNSVAFSPDGYL 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081602 954 LednpsiraitlghghiLVGTKNGEILEID-KSGPMTLLVQGHmEGEVWGLAAHPLLPICATVSDDKTLRIWE 1025
Cdd:cd00200 234 L----------------ASGSEDGTIRVWDlRTGECVQTLSGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
222-591 |
3.79e-32 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 131.19 E-value: 3.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 222 VWKGLTLVRTIQGAHSAGIFSLYACEEG--FATGGRDGCIRLWDTDfkpiTKIDLReTEQGYKGlSIRSVCWKAD--RLL 297
Cdd:COG2319 63 LDAAAGALLATLLGHTAAVLSVAFSPDGrlLASASADGTVRLWDLA----TGLLLR-TLTGHTG-AVRSVAFSPDgkTLA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 298 AGTQDSEIfEVIVRERDKPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWSLADHALIARCN-MEEAVRSVSFSP 376
Cdd:COG2319 137 SGSADGTV-RLWDLATGKLLRTLTGH-SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSP 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 377 DGSQLALGMKDGSFIVLRVRDMTEVVHIKDRKEVIHEMKFSPDGSYLAVGSNDGPVDVYAVAQrykkiGECNKSL----S 452
Cdd:COG2319 215 DGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-----GELLRTLtghsG 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 453 FITHIDWSLDSKYLQTNDGAGE-RLfykmpWKpltskeeikgipWASWTCVRGPEVSGIWpkytevidINSVDANYNSSV 531
Cdd:COG2319 290 GVNSVAFSPDGKLLASGSDDGTvRL-----WD------------LATGKLLRTLTGHTGA--------VRSVAFSPDGKT 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 532 LVSGDDFGLVKLFKfpcLKKGAKFRKYVGHSAHVTNVRWSHDFQWVLStGGADHSVFQWR 591
Cdd:COG2319 345 LASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWD 400
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1427-1807 |
2.14e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.88 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1427 LTVNQHPKYRNVVATSQIGTT-------PSIHIWDAMTKHTLSMLRcFHTKGVNYINFSATGKLLVSVGVDpeHTITVWR 1499
Cdd:COG2319 72 ATLLGHTAAVLSVAFSPDGRLlasasadGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1500 WQEGTKVASRGGHLERIFVVEFRPDSdTQFVSVGV-KHMKFWTLAGSALLYKkgVIGSMEAAkmqtmLSVAFGANNLTF- 1577
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSPDG-KLLASGSDdGTVRLWDLATGKLLRT--LTGHTGAV-----RSVAFSPDGKLLa 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1578 TGAINGDVYVWK-EHFLIRLVAKAHTGPVFTMyTTLRDG-LIVTGGkerptkEGGAVKLWDqemkrcrafqLETGQLVEc 1655
Cdd:COG2319 221 SGSADGTVRLWDlATGKLLRTLTGHSGSVRSV-AFSPDGrLLASGS------ADGTVRLWD----------LATGELLR- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1656 vrsvcrgkgkilvgtkdgeiievgeksaasniLIDGHmEGEIWGLATHPSKDMFISASNDGTARIWDLADKKLLNKVNlG 1735
Cdd:COG2319 283 --------------------------------TLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-G 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907081602 1736 HAA--RCAAYSPDGEMVAIGMKNGEFVILLVNTLKVWGKKRDRKSAIQDIRISPDNRFLAVGSSEQTVDFYDLT 1807
Cdd:COG2319 329 HTGavRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1478-1963 |
2.26e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 128.88 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1478 SATGKLLVSVGVDPEHTITVWRWQEGTKVASRGGHLERIFVVEFRPDSDTQFVSVGVKHMKFWTLAGSALLYKKGVIGSm 1557
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1558 eaakmqTMLSVAFGANNLTF-TGAINGDVYVWK-EHFLIRLVAKAHTGPVFTMyTTLRDG-LIVTGGkerptkEGGAVKL 1634
Cdd:COG2319 80 ------AVLSVAFSPDGRLLaSASADGTVRLWDlATGLLLRTLTGHTGAVRSV-AFSPDGkTLASGS------ADGTVRL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1635 WDqemkrcrafqLETGQLVEcvrsvcrgkgkilvgtkdgeiievgeksaasniLIDGHmEGEIWGLATHPSKDMFISASN 1714
Cdd:COG2319 147 WD----------LATGKLLR---------------------------------TLTGH-SGAVTSVAFSPDGKLLASGSD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1715 DGTARIWDLADKKLLNKVNlGHAA--RCAAYSPDGEMVAIGMKNGEFVILLVNTLKVWGKKRDRKSAIQDIRISPDNRFL 1792
Cdd:COG2319 183 DGTVRLWDLATGKLLRTLT-GHTGavRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1793 AVGSSEQTVDFYDLTQGTSLNRIGyckDIPSFVIQMDFSADSKYIqVSTGAYKR-QVHEVPLGKQvteamvvekitwasw 1871
Cdd:COG2319 262 ASGSADGTVRLWDLATGELLRTLT---GHSGGVNSVAFSPDGKLL-ASGSDDGTvRLWDLATGKL--------------- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1872 tsvlgdevigIWPRNADKADVNCACVTHAGLNIVTGDDFGLLKLFDfpcTEKFAKHKRYFGHSAHVTNIRFSSDDKYVVS 1951
Cdd:COG2319 323 ----------LRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS 389
|
490
....*....|..
