|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
720-1074 |
7.14e-38 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 148.14 E-value: 7.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 720 QRFYLGHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVV 799
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTGHTGA-VRSVAFSPDGKTLASGSAD--GTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 800 LWDWKKGEKLSIARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRKAGDVCIWrdiflvkTVKAHDGPVFSMHALEK 876
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSP---DgkLLASGSDdGTVRLWDLATGKLLR-------TLTGHTGAVRSVAFSPD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 877 G--FVTGGKDGIVALWDDSFERCLKTYAikraalapgskglllEDNPSIRAISLGH-GHILV-GTKNGEILEVD-KSGPI 951
Cdd:COG2319 216 GklLASGSADGTVRLWDLATGKLLRTLT---------------GHSGSVRSVAFSPdGRLLAsGSADGTVRLWDlATGEL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 952 TLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLM 1028
Cdd:COG2319 281 LRTLTGH-SGGVNSVAFSPdgkLL---ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2217296595 1029 ANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNV 1074
Cdd:COG2319 357 WDLATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
9.40e-31 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.95 E-value: 9.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 58 RGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 218 GDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETdqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 293 --GDHILVGTQDSEIFeIVVQERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPI 369
Cdd:COG2319 256 pdGRLLASGSADGTVR-LWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217296595 370 RCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1382-1769 |
1.21e-30 |
|
WD40 repeat [General function prediction only];
:
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.56 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1382 LTVNQHPKFINIVATGQVGDSADMSATAPSIHIWDAMNKQTLSILRcYHSKGVCSVSFSATGKLLLSVGLDpeHTITIWR 1461
Cdd:COG2319 72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1462 WQEGAKIASRAGHNQRIFVAEFRPDSdTQFVSVGV-KHVKFWTLAGRALLSkkgllsTLEdARMQTMLAIAFGANNLTF- 1539
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSPDG-KLLASGSDdGTVRLWDLATGKLLR------TLT-GHTGAVRSVAFSPDGKLLa 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1540 TGTISGDVCVWK-DHILCRIVARAHNGPVFAMyTTLRDG-LIVTGGkerpskEGGAVKLWDqelrrcrafrLETGQatdC 1617
Cdd:COG2319 221 SGSADGTVRLWDlATGKLLRTLTGHSGSVRSV-AFSPDGrLLASGS------ADGTVRLWD----------LATGE---L 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1618 VRSVcrgkgkilvgtrnaeiievgeknaacnilvnGHVDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVNlG 1697
Cdd:COG2319 281 LRTL-------------------------------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-G 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217296595 1698 HAA--RTVCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCAIHDIRFSPDSRYLAVGSSENSVDFYDLT 1769
Cdd:COG2319 329 HTGavRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
6.91e-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: 6.91e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217296595 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
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 ... |
1651-1924 |
2.96e-18 |
|
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: 87.39 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1651 VNGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLnKVNLGHAA--RTVCYSPEGDMVAIGMKNGefiillvsS 1728
Cdd:cd00200 5 LKGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-RTLKGHTGpvRDVAASADGTYLASGSSDK--------T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1729 LKIWgKKRDRRC---------AIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRISYCKDipsFVIQMDFSADSSYl 1799
Cdd:cd00200 75 IRLW-DLETGECvrtltghtsYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD---WVNSVAFSPDGTF- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1800 qVSSGCYKR--HVYEVPSGKHLMDHaaidritwatwtsilgdevlgiwsrHAEKADVNCACVSHSGISLVTGDDFGMVKL 1877
Cdd:cd00200 150 -VASSSQDGtiKLWDLRTGKCVATL-------------------------TGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2217296595 1878 FDfpcPEKFAKHKRFLGHSPHVTNIRFtSGDRHVVSAGGDDCSLFVW 1924
Cdd:cd00200 204 WD---LSTGKCLGTLRGHENGVNSVAF-SPDGYLLASGSEDGTIRVW 246
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
8.88e-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: 8.88e-18
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217296595 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 ... |
1317-1364 |
1.30e-14 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
:
Pssm-ID: 460922 Cd Length: 72 Bit Score: 70.27 E-value: 1.30e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217296595 1317 KKKRPIEDLVLELIFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1364
Cdd:pfam03451 26 KKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
720-1074 |
7.14e-38 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 148.14 E-value: 7.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 720 QRFYLGHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVV 799
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTGHTGA-VRSVAFSPDGKTLASGSAD--GTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 800 LWDWKKGEKLSIARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRKAGDVCIWrdiflvkTVKAHDGPVFSMHALEK 876
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSP---DgkLLASGSDdGTVRLWDLATGKLLR-------TLTGHTGAVRSVAFSPD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 877 G--FVTGGKDGIVALWDDSFERCLKTYAikraalapgskglllEDNPSIRAISLGH-GHILV-GTKNGEILEVD-KSGPI 951
Cdd:COG2319 216 GklLASGSADGTVRLWDLATGKLLRTLT---------------GHSGSVRSVAFSPdGRLLAsGSADGTVRLWDlATGEL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 952 TLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLM 1028
Cdd:COG2319 281 LRTLTGH-SGGVNSVAFSPdgkLL---ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2217296595 1029 ANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNV 1074
Cdd:COG2319 357 WDLATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
725-1025 |
4.16e-34 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 133.61 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 725 GHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWDWK 804
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKGHTG-PVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 805 KGEKLSIARGSKDKIFVVKMNPYvpDKLITAGikhmkfwRKAGDVCIW--RDIFLVKTVKAHDGPVFSMHALE-KGFVTG 881
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPD--GRILSSS-------SRDKTIKVWdvETGKCLTTLRGHTDWVNSVAFSPdGTFVAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 882 GK-DGIVALWDDSFERCLKTYaikraalaPGSKGlllednpSIRAISLGH--GHILVGTKNGEILEVDKSGPITL-LVQG 957
