|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
62-132 |
6.03e-37 |
|
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: 132.29 E-value: 6.03e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47550919 62 RIYLRGRPVTNYLPSD-VEDYDLNAKHPAPTEKLKLDWVYGYRGRDCRCNLYLLPTGEIIYFMAAVVVLYNV 132
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNyYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
141-574 |
1.51e-30 |
|
WD40 repeat [General function prediction only]; :
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 124.25 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 141 TGHNDDVKSIAVHPDSVTIATGQVAGHdpdegkphVRIWNSITMETLHVLGLGFFDRAVCALSFSkvnvGVHLAAVdeSN 220
Cdd:COG2319 33 LGLAAAVASLAASPDGARLAAGAGDLT--------LLLLDAAAGALLATLLGHTAAVLSVAFSPD----GRLLASA--SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 221 EHVLSVWDWKKEKKLSDTKSSQDPVLACEYHPmNDEQIITLGKGH-IHFWNTTGGKLVKksgIFEKYDKPkfVLSLAFTG 299
Cdd:COG2319 99 DGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKLLR---TLTGHSGA--VTSVAFSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 300 NGDVI-TGDSNGNMYIWGKGNTRISQAILGaHEGGIFSLCVMNDGQILSGGGKDKKVILWTADyqqsevtqvteaTG-PV 377
Cdd:COG2319 173 DGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWDLA------------TGkLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 378 RTLckgkgedfyvgttrnailsgnmggefntlvQAHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPMWNKLMEDG 457
Cdd:COG2319 240 RTL------------------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 458 C-QSAGFHPSGAVVAIGMTSGRWVALDVESQDLITVHTDGKEQHDIIRYSPDGNFLAVASHDNYIYIYSVTEEGRkyskV 536
Cdd:COG2319 290 GvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL----L 365
|
410 420 430
....*....|....*....|....*....|....*...
gi 47550919 537 GKCSGHSSFVTHIDWSADSTKLQSNSGDYELLFWDAAT 574
Cdd:COG2319 366 RTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
649-684 |
1.11e-03 |
|
WD domain, G-beta repeat; :
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 1.11e-03
10 20 30
....*....|....*....|....*....|....*.
gi 47550919 649 TSFKGHSSHVTSVAFNGDStKLISTGGRDMSCMQWS 684
Cdd:pfam00400 5 KTLEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
62-132 |
6.03e-37 |
|
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: 132.29 E-value: 6.03e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47550919 62 RIYLRGRPVTNYLPSD-VEDYDLNAKHPAPTEKLKLDWVYGYRGRDCRCNLYLLPTGEIIYFMAAVVVLYNV 132
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNyYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
141-574 |
1.51e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 124.25 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 141 TGHNDDVKSIAVHPDSVTIATGQVAGHdpdegkphVRIWNSITMETLHVLGLGFFDRAVCALSFSkvnvGVHLAAVdeSN 220
Cdd:COG2319 33 LGLAAAVASLAASPDGARLAAGAGDLT--------LLLLDAAAGALLATLLGHTAAVLSVAFSPD----GRLLASA--SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 221 EHVLSVWDWKKEKKLSDTKSSQDPVLACEYHPmNDEQIITLGKGH-IHFWNTTGGKLVKksgIFEKYDKPkfVLSLAFTG 299
Cdd:COG2319 99 DGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKLLR---TLTGHSGA--VTSVAFSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 300 NGDVI-TGDSNGNMYIWGKGNTRISQAILGaHEGGIFSLCVMNDGQILSGGGKDKKVILWTADyqqsevtqvteaTG-PV 377
Cdd:COG2319 173 DGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWDLA------------TGkLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 378 RTLckgkgedfyvgttrnailsgnmggefntlvQAHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPMWNKLMEDG 457
Cdd:COG2319 240 RTL------------------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 458 C-QSAGFHPSGAVVAIGMTSGRWVALDVESQDLITVHTDGKEQHDIIRYSPDGNFLAVASHDNYIYIYSVTEEGRkyskV 536
Cdd:COG2319 290 GvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL----L 365
|
410 420 430
....*....|....*....|....*....|....*...