gi 1907081602 1952 tGGDDCSVFVWR 1963
Cdd:COG2319 390 -GSADGTVRLWD 400
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
879-1265 |
7.61e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 124.25 E-value: 7.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 879 SGAATGDIFIWKDVLLLKTVKAHDGPVF--AMYALDKGFVTGGKDGIVELWDdmferclktyaikrtALSTSSKGLLLED 956
Cdd:COG2319 55 AGDLTLLLLDAAAGALLATLLGHTAAVLsvAFSPDGRLLASASADGTVRLWD---------------LATGLLLRTLTGH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 957 NPSIRAITLGH-GHILV-GTKNGEILEID-KSGPMTLLVQGHmEGEVWGLAAHP---LLpicATVSDDKTLRIWELSSQH 1030
Cdd:COG2319 120 TGAVRSVAFSPdGKTLAsGSADGTVRLWDlATGKLLRTLTGH-SGAVTSVAFSPdgkLL---ASGSDDGTVRLWDLATGK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1031 RMLAVRKLKKGGRCCAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAVASHDNFVDIYN 1110
Cdd:COG2319 196 LLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPD-GRLLASGSADGTVRLWD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1111 VLTSKRVGICKGASSYITHIDWDSRGKLLqvnsgakeqlffeAPRGRKHTIRPseaekieWDTWTcvlgPTCEGIWPAHS 1190
Cdd:COG2319 275 LATGELLRTLTGHSGGVNSVAFSPDGKLL-------------ASGSDDGTVRL-------WDLAT----GKLLRTLTGHT 330
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081602 1191 DvtDVNAANLTKDGSLLATGDDFGFVKLFSYPVKGQHARFKkyvGHSAHVTNVRWLHNDSVLLTvGGADTALMIW 1265
Cdd:COG2319 331 G--AVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
742-1139 |
1.71e-29 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 123.10 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 742 ATGQVGRDAAVHVWDTQTLKCLSLLKGHHQRGVcALDFSADGKCLVSVGLDDfhSVVFWDWKKGEKIATTRGHKDKIFVV 821
Cdd:COG2319 8 ALAAASADLALALLAAALGALLLLLLGLAAAVA-SLAASPDGARLAAGAGDL--TLLLLDAAAGALLATLLGHTAAVLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 822 KCNPQHADKLVTVGIKHIKFWQQAGGGFTSKRGSFGSAGKletmmCVSY---GRMedlVFSGAATGDIFIWkDVL---LL 895
Cdd:COG2319 85 AFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVR-----SVAFspdGKT---LASGSADGTVRLW-DLAtgkLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 896 KTVKAHDGPVFAM-YALD-KGFVTGGKDGIVELWDDMFERCLKTyaikrtalstsskglLLEDNPSIRAITLGH-GHILV 972
Cdd:COG2319 156 RTLTGHSGAVTSVaFSPDgKLLASGSDDGTVRLWDLATGKLLRT---------------LTGHTGAVRSVAFSPdGKLLA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 973 -GTKNGEILEID-KSGPMTLLVQGHmEGEVWGLAAHP---LLpicATVSDDKTLRIWELSSQHRMLAVRKLKKGGRCCAF 1047
Cdd:COG2319 221 sGSADGTVRLWDlATGKLLRTLTGH-SGSVRSVAFSPdgrLL---ASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAF 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1048 SPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAVASHDNFVDIYNVLTSKRVGICKGASSYI 1127
Cdd:COG2319 297 SPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPD-GKTLASGSDDGTVRLWDLATGELLRTLTGHTGAV 375
|
410
....*....|..