Cdd:cd00200 153 SSqDGTIKLWDLRTGKCVATL--------TGHTG-------EVNSVAFSPdgEKLLSSSSDGTIKLWDLSTGKCLgTLRG 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217296595 958 HmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGS 1025
Cdd:cd00200 218 H-ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
9.40e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.95 E-value: 9.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 58 RGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 218 GDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETdqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 293 --GDHILVGTQDSEIFeIVVQERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPI 369
Cdd:COG2319 256 pdGRLLASGSADGTVR-LWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217296595 370 RCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1382-1769 |
1.21e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.56 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1382 LTVNQHPKFINIVATGQVGDSADMSATAPSIHIWDAMNKQTLSILRcYHSKGVCSVSFSATGKLLLSVGLDpeHTITIWR 1461
Cdd:COG2319 72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1462 WQEGAKIASRAGHNQRIFVAEFRPDSdTQFVSVGV-KHVKFWTLAGRALLSkkgllsTLEdARMQTMLAIAFGANNLTF- 1539
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSPDG-KLLASGSDdGTVRLWDLATGKLLR------TLT-GHTGAVRSVAFSPDGKLLa 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1540 TGTISGDVCVWK-DHILCRIVARAHNGPVFAMyTTLRDG-LIVTGGkerpskEGGAVKLWDqelrrcrafrLETGQatdC 1617
Cdd:COG2319 221 SGSADGTVRLWDlATGKLLRTLTGHSGSVRSV-AFSPDGrLLASGS------ADGTVRLWD----------LATGE---L 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1618 VRSVcrgkgkilvgtrnaeiievgeknaacnilvnGHVDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVNlG 1697
Cdd:COG2319 281 LRTL-------------------------------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-G 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217296595 1698 HAA--RTVCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCAIHDIRFSPDSRYLAVGSSENSVDFYDLT 1769
Cdd:COG2319 329 HTGavRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
57-353 |
4.94e-30 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 121.67 E-value: 4.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 57 YRGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKdVHTHGIACLAFDLDGQRLVSVGLDskNAVCVWD 136
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGT--IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSD--KTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 137 WKRGKMLSMAPGHTDRIFDISWDlyqPNK--LVSCGV-KHIKFWSLcgNALTPKRGVFGKTGDlqtILCLACARDE-LTY 212
Cdd:cd00200 80 LETGECVRTLTGHTSYVSSVAFS---PDGriLSSSSRdKTIKVWDV--ETGKCLTTLRGHTDW---VNSVAFSPDGtFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 213 SGALNGDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDlretdqgYKGLSVR 287
Cdd:cd00200 152 SSSQDGTIKLWdlRTGKCVATLTG-HTGEVNSVAFSPDGekLLSSSSDGTIKLWDLsTGKCLGTLR-------GHENGVN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 288 SVCW--RGDHILVGTQDS--EIFEIVVQERNKPFlimQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:cd00200 224 SVAFspDGYLLASGSEDGtiRVWDLRTGECVQTL---SGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1430-1732 |
8.12e-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: 94.71 E-value: 8.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1430 HSKGVCSVSFSATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSdTQFVSVGV-KHVKFWTLagra 1508
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGD--GTIKVWDLETGELLRTLKGHTGPVRDVAASADG-TYLASGSSdKTIRLWDL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1509 llSKKGLLSTLEDARmQTMLAIAFGANNLTFTGTIS-GDVCVWK-DHILCRIVARAHNGPVFAMyTTLRDGLIVTGgker 1586
Cdd:cd00200 81 --ETGECVRTLTGHT-SYVSSVAFSPDGRILSSSSRdKTIKVWDvETGKCLTTLRGHTDWVNSV-AFSPDGTFVAS---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1587 pSKEGGAVKLWD-QELRRCRAFRLETGQatdcVRSVC--RGKGKILVGTRNAEIIEVGEKNAACNILVNGHvDGPIWGLA 1663
Cdd:cd00200 153 -SSQDGTIKLWDlRTGKCVATLTGHTGE----VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-ENGVNSVA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217296595 1664 THPSRDFFLSAAEDGTVRLWDIADKKMLNKVNlGHAAR--TVCYSPEGDMVAIGMKNGefiillvsSLKIW 1732
Cdd:cd00200 227 FSPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSvtSLAWSPDGKRLASGSADG--------TIRIW 288
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
6.91e-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: 6.91e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217296595 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1651-1924 |
2.96e-18 |
|
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: 87.39 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1651 VNGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLnKVNLGHAA--RTVCYSPEGDMVAIGMKNGefiillvsS 1728
Cdd:cd00200 5 LKGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-RTLKGHTGpvRDVAASADGTYLASGSSDK--------T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1729 LKIWgKKRDRRC---------AIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRISYCKDipsFVIQMDFSADSSYl 1799
Cdd:cd00200 75 IRLW-DLETGECvrtltghtsYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD---WVNSVAFSPDGTF- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1800 qVSSGCYKR--HVYEVPSGKHLMDHaaidritwatwtsilgdevlgiwsrHAEKADVNCACVSHSGISLVTGDDFGMVKL 1877
Cdd:cd00200 150 -VASSSQDGtiKLWDLRTGKCVATL-------------------------TGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2217296595 1878 FDfpcPEKFAKHKRFLGHSPHVTNIRFtSGDRHVVSAGGDDCSLFVW 1924
Cdd:cd00200 204 WD---LSTGKCLGTLRGHENGVNSVAF-SPDGYLLASGSEDGTIRVW 246
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
8.88e-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: 8.88e-18
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217296595 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 ... |
1317-1364 |
1.30e-14 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 70.27 E-value: 1.30e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217296595 1317 KKKRPIEDLVLELIFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1364
Cdd:pfam03451 26 KKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1663-1929 |
2.72e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 61.47 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1663 ATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVNLGHAARTVC-YSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCA 1741
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLaASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1742 IHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRIsycKDIPSFVIQMDFSADSSYLqVSSGCYKR-HVYEVPSGKhlm 1820
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTL---TGHTGAVRSVAFSPDGKTL-ASGSADGTvRLWDLATGK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1821 dhaaidritwatwtsilgdeVLGIWSRHAEkaDVNCACVSHSGISLVTGDDFGMVKLFDfpcPEKFAKHKRFLGHSPHVT 1900
Cdd:COG2319 154 --------------------LLRTLTGHSG--AVTSVAFSPDGKLLASGSDDGTVRLWD---LATGKLLRTLTGHTGAVR 208
|
250 260 270
....*....|....*....|....*....|....
