|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
217-285 |
3.06e-32 |
|
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: 119.58 E-value: 3.06e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1759490504 217 KMFLRGRPITMYIPSGIRSLEELPS--GPPPETLSLDWVYGYRGRDSRSNLFVLRSGEVVYFIACVVVLYR 285
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNYYPKDDLDQkkEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
505-869 |
2.18e-28 |
|
WD40 repeat [General function prediction only]; :
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.48 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 505 TIVAQAHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWGPgLVALQEAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRG 583
Cdd:COG2319 69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL-ATGLLLRTLTGHTGAVRSVAfSPDGKTLASGSADGTVRLW 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 584 DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEGHALAWSMDLKETGL-CADFHPSGAVVVVGLNTGR 661
Cdd:COG2319 148 DLATGkLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVrSVAFSPDGKLLASGSADGT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 662 WLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIYSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFI 741
Cdd:COG2319 228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELLRTLT---GHSGGVNSVAFSPDGKLL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 742 MSNSGDYEILYWDVAGGcKLLRnryesrdrewatytcVLGFHVYGVWpdgsdgtdinSLCRSHNERVVAVADDFCKVHLF 821
Cdd:COG2319 304 ASGSDDGTVRLWDLATG-KLLR---------------TLTGHTGAVR----------SVAFSPDGKTLASGSDDGTVRLW 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1759490504 822 QypcARAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQWRV 869
Cdd:COG2319 358 D---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
299-625 |
8.30e-24 |
|
WD40 repeat [General function prediction only]; :
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 299 RHYRGHTDCVRCLAVHPDGVRVASGqtaGVDKdgkplqpVVHIWDSETLLKLQEigLGAFERGVGALAFSAadQGAFLcv 378
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASG---SADG-------TVRLWDLATGKLLRT--LTGHSGAVTSVAFSP--DGKLL-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 379 VDDSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 457
Cdd:COG2319 178 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGK------LLRTLTG------ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 458 KPKFIPCFVFLPDGDIL-TGDSEGNILTWGRsvsdsktpgrggakETYTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 536
Cdd:COG2319 245 HSGSVRSVAFSPDGRLLaSGSADGTVRLWDL--------------ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 537 RLVQWGPGLVALQeAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRGDLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 614
Cdd:COG2319 311 TVRLWDLATGKLL-RTLTGHTGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGeLLRTLTGHTGAVTSVAFSPDGRTLAS 389
|
330
....*....|.
gi 1759490504 615 CGHDRQLCLWD 625
Cdd:COG2319 390 GSADGTVRLWD 400
|
|
| TD_EMAP3 |
cd21949 |
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ... |
6-34 |
7.59e-07 |
|
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4. :
Pssm-ID: 409270 Cd Length: 48 Bit Score: 46.55 E-value: 7.59e-07
10 20
....*....|....*....|....*....
gi 1759490504 6 GPGEGPAHETLQTLSQRLRVQEEEMELVK 34
Cdd:cd21949 1 GPGSGEAPDPLAPLEQRLRTQEEEIALLK 29
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
217-285 |
3.06e-32 |
|
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: 119.58 E-value: 3.06e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1759490504 217 KMFLRGRPITMYIPSGIRSLEELPS--GPPPETLSLDWVYGYRGRDSRSNLFVLRSGEVVYFIACVVVLYR 285
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNYYPKDDLDQkkEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
505-869 |
2.18e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.48 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 505 TIVAQAHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWGPgLVALQEAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRG 583
Cdd:COG2319 69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL-ATGLLLRTLTGHTGAVRSVAfSPDGKTLASGSADGTVRLW 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 584 DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEGHALAWSMDLKETGL-CADFHPSGAVVVVGLNTGR 661
Cdd:COG2319 148 DLATGkLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVrSVAFSPDGKLLASGSADGT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 662 WLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIYSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFI 741
Cdd:COG2319 228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELLRTLT---GHSGGVNSVAFSPDGKLL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 742 MSNSGDYEILYWDVAGGcKLLRnryesrdrewatytcVLGFHVYGVWpdgsdgtdinSLCRSHNERVVAVADDFCKVHLF 821
Cdd:COG2319 304 ASGSDDGTVRLWDLATG-KLLR---------------TLTGHTGAVR----------SVAFSPDGKTLASGSDDGTVRLW 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1759490504 822 QypcARAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQWRV 869
Cdd:COG2319 358 D---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
551-868 |
4.21e-27 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 112.04 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 551 AEIPEHFGAVRAIAEGLGSELLVGTTKNALLRG-DLAQGFSP-VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEG 628
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVwDLETGELLrTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 629 HALAWSMDL-KETGLCADFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIY 707
Cdd:cd00200 83 GECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 708 SVSSCgtksSRFGRCMGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGcKLLrnryesrdrewatytCVLGFHVYGV 787
Cdd:cd00200 163 DLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCL---------------GTLRGHENGV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 788 WpdgsdgtdinSLCRSHNERVVAVADDFCKVHLFQYpcaRAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQW 867
Cdd:cd00200 223 N----------SVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIW 288
|
.