gi 1907081602 1128 THIDWDSRGKLL 1139
Cdd:COG2319 376 TSVAFSPDGRTL 387
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
274-843 |
6.54e-29 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 121.56 E-value: 6.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 274 LRETEQGYKGLSIRSVCWKADRLLAGTQDSEIFEVIVRERDKPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWS 353
Cdd:COG2319 28 LLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH-TAAVLSVAFSPDGRLLASASADGTVRLWD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 354 LADHALIARCNM-EEAVRSVSFSPDGSQLALGMKDGSFIVLRVRDMTEVVHIKDRKEVIHEMKFSPDGSYLAVGSNDGPV 432
Cdd:COG2319 107 LATGLLLRTLTGhTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 433 DVYAVAQrykkiGECNKSL----SFITHIDWSLDSKYLqtndgagerlfykmpwkpltskeeikgipwaswtcvrgpevs 508
Cdd:COG2319 187 RLWDLAT-----GKLLRTLtghtGAVRSVAFSPDGKLL------------------------------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 509 giwpkytevidinsvdanynssvlVSGDDFGLVKLFKfpcLKKGAKFRKYVGHSAHVTNVRWSHDFQWVLStGGADHSVF 588
Cdd:COG2319 220 ------------------------ASGSADGTVRLWD---LATGKLLRTLTGHSGSVRSVAFSPDGRLLAS-GSADGTVR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 589 QWRfipeavsngvlettpqeggadsyseesdsdfsdvpeldsdieqetqinydrqvykedlpqlkqqskeknhavpflkr 668
Cdd:COG2319 272 LWD----------------------------------------------------------------------------- 274
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 669 ekapedslklqfihgyrgydcrnnlfyTQAGEVVyhiaavavvynrqqhaqRLYLGHDDDILSLTIHPVKDYVATGqvGR 748
Cdd:COG2319 275 ---------------------------LATGELL-----------------RTLTGHSGGVNSVAFSPDGKLLASG--SD 308
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 749 DAAVHVWDTQTLKCLSLLKGHHQRgVCALDFSADGKCLVSVGLDdfHSVVFWDWKKGEKIATTRGHKDKIFVVKCNPQHa 828
Cdd:COG2319 309 DGTVRLWDLATGKLLRTLTGHTGA-VRSVAFSPDGKTLASGSDD--GTVRLWDLATGELLRTLTGHTGAVTSVAFSPDG- 384
|
570
....*....|....*.
gi 1907081602 829 DKLVTVGI-KHIKFWQ 843
Cdd:COG2319 385 RTLASGSAdGTVRLWD 400
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
942-1265 |
5.49e-27 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 115.78 E-value: 5.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 942 RTALSTSSKGLLLEDNPSIRAITLGHGHILVGTKNGEILEIDKSGPMTLLVQGHmEGEVWGLAAHPLLPICATVSDDKTL 1021
Cdd:COG2319 24 ALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH-TAAVLSVAFSPDGRLLASASADGTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1022 RIWELSSQHRMLAVRKLKKGGRCCAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAVAS 1101
Cdd:COG2319 103 RLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSPD-GKLLASGS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1102 HDNFVDIYNVLTSKRVGICKGASSYITHIDWDSRGKLLqVnSGakeqlffeaprGRKHTIRPseaekieWDtwtcVLGPT 1181
Cdd:COG2319 182 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLL-A-SG-----------SADGTVRL-------WD----LATGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1182 CEGIWPAHSDVtdVNAANLTKDGSLLATGDDFGFVKLFSyPVKGQHARFKKyvGHSAHVTNVRWLHNDSVLLTvGGADTA 1261
Cdd:COG2319 238 LLRTLTGHSGS--VRSVAFSPDGRLLASGSADGTVRLWD-LATGELLRTLT--GHSGGVNSVAFSPDGKLLAS-GSDDGT 311
|
....
gi 1907081602 1262 LMIW 1265
Cdd:COG2319 312 VRLW 315
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1408-1725 |
6.26e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 106.53 E-value: 6.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1408 NLSTGSQSFYLE-HTDDILCLTVnqHPKYRNVVATSQIGTtpsIHIWDAMTKHTLSMLRCfHTKGVNYINFSATGKLLVS 1486
Cdd:COG2319 106 DLATGLLLRTLTgHTGAVRSVAF--SPDGKTLASGSADGT---VRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLAS 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1487 VGVDpeHTITVWRWQEGTKVASRGGHLERIFVVEFRPDSDTqFVSVGV-KHMKFWTLAGSALLYKKGVIGSmeaakmqTM 1565
Cdd:COG2319 180 GSDD--GTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKL-LASGSAdGTVRLWDLATGKLLRTLTGHSG-------SV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1566 LSVAFGANNLTF-TGAINGDVYVWK-EHFLIRLVAKAHTGPVFTMYTTLRDGLIVTGGkerptkEGGAVKLWDqemkrcr 1643