gi 2217296595 1901 NIRFTSGDRHVVSaGGDDCSLFVW-----KCVHT 1929
Cdd:COG2319 209 SVAFSPDGKLLAS-GSADGTVRLWdlatgKLLRT 241
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
1703-1785 |
1.64e-05 |
|
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: 44.96 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1703 VCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRR-CAIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRISYCK 1781
Cdd:pfam12894 1 MSWCPTMDLIALATEDGELLLHRLNWQRVWTLSPDKEdLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGS 80
|
....
gi 2217296595 1782 DIPS 1785
Cdd:pfam12894 81 DLIT 84
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
760-802 |
4.33e-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: 39.60 E-value: 4.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217296595 760 TIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:smart00320 1 SGELLKTLKGHTGP-VTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1652-1684 |
4.73e-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: 39.22 E-value: 4.73e-04
10 20 30
....*....|....*....|....*....|...
gi 2217296595 1652 NGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWD 1684
Cdd:smart00320 9 KGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
314-353 |
1.46e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.10 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2217296595 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 |
2.43e-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: 37.29 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2217296595 315 KPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:smart00320 3 ELLKTLKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
762-802 |
5.62e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.17 E-value: 5.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2217296595 762 KPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:pfam00400 2 KLLKTLEGHTG-SVTSLAFSPDGKLLASGSDD--GTVKVWD 39
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
720-1074 |
7.14e-38 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 148.14 E-value: 7.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 720 QRFYLGHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVV 799
Cdd:COG2319 71 LATLLGHTAAVLSVAFSPDGRLLASA--SADGTVRLWDLATGLLLRTLTGHTGA-VRSVAFSPDGKTLASGSAD--GTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 800 LWDWKKGEKLSIARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRKAGDVCIWrdiflvkTVKAHDGPVFSMHALEK 876
Cdd:COG2319 146 LWDLATGKLLRTLTGHSGAVTSVAFSP---DgkLLASGSDdGTVRLWDLATGKLLR-------TLTGHTGAVRSVAFSPD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 877 G--FVTGGKDGIVALWDDSFERCLKTYAikraalapgskglllEDNPSIRAISLGH-GHILV-GTKNGEILEVD-KSGPI 951
Cdd:COG2319 216 GklLASGSADGTVRLWDLATGKLLRTLT---------------GHSGSVRSVAFSPdGRLLAsGSADGTVRLWDlATGEL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 952 TLLVQGHmEGEVWGLATHP---YLpicATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGSFLM 1028
Cdd:COG2319 281 LRTLTGH-SGGVNSVAFSPdgkLL---ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2217296595 1029 ANADTLEDLVSFHHRKDMISDIRFSPgSGKYLAVASHDSFIDIYNV 1074
Cdd:COG2319 357 WDLATGELLRTLTGHTGAVTSVAFSP-DGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
725-1025 |
4.16e-34 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 133.61 E-value: 4.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 725 GHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWDWK 804
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATG--SGDGTIKVWDLETGELLRTLKGHTG-PVRDVAASADGTYLASGSSD--KTIRLWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 805 KGEKLSIARGSKDKIFVVKMNPYvpDKLITAGikhmkfwRKAGDVCIW--RDIFLVKTVKAHDGPVFSMHALE-KGFVTG 881
Cdd:cd00200 82 TGECVRTLTGHTSYVSSVAFSPD--GRILSSS-------SRDKTIKVWdvETGKCLTTLRGHTDWVNSVAFSPdGTFVAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 882 GK-DGIVALWDDSFERCLKTYaikraalaPGSKGlllednpSIRAISLGH--GHILVGTKNGEILEVDKSGPITL-LVQG 957
Cdd:cd00200 153 SSqDGTIKLWDLRTGKCVATL--------TGHTG-------EVNSVAFSPdgEKLLSSSSDGTIKLWDLSTGKCLgTLRG 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217296595 958 HmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGS 1025
Cdd:cd00200 218 H-ENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
719-1025 |
2.46e-33 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 134.65 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 719 TQRFYLGHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTV 798
Cdd:COG2319 112 LLRTLTGHTGAVRSVAFSPDGKTLASG--SADGTVRLWDLATGKLLRTLTGHSG-AVTSVAFSPDGKLLASGSDD--GTV 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 799 VLWDWKKGEKLSIARGSKDKIFVVKMNPyvpD--KLITAGI-KHMKFWRKAGDVCIwrdiflvKTVKAHDGPVFSMHALE 875
Cdd:COG2319 187 RLWDLATGKLLRTLTGHTGAVRSVAFSP---DgkLLASGSAdGTVRLWDLATGKLL-------RTLTGHSGSVRSVAFSP 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 876 KG--FVTGGKDGIVALWDDSFERCLKTY-----AIKRAALAPGSKglllednpsiraislghgHILVGTKNGEILEVD-K 947
Cdd:COG2319 257 DGrlLASGSADGTVRLWDLATGELLRTLtghsgGVNSVAFSPDGK------------------LLASGSDDGTVRLWDlA 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217296595 948 SGPITLLVQGHmEGEVWGLATHPYLPICATVSDDKTLRIWDLSPSHCMLAVRKLKKGGRCCCFSPDGKALAVGLNDGS 1025
Cdd:COG2319 319 TGKLLRTLTGH-TGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGT 395
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
58-438 |
9.40e-31 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.95 E-value: 9.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 58 RGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKDvHTHGIACLAFDLDGQRLVSVGLDskNAVCVWDW 137
Cdd:COG2319 75 LGHTAAVLSVAFSPDGRLLASASADGT--VRLWDLATGLLLRTLTG-HTGAVRSVAFSPDGKTLASGSAD--GTVRLWDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 138 KRGKMLSMAPGHTDRIFDISWDlyqPNklvscgvkhikfwslcgnaltpkrgvfGKTgdlqtilcLAcardeltySGALN 217
Cdd:COG2319 150 ATGKLLRTLTGHSGAVTSVAFS---PD---------------------------GKL--------LA--------SGSDD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 218 GDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDLRETdqgykglSVRSVCWR 292
Cdd:COG2319 184 GTVRLWdlATGKLLRTLTG-HTGAVRSVAFSPDGklLASGSADGTVRLWDLaTGKLLRTLTGHSG-------SVRSVAFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 293 --GDHILVGTQDSEIFeIVVQERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPI 369