gi 47550919 537 GKCSGHSSFVTHIDWSADSTKLQSNSGDYELLFWDAAT 574
Cdd:COG2319 366 RTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
330-684 |
6.19e-29 |
|
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: 117.05 E-value: 6.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 330 HEGGIFSLCVMNDGQILSGGGKDKKVILWTADYQQSEVTQvTEATGPVRTL---CKGK-----GEDfyvGTTRnaILSGN 401
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-KGHTGPVRDVaasADGTylasgSSD---KTIR--LWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 402 MGGEFNTLVQaHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPmwnklmedgCQSAGFHpSGAVVAIgmtsgrwva 481
Cdd:cd00200 82 TGECVRTLTG-HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC---------LTTLRGH-TDWVNSV--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 482 ldvesqdlitvhtdgkeqhdiiRYSPDGNFLAVASHDNYIYIYSVTEEgrkySKVGKCSGHSSFVTHIDWSADSTKLQSN 561
Cdd:cd00200 142 ----------------------AFSPDGTFVASSSQDGTIKLWDLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 562 SGDYELLFWDAATCKQIvisketrdvewATFTGVLGYpvcgiwpegsdgtdVNTTARSANGNLLASGDDFGKINLFRYpv 641
Cdd:cd00200 196 SSDGTIKLWDLSTGKCL-----------GTLRGHENG--------------VNSVAFSPDGYLLASGSEDGTIRVWDL-- 248
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 47550919 642 nHPKADCTSFKGHSSHVTSVAFNGDSTKLISTGGrDMSCMQWS 684
Cdd:cd00200 249 -RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSA-DGTIRIWD 289
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
411-442 |
9.14e-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: 37.29 E-value: 9.14e-04
10 20 30
....*....|....*....|....*....|..
gi 47550919 411 QAHTEELWGLALHPTQGLFLTCGYDKNVIMWD 442
Cdd:smart00320 9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
649-684 |
1.11e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 1.11e-03
10 20 30
....*....|....*....|....*....|....*.
gi 47550919 649 TSFKGHSSHVTSVAFNGDStKLISTGGRDMSCMQWS 684
Cdd:pfam00400 5 KTLEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
650-684 |
1.37e-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: 1.37e-03
10 20 30
....*....|....*....|....*....|....*
gi 47550919 650 SFKGHSSHVTSVAFNGDSTKLIStGGRDMSCMQWS 684
Cdd:smart00320 7 TLKGHTGPVTSVAFSPDGKYLAS-GSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
404-442 |
5.25e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.01 E-value: 5.25e-03
10 20 30
....*....|....*....|....*....|....*....
gi 47550919 404 GEFNTLVQAHTEELWGLALHPTQGLFLTCGYDKNVIMWD 442
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
62-132 |
6.03e-37 |
|
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: 132.29 E-value: 6.03e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47550919 62 RIYLRGRPVTNYLPSD-VEDYDLNAKHPAPTEKLKLDWVYGYRGRDCRCNLYLLPTGEIIYFMAAVVVLYNV 132
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNyYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
141-574 |
1.51e-30 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 124.25 E-value: 1.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 141 TGHNDDVKSIAVHPDSVTIATGQVAGHdpdegkphVRIWNSITMETLHVLGLGFFDRAVCALSFSkvnvGVHLAAVdeSN 220
Cdd:COG2319 33 LGLAAAVASLAASPDGARLAAGAGDLT--------LLLLDAAAGALLATLLGHTAAVLSVAFSPD----GRLLASA--SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 221 EHVLSVWDWKKEKKLSDTKSSQDPVLACEYHPmNDEQIITLGKGH-IHFWNTTGGKLVKksgIFEKYDKPkfVLSLAFTG 299
Cdd:COG2319 99 DGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLATGKLLR---TLTGHSGA--VTSVAFSP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 300 NGDVI-TGDSNGNMYIWGKGNTRISQAILGaHEGGIFSLCVMNDGQILSGGGKDKKVILWTADyqqsevtqvteaTG-PV 377
Cdd:COG2319 173 DGKLLaSGSDDGTVRLWDLATGKLLRTLTG-HTGAVRSVAFSPDGKLLASGSADGTVRLWDLA------------TGkLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 378 RTLckgkgedfyvgttrnailsgnmggefntlvQAHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPMWNKLMEDG 457
Cdd:COG2319 240 RTL------------------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 458 C-QSAGFHPSGAVVAIGMTSGRWVALDVESQDLITVHTDGKEQHDIIRYSPDGNFLAVASHDNYIYIYSVTEEGRkyskV 536
Cdd:COG2319 290 GvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGEL----L 365
|
410 420 430
....*....|....*....|....*....|....*...