Cdd:COG2319 250 RSVAFSPDGRLLaSGSADGTVRLWDlATGELLRTLTGHSGGVNSVAFSPDGKLLASGS------DDGTVRLWD------- 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1644 afqLETGQLV-------ECVRSVC-RGKGKILV-GTKDGEI----IEVGEKSAAsnilIDGHmEGEIWGLATHPSKDMFI 1710
Cdd:COG2319 317 ---LATGKLLrtltghtGAVRSVAfSPDGKTLAsGSDDGTVrlwdLATGELLRT----LTGH-TGAVTSVAFSPDGRTLA 388
|
330
....*....|....*
gi 1907081602 1711 SASNDGTARIWDLAD 1725
Cdd:COG2319 389 SGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
722-928 |
1.15e-22 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 100.49 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 722 YLGHDDDILSLTIHPVKDYVATGqvGRDAAVHVWDTQTLKCLSLLKGhHQRGVCALDFSADGKCLVSVGLDdfHSVVFWD 801
Cdd:cd00200 89 LTGHTSYVSSVAFSPDGRILSSS--SRDKTIKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQD--GTIKLWD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 802 WKKGEKIATTRGHKDKIFVVKCNPQHADKLVTVGIKHIKFWQQAGGgftSKRGSFgsAGKLETMMCVSYGRMEDLVFSGA 881
Cdd:cd00200 164 LRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG---KCLGTL--RGHENGVNSVAFSPDGYLLASGS 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1907081602 882 ATGDIFIW--KDVLLLKTVKAHDGPVFAMYALDKG--FVTGGKDGIVELWD 928
Cdd:cd00200 239 EDGTIRVWdlRTGECVQTLSGHTNSVTSLAWSPDGkrLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1468-1770 |
2.53e-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: 96.25 E-value: 2.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1468 HTKGVNYINFSATGKLLVSVGVDpeHTITVWRWQEGTKVASRGGHLERIFVVEFRPDSdTQFVSVGVKHM-KFWTLAGSA 1546
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGD--GTIKVWDLETGELLRTLKGHTGPVRDVAASADG-TYLASGSSDKTiRLWDLETGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1547 LLYkkgvigSMEAAKmQTMLSVAFGANNLTFTGAI-NGDVYVWK-EHFLIRLVAKAHTGPVFTMyTTLRDGLIVTGGker 1624
Cdd:cd00200 85 CVR------TLTGHT-SYVSSVAFSPDGRILSSSSrDKTIKVWDvETGKCLTTLRGHTDWVNSV-AFSPDGTFVASS--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1625 ptKEGGAVKLWD-QEMKRCRAFQLETGQlvecVRSVC--RGKGKILVGTKDGEIIeVGEKSAASNI-LIDGHmEGEIWGL 1700
Cdd:cd00200 154 --SQDGTIKLWDlRTGKCVATLTGHTGE----VNSVAfsPDGEKLLSSSSDGTIK-LWDLSTGKCLgTLRGH-ENGVNSV 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907081602 1701 ATHPSKDMFISASNDGTARIWDLADKKLLNKVNlGHAAR--CAAYSPDGEMVAIGMKNgefvillvNTLKVW 1770
Cdd:cd00200 226 AFSPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSvtSLAWSPDGKRLASGSAD--------GTIRIW 288
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
520-1070 |
3.92e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 98.06 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 520 INSVDANYNSSVLVSGDDFGLVKLFKfpcLKKGAKFRKYVGHSAHVTNVRWSHDFQWVLStGGADHSVFQWRfipeavsn 599
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGTVRLWD---LATGLLLRTLTGHTGAVRSVAFSPDGKTLAS-GSADGTVRLWD-------- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 600 gvlettpqeggadsyseesdsdfsdvpeldsdieqetqinydrqvykedlpqlkqqskeknhavpflkrekapedslklq 679
Cdd:COG2319 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 680 fihgyrgydcrnnlfyTQAGEVVYHIAavavvynrqqhaqrlylGHDDDILSLTIHPVKDYVATGqvGRDAAVHVWDTQT 759
Cdd:COG2319 149 ----------------LATGKLLRTLT-----------------GHSGAVTSVAFSPDGKLLASG--SDDGTVRLWDLAT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 760 LKCLSLLKGhHQRGVCALDFSADGKCLVSVGLDdfHSVVFWDWKKGEKIATTRGHKDKIFVVkcnpqhadklvtvgikhi 839
Cdd:COG2319 194 GKLLRTLTG-HTGAVRSVAFSPDGKLLASGSAD--GTVRLWDLATGKLLRTLTGHSGSVRSV------------------ 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 840 kfwqqagggftskrgSFGSAGKletmmcvsygrmedLVFSGAATGDIFIWkDV---LLLKTVKAHDGPVFAM-YALD-KG 914
Cdd:COG2319 253 ---------------AFSPDGR--------------LLASGSADGTVRLW-DLatgELLRTLTGHSGGVNSVaFSPDgKL 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 915 FVTGGKDGIVELWDdmferclktyaikrtalstsskglllednpsiraitlghghilvgTKNGEILEIdksgpmtllVQG 994
Cdd:COG2319 303 LASGSDDGTVRLWD---------------------------------------------LATGKLLRT---------LTG 328
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081602 995 HmEGEVWGLAAHPLLPICATVSDDKTLRIWELSSQHRMLAVRKLKKGGRCCAFSPDGKALAVGLNDGSFLVVNADT 1070