gi 1759490504 868 R 868
Cdd:cd00200 289 D 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
299-625 |
8.30e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 299 RHYRGHTDCVRCLAVHPDGVRVASGqtaGVDKdgkplqpVVHIWDSETLLKLQEigLGAFERGVGALAFSAadQGAFLcv 378
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASG---SADG-------TVRLWDLATGKLLRT--LTGHSGAVTSVAFSP--DGKLL-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 379 VDDSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 457
Cdd:COG2319 178 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGK------LLRTLTG------ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 458 KPKFIPCFVFLPDGDIL-TGDSEGNILTWGRsvsdsktpgrggakETYTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 536
Cdd:COG2319 245 HSGSVRSVAFSPDGRLLaSGSADGTVRLWDL--------------ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 537 RLVQWGPGLVALQeAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRGDLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 614
Cdd:COG2319 311 TVRLWDLATGKLL-RTLTGHTGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGeLLRTLTGHTGAVTSVAFSPDGRTLAS 389
|
330
....*....|.
gi 1759490504 615 CGHDRQLCLWD 625
Cdd:COG2319 390 GSADGTVRLWD 400
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
299-625 |
3.64e-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: 91.63 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 299 RHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWDSETllKLQEIGLGAFERGVGALAFSAADQGAFLCv 378
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLET--GELLRTLKGHTGPVRDVAASADGTYLASG- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 379 vddSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 457
Cdd:cd00200 70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGK------CLTTLRG------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 458 KPKFIPCFVFLPDGDILT-GDSEGNILTWgrsvsDSKTPgrggaketyTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 536
Cdd:cd00200 134 HTDWVNSVAFSPDGTFVAsSSQDGTIKLW-----DLRTG---------KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 537 RLVQWGPGLVALQeAEIPEHFGAVRAIAEGLGSELLVGTTKNALLRG-DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 614
Cdd:cd00200 200 TIKLWDLSTGKCL-GTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVwDLRTGeCVQTLSGHTNSVTSLAWSPDGKRLAS 278
|
330
....*....|.
gi 1759490504 615 CGHDRQLCLWD 625
Cdd:cd00200 279 GSADGTIRIWD 289
|
|
| TD_EMAP3 |
cd21949 |
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ... |
6-34 |
7.59e-07 |
|
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4.
Pssm-ID: 409270 Cd Length: 48 Bit Score: 46.55 E-value: 7.59e-07
10 20
....*....|....*....|....*....
gi 1759490504 6 GPGEGPAHETLQTLSQRLRVQEEEMELVK 34
Cdd:cd21949 1 GPGSGEAPDPLAPLEQRLRTQEEEIALLK 29
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
592-625 |
3.05e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.91 E-value: 3.05e-05
10 20 30
....*....|....*....|....*....|....
gi 1759490504 592 VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD 625
Cdd:smart00320 7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
592-625 |
2.77e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 2.77e-04
10 20 30
....*....|....*....|....*....|....