gi 47550919 537 GKCSGHSSFVTHIDWSADSTKLQSNSGDYELLFWDAAT 574
Cdd:COG2319 366 RTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
330-684 |
6.19e-29 |
|
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: 117.05 E-value: 6.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 330 HEGGIFSLCVMNDGQILSGGGKDKKVILWTADYQQSEVTQvTEATGPVRTL---CKGK-----GEDfyvGTTRnaILSGN 401
Cdd:cd00200 8 HTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-KGHTGPVRDVaasADGTylasgSSD---KTIR--LWDLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 402 MGGEFNTLVQaHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPmwnklmedgCQSAGFHpSGAVVAIgmtsgrwva 481
Cdd:cd00200 82 TGECVRTLTG-HTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKC---------LTTLRGH-TDWVNSV--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 482 ldvesqdlitvhtdgkeqhdiiRYSPDGNFLAVASHDNYIYIYSVTEEgrkySKVGKCSGHSSFVTHIDWSADSTKLQSN 561
Cdd:cd00200 142 ----------------------AFSPDGTFVASSSQDGTIKLWDLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 562 SGDYELLFWDAATCKQIvisketrdvewATFTGVLGYpvcgiwpegsdgtdVNTTARSANGNLLASGDDFGKINLFRYpv 641
Cdd:cd00200 196 SSDGTIKLWDLSTGKCL-----------GTLRGHENG--------------VNSVAFSPDGYLLASGSEDGTIRVWDL-- 248
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 47550919 642 nHPKADCTSFKGHSSHVTSVAFNGDSTKLISTGGrDMSCMQWS 684
Cdd:cd00200 249 -RTGECVQTLSGHTNSVTSLAWSPDGKRLASGSA-DGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
214-677 |
1.38e-28 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 118.48 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 214 AAVDESNEHVLSVWDWKKEKKLSDTKSSQDPVLACEYHPMNDEQIITLGKGHIHFWNTTGGKLVKKSGIFEKydkpkFVL 293
Cdd:COG2319 8 ALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA-----AVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 294 SLAFTGNGDVI-TGDSNGNMYIWgKGNTRISQAILGAHEGGIFSLCVMNDGQILSGGGKDKKVILWTAdyqqsevtqvte 372
Cdd:COG2319 83 SVAFSPDGRLLaSASADGTVRLW-DLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 373 ATG-PVRTLckgkgedfyvgttrnailsgnmggefntlvQAHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPMWN 451
Cdd:COG2319 150 ATGkLLRTL------------------------------TGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 452 -KLMEDGCQSAGFHPSGAVVAIGMTSGRWVALDVESQDLITVHTDGKEQHDIIRYSPDGNFLAVASHDNYIYIYSVtEEG 530
Cdd:COG2319 200 lTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 531 RKyskVGKCSGHSSFVTHIDWSADSTKLQSNSGDYELLFWDAATCKQIvisketrdvewATFTGvlgypvcgiwpegsDG 610
Cdd:COG2319 279 EL---LRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLL-----------RTLTG--------------HT 330
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47550919 611 TDVNTTARSANGNLLASGDDFGKINLFRypVNHPKADCTsFKGHSSHVTSVAFNGDSTKLIStGGRD 677
Cdd:COG2319 331 GAVRSVAFSPDGKTLASGSDDGTVRLWD--LATGELLRT-LTGHTGAVTSVAFSPDGRTLAS-GSAD 393
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
213-638 |
7.59e-27 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 113.47 E-value: 7.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 213 LAAVDESNEHVLSVWDWKKEKKLSDTKSSQDPVLACEYHPMNDEQIITLGKGHIHFWNTTGGKLVKKSGIFEKYdkpkfV 292
Cdd:COG2319 49 ARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGA-----V 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 293 LSLAFTGNGD-VITGDSNGNMYIWGKGNTRISQAILGaHEGGIFSLCVMNDGQILSGGGKDKKVILWTAdyqqsevtqvt 371
Cdd:COG2319 124 RSVAFSPDGKtLASGSADGTVRLWDLATGKLLRTLTG-HSGAVTSVAFSPDGKLLASGSDDGTVRLWDL----------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 372 eATG-PVRTLckgkgedfyvgttrnailsgnmggefntlvQAHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPMW 450
Cdd:COG2319 192 -ATGkLLRTL------------------------------TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 451 N-KLMEDGCQSAGFHPSGAVVAIGMTSGRWVALDVESQDLITVHTDGKEQHDIIRYSPDGNFLAVASHDNYIYIYSVtEE 529
Cdd:COG2319 241 TlTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL-AT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 530 GRKyskVGKCSGHSSFVTHIDWSADSTKLQSNSGDYELLFWDAATCKQIvisketrdvewATFTGVLGYpvcgiwpegsd 609
Cdd:COG2319 320 GKL---LRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGELL-----------RTLTGHTGA----------- 374
|
410 420
....*....|....*....|....*....