Cdd:COG2319 256 pdGRLLASGSADGTVR-LWDLATGELLRTLTGH-SGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAV 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217296595 370 RCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVA 438
Cdd:COG2319 334 RSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1382-1769 |
1.21e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 126.56 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1382 LTVNQHPKFINIVATGQVGDSADMSATAPSIHIWDAMNKQTLSILRcYHSKGVCSVSFSATGKLLLSVGLDpeHTITIWR 1461
Cdd:COG2319 72 ATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLT-GHTGAVRSVAFSPDGKTLASGSAD--GTVRLWD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1462 WQEGAKIASRAGHNQRIFVAEFRPDSdTQFVSVGV-KHVKFWTLAGRALLSkkgllsTLEdARMQTMLAIAFGANNLTF- 1539
Cdd:COG2319 149 LATGKLLRTLTGHSGAVTSVAFSPDG-KLLASGSDdGTVRLWDLATGKLLR------TLT-GHTGAVRSVAFSPDGKLLa 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1540 TGTISGDVCVWK-DHILCRIVARAHNGPVFAMyTTLRDG-LIVTGGkerpskEGGAVKLWDqelrrcrafrLETGQatdC 1617
Cdd:COG2319 221 SGSADGTVRLWDlATGKLLRTLTGHSGSVRSV-AFSPDGrLLASGS------ADGTVRLWD----------LATGE---L 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1618 VRSVcrgkgkilvgtrnaeiievgeknaacnilvnGHVDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVNlG 1697
Cdd:COG2319 281 LRTL-------------------------------TGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-G 328
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217296595 1698 HAA--RTVCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCAIHDIRFSPDSRYLAVGSSENSVDFYDLT 1769
Cdd:COG2319 329 HTGavRSVAFSPDGKTLASGSDDGTVRLWDLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLA 402
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
57-353 |
4.94e-30 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 121.67 E-value: 4.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 57 YRGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKdVHTHGIACLAFDLDGQRLVSVGLDskNAVCVWD 136
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLLATGSGDGT--IKVWDLETGELLRTLK-GHTGPVRDVAASADGTYLASGSSD--KTIRLWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 137 WKRGKMLSMAPGHTDRIFDISWDlyqPNK--LVSCGV-KHIKFWSLcgNALTPKRGVFGKTGDlqtILCLACARDE-LTY 212
Cdd:cd00200 80 LETGECVRTLTGHTSYVSSVAFS---PDGriLSSSSRdKTIKVWDV--ETGKCLTTLRGHTDW---VNSVAFSPDGtFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 213 SGALNGDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIDlretdqgYKGLSVR 287
Cdd:cd00200 152 SSSQDGTIKLWdlRTGKCVATLTG-HTGEVNSVAFSPDGekLLSSSSDGTIKLWDLsTGKCLGTLR-------GHENGVN 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 288 SVCW--RGDHILVGTQDS--EIFEIVVQERNKPFlimQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:cd00200 224 SVAFspDGYLLASGSEDGtiRVWDLRTGECVQTL---SGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
52-354 |
4.95e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 125.02 E-value: 4.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 52 HRQKFYRGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKDvHTHGIACLAFDLDGQRLVSVGLDskNA 131
Cdd:COG2319 111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT--VRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDD--GT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 132 VCVWDWKRGKMLSMAPGHTDRIFDISWDlyqPN--KLVSCGV-KHIKFWSLcgnaltpKRGVFGKT--GDLQTILCLACA 206
Cdd:COG2319 186 VRLWDLATGKLLRTLTGHTGAVRSVAFS---PDgkLLASGSAdGTVRLWDL-------ATGKLLRTltGHSGSVRSVAFS 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 207 RDELT-YSGALNGDIYVW--KGINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIdlretdQG 280
Cdd:COG2319 256 PDGRLlASGSADGTVRLWdlATGELLRTLTG-HSGGVNSVAFSPDGklLASGSDDGTVRLWDLaTGKLLRTL------TG 328
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217296595 281 YKGlSVRSVCWR--GDHILVGTQDSEI--FEIvvqERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSL 354
Cdd:COG2319 329 HTG-AVRSVAFSpdGKTLASGSDDGTVrlWDL---ATGELLRTLTGH-TGAVTSVAFSPDGRTLASGSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
260-802 |
1.58e-27 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 117.32 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 260 RLWDLTFKPITVIDLRETDQGYKGLSVRSVCWRGDHILVGTQDSEIFEIVVQERNKPFLIMQGHcEGELWALAVHPTKPL 339
Cdd:COG2319 14 ADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGH-TAAVLSVAFSPDGRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 340 AVTGSDDRSVRIWSLVDHALIARCNM-EEPIRCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSP 418
Cdd:COG2319 93 LASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSGAVTSVAFSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 419 DGTYLAVGCNDSSVDIYGVAQrykkvGECLGSL----SFITHLDWSSDSRYLQTNDGNGK-RLfYRMPGGKEVTSTEEik 493
Cdd:COG2319 173 DGKLLASGSDDGTVRLWDLAT-----GKLLRTLtghtGAVRSVAFSPDGKLLASGSADGTvRL-WDLATGKLLRTLTG-- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 494 gvHWASWTCVSglevngiWpkysdindinSVDGnyigQVLVTADDYGIIKLFRypcLRKGAKFRKYIGHSAHVTNVRWSH 573
Cdd:COG2319 245 --HSGSVRSVA-------F----------SPDG----RLLASGSADGTVRLWD---LATGELLRTLTGHSGGVNSVAFSP 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 574 DYQWVISiGGADHSVFQWkfiperklkdavhiapqesladshsdesdsdlsdvpeldseieqetqltyrrqvykedlpql 653
Cdd:COG2319 299 DGKLLAS-GSDDGTVRLW-------------------------------------------------------------- 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 654 keqckekqksatskrrERAPGNSIRLHfvhgyrgydcrsnlfytqigeivyhvaavgviynrqqntqrfyLGHDDDILCL 733
Cdd:COG2319 316 ----------------DLATGKLLRTL-------------------------------------------TGHTGAVRSV 336
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217296595 734 TIHPLKDYVATGqvGRDPSIHIWDTETIKPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:COG2319 337 AFSPDGKTLASG--SDDGTVRLWDLATGELLRTLTGHTG-AVTSVAFSPDGRTLASGSAD--GTVRLWD 400
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1456-1924 |
1.78e-27 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 117.32 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1456 TITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTQFVSVGVKHVKFWTLAGRALLSkkgllsTLEDARMQTMLAIAFGAN 1535