gi 1759490504 592 VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD 625
Cdd:pfam00400 6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
299-343 |
8.89e-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: 37.68 E-value: 8.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1759490504 299 RHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWD 343
Cdd:smart00320 6 KTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
298-343 |
2.36e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.55 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1759490504 298 QRHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWD 343
Cdd:pfam00400 4 LKTLEGHTGSVTSLAFSPDGKLLASG-----SDDGT-----VKVWD 39
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
217-285 |
3.06e-32 |
|
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: 119.58 E-value: 3.06e-32
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1759490504 217 KMFLRGRPITMYIPSGIRSLEELPS--GPPPETLSLDWVYGYRGRDSRSNLFVLRSGEVVYFIACVVVLYR 285
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNYYPKDDLDQkkEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
505-869 |
2.18e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.48 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 505 TIVAQAHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWGPgLVALQEAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRG 583
Cdd:COG2319 69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDL-ATGLLLRTLTGHTGAVRSVAfSPDGKTLASGSADGTVRLW 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 584 DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEGHALAWSMDLKETGL-CADFHPSGAVVVVGLNTGR 661
Cdd:COG2319 148 DLATGkLLRTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVrSVAFSPDGKLLASGSADGT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 662 WLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIYSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFI 741
Cdd:COG2319 228 VRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLAT-GELLRTLT---GHSGGVNSVAFSPDGKLL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 742 MSNSGDYEILYWDVAGGcKLLRnryesrdrewatytcVLGFHVYGVWpdgsdgtdinSLCRSHNERVVAVADDFCKVHLF 821
Cdd:COG2319 304 ASGSDDGTVRLWDLATG-KLLR---------------TLTGHTGAVR----------SVAFSPDGKTLASGSDDGTVRLW 357
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1759490504 822 QypcARAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQWRV 869
Cdd:COG2319 358 D---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
311-757 |
1.27e-27 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 116.55 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 311 LAVHPDGVRVASGQTAGVDKDGKPLQPVVHIWDSETLLKLQEigLGAFERGVGALAFSAADQGaflcVVDDSNEHMLSVW 390
Cdd:COG2319 32 LLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLAT--LLGHTAAVLSVAFSPDGRL----LASASADGTVRLW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 391 DCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkykKPKFIPCFVFLP 469
Cdd:COG2319 106 DLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGK------LLRTLTG------HSGAVTSVAFSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 470 DGDIL-TGDSEGNILTWgrsvsDSKTPgrggaKETYTIvaqaHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWgpglval 548
Cdd:COG2319 173 DGKLLaSGSDDGTVRLW-----DLATG-----KLLRTL----TGHTGAVRSVAFSPDGKLLASGSADGTVRLW------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 549 qeaeipehfgavraiaeglgsellvgttknallrgDLAQGFSP-VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGE 627
Cdd:COG2319 232 -----------------------------------DLATGKLLrTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 628 GHALAWSMDLKETGLCA-DFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYI 706
Cdd:COG2319 277 TGELLRTLTGHSGGVNSvAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRL 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1759490504 707 YSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAG 757
Cdd:COG2319 357 WDLAT-GELLRTLT---GHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
551-868 |
4.21e-27 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 112.04 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 551 AEIPEHFGAVRAIAEGLGSELLVGTTKNALLRG-DLAQGFSP-VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGEG 628
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVwDLETGELLrTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 629 HALAWSMDL-KETGLCADFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIY 707
Cdd:cd00200 83 GECVRTLTGhTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 708 SVSSCgtksSRFGRCMGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGcKLLrnryesrdrewatytCVLGFHVYGV 787
Cdd:cd00200 163 DLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTG-KCL---------------GTLRGHENGV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 788 WpdgsdgtdinSLCRSHNERVVAVADDFCKVHLFQYpcaRAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQW 867
Cdd:cd00200 223 N----------SVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAWSPDGKRLAS-GSADGTIRIW 288
|
.