gi 47550919 610 gtdVNTTARSANGNLLASGDDFGKINLFR 638
Cdd:COG2319 375 ---VTSVAFSPDGRTLASGSADGTVRLWD 400
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
138-442 |
7.50e-25 |
|
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: 105.11 E-value: 7.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 138 RHYTGHNDDVKSIAVHPDSVTIATGqvaGHDpdeGKphVRIWNSITMETLHVL-GLGFFDRAVCALSFSKVnvgvhLAAV 216
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATG---SGD---GT--IKVWDLETGELLRTLkGHTGPVRDVAASADGTY-----LASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 217 deSNEHVLSVWDWKKEKKLSDTKSSQDPVLACEYHPmnDEQIITLGKGH--IHFWNTTGGKLVkksgiFEKYDKPKFVLS 294
Cdd:cd00200 70 --SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP--DGRILSSSSRDktIKVWDVETGKCL-----TTLRGHTDWVNS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 295 LAFTGNGDVIT-GDSNGNMYIWgKGNTRISQAILGAHEGGIFSLCVMNDGQILSGGGKDKKVILWTADyQQSEVTQVTEA 373
Cdd:cd00200 141 VAFSPDGTFVAsSSQDGTIKLW-DLRTGKCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLS-TGKCLGTLRGH 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47550919 374 TGPVRTLCKGKGEDFYVGTTRNAIL---SGNMGGEFNTLvQAHTEELWGLALHPTQGLFLTCGYDKNVIMWD 442
Cdd:cd00200 219 ENGVNSVAFSPDGYLLASGSEDGTIrvwDLRTGECVQTL-SGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
239-571 |
1.29e-21 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 95.48 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 239 KSSQDPVLACEYHPmNDEQIITLGK-GHIHFWNTTGGKLvkksgIFEKYDKPKFVLSLAFTGNGD-VITGDSNGNMYIWg 316
Cdd:cd00200 6 KGHTGGVTCVAFSP-DGKLLATGSGdGTIKVWDLETGEL-----LRTLKGHTGPVRDVAASADGTyLASGSSDKTIRLW- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 317 KGNTRISQAILGAHEGGIFSLCVMNDGQILSGGGKDKKVILWTadyqqsevtqvteatgpVRTlckgkgedfyvgttrna 396
Cdd:cd00200 79 DLETGECVRTLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVWD-----------------VET----------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 397 ilsgnmgGEFNTLVQAHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPMWN-KLMEDGCQSAGFHPSGAVVAIG-- 473
Cdd:cd00200 125 -------GKCLTTLRGHTDWVNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATlTGHTGEVNSVAFSPDGEKLLSSss 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 474 -MTSGRWVALDVESQDLITVHTDGkeqhdI--IRYSPDGNFLAVASHDNYIYIYSVteegRKYSKVGKCSGHSSFVTHID 550
Cdd:cd00200 198 dGTIKLWDLSTGKCLGTLRGHENG-----VnsVAFSPDGYLLASGSEDGTIRVWDL----RTGECVQTLSGHTNSVTSLA 268
|
330 340
....*....|....*....|.
gi 47550919 551 WSADSTKLQSNSGDYELLFWD 571
Cdd:cd00200 269 WSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
391-685 |
2.60e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 96.90 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 391 GTTRNAILSGNMGGEFNTLVQAHTEELWGLALHPTQGLFLTCGYDKNVIMWDFEQHKPMWNKLM-EDGCQSAGFHPSGAV 469
Cdd:COG2319 55 AGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGhTGAVRSVAFSPDGKT 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 470 VAIGmTSGRWVAL-DVESQDLITV---HTDGKEQhdiIRYSPDGNFLAVASHDNYIYIYSVTEegrkyskvGKC----SG 541
Cdd:COG2319 135 LASG-SADGTVRLwDLATGKLLRTltgHSGAVTS---VAFSPDGKLLASGSDDGTVRLWDLAT--------GKLlrtlTG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 542 HSSFVTHIDWSADSTKLQSNSGDYELLFWDAATCKQIvisketrdvewATFTGvlgypvcