|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
725-1063 |
4.97e-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.
The actual alignment was detected with superfamily member cd00200:
Pssm-ID: 475233 [Multi-domain] Cd Length: 289 Bit Score: 135.93 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 725 GHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWDWK 804
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKGHTG-PVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 805 KGEKLSIARGSKDKIFVVKMNPYvpDKLITAGIKH--MKFWRKAGGGLIGRkgyigTLGKNDTMMCAVYGWTEEMAFSGT 882
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVETGKCLTT-----LRGHTDWVNSVAFSPDGTFVASSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 883 STGDVCIW--RDIFLVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTYaikraalapgskgllledn 958
Cdd:cd00200 155 QDGTIKLWdlRTGKCVATLTGHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGTL------------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 959 psiraislghghilvgtkngeilevdksgpitllvQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRK 1038
Cdd:cd00200 216 -----------------------------------RGH-ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG 259
|
330 340
....*....|....*....|....*
gi 767979965 1039 LKKGGRCCCFSPDGKALAVGLNDGS 1063
Cdd:cd00200 260 HTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
5.20e-31 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 127.33 E-value: 5.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 58 RGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 218 GDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETdqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 293 --GDHILVGTQDSEIFeIVVQERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPI 369
Cdd:COG2319 256 pdGRLLASGSADGTVR-LWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979965 370 RCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
895-1266 |
1.17e-23 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 105.38 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 895 LVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTY-----AIKRAALAPGSKglllednpsiraislg 967
Cdd:COG2319 70 LLATLLGHTAAVLSVAFSPDGrlLASASADGTVRLWDLATGLLLRTLtghtgAVRSVAFSPDGK---------------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 968 hgHILVGTKNGEILEVD-KSGPITLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLSPSHCMLAVRKLKKGG 1043
Cdd:COG2319 134 --TLASGSADGTVRLWDlATGKLLRTLTGH-SGAVTSVAFSPdgkLL---ASGSDDGTVRLWDLATGKLLRTLTGHTGAV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1044 RCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNVMSSKRVGICKG 1123
Cdd:COG2319 208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGELLRTLTG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1124 ATSYITHIDWDIRGKLLqvntgakeqlffeAPRGKKQTIpsveveKIawasWTSVLGLCcegIWPVIGEVTDVTASCLTS 1203
Cdd:COG2319 287 HSGGVNSVAFSPDGKLL-------------ASGSDDGTV------RL----WDLATGKL---LRTLTGHTGAVRSVAFSP 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979965 1204 DKMVLATGDDLGFVKLFRYPTKGKFGKFKryvAHSTHVTNVRWTYDDSMLVTlGGTDMSLMVW 1266
Cdd:COG2319 341 DGKTLASGSDDGTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
5.67e-19 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
:
Pssm-ID: 460922 Cd Length: 72 Bit Score: 82.60 E-value: 5.67e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767979965 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
7.28e-18 |
|
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: 79.13 E-value: 7.28e-18
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767979965 672 APGNSIRLHFVHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNR 715
Cdd:pfam03451 29 PPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1339-1410 |
7.10e-15 |
|
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: 70.66 E-value: 7.10e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979965 1339 VRGSRPPVSraPPQPEKLQTNNVGKKKRPIEDLVLELIFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1410
Cdd:pfam03451 4 IRGRPGAVY--PPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1407-1556 |
4.91e-12 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.94 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1407 LHNVATGSQSF-YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSIHIWDAMNKQTLSILRcYHSKGVCSVSF 1485
Cdd:COG2319 188 LWDLATGKLLRtLTGHTGAVRSVAFSPDGKLL---ASG----SAD-----GTVRLWDLATGKLLRTLT-GHSGSVRSVAF 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979965 1486 SATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTqFVSVGV-KHVKFWTLAGRALL 1556
Cdd:COG2319 255 SPDGRLLASGSAD--GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKL-LASGSDdGTVRLWDLATGKLL 323
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
725-1063 |
4.97e-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: 135.93 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 725 GHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWDWK 804
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKGHTG-PVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 805 KGEKLSIARGSKDKIFVVKMNPYvpDKLITAGIKH--MKFWRKAGGGLIGRkgyigTLGKNDTMMCAVYGWTEEMAFSGT 882
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVETGKCLTT-----LRGHTDWVNSVAFSPDGTFVASSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 883 STGDVCIW--RDIFLVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTYaikraalapgskgllledn 958
Cdd:cd00200 155 QDGTIKLWdlRTGKCVATLTGHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGTL------------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 959 psiraislghghilvgtkngeilevdksgpitllvQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRK 1038
Cdd:cd00200 216 -----------------------------------RGH-ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG 259
|
330 340
....*....|....*....|....*
gi 767979965 1039 LKKGGRCCCFSPDGKALAVGLNDGS 1063
Cdd:cd00200 260 HTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
720-1112 |
3.32e-34 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 136.96 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 720 QRFYLGHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVV 799
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTGHTGA-VRSVAFSPDGKTLASGSAD--GTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 800 LWDWKKGEKLSIARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRKAGGGLIgrkgyigtlgkndtmmcavygwtee 876
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSP---DgkLLASGSDdGTVRLWDLATGKLL------------------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 877 mafsgtstgdvciwrdiflvKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTYAikraalapgskgll 954
Cdd:COG2319 198 --------------------RTLTGHTGAVRSVAFSPDGklLASGSADGTVRLWDLATGKLLRTLT-------------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 955 lEDNPSIRAISLGH-GHILV-GTKNGEILEVD-KSGPITLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLS 1028
Cdd:COG2319 244 -GHSGSVRSVAFSPdGRLLAsGSADGTVRLWDlATGELLRTLTGH-SGGVNSVAFSPdgkLL---ASGSDDGTVRLWDLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1029 PSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFID 1108
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVR 397
|
....
gi 767979965 1109 IYNV 1112
Cdd:COG2319 398 LWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
5.20e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 127.33 E-value: 5.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 58 RGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 218 GDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETdqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 293 --GDHILVGTQDSEIFeIVVQERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPI 369
Cdd:COG2319 256 pdGRLLASGSADGTVR-LWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979965 370 RCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
57-353 |
1.32e-30 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 123.21 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 57 YRGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKdVHTHGIACLAFDLDGQRLVSVGLDskNAVCVWD 136
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGT--IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSD--KTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 137 WKRGKMLSMAPGHTDRIFDISWDlyqPNK--LVSCGV-KHIKFWSLcgNALTPKRGVFGKTGDlqtILCLACARDE-LTY 212
Cdd:cd00200 80 LETGECVRTLTGHTSYVSSVAFS---PDGriLSSSSRdKTIKVWDV--ETGKCLTTLRGHTDW---VNSVAFSPDGtFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 213 SGALNGDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDlretdqgYKGLSVR 287
Cdd:cd00200 152 SSSQDGTIKLWdlRTGKCVATLTG-HTGEVNSVAFSPDGekLLSSSSDGTIKLWDLsTGKCLGTLR-------GHENGVN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 288 SVCW--RGDHILVGTQDS--EIFEIVVQERNKPFlimQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:cd00200 224 SVAFspDGYLLASGSEDGtiRVWDLRTGECVQTL---SGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
895-1266 |
1.17e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 105.38 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 895 LVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTY-----AIKRAALAPGSKglllednpsiraislg 967
Cdd:COG2319 70 LLATLLGHTAAVLSVAFSPDGrlLASASADGTVRLWDLATGLLLRTLtghtgAVRSVAFSPDGK---------------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 968 hgHILVGTKNGEILEVD-KSGPITLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLSPSHCMLAVRKLKKGG 1043
Cdd:COG2319 134 --TLASGSADGTVRLWDlATGKLLRTLTGH-SGAVTSVAFSPdgkLL---ASGSDDGTVRLWDLATGKLLRTLTGHTGAV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1044 RCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNVMSSKRVGICKG 1123
Cdd:COG2319 208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGELLRTLTG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1124 ATSYITHIDWDIRGKLLqvntgakeqlffeAPRGKKQTIpsveveKIawasWTSVLGLCcegIWPVIGEVTDVTASCLTS 1203
Cdd:COG2319 287 HSGGVNSVAFSPDGKLL-------------ASGSDDGTV------RL----WDLATGKL---LRTLTGHTGAVRSVAFSP 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979965 1204 DKMVLATGDDLGFVKLFRYPTKGKFGKFKryvAHSTHVTNVRWTYDDSMLVTlGGTDMSLMVW 1266
Cdd:COG2319 341 DGKTLASGSDDGTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
895-1140 |
2.01e-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: 93.55 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 895 LVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTYAIKRAALApgskglllednpsiRAISLGHGH-I 971
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGklLATGSGDGTIKVWDLETGELLRTLKGHTGPVR--------------DVAASADGTyL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 972 LVGTKNGEILEVDKSGP---ITLlvQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCF 1048
Cdd:cd00200 67 ASGSSDKTIRLWDLETGecvRTL--TGH-TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1049 SPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNVMSSKRVGICKGATSYI 1128
Cdd:cd00200 144 SPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222
|
250
....*....|..
gi 767979965 1129 THIDWDIRGKLL 1140
Cdd:cd00200 223 NSVAFSPDGYLL 234
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
5.67e-19 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 82.60 E-value: 5.67e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767979965 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
7.28e-18 |
|
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: 79.13 E-value: 7.28e-18
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767979965 672 APGNSIRLHFVHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNR 715
Cdd:pfam03451 29 PPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1339-1410 |
7.10e-15 |
|
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: 70.66 E-value: 7.10e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979965 1339 VRGSRPPVSraPPQPEKLQTNNVGKKKRPIEDLVLELIFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1410
Cdd:pfam03451 4 IRGRPGAVY--PPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1407-1556 |
4.91e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.94 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1407 LHNVATGSQSF-YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSIHIWDAMNKQTLSILRcYHSKGVCSVSF 1485
Cdd:COG2319 188 LWDLATGKLLRtLTGHTGAVRSVAFSPDGKLL---ASG----SAD-----GTVRLWDLATGKLLRTLT-GHSGSVRSVAF 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979965 1486 SATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTqFVSVGV-KHVKFWTLAGRALL 1556
Cdd:COG2319 255 SPDGRLLASGSAD--GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKL-LASGSDdGTVRLWDLATGKLL 323
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1418-1556 |
2.55e-10 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 63.12 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1418 YQEHNDDILCLTVNQHPKFInivatgqVGDSADMSatapsIHIWDAMNKQTLSILRCyHSKGVCSVSFSATGKLLLSVGL 1497
Cdd:cd00200 89 LTGHTSYVSSVAFSPDGRIL-------SSSSRDKT-----IKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQ 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767979965 1498 DpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTQFVSVGVKHVKFWTLAGRALL 1556
Cdd:cd00200 156 D--GTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL 212
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
760-802 |
2.57e-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: 2.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767979965 760 TIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:smart00320 1 SGELLKTLKGHTGP-VTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
314-353 |
9.01e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 9.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767979965 314 NKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:pfam00400 1 GKLLKTLEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
315-353 |
1.43e-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: 1.43e-03
10 20 30
....*....|....*....|....*....|....*....
gi 767979965 315 KPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:smart00320 3 ELLKTLKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
762-802 |
3.40e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.55 E-value: 3.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767979965 762 KPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:pfam00400 2 KLLKTLEGHTG-SVTSLAFSPDGKLLASGSDD--GTVKVWD 39
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
725-1063 |
4.97e-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: 135.93 E-value: 4.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 725 GHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWDWK 804
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKGHTG-PVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 805 KGEKLSIARGSKDKIFVVKMNPYvpDKLITAGIKH--MKFWRKAGGGLIGRkgyigTLGKNDTMMCAVYGWTEEMAFSGT 882
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVETGKCLTT-----LRGHTDWVNSVAFSPDGTFVASSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 883 STGDVCIW--RDIFLVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTYaikraalapgskgllledn 958
Cdd:cd00200 155 QDGTIKLWdlRTGKCVATLTGHTGEVNSVAFSPDGekLLSSSSDGTIKLWDLSTGKCLGTL------------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 959 psiraislghghilvgtkngeilevdksgpitllvQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRK 1038
Cdd:cd00200 216 -----------------------------------RGH-ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSG 259
|
330 340
....*....|....*....|....*
gi 767979965 1039 LKKGGRCCCFSPDGKALAVGLNDGS 1063
Cdd:cd00200 260 HTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
720-1112 |
3.32e-34 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 136.96 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 720 QRFYLGHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVV 799
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTGHTGA-VRSVAFSPDGKTLASGSAD--GTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 800 LWDWKKGEKLSIARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRKAGGGLIgrkgyigtlgkndtmmcavygwtee 876
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSP---DgkLLASGSDdGTVRLWDLATGKLL------------------------- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 877 mafsgtstgdvciwrdiflvKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTYAikraalapgskgll 954
Cdd:COG2319 198 --------------------RTLTGHTGAVRSVAFSPDGklLASGSADGTVRLWDLATGKLLRTLT-------------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 955 lEDNPSIRAISLGH-GHILV-GTKNGEILEVD-KSGPITLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLS 1028
Cdd:COG2319 244 -GHSGSVRSVAFSPdGRLLAsGSADGTVRLWDlATGELLRTLTGH-SGGVNSVAFSPdgkLL---ASGSDDGTVRLWDLA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1029 PSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFID 1108
Cdd:COG2319 319 TGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVR 397
|
....
gi 767979965 1109 IYNV 1112
Cdd:COG2319 398 LWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
5.20e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 127.33 E-value: 5.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 58 RGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 218 GDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETdqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 293 --GDHILVGTQDSEIFeIVVQERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPI 369
Cdd:COG2319 256 pdGRLLASGSADGTVR-LWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979965 370 RCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
57-353 |
1.32e-30 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 123.21 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 57 YRGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKdVHTHGIACLAFDLDGQRLVSVGLDskNAVCVWD 136
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGT--IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSD--KTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 137 WKRGKMLSMAPGHTDRIFDISWDlyqPNK--LVSCGV-KHIKFWSLcgNALTPKRGVFGKTGDlqtILCLACARDE-LTY 212
Cdd:cd00200 80 LETGECVRTLTGHTSYVSSVAFS---PDGriLSSSSRdKTIKVWDV--ETGKCLTTLRGHTDW---VNSVAFSPDGtFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 213 SGALNGDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDlretdqgYKGLSVR 287
Cdd:cd00200 152 SSSQDGTIKLWdlRTGKCVATLTG-HTGEVNSVAFSPDGekLLSSSSDGTIKLWDLsTGKCLGTLR-------GHENGVN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 288 SVCW--RGDHILVGTQDS--EIFEIVVQERNKPFlimQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:cd00200 224 SVAFspDGYLLASGSEDGtiRVWDLRTGECVQTL---SGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
52-354 |
2.79e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 125.41 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 52 HRQKFYRGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKDvHTHGIACLAFDLDGQRLVSVGLDskNA 131
Cdd:COG2319 111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT--VRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDD--GT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 132 VCVWDWKRGKMLSMAPGHTDRIFDISWDlyqPN--KLVSCGV-KHIKFWSLcgnaltpKRGVFGKT--GDLQTILCLACA 206
Cdd:COG2319 186 VRLWDLATGKLLRTLTGHTGAVRSVAFS---PDgkLLASGSAdGTVRLWDL-------ATGKLLRTltGHSGSVRSVAFS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 207 RDELT-YSGALNGDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIdlretdQG 280
Cdd:COG2319 256 PDGRLlASGSADGTVRLWdlATGELLRTLTG-HSGGVNSVAFSPDGklLASGSDDGTVRLWDLaTGKLLRTL------TG 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767979965 281 YKGlSVRSVCWR--GDHILVGTQDSEI--FEIvvqERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSL 354
Cdd:COG2319 329 HTG-AVRSVAFSpdGKTLASGSDDGTVrlWDL---ATGELLRTLTGH-TGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
719-1063 |
3.69e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 125.02 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 719 TQRFYLGHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTV 798
Cdd:COG2319 112 LLRTLTGHTGAVRSVAFSPDGKTLASG--SADGTVRLWDLATGKLLRTLTGHSG-AVTSVAFSPDGKLLASGSDD--GTV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 799 VLWDWKKGEKLSIARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRKAGGGLIGrkgyigTLGKNDtmmcavyGWTE 875
Cdd:COG2319 187 RLWDLATGKLLRTLTGHTGAVRSVAFSP---DgkLLASGSAdGTVRLWDLATGKLLR------TLTGHS-------GSVR 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 876 EMAFS--------GTSTGDVCIWR--DIFLVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTYaikr 943
Cdd:COG2319 251 SVAFSpdgrllasGSADGTVRLWDlaTGELLRTLTGHSGGVNSVAFSPDGklLASGSDDGTVRLWDLATGKLLRTL---- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 944 aalapgskglllednpsiraislghghilvgtkngeilevdksgpitllvQGHmEGEVWGLATHPYLPICATVSDDKTLR 1023
Cdd:COG2319 327 --------------------------------------------------TGH-TGAVRSVAFSPDGKTLASGSDDGTVR 355
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 767979965 1024 IWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGS 1063
Cdd:COG2319 356 LWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
260-802 |
9.25e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 117.70 E-value: 9.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 260 RLWDLTFKPITVIDLRETDQGYKGLSVRSVCWRGDHILVGTQDSEIFEIVVQERNKPFLIMQGHcEGELWALAVHPTKPL 339
Cdd:COG2319 14 ADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH-TAAVLSVAFSPDGRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 340 AVTGSDDRSVRIWSLVDHALIARCNM-EEPIRCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSP 418
Cdd:COG2319 93 LASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 419 DGTYLAVGCNDSSVDIYGVAQrykkvGECLGSL----SFITHLDWSSDSRYLQTNDGNGK-RLfYRMPGGKEVTSTEEik 493
Cdd:COG2319 173 DGKLLASGSDDGTVRLWDLAT-----GKLLRTLtghtGAVRSVAFSPDGKLLASGSADGTvRL-WDLATGKLLRTLTG-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 494 gvHWASWTCVSglevngiWpkysdindinSVDGnyigQVLVTADDYGIIKLFRypcLRKGAKFRKYIGHSAHVTNVRWSH 573
Cdd:COG2319 245 --HSGSVRSVA-------F----------SPDG----RLLASGSADGTVRLWD---LATGELLRTLTGHSGGVNSVAFSP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 574 DYQWVISiGGADHSVFQWkfiperklkdavhiapqesladshsdesdsdlsdvpeldseieqetqltyrrqvykedlpql 653
Cdd:COG2319 299 DGKLLAS-GSDDGTVRLW-------------------------------------------------------------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 654 keqckekqksatskrrERAPGNSIRLHfvhgyrgydcrsnlfytqigeivyhvaavgviynrqqntqrfyLGHDDDILCL 733
Cdd:COG2319 316 ----------------DLATGKLLRTL-------------------------------------------TGHTGAVRSV 336
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979965 734 TIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:COG2319 337 AFSPDGKTLASG--SDDGTVRLWDLATGELLRTLTGHTG-AVTSVAFSPDGRTLASGSAD--GTVRLWD 400
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
148-435 |
1.23e-26 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 111.66 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 148 GHTDRIFDISWDlYQPNKLVSCGV-KHIKFWSLCGNalTPKRGVFGKTGDLQTilCLACARDELTYSGALNGDIYVW--K 224
Cdd:cd00200 7 GHTGGVTCVAFS-PDGKLLATGSGdGTIKVWDLETG--ELLRTLKGHTGPVRD--VAASADGTYLASGSSDKTIRLWdlE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 225 GINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIdlretdQGYKGlSVRSVCWRGDHILV--G 299
Cdd:cd00200 82 TGECVRTLTG-HTSYVSSVAFSPDGriLSSSSRDKTIKVWDVeTGKCLTTL------RGHTD-WVNSVAFSPDGTFVasS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 300 TQDSEIFEIVVQErNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPIRCAAVNADG 378
Cdd:cd00200 154 SQDGTIKLWDLRT-GKCVATLTGH-TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRgHENGVNSVAFSPDG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 767979965 379 IHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIY 435
Cdd:cd00200 232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
251-591 |
1.23e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 114.24 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 251 ATGGRDGCIRLWDLTFKPITVIDLRETDqgykglSVRSVCWR--GDHILVGTQDSEI--FEIvvqERNKPFLIMQGHcEG 326
Cdd:COG2319 94 ASASADGTVRLWDLATGLLLRTLTGHTG------AVRSVAFSpdGKTLASGSADGTVrlWDL---ATGKLLRTLTGH-SG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 327 ELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPIRCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIK 405
Cdd:COG2319 164 AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 406 DRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQrykkvGECLGSL----SFITHLDWSSDSRYLQTNDGNGKrlfyrmp 481
Cdd:COG2319 244 GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-----GELLRTLtghsGGVNSVAFSPDGKLLASGSDDGT------- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 482 ggkevtsteeIKGVHWASWTCVSGLEVNGIWpkysdindINSVDGNYIGQVLVTADDYGIIKLFRypcLRKGAKFRKYIG 561
Cdd:COG2319 312 ----------VRLWDLATGKLLRTLTGHTGA--------VRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTG 370
|
330 340 350
....*....|....*....|....*....|
gi 767979965 562 HSAHVTNVRWSHDYQWVISiGGADHSVFQW 591
Cdd:COG2319 371 HTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
895-1266 |
1.17e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 105.38 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 895 LVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTY-----AIKRAALAPGSKglllednpsiraislg 967
Cdd:COG2319 70 LLATLLGHTAAVLSVAFSPDGrlLASASADGTVRLWDLATGLLLRTLtghtgAVRSVAFSPDGK---------------- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 968 hgHILVGTKNGEILEVD-KSGPITLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLSPSHCMLAVRKLKKGG 1043
Cdd:COG2319 134 --TLASGSADGTVRLWDlATGKLLRTLTGH-SGAVTSVAFSPdgkLL---ASGSDDGTVRLWDLATGKLLRTLTGHTGAV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1044 RCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNVMSSKRVGICKG 1123
Cdd:COG2319 208 RSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDLATGELLRTLTG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1124 ATSYITHIDWDIRGKLLqvntgakeqlffeAPRGKKQTIpsveveKIawasWTSVLGLCcegIWPVIGEVTDVTASCLTS 1203
Cdd:COG2319 287 HSGGVNSVAFSPDGKLL-------------ASGSDDGTV------RL----WDLATGKL---LRTLTGHTGAVRSVAFSP 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767979965 1204 DKMVLATGDDLGFVKLFRYPTKGKFGKFKryvAHSTHVTNVRWTYDDSMLVTlGGTDMSLMVW 1266
Cdd:COG2319 341 DGKTLASGSDDGTVRLWDLATGELLRTLT---GHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
712-929 |
7.66e-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: 97.79 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 712 IYNRQQNTQRFYL-GHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQYgVSAVDFSADGKRLASV 790
Cdd:cd00200 77 LWDLETGECVRTLtGHTSYVSSVAFSPDGRILSSS--SRDKTIKVWDVETGKCLTTLRGHTDW-VNSVAFSPDGTFVASS 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 791 GIDdsHTVVLWDWKKGEKLSIARGSKDKIFVVKmnpYVPD--KLITAGI-KHMKFWRKAGGGLigrkgyIGTL-GKNDTM 866
Cdd:cd00200 154 SQD--GTIKLWDLRTGKCVATLTGHTGEVNSVA---FSPDgeKLLSSSSdGTIKLWDLSTGKC------LGTLrGHENGV 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767979965 867 MCAVYGWTEEMAFSGTSTGDVCIW--RDIFLVKTVKAHDGPVFSM--HALEKGFVTGGKDGIVALWD 929