gi 1759490504 868 R 868
Cdd:cd00200 289 D 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
522-869 |
3.96e-25 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 108.85 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 522 LRRDGTVLSGGGRDRRLVQWGPGLVALQEAEIPEHFGAVRAIAEGLGSELLVGTTKNALLRGDLAQG-FSPVIQGHTDEL 600
Cdd:COG2319 2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGaLLATLLGHTAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 601 WGLCTHPSQNRFLTCGHDRQLCLWDGE-GHALAWSMDLKETGLCADFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDG 679
Cdd:COG2319 82 LSVAFSPDGRLLASASADGTVRLWDLAtGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 680 NEQLSVVRYSPDGLYLAIGSHDNMIYIYSVSScGTKSSRFGrcmGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGc 759
Cdd:COG2319 162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLAT-GKLLRTLT---GHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 760 KLLRnryesrdrewatytcVLGFHVYGVWpdgsdgtdinSLCRSHNERVVAVADDFCKVHLFQypcARAKAPSRMYSGHG 839
Cdd:COG2319 237 KLLR---------------TLTGHSGSVR----------SVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHS 288
|
330 340 350
....*....|....*....|....*....|
gi 1759490504 840 SHVTSVRFTHDDSYLVSlGGKDASIFQWRV 869
Cdd:COG2319 289 GGVNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
299-625 |
8.30e-24 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 104.99 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 299 RHYRGHTDCVRCLAVHPDGVRVASGqtaGVDKdgkplqpVVHIWDSETLLKLQEigLGAFERGVGALAFSAadQGAFLcv 378
Cdd:COG2319 114 RTLTGHTGAVRSVAFSPDGKTLASG---SADG-------TVRLWDLATGKLLRT--LTGHSGAVTSVAFSP--DGKLL-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 379 VDDSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 457
Cdd:COG2319 178 ASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATGK------LLRTLTG------ 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 458 KPKFIPCFVFLPDGDIL-TGDSEGNILTWGRsvsdsktpgrggakETYTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 536
Cdd:COG2319 245 HSGSVRSVAFSPDGRLLaSGSADGTVRLWDL--------------ATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDG 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 537 RLVQWGPGLVALQeAEIPEHFGAVRAIA-EGLGSELLVGTTKNALLRGDLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 614
Cdd:COG2319 311 TVRLWDLATGKLL-RTLTGHTGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGeLLRTLTGHTGAVTSVAFSPDGRTLAS 389
|
330
....*....|.
gi 1759490504 615 CGHDRQLCLWD 625
Cdd:COG2319 390 GSADGTVRLWD 400
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
398-708 |
5.00e-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: 94.32 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 398 LAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkykKPKFIPCFVFLPDGD-ILT 475
Cdd:cd00200 2 RRTLKGHTGGVTCVAFSP-DGKLLATGSGDGtIKVWDLETGE------LLRTLKG------HTGPVRDVAASADGTyLAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 476 GDSEGNILTWgrsvsDSKTPgrggaKETYTIvaqaHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWgPGLVALQEAEIPE 555
Cdd:cd00200 69 GSSDKTIRLW-----DLETG-----ECVRTL----TGHTSYVSSVAFSPDGRILSSSSRDKTIKVW-DVETGKCLTTLRG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 556 HFGAVRAIAEGLGSELLVGTTKNALLR-GDLAQGfSPV--IQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD-GEGHAL 631
Cdd:cd00200 134 HTDWVNSVAFSPDGTFVASSSQDGTIKlWDLRTG-KCVatLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDlSTGKCL 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1759490504 632 AwSMDLKETGLCA-DFHPSGAVVVVGLNTGRWLVLDTETREIVSDVTDGNEQLSVVRYSPDGLYLAIGSHDNMIYIYS 708
Cdd:cd00200 213 G-TLRGHENGVNSvAFSPDGYLLASGSEDGTIRVWDLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
299-625 |
3.64e-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: 91.63 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 299 RHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWDSETllKLQEIGLGAFERGVGALAFSAADQGAFLCv 378
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLET--GELLRTLKGHTGPVRDVAASADGTYLASG- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 379 vddSNEHMLSVWDCSRGVKLAEIKSTNDSVLAVGFSPrDSSCIVTSGKSH-VHFWNWSGGTgapgngLLARKQGvfgkyk 457
Cdd:cd00200 70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGK------CLTTLRG------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 458 KPKFIPCFVFLPDGDILT-GDSEGNILTWgrsvsDSKTPgrggaketyTIVAQAHAHEGSIFALCLRRDGTVLSGGGRDR 536
Cdd:cd00200 134 HTDWVNSVAFSPDGTFVAsSSQDGTIKLW-----DLRTG---------KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 537 RLVQWGPGLVALQeAEIPEHFGAVRAIAEGLGSELLVGTTKNALLRG-DLAQG-FSPVIQGHTDELWGLCTHPSQNRFLT 614
Cdd:cd00200 200 TIKLWDLSTGKCL-GTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVwDLRTGeCVQTLSGHTNSVTSLAWSPDGKRLAS 278
|
330
....*....|.
gi 1759490504 615 CGHDRQLCLWD 625
Cdd:cd00200 279 GSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
724-869 |
1.43e-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: 53.88 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1759490504 724 GHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGCKLLRNRyesrdrewatytcvlgfhvygvwpdGSDGTDINSLCRS 803
Cdd:cd00200 7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTLK-------------------------GHTGPVRDVAASA 61
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1759490504 804 HNERVVAVADDFCkVHLFQYpcaRAKAPSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQWRV 869
Cdd:cd00200 62 DGTYLASGSSDKT-IRLWDL---ETGECVRTLTGHTSYVSSVAFSPDGRILSS-SSRDKTIKVWDV 122
|
|
| TD_EMAP3 |
cd21949 |
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ... |
6-34 |
7.59e-07 |
|
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4.
Pssm-ID: 409270 Cd Length: 48 Bit Score: 46.55 E-value: 7.59e-07
10 20
....*....|....*....|....*....
gi 1759490504 6 GPGEGPAHETLQTLSQRLRVQEEEMELVK 34
Cdd:cd21949 1 GPGSGEAPDPLAPLEQRLRTQEEEIALLK 29
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
592-625 |
3.05e-05 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 41.91 E-value: 3.05e-05
10 20 30
....*....|....*....|....*....|....
gi 1759490504 592 VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD 625
Cdd:smart00320 7 TLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
592-625 |
2.77e-04 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 39.25 E-value: 2.77e-04
10 20 30
....*....|....*....|....*....|....
gi 1759490504 592 VIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWD 625
Cdd:pfam00400 6 TLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
722-754 |
7.09e-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: 38.06 E-value: 7.09e-04
10 20 30
....*....|....*....|....*....|...
gi 1759490504 722 CMGHSSFITHLDWSKDGNFIMSNSGDYEILYWD 754
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
299-343 |
8.89e-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: 37.68 E-value: 8.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1759490504 299 RHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWD 343
Cdd:smart00320 6 KTLKGHTGPVTSVAFSPDGKYLASG-----SDDGT-----IKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
831-867 |
2.36e-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: 36.52 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1759490504 831 PSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQW 867
Cdd:smart00320 4 LLKTLKGHTGPVTSVAFSPDGKYLAS-GSDDGTIKLW 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
298-343 |
2.36e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.55 E-value: 2.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1759490504 298 QRHYRGHTDCVRCLAVHPDGVRVASGqtagvDKDGKplqpvVHIWD 343
Cdd:pfam00400 4 LKTLEGHTGSVTSLAFSPDGKLLASG-----SDDGT-----VKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
724-754 |
4.03e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.78 E-value: 4.03e-03
10 20 30
....*....|....*....|....*....|.
gi 1759490504 724 GHSSFITHLDWSKDGNFIMSNSGDYEILYWD 754
Cdd:pfam00400 9 GHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
831-867 |
6.33e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.40 E-value: 6.33e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1759490504 831 PSRMYSGHGSHVTSVRFTHDDSYLVSlGGKDASIFQW 867
Cdd:pfam00400 3 LLKTLEGHTGSVTSLAFSPDGKLLAS-GSDDGTVKVW 38
|
|
|