Cdd:COG2319 17 ALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLA------TLLGHTAAVLSVAFSPDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1536 NLTFTGTISGDVCVWK-DHILCRIVARAHNGPVFAMyTTLRDG-LIVTGGkerpskEGGAVKLWDqelrrcrafrLETGQ 1613
Cdd:COG2319 91 RLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSV-AFSPDGkTLASGS------ADGTVRLWD----------LATGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1614 atdcvrsvcrgkgkiLVGTrnaeiievgeknaacnilVNGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLNK 1693
Cdd:COG2319 154 ---------------LLRT------------------LTGH-SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1694 VNlGHAA--RTVCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCAIHDIRFSPDSRYLAVGSSENSVDFYDLTLG 1771
Cdd:COG2319 200 LT-GHTGavRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1772 PTLNRIsycKDIPSFVIQMDFSADSSYLqVSSGCYKR-HVYEVPSGKhlmdhaaidritwatwtsilgdeVLGIWSRHAe 1850
Cdd:COG2319 279 ELLRTL---TGHSGGVNSVAFSPDGKLL-ASGSDDGTvRLWDLATGK-----------------------LLRTLTGHT- 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217296595 1851 kADVNCACVSHSGISLVTGDDFGMVKLFDfpcPEKFAKHKRFLGHSPHVTNIRFTSGDRHVVSaGGDDCSLFVW 1924
Cdd:COG2319 331 -GAVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
251-591 |
1.88e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 114.24 E-value: 1.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 251 ATGGRDGCIRLWDLTFKPITVIDLRETDqgykglSVRSVCWR--GDHILVGTQDSEI--FEIvvqERNKPFLIMQGHcEG 326
Cdd:COG2319 94 ASASADGTVRLWDLATGLLLRTLTGHTG------AVRSVAFSpdGKTLASGSADGTVrlWDL---ATGKLLRTLTGH-SG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 327 ELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPIRCAAVNADGIHLALGMKDGSFTVLRVRDMTEVVHIK 405
Cdd:COG2319 164 AVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTgHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 406 DRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQrykkvGECLGSL----SFITHLDWSSDSRYLQTNDGNGKrlfyrmp 481
Cdd:COG2319 244 GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-----GELLRTLtghsGGVNSVAFSPDGKLLASGSDDGT------- 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 482 ggkevtsteeIKGVHWASWTCVSGLEVNGIWpkysdindINSVDGNYIGQVLVTADDYGIIKLFRypcLRKGAKFRKYIG 561
Cdd:COG2319 312 ----------VRLWDLATGKLLRTLTGHTGA--------VRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTG 370
|
330 340 350
....*....|....*....|....*....|
gi 2217296595 562 HSAHVTNVRWSHDYQWVISiGGADHSVFQW 591
Cdd:COG2319 371 HTGAVTSVAFSPDGRTLAS-GSADGTVRLW 399
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
148-435 |
3.85e-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: 110.50 E-value: 3.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 148 GHTDRIFDISWDlYQPNKLVSCGV-KHIKFWSLCGNalTPKRGVFGKTGDLQTilCLACARDELTYSGALNGDIYVW--K 224
Cdd:cd00200 7 GHTGGVTCVAFS-PDGKLLATGSGdGTIKVWDLETG--ELLRTLKGHTGPVRD--VAASADGTYLASGSSDKTIRLWdlE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 225 GINLIRTIQGaHAAGIFSMNACEEG--FATGGRDGCIRLWDL-TFKPITVIdlretdQGYKGlSVRSVCWRGDHILV--G 299
Cdd:cd00200 82 TGECVRTLTG-HTSYVSSVAFSPDGriLSSSSRDKTIKVWDVeTGKCLTTL------RGHTD-WVNSVAFSPDGTFVasS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 300 TQDSEIFEIVVQErNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCN-MEEPIRCAAVNADG 378
Cdd:cd00200 154 SQDGTIKLWDLRT-GKCVATLTGH-TGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRgHENGVNSVAFSPDG 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2217296595 379 IHLALGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIY 435
Cdd:cd00200 232 YLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1411-1687 |
9.98e-25 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 108.85 E-value: 9.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1411 SIHIWDAMNKQTLSILRCyHSKGVCSVSFSATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTq 1490
Cdd:COG2319 143 TVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDD--GTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKL- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1491 FVSVGV-KHVKFWTLAGRALLSkkgllsTLEDARmQTMLAIAFGANNLTF-TGTISGDVCVWK-DHILCRIVARAHNGPV 1567
Cdd:COG2319 219 LASGSAdGTVRLWDLATGKLLR------TLTGHS-GSVRSVAFSPDGRLLaSGSADGTVRLWDlATGELLRTLTGHSGGV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1568 FAMYTTLRDGLIVTGGkerpskEGGAVKLWDQELRRC-RAFRLETGQatdcVRSVC-RGKGKILVGTRNAEIIEVGE-KN 1644
Cdd:COG2319 292 NSVAFSPDGKLLASGS------DDGTVRLWDLATGKLlRTLTGHTGA----VRSVAfSPDGKTLASGSDDGTVRLWDlAT 361
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2217296595 1645 AACNILVNGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWDIAD 1687
Cdd:COG2319 362 GELLRTLTGH-TGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1382-1879 |
8.31e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 106.15 E-value: 8.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1382 LTVNQHPKFINIVATGQVGDSADMSATAPSIHIWDAMNKQTLSILRcYHSKGVCSVSFSATGKLLLSVGLDpeHTITIWR 1461
Cdd:COG2319 30 LLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLL-GHTAAVLSVAFSPDGRLLASASAD--GTVRLWD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1462 WQEGAKIASRAGHNQRIFVAEFRPDSDTqFVSVGV-KHVKFWTLAGRALLSkkgllstledarmqtmlaiafgannlTFT 1540
Cdd:COG2319 107 LATGLLLRTLTGHTGAVRSVAFSPDGKT-LASGSAdGTVRLWDLATGKLLR--------------------------TLT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1541 GtisgdvcvwkdhilcrivaraHNGPVFAMyTTLRDG-LIVTGGkerpskEGGAVKLWDqelrrcrafrLETGQatdCVR 1619
Cdd:COG2319 160 G---------------------HSGAVTSV-AFSPDGkLLASGS------DDGTVRLWD----------LATGK---LLR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1620 SVcrgkgkilvgtrnaeiievgeknaacnilvNGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVNlGHA 1699
Cdd:COG2319 199 TL------------------------------TGH-TGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLT-GHS 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1700 A--RTVCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCAIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRI 1777
Cdd:COG2319 247 GsvRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1778 sycKDIPSFVIQMDFSADSSYLQVSSGCYKRHVYEVPSGKhlmdhaaidritwatwtsilgdeVLGIWSRHAekADVNCA 1857
Cdd:COG2319 327 ---TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGE-----------------------LLRTLTGHT--GAVTSV 378
|
490 500
....*....|....*....|..