Cdd:cd00200 223 NSVAFSPDGYLLASGSEDGTIRVWdlRTGECVQTLSGHTNSVTSLawSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
228-592 |
1.08e-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: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 228 LIRTIQGaHAAGIFSM--NACEEGFATGGRDGCIRLWDLTFKpitviDLRETDQGYKGlSVRSVCWRGDH--ILVGTQDS 303
Cdd:cd00200 1 LRRTLKG-HTGGVTCVafSPDGKLLATGSGDGTIKVWDLETG-----ELLRTLKGHTG-PVRDVAASADGtyLASGSSDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 304 EIFeIVVQERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCNM-EEPIRCAAVNADGIHLA 382
Cdd:cd00200 74 TIR-LWDLETGECVRTLTGH-TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDGTFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 383 LGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQRyKKVGECLGSLSFITHLDWSSD 462
Cdd:cd00200 152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCLGTLRGHENGVNSVAFSPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 463 SRYLqtndgngkrlfyrmpggkevtsteeikgvhwaswtcvsglevngiwpkysdindinsvdgnyigqvlVTADDYGII 542
Cdd:cd00200 231 GYLL-------------------------------------------------------------------ASGSEDGTI 243
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 767979965 543 KLFRypcLRKGAKFRKYIGHSAHVTNVRWSHDYQWVISiGGADHSVFQWK 592
Cdd:cd00200 244 RVWD---LRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
895-1140 |
2.01e-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: 93.55 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 895 LVKTVKAHDGPVFSMHALEKG--FVTGGKDGIVALWDDSFERCLKTYAIKRAALApgskglllednpsiRAISLGHGH-I 971
Cdd:cd00200 1 LRRTLKGHTGGVTCVAFSPDGklLATGSGDGTIKVWDLETGELLRTLKGHTGPVR--------------DVAASADGTyL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 972 LVGTKNGEILEVDKSGP---ITLlvQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCF 1048
Cdd:cd00200 67 ASGSSDKTIRLWDLETGecvRTL--TGH-TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1049 SPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNVMSSKRVGICKGATSYI 1128
Cdd:cd00200 144 SPDGTFVASSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSP-DGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGV 222
|
250
....*....|..
gi 767979965 1129 THIDWDIRGKLL 1140
Cdd:cd00200 223 NSVAFSPDGYLL 234
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
5.67e-19 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 82.60 E-value: 5.67e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767979965 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
7.28e-18 |
|
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: 79.13 E-value: 7.28e-18
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767979965 672 APGNSIRLHFVHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNR 715
Cdd:pfam03451 29 PPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
943-1552 |
1.08e-16 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 84.19 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 943 RAALAPGSKGLLLEDNPSIRAISLGHGHILVGTKNGEILEVDKSGPITLLVQGHmEGEVWGLATHPYLPICATVSDDKTL 1022
Cdd:COG2319 24 ALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH-TAAVLSVAFSPDGRLLASASADGTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1023 RIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVAS 1102
Cdd:COG2319 103 RLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP-DGKLLASGS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1103 HDSFIDIYNVMSSKRVGICKGATSYITHIDWdirgkllqvntgakeqlffeAPRGKkqtipsvevekiawaswtsvlglc 1182
Cdd:COG2319 182 DDGTVRLWDLATGKLLRTLTGHTGAVRSVAF--------------------SPDGK------------------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1183 cegiwpvigevtdvtascltsdkmVLATGDDLGFVKLFRYPTkGKFGKfkRYVAHSTHVTNVRWTYDDSMLVTlGGTDMS 1262
Cdd:COG2319 218 ------------------------LLASGSADGTVRLWDLAT-GKLLR--TLTGHSGSVRSVAFSPDGRLLAS-GSADGT 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1263 LMVWtnemegyrekrpcdseesDIDSeedggydsdvtreneisytiralstnirpmlgikphlqqkepsiDERQGVVRGS 1342
Cdd:COG2319 270 VRLW------------------DLAT--------------------------------------------GELLRTLTGH 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1343 RPPVsrappqpeklqtnnvgkkkrpiedlvlelifgyrgrdcrNNVHYLNDGddiiyhtasvgilhnvatgsqsfyqehn 1422
Cdd:COG2319 288 SGGV---------------------------------------NSVAFSPDG---------------------------- 300
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1423 ddilcltvnqhpkfiNIVATGqvgdSADmsataPSIHIWDAMNKQTLSILRcYHSKGVCSVSFSATGKLLLSVGLDpeHT 1502
Cdd:COG2319 301 ---------------KLLASG----SDD-----GTVRLWDLATGKLLRTLT-GHTGAVRSVAFSPDGKTLASGSDD--GT 353
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 767979965 1503 ITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTqFVSVGV-KHVKFWTLAG 1552
Cdd:COG2319 354 VRLWDLATGELLRTLTGHTGAVTSVAFSPDGRT-LASGSAdGTVRLWDLAT 403
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1339-1410 |
7.10e-15 |
|
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: 70.66 E-value: 7.10e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979965 1339 VRGSRPPVSraPPQPEKLQTNNVGKKKRPIEDLVLELIFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1410
Cdd:pfam03451 4 IRGRPGAVY--PPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
46-178 |
2.46e-12 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 69.29 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 46 VYSPREHR-QKFYRGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKdVHTHGIACLAFDLDGQRLVSV 124
Cdd:cd00200 161 LWDLRTGKcVATLTGHTGEVNSVAFSPDGEKLLSSSSDGT--IKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASG 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 767979965 125 GLDSKnaVCVWDWKRGKMLSMAPGHTDRIFDISWDlYQPNKLVSCGV-KHIKFWS 178
Cdd:cd00200 238 SEDGT--IRVWDLRTGECVQTLSGHTNSVTSLAWS-PDGKRLASGSAdGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1407-1556 |
4.91e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.94 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1407 LHNVATGSQSF-YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSIHIWDAMNKQTLSILRcYHSKGVCSVSF 1485
Cdd:COG2319 188 LWDLATGKLLRtLTGHTGAVRSVAFSPDGKLL---ASG----SAD-----GTVRLWDLATGKLLRTLT-GHSGSVRSVAF 254
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979965 1486 SATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTqFVSVGV-KHVKFWTLAGRALL 1556
Cdd:COG2319 255 SPDGRLLASGSAD--GTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKL-LASGSDdGTVRLWDLATGKLL 323
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1457-1556 |
5.86e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.55 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1457 SIHIWDAMNKQTLSILRCyHSKGVCSVSFSATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTq 1536
Cdd:COG2319 143 TVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDD--GTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKL- 218
|
90 100
....*....|....*....|.
gi 767979965 1537 FVSVGV-KHVKFWTLAGRALL 1556
Cdd:COG2319 219 LASGSAdGTVRLWDLATGKLL 239
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1407-1556 |
8.88e-12 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 69.17 E-value: 8.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1407 LHNVATGSQ-SFYQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSIHIWDAMNKQTLSILRcYHSKGVCSVSF 1485
Cdd:COG2319 230 LWDLATGKLlRTLTGHSGSVRSVAFSPDGRLL---ASG----SAD-----GTVRLWDLATGELLRTLT-GHSGGVNSVAF 296
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767979965 1486 SATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTqFVSVGV-KHVKFWTLAGRALL 1556
Cdd:COG2319 297 SPDGKLLASGSDD--GTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKT-LASGSDdGTVRLWDLATGELL 365
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1428-1556 |
2.21e-11 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 67.63 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1428 LTVNQHPKFINIVATGQVGDSADMSATAPSIHIWDAMNKQTLSILRcYHSKGVCSVSFSATGKLLLSVGLDpeHTITIWR 1507
Cdd:COG2319 72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 767979965 1508 WQEGAKIASRAGHNQRIFVAEFRPDSdTQFVSVGV-KHVKFWTLAGRALL 1556
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSPDG-KLLASGSDdGTVRLWDLATGKLL 197
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1418-1556 |
2.55e-10 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 63.12 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1418 YQEHNDDILCLTVNQHPKFInivatgqVGDSADMSatapsIHIWDAMNKQTLSILRCyHSKGVCSVSFSATGKLLLSVGL 1497
Cdd:cd00200 89 LTGHTSYVSSVAFSPDGRIL-------SSSSRDKT-----IKVWDVETGKCLTTLRG-HTDWVNSVAFSPDGTFVASSSQ 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 767979965 1498 DpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTQFVSVGVKHVKFWTLAGRALL 1556
Cdd:cd00200 156 D--GTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL 212
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1406-1548 |
4.59e-09 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 59.66 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1406 ILHNVATGSQSF-YQEHNDDILCLTVNQHPKFInivatgqVGDSADMSatapsIHIWDamnkqtLSILRCY-----HSKG 1479
Cdd:cd00200 118 KVWDVETGKCLTtLRGHTDWVNSVAFSPDGTFV-------ASSSQDGT-----IKLWD------LRTGKCVatltgHTGE 179
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767979965 1480 VCSVSFSATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTQFVSVGVKHVKFW 1548
Cdd:cd00200 180 VNSVAFSPDGEKLLSSSSD--GTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVW 246
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1418-1551 |
1.06e-08 |
|
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: 58.50 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1418 YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSIHIWDaMNKQTLSILRCYHSKGVCSVSFSATGKLLLSVGL 1497
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLL---ATG----SGD-----GTIKVWD-LETGELLRTLKGHTGPVRDVAASADGTYLASGSS 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 767979965 1498 DpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSdtQFVSVGVKH--VKFWTLA 1551
Cdd:cd00200 72 D--KTIRLWDLETGECVRTLTGHTSYVSSVAFSPDG--RILSSSSRDktIKVWDVE 123
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1421-1548 |
8.87e-08 |
|
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: 55.42 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1421 HNDDILCLTVnqHPKFINIVATGqvGDSadmsatapSIHIWDAMNKQTLSILRcYHSKGVCSVSFSATGKLLLSVGLDpe 1500
Cdd:cd00200 176 HTGEVNSVAF--SPDGEKLLSSS--SDG--------TIKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASGSED-- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767979965 1501 HTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSdTQFVSVGV-KHVKFW 1548
Cdd:cd00200 241 GTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDG-KRLASGSAdGTIRIW 288
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
993-1507 |
1.01e-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: 52.34 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 993 VQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLMANADTL 1072
Cdd:cd00200 5 LKGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1073 EDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNVMSSKRVGICKGATSYITHIDWDirgkllqvntgakeqlff 1152
Cdd:cd00200 84 ECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFS------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1153 eaprgkkqtipsvevekiawaswtsvlglccegiwpvigevtdvtascltSDKMVLATGDDLGFVKLFRYPTkgkFGKFK 1232
Cdd:cd00200 145 --------------------------------------------------PDGTFVASSSQDGTIKLWDLRT---GKCVA 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1233 RYVAHSTHVTNVRWTYDDSMLVTlGGTDMSLMVWtnemegyrekrpcdseesDIDSEEdggydsdvtreneisytirals 1312
Cdd:cd00200 172 TLTGHTGEVNSVAFSPDGEKLLS-SSSDGTIKLW------------------DLSTGK---------------------- 210
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1313 tnirpmlgikphlqqkepsiderqgvvrgsrppvsrappqpeKLQTnnvgkkkrpiedlvlelifgyrgrdcrnnvhyln 1392
Cdd:cd00200 211 ------------------------------------------CLGT---------------------------------- 214
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1393 dgddiiyhtasvgilhnvatgsqsfYQEHNDDILCLTVNQHPKFInivatgqVGDSADmsataPSIHIWDAMNKQTLSIL 1472
Cdd:cd00200 215 -------------------------LRGHENGVNSVAFSPDGYLL-------ASGSED-----GTIRVWDLRTGECVQTL 257
|
490 500 510
....*....|....*....|....*....|....*
gi 767979965 1473 RCyHSKGVCSVSFSATGKLLLSVGLDpeHTITIWR 1507
Cdd:cd00200 258 SG-HTNSVTSLAWSPDGKRLASGSAD--GTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1476-1557 |
9.35e-05 |
|
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: 46.17 E-value: 9.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 1476 HSKGVCSVSFSATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSdTQFVSVGV-KHVKFWTLAGRA 1554
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGD--GTIKVWDLETGELLRTLKGHTGPVRDVAASADG-TYLASGSSdKTIRLWDLETGE 84
|
...
gi 767979965 1555 LLS 1557
Cdd:cd00200 85 CVR 87
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
760-802 |
2.57e-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: 2.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 767979965 760 TIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:smart00320 1 SGELLKTLKGHTGP-VTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
314-353 |
9.01e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.48 E-value: 9.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 767979965 314 NKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:pfam00400 1 GKLLKTLEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
315-353 |
1.43e-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: 1.43e-03
10 20 30
....*....|....*....|....*....|....*....
gi 767979965 315 KPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:smart00320 3 ELLKTLKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
250-354 |
1.57e-03 |
|
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.
Pssm-ID: 439303 [Multi-domain] Cd Length: 325 Bit Score: 42.60 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767979965 250 FATGGRDGCIRLWDLTF--KPITVIDLRETdqGYKGLSVRSvcwRGDHILVGTQDSEIFEIVVQErNKPFLIMQGHCEGE 327
Cdd:cd22857 195 IVTGTGYHQVRLYDTRAqrRPVVSVDFGET--PIKAVAEDP---DGHTVYVGDTSGDLASIDLRT-GKLLGCFKGKCGGS 268
|
90 100
....*....|....*....|....*..
gi 767979965 328 LWALAVHPTKPLAVTGSDDRSVRIWSL 354
Cdd:cd22857 269 IRSIARHPELPLIASCGLDRYLRIWDT 295
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
994-1026 |
2.18e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 37.29 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|...
gi 767979965 994 QGHmEGEVWGLATHPYLPICATVSDDKTLRIWD 1026
Cdd:smart00320 9 KGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
762-802 |
3.40e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.55 E-value: 3.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 767979965 762 KPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:pfam00400 2 KLLKTLEGHTG-SVTSLAFSPDGKLLASGSDD--GTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
994-1026 |
8.51e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.40 E-value: 8.51e-03
10 20 30
....*....|....*....|....*....|...
gi 767979965 994 QGHmEGEVWGLATHPYLPICATVSDDKTLRIWD 1026
Cdd:pfam00400 8 EGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| |