Cdd:COG2319 329 H-TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
228-466 |
1.31e-20 |
|
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: 94.32 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 228 LVRTIQGaHSAGIFSL--YACEEGFATGGRDGCIRLWDTDFKpitkiDLRETEQGYKGlSIRSVCWKAD--RLLAGTQDS 303
Cdd:cd00200 1 LRRTLKG-HTGGVTCVafSPDGKLLATGSGDGTIKVWDLETG-----ELLRTLKGHTG-PVRDVAASADgtYLASGSSDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 304 EIFevIVRERDKPML-ILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWSLADHALIARCNM-EEAVRSVSFSPDGSQL 381
Cdd:cd00200 74 TIR--LWDLETGECVrTLTGH-TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDGTFV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 382 ALGMKDGSFIVLRVRDMTEVVHIKDRKEVIHEMKFSPDGSYLAVGSNDGPVDVYAVAQRyKKIGECNKSLSFITHIDWSL 461
Cdd:cd00200 151 ASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCLGTLRGHENGVNSVAFSP 229
|
....*
gi 1907081602 462 DSKYL 466
Cdd:cd00200 230 DGYLL 234
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-48 |
5.49e-20 |
|
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: 85.68 E-value: 5.49e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1907081602 2 ADRTAPRCQLRLEWVYGYRGHQCRNNLYYTAGKEVVYFVAGVGVVYN 48
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
667-714 |
5.70e-20 |
|
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: 85.68 E-value: 5.70e-20
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1907081602 667 KREKAPEDSLKLQFIHGYRGYDCRNNLFYTQAGEVVYHIAAVAVVYNR 714
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1599-1963 |
6.14e-20 |
|
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: 92.40 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1599 KAHTGPVFTMYTTLRDGLIVTGGkerptkEGGAVKLWDQEMKRC-RAFQLETGQlVECVRSVCRGKgKILVGTKDGEIIE 1677
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGS------GDGTIKVWDLETGELlRTLKGHTGP-VRDVAASADGT-YLASGSSDKTIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1678 VGEKSAASNILIDGHmEGEIWGLATHPSKDMFISASNDGTARIWDLADKKLLnKVNLGH--AARCAAYSPDGEMVAIGMK 1755
Cdd:cd00200 78 WDLETGECVRTLTGH-TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCL-TTLRGHtdWVNSVAFSPDGTFVASSSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1756 NGefvillvnTLKVW----GKKRDR----KSAIQDIRISPDNRFLAVGSSEQTVDFYDLTQGTSLNRIGYCKDipsFVIQ 1827
Cdd:cd00200 156 DG--------TIKLWdlrtGKCVATltghTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHEN---GVNS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1828 MDFSADSKYIqvstgaykrqvhevplgkqvteamvvekitwaswTSVLGDEVIGIWprnadkadvncacvthaglNIVTG 1907
Cdd:cd00200 225 VAFSPDGYLL----------------------------------ASGSEDGTIRVW-------------------DLRTG 251
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907081602 1908 DdfgllklfdfpctekfaKHKRYFGHSAHVTNIRFSSDDKYVVStGGDDCSVFVWR 1963
Cdd:cd00200 252 E-----------------CVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
894-1220 |
2.01e-19 |
|
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: 90.86 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 894 LLKTVKAHDGPVFAMYALDKG--FVTGGKDGIVELWD---DMFERCLKTYAIKRTALSTSSKGLLL----EDNpSIRait 964
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGklLATGSGDGTIKVWDletGELLRTLKGHTGPVRDVAASADGTYLasgsSDK-TIR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 965 lghghiLVGTKNGEILEIdksgpmtllVQGHmEGEVWGLAAHPLLPICATVSDDKTLRIWELSSQHRMLAVRKLKKGGRC 1044
Cdd:cd00200 77 ------LWDLETGECVRT---------LTGH-TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1045 CAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAVASHDNFVDIYNVLTSKRVGICKGAS 1124
Cdd:cd00200 141 VAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPD-GEKLLSSSSDGTIKLWDLSTGKCLGTLRGHE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1125 SYITHIDWDSRGKLLQvnSGAKEQlffeaprgrkhTIRpseaekiEWDTWTCVLGPTCEGiwpaHSdvTDVNAANLTKDG 1204
Cdd:cd00200 220 NGVNSVAFSPDGYLLA--SGSEDG-----------TIR-------VWDLRTGECVQTLSG----HT--NSVTSLAWSPDG 273
|
330
....*....|....*.
gi 1907081602 1205 SLLATGDDFGFVKLFS 1220
Cdd:cd00200 274 KRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1689-1963 |
2.01e-19 |
|
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: 90.86 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1689 IDGHmEGEIWGLATHPSKDMFISASNDGTARIWDLADKKLLnKVNLGHAA--RCAAYSPDGEMVAIGMKNgefvillvNT 1766
Cdd:cd00200 5 LKGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-RTLKGHTGpvRDVAASADGTYLASGSSD--------KT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1767 LKVW----GKKRDR----KSAIQDIRISPDNRFLAVGSSEQTVDFYDLTQGTSLNRIGYCKDipsFVIQMDFSADSKYiq 1838
Cdd:cd00200 75 IRLWdletGECVRTltghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD---WVNSVAFSPDGTF-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1839 VSTGAYKRQVH--EVPLGKqvteamVVEKITwaswtsvlgdevigiwprnADKADVNCACVTHAGLNIVTGDDFGLLKLF 1916
Cdd:cd00200 150 VASSSQDGTIKlwDLRTGK------CVATLT-------------------GHTGEVNSVAFSPDGEKLLSSSSDGTIKLW 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907081602 1917 DFpctEKFAKHKRYFGHSAHVTNIRFSSDDKYVVStGGDDCSVFVWR 1963
Cdd:cd00200 205 DL---STGKCLGTLRGHENGVNSVAFSPDGYLLAS-GSEDGTIRVWD 247
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
46-177 |
8.20e-16 |
|
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: 80.07 E-value: 8.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 46 VYNTREHS-QKFFLGHNDDIISLALHPDKTLIATGQVGKEpyICIWNSYNVHTVSILKdVHTHGVACLAFDSDGQHLASV 124
Cdd:cd00200 161 LWDLRTGKcVATLTGHTGEVNSVAFSPDGEKLLSSSSDGT--IKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASG 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907081602 125 GLDakNTVCIWDWRKGKLLASATGHSDRIFDISWDPyQPNRMVSCGV-KHIKFW 177
Cdd:cd00200 238 SED--GTIRVWDLRTGECVQTLSGHTNSVTSLAWSP-DGKRLASGSAdGTIRIW 288
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
55-179 |
5.10e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 79.57 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 55 KFFLGHNDDIISLALHPDKTLIATGqvGKEPYICIWNSYNVHTVSILKDvHTHGVACLAFDSDGQHLASVGLDakNTVCI 134
Cdd:COG2319 282 RTLTGHSGGVNSVAFSPDGKLLASG--SDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKTLASGSDD--GTVRL 356
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907081602 135 WDWRKGKLLASATGHSDRIFDISWDPyQPNRMVSCGV-KHIKFWTL 179
Cdd:COG2319 357 WDLATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSAdGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1405-1636 |
1.05e-14 |
|
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: 76.99 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1405 IVQNLSTGSQSFYLE-HTDDILCLTVNQHPKYrnVVATSQIGTtpsIHIWDAMTKHTLSMLRCfHTKGVNYINFSATGKL 1483
Cdd:cd00200 76 RLWDLETGECVRTLTgHTSYVSSVAFSPDGRI--LSSSSRDKT---IKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1484 LVSVGVDpeHTITVWRWQEGTKVASRGGHLERIFVVEFRPDSDTQFVSVGVKHMKFWTLAGSALLykkGVIGSMEAAkmq 1563
Cdd:cd00200 150 VASSSQD--GTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL---GTLRGHENG--- 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907081602 1564 tMLSVAFGANNLTFTGA-INGDVYVWK-EHFLIRLVAKAHTGPVFTMYTTLRDGLIVTGGkerptkEGGAVKLWD 1636
Cdd:cd00200 222 -VNSVAFSPDGYLLASGsEDGTIRVWDlRTGECVQTLSGHTNSVTSLAWSPDGKRLASGS------ADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
520-825 |
4.89e-14 |
|
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: 74.68 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 520 INSVDANYNSSVLVSGDDFGLVKLFKfpcLKKGAKFRKYVGHSAHVTNVRWSHDFQWVLStGGADHSVFQWRfipeaVSN 599
Cdd:cd00200 12 VTCVAFSPDGKLLATGSGDGTIKVWD---LETGELLRTLKGHTGPVRDVAASADGTYLAS-GSSDKTIRLWD-----LET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 600 GVLETTpQEGgadsyseesdsDFSDVpeLDSDIEQETQI----NYDRQVYKEDLPQLKQQSKEKNHavpflkrekapEDS 675
Cdd:cd00200 83 GECVRT-LTG-----------HTSYV--SSVAFSPDGRIlsssSRDKTIKVWDVETGKCLTTLRGH-----------TDW 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 676 LklqfihgyrgydcrNNLFYTQAGEVVYHIAA--VAVVYN-RQQHAQRLYLGHDDDILSLTIHPVKDYVATGqvGRDAAV 752
Cdd:cd00200 138 V--------------NSVAFSPDGTFVASSSQdgTIKLWDlRTGKCVATLTGHTGEVNSVAFSPDGEKLLSS--SSDGTI 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907081602 753 HVWDTQTLKCLSLLKGhHQRGVCALDFSADGKCLVSVGLDdfHSVVFWDWKKGEKIATTRGHKDKIFVVKCNP 825
Cdd:cd00200 202 KLWDLSTGKCLGTLRG-HENGVNSVAFSPDGYLLASGSED--GTIRVWDLRTGECVQTLSGHTNSVTSLAWSP 271
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1039-1265 |
3.78e-13 |
|
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: 71.98 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1039 KKGGRCCAFSPDGKALAVGLNDGSFLVVNADTVEDMLSFHHRKEMISDIKFSKDtGKYLAVASHDNFVDIYNVLTSKRVG 1118
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASAD-GTYLASGSSDKTIRLWDLETGECVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1119 ICKGASSYITHIDWDSRGKLLqvnSGAkeqlffeaprGRKHTIRpseaekiEWDTWTcvlgPTCEGIWPAHSDvtDVNAA 1198
Cdd:cd00200 88 TLTGHTSYVSSVAFSPDGRIL---SSS----------SRDKTIK-------VWDVET----GKCLTTLRGHTD--WVNSV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907081602 1199 NLTKDGSLLATGDDFGFVKLFSyPVKGQhaRFKKYVGHSAHVTNVRWlHNDSVLLTVGGADTALMIW 1265
Cdd:cd00200 142 AFSPDGTFVASSSQDGTIKLWD-LRTGK--CVATLTGHTGEVNSVAF-SPDGEKLLSSSSDGTIKLW 204
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1357-1408 |
7.91e-13 |
|
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: 65.27 E-value: 7.91e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1907081602 1357 KNNITKKKKLVEE-LALDHVFGYRGFDCRNNLHYLNDGaDIIFHTAAAGIVQN 1408
Cdd:pfam03451 20 KDDLDQKKEPPDKkLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYD 71
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1182-1540 |
2.62e-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: 54.26 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1182 CEGIWPAHSDVtdVNAANLTKDGSLLATGDDFGFVKLFSYPVKGQHARFKkyvGHSAHVTNVRWLHNDSVLLTvGGADTA 1261
Cdd:cd00200 1 LRRTLKGHTGG--VTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK---GHTGPVRDVAASADGTYLAS-GSSDKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1262 LMIW---TREFVGTQEsklvdseesdtdaeedgGYDSDVareKAIDYTTKIYAVSiremeGTKPHQQLK--EVSMEERQG 1336
Cdd:cd00200 75 IRLWdleTGECVRTLT-----------------GHTSYV---SSVAFSPDGRILS-----SSSRDKTIKvwDVETGKCLT 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1337 IVKGSRPPVSRAAPQPEKlqknnitkkkklveelalDHVFGYRgfdcrnnlhylNDGADIIFHTAAAGIVQNLSTgsqsf 1416
Cdd:cd00200 130 TLRGHTDWVNSVAFSPDG------------------TFVASSS-----------QDGTIKLWDLRTGKCVATLTG----- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1417 yleHTDDILCLTVnqHPKYRNVVATSQIGTtpsIHIWDAMTKHTLSMLRcFHTKGVNYINFSATGKLLVSVGVDpeHTIT 1496
Cdd:cd00200 176 ---HTGEVNSVAF--SPDGEKLLSSSSDGT---IKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASGSED--GTIR 244
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1907081602 1497 VWRWQEGTKVASRGGHLERIFVVEFRPDSdTQFVSVGV-KHMKFW 1540
Cdd:cd00200 245 VWDLRTGECVQTLSGHTNSVTSLAWSPDG-KRLASGSAdGTIRIW 288
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1079-1265 |
7.39e-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: 7.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1079 HRKEmISDIKFSKDtGKYLAVASHDNFVDIYNVLTSKRVGICKGASSYITHIDWDSRGKLLQVNSGAKeqlffeaprgrk 1158
Cdd:cd00200 8 HTGG-VTCVAFSPD-GKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDK------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1159 hTIRpseaekiEWDTWTcvlgPTCEGIWPAHSDvtDVNAANLTKDGSLLATGDDFGFVKLFSYPVKGQHARFKkyvGHSA 1238
Cdd:cd00200 74 -TIR-------LWDLET----GECVRTLTGHTS--YVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLR---GHTD 136
|
170 180
....*....|....*....|....*..
gi 1907081602 1239 HVTNVRWLHNDSvLLTVGGADTALMIW 1265
Cdd:cd00200 137 WVNSVAFSPDGT-FVASSSQDGTIKLW 162
|
|
| COG4946 |
COG4946 |
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown] ... |
368-466 |
1.32e-04 |
|
Uncharacterized N-terminal domain of tricorn protease, contains WD40 repeats [Function unknown];
Pssm-ID: 443973 [Multi-domain] Cd Length: 1072 Bit Score: 47.34 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 368 AVRSVSFSPDGSQLA-LGMKDGSF-IVLR--VRDMTEVVHIKDRKEVIHEMKFSPDGSYLAVGSNDGPVDVYAVA-QRYK 442
Cdd:COG4946 344 RERLPAWSPDGKSIAyFSDASGEYeLYIApaDGSGEPKQLTLGDLGRVFNPVWSPDGKKIAFTDNRGRLWVVDLAsGKVR 423
|
90 100
....*....|....*....|....
gi 1907081602 443 KIGECNKSLSFIThIDWSLDSKYL 466
Cdd:COG4946 424 KVDTDGYGDGISD-LAWSPDSKWL 446
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
105-136 |
2.33e-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: 40.37 E-value: 2.33e-04
10 20 30
....*....|....*....|....*....|..
gi 1907081602 105 HTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:smart00320 11 HTGPVTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1689-1722 |
2.78e-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: 39.99 E-value: 2.78e-04
10 20 30
....*....|....*....|....*....|....
gi 1907081602 1689 IDGHmEGEIWGLATHPSKDMFISASNDGTARIWD 1722
Cdd:smart00320 8 LKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
1698-1794 |
3.29e-04 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 44.30 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1698 WGLATHPSKD-MFISASNDGTARIWDLADKKLLNKVNLGHAARCAAYSPDGEMVAIGMKNGEFVILLV-----NTLKVWg 1771
Cdd:COG3391 113 RGLAVDPDGGrLYVADSGNGRVSVIDTATGKVVATIPVGAGPHGIAVDPDGKRLYVANSGSNTVSVIVsvidtATGKVV- 191
|
90 100
....*....|....*....|...
gi 1907081602 1772 KKRDRKSAIQDIRISPDNRFLAV 1794
Cdd:COG3391 192 ATIPVGGGPVGVAVSPDGRRLYV 214
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1689-1722 |
5.60e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 5.60e-04
10 20 30
....*....|....*....|....*....|....
gi 1907081602 1689 IDGHmEGEIWGLATHPSKDMFISASNDGTARIWD 1722
Cdd:pfam00400 7 LEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
315-353 |
7.53e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.87 E-value: 7.53e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1907081602 315 KPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWS 353
Cdd:pfam00400 2 KLLKTLEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
1709-1837 |
8.66e-04 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 43.14 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1709 FISASNDGTARIWDLADKKLLNKVNLGHAARCAAYSPDGEMVAI-GMKNGEFVILLVNTLKVWGKKRDRKSAiQDIRISP 1787
Cdd:COG3391 83 YVANSGSGRVSVIDLATGKVVATIPVGGGPRGLAVDPDGGRLYVaDSGNGRVSVIDTATGKVVATIPVGAGP-HGIAVDP 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907081602 1788 DNRFLAVGSSEQT-----VDFYDLTQGTSLNRIgyckDIPSFVIQMDFSADSKYI 1837
Cdd:COG3391 162 DGKRLYVANSGSNtvsviVSVIDTATGKVVATI----PVGGGPVGVAVSPDGRRL 212
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
105-136 |
9.91e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 9.91e-04
10 20 30
....*....|....*....|....*....|..
gi 1907081602 105 HTHGVACLAFDSDGQHLASVGLDakNTVCIWD 136
Cdd:pfam00400 10 HTGSVTSLAFSPDGKLLASGSDD--GTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
759-801 |
1.42e-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: 38.06 E-value: 1.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1907081602 759 TLKCLSLLKGHhQRGVCALDFSADGKCLVSVGLDdfHSVVFWD 801
Cdd:smart00320 1 SGELLKTLKGH-TGPVTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1923-1962 |
1.42e-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: 38.06 E-value: 1.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1907081602 1923 KFAKHKRYFGHSAHVTNIRFSSDDKYVVStGGDDCSVFVW 1962
Cdd:smart00320 1 SGELLKTLKGHTGPVTSVAFSPDGKYLAS-GSDDGTIKLW 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1928-1962 |
1.61e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 37.71 E-value: 1.61e-03
10 20 30
....*....|....*....|....*....|....*
gi 1907081602 1928 KRYFGHSAHVTNIRFSSDDKYVVStGGDDCSVFVW 1962
Cdd:pfam00400 5 KTLEGHTGSVTSLAFSPDGKLLAS-GSDDGTVKVW 38
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
315-353 |
1.77e-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: 37.68 E-value: 1.77e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1907081602 315 KPMLILQGHcEGELWALALHPKKPLAVTGSDDRSVRLWS 353
Cdd:smart00320 3 ELLKTLKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
1741-1823 |
5.58e-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: 38.03 E-value: 5.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907081602 1741 AAYSPDGEMVAIGMKNGEFVILLVNTLKVWGKKRD-RKSAIQDIRISPDNRFLAVGSSEQTVDFYDLTQGTSLNRIGYCK 1819
Cdd:pfam12894 1 MSWCPTMDLIALATEDGELLLHRLNWQRVWTLSPDkEDLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGS 80
|
....
gi 1907081602 1820 DIPS 1823
Cdd:pfam12894 81 DLIT 84
|
|
| |