gi 2217296595 1858 CVSHSGISLVTGDDFGMVKLFD 1879
Cdd:COG2319 379 AFSPDGRTLASGSADGTVRLWD 400
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1430-1732 |
8.12e-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: 94.71 E-value: 8.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1430 HSKGVCSVSFSATGKLLLSVGLDpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSdTQFVSVGV-KHVKFWTLagra 1508
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGD--GTIKVWDLETGELLRTLKGHTGPVRDVAASADG-TYLASGSSdKTIRLWDL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1509 llSKKGLLSTLEDARmQTMLAIAFGANNLTFTGTIS-GDVCVWK-DHILCRIVARAHNGPVFAMyTTLRDGLIVTGgker 1586
Cdd:cd00200 81 --ETGECVRTLTGHT-SYVSSVAFSPDGRILSSSSRdKTIKVWDvETGKCLTTLRGHTDWVNSV-AFSPDGTFVAS---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1587 pSKEGGAVKLWD-QELRRCRAFRLETGQatdcVRSVC--RGKGKILVGTRNAEIIEVGEKNAACNILVNGHvDGPIWGLA 1663
Cdd:cd00200 153 -SSQDGTIKLWDlRTGKCVATLTGHTGE----VNSVAfsPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGH-ENGVNSVA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217296595 1664 THPSRDFFLSAAEDGTVRLWDIADKKMLNKVNlGHAAR--TVCYSPEGDMVAIGMKNGefiillvsSLKIW 1732
Cdd:cd00200 227 FSPDGYLLASGSEDGTIRVWDLRTGECVQTLS-GHTNSvtSLAWSPDGKRLASGSADG--------TIRIW 288
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
228-592 |
3.24e-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: 93.17 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 228 LIRTIQGaHAAGIFSM--NACEEGFATGGRDGCIRLWDLTFKpitviDLRETDQGYKGlSVRSVCWRGDH--ILVGTQDS 303
Cdd:cd00200 1 LRRTLKG-HTGGVTCVafSPDGKLLATGSGDGTIKVWDLETG-----ELLRTLKGHTG-PVRDVAASADGtyLASGSSDK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 304 EIFeIVVQERNKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWSLVDHALIARCNM-EEPIRCAAVNADGIHLA 382
Cdd:cd00200 74 TIR-LWDLETGECVRTLTGH-TSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGhTDWVNSVAFSPDGTFVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 383 LGMKDGSFTVLRVRDMTEVVHIKDRKEAIHELKYSPDGTYLAVGCNDSSVDIYGVAQRyKKVGECLGSLSFITHLDWSSD 462
Cdd:cd00200 152 SSSQDGTIKLWDLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCLGTLRGHENGVNSVAFSPD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 463 SRYLqtndgngkrlfyrmpggkevtsteeikgvhwaswtcvsglevngiwpkysdindinsvdgnyigqvlVTADDYGII 542
Cdd:cd00200 231 GYLL-------------------------------------------------------------------ASGSEDGTI 243
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2217296595 543 KLFRypcLRKGAKFRKYIGHSAHVTNVRWSHDYQWVISiGGADHSVFQWK 592
Cdd:cd00200 244 RVWD---LRTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIWD 289
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
2-49 |
6.91e-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: 6.91e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217296595 2 AARSAPSCHLRLEWVYGYRGHQCRNNLYYTAAKEIVYFVAGVGVVYSP 49
Cdd:pfam03451 25 QKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1651-1924 |
2.96e-18 |
|
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: 87.39 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1651 VNGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLnKVNLGHAA--RTVCYSPEGDMVAIGMKNGefiillvsS 1728
Cdd:cd00200 5 LKGH-TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELL-RTLKGHTGpvRDVAASADGTYLASGSSDK--------T 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1729 LKIWgKKRDRRC---------AIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRISYCKDipsFVIQMDFSADSSYl 1799
Cdd:cd00200 75 IRLW-DLETGECvrtltghtsYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTD---WVNSVAFSPDGTF- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1800 qVSSGCYKR--HVYEVPSGKHLMDHaaidritwatwtsilgdevlgiwsrHAEKADVNCACVSHSGISLVTGDDFGMVKL 1877
Cdd:cd00200 150 -VASSSQDGtiKLWDLRTGKCVATL-------------------------TGHTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2217296595 1878 FDfpcPEKFAKHKRFLGHSPHVTNIRFtSGDRHVVSAGGDDCSLFVW 1924
Cdd:cd00200 204 WD---LSTGKCLGTLRGHENGVNSVAF-SPDGYLLASGSEDGTIRVW 246
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
672-715 |
8.88e-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: 8.88e-18
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2217296595 672 APGNSIRLHFVHGYRGYDCRSNLFYTQIGEIVYHVAAVGVIYNR 715
Cdd:pfam03451 29 PPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1372-1684 |
2.03e-17 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 84.69 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1372 YQEHNDDILCLTVNQHPKFInivATGqvgdSADmsataPSIHIWDaMNKQTLSILRCYHSKGVCSVSFSATGKLLLSVGL 1451
Cdd:cd00200 5 LKGHTGGVTCVAFSPDGKLL---ATG----SGD-----GTIKVWD-LETGELLRTLKGHTGPVRDVAASADGTYLASGSS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1452 DpeHTITIWRWQEGAKIASRAGHNQRIFVAEFRPDSDTQFVSVGVKHVKFWTLAgrallsKKGLLSTLEDARMQTMlAIA 1531
Cdd:cd00200 72 D--KTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVE------TGKCLTTLRGHTDWVN-SVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1532 F-GANNLTFTGTISGDVCVWKDHIL-CRIVARAHNGPVFAMYTTLRDGLIVTGGkerpskEGGAVKLWDQELRRCRA-FR 1608
Cdd:cd00200 143 FsPDGTFVASSSQDGTIKLWDLRTGkCVATLTGHTGEVNSVAFSPDGEKLLSSS------SDGTIKLWDLSTGKCLGtLR 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217296595 1609 LETGQATDCVRSvcrGKGKILVGTRNAEIIEVGE-KNAACNILVNGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWD 1684
Cdd:cd00200 217 GHENGVNSVAFS---PDGYLLASGSEDGTIRVWDlRTGECVQTLSGH-TNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
444-891 |
9.51e-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: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 444 VGECLGSLSFITHLDWSSDSRYLQTNDGNGKRLFYRMPGGKEVTS-TEEIKGVHWASWtcvsglevngiwpkysdindin 522
Cdd:cd00200 2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAA---------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 523 SVDGNYIgqvLVTADDyGIIKLFRypcLRKGAKFRKYIGHSAHVTNVRWSHDYQWVISiGGADHSVFQWKFIPERKLKDa 602
Cdd:cd00200 60 SADGTYL---ASGSSD-KTIRLWD---LETGECVRTLTGHTSYVSSVAFSPDGRILSS-SSRDKTIKVWDVETGKCLTT- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 603 vhiapqesladshsdesdsdlsdvpeldseieqetqltyrrqvykedlpqlkeqckekqksatskrrerapgnsirlhfv 682
Cdd:cd00200 --------------------------------------------------------------------------------
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 683 hgyrgydcrsnlfytqigeivyhvaavgviynrqqntqrfYLGHDDDILCLTIHPLKDYVATGqvGRDPSIHIWDTETIK 762
Cdd:cd00200 131 ----------------------------------------LRGHTDWVNSVAFSPDGTFVASS--SQDGTIKLWDLRTGK 168
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 763 PLSILKGhHQYGVSAVDFSADGKRLASVGIDDshTVVLWDWKKGEKLSIARGSKDKIFVVKMNPyvPDKLITAGIK--HM 840
Cdd:cd00200 169 CVATLTG-HTGEVNSVAFSPDGEKLLSSSSDG--TIKLWDLSTGKCLGTLRGHENGVNSVAFSP--DGYLLASGSEdgTI 243
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2217296595 841 KFWRKAGDVCiwrdiflVKTVKAHDGPVFSM--HALEKGFVTGGKDGIVALWD 891
Cdd:cd00200 244 RVWDLRTGEC-------VQTLSGHTNSVTSLawSPDGKRLASGSADGTIRIWD 289
|
|
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
1317-1364 |
1.30e-14 |
|
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm Microtubule-Associated Protein, so-named for its abundance in sea urchin, sand dollar and starfish eggs. The Hydrophobic EMAP-Like Protein (HELP) motif was identified initially in the human EMAP-Like Protein 2 (EML2) and subsequently in the entire EMAP Protein family. The HELP motif is approximately 60-70 amino acids in length and is conserved amongst metazoans. Although the HELP motif is hydrophobic, there is no evidence that EMAP-Like Proteins are membrane-associated. All members of the EMAP-Like Protein family, identified to-date, are constructed with an amino terminal HELP motif followed by a WD domain. In C. elegans, EMAP-Like Protein-1 (ELP-1) is required for touch sensation indicating that ELP-1 may play a role in mechanosensation. The localization of ELP-1 to microtubules and adhesion sites implies that ELP-1 may transmit forces between the body surface and the touch receptor neurons.
Pssm-ID: 460922 Cd Length: 72 Bit Score: 70.27 E-value: 1.30e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2217296595 1317 KKKRPIEDLVLELIFGYRGRDCRNNVHYLNDGdDIIYHTASVGILHNV 1364
Cdd:pfam03451 26 KKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTG-EIVYFTAAVVVLYDV 72
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1618-1925 |
2.60e-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: 75.45 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1618 VRSVC--RGKGKILVGTRNAEIIEVGEKNAACNILVNGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVN 1695
Cdd:cd00200 12 VTCVAfsPDGKLLATGSGDGTIKVWDLETGELLRTLKGH-TGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRTLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1696 lGHAA--RTVCYSPEGDMVAIGMKNGefiillvsSLKIW----GKK----RDRRCAIHDIRFSPDSRYLAVGSSENSVDF 1765
Cdd:cd00200 91 -GHTSyvSSVAFSPDGRILSSSSRDK--------TIKVWdvetGKClttlRGHTDWVNSVAFSPDGTFVASSSQDGTIKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1766 YDLTLGPTLNRIsycKDIPSFVIQMDFSADSSYLQVSSGCYKRHVYEVPSGKHLMDHaaidritwatwtsilgdevlgiw 1845
Cdd:cd00200 162 WDLRTGKCVATL---TGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTL----------------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1846 srHAEKADVNCACVSHSGISLVTGDDFGMVKLFDFpcpEKFAKHKRFLGHSPHVTNIRFtSGDRHVVSAGGDDCSLFVWK 1925
Cdd:cd00200 216 --RGHENGVNSVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
46-178 |
4.81e-12 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 68.90 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 46 VYSPREHR-QKFYRGHSDDIISLALHPERVLVATGQVGKEpyICIWDSYTVQTISVLKdVHTHGIACLAFDLDGQRLVSV 124
Cdd:cd00200 161 LWDLRTGKcVATLTGHTGEVNSVAFSPDGEKLLSSSSDGT--IKLWDLSTGKCLGTLR-GHENGVNSVAFSPDGYLLASG 237
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2217296595 125 GLDSKnaVCVWDWKRGKMLSMAPGHTDRIFDISWDlYQPNKLVSCGV-KHIKFWS 178
Cdd:cd00200 238 SEDGT--IRVWDLRTGECVQTLSGHTNSVTSLAWS-PDGKRLASGSAdGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
1663-1929 |
2.72e-09 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 61.47 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1663 ATHPSRDFFLSAAEDGTVRLWDIADKKMLNKVNLGHAARTVC-YSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRRCA 1741
Cdd:COG2319 1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLaASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1742 IHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRIsycKDIPSFVIQMDFSADSSYLqVSSGCYKR-HVYEVPSGKhlm 1820
Cdd:COG2319 81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTL---TGHTGAVRSVAFSPDGKTL-ASGSADGTvRLWDLATGK--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1821 dhaaidritwatwtsilgdeVLGIWSRHAEkaDVNCACVSHSGISLVTGDDFGMVKLFDfpcPEKFAKHKRFLGHSPHVT 1900
Cdd:COG2319 154 --------------------LLRTLTGHSG--AVTSVAFSPDGKLLASGSDDGTVRLWD---LATGKLLRTLTGHTGAVR 208
|
250 260 270
....*....|....*....|....*....|....
gi 2217296595 1901 NIRFTSGDRHVVSaGGDDCSLFVW-----KCVHT 1929
Cdd:COG2319 209 SVAFSPDGKLLAS-GSADGTVRLWdlatgKLLRT 241
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
1739-1929 |
3.14e-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: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1739 RCAIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRisyCKDIPSFVIQMDFSADSSYLQVSSGCYKRHVYEVPSGK- 1817
Cdd:cd00200 9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT---LKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGEc 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1818 --HLMDHAaiDRITWATW-------TSILGDEVLGIWSRHAEK---------ADVNCACVSHSGISLVTGDDFGMVKLFD 1879
Cdd:cd00200 86 vrTLTGHT--SYVSSVAFspdgrilSSSSRDKTIKVWDVETGKclttlrghtDWVNSVAFSPDGTFVASSSQDGTIKLWD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2217296595 1880 FPCPEKFakhKRFLGHSPHVTNIRFtSGDRHVVSAGGDDCSLFVW-----KCVHT 1929
Cdd:cd00200 164 LRTGKCV---ATLTGHTGEVNSVAF-SPDGEKLLSSSSDGTIKLWdlstgKCLGT 214
|
|
| ANAPC4_WD40 |
pfam12894 |
Anaphase-promoting complex subunit 4 WD40 domain; Apc4 contains an N-terminal propeller-shaped ... |
1703-1785 |
1.64e-05 |
|
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: 44.96 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 1703 VCYSPEGDMVAIGMKNGEFIILLVSSLKIWGKKRDRR-CAIHDIRFSPDSRYLAVGSSENSVDFYDLTLGPTLNRISYCK 1781
Cdd:pfam12894 1 MSWCPTMDLIALATEDGELLLHRLNWQRVWTLSPDKEdLEVTSLAWRPDGKLLAVGYSDGTVRLLDAENGKIVHHFSAGS 80
|
....
gi 2217296595 1782 DIPS 1785
Cdd:pfam12894 81 DLIT 84
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
1652-1684 |
3.71e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.64 E-value: 3.71e-04
10 20 30
....*....|....*....|....*....|...
gi 2217296595 1652 NGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWD 1684
Cdd:pfam00400 8 EGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
760-802 |
4.33e-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: 39.60 E-value: 4.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2217296595 760 TIKPLSILKGHHQYgVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:smart00320 1 SGELLKTLKGHTGP-VTSVAFSPDGKYLASGSDD--GTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
1652-1684 |
4.73e-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: 39.22 E-value: 4.73e-04
10 20 30
....*....|....*....|....*....|...
gi 2217296595 1652 NGHvDGPIWGLATHPSRDFFLSAAEDGTVRLWD 1684
Cdd:smart00320 9 KGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
314-353 |
1.46e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 38.10 E-value: 1.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2217296595 314 NKPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:pfam00400 1 GKLLKTLEGH-TGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WDR74 |
cd22857 |
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and ... |
250-354 |
2.31e-03 |
|
WD repeat-containing protein 74; WDR74 (WD repeat-containing protein 74) from mammals and plants is an essential factor for ribosome assembly. In cooperation with the assembly factor NVL2, WDR74 participates in an early cleavage of the pre-rRNA processing pathway. NVL2 is a type II double ring, AAA-ATPase, that may mediate the release of WDR74 from nucleolar pre-60S particles. WDR74 has been implicated in tumorigenesis. In lung cancer, it regulates cell proliferation, cell cycle progression, chemoresistance and cell aggressiveness, by inducing nuclear beta-catenin accumulation and driving downstream Wnt-responsive genes expression. In melanoma, it promotes apoptosis resistance and aggressive behavior by regulating the RPL5-MDM2-p53 pathway. WDR74 contains an N-terminal seven-bladed beta-propeller WD40 domain that associates with the D1-AAA domain of the AAA-ATPase NVL2, and a flexible lysine-rich C-terminus that extends outward from the WD40 domain, and is required for nucleolar localization.
Pssm-ID: 439303 [Multi-domain] Cd Length: 325 Bit Score: 42.21 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217296595 250 FATGGRDGCIRLWDLTF--KPITVIDLRETdqGYKGLSVRSvcwRGDHILVGTQDSEIFEIVVQErNKPFLIMQGHCEGE 327
Cdd:cd22857 195 IVTGTGYHQVRLYDTRAqrRPVVSVDFGET--PIKAVAEDP---DGHTVYVGDTSGDLASIDLRT-GKLLGCFKGKCGGS 268
|
90 100
....*....|....*....|....*..
gi 2217296595 328 LWALAVHPTKPLAVTGSDDRSVRIWSL 354
Cdd:cd22857 269 IRSIARHPELPLIASCGLDRYLRIWDT 295
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
315-353 |
2.43e-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: 37.29 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2217296595 315 KPFLIMQGHcEGELWALAVHPTKPLAVTGSDDRSVRIWS 353
Cdd:smart00320 3 ELLKTLKGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
956-988 |
3.56e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 36.91 E-value: 3.56e-03
10 20 30
....*....|....*....|....*....|...
gi 2217296595 956 QGHmEGEVWGLATHPYLPICATVSDDKTLRIWD 988
Cdd:smart00320 9 KGH-TGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
762-802 |
5.62e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.17 E-value: 5.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2217296595 762 KPLSILKGHHQyGVSAVDFSADGKRLASVGIDdsHTVVLWD 802
Cdd:pfam00400 2 KLLKTLEGHTG-SVTSLAFSPDGKLLASGSDD--GTVKVWD 39
|
|
| |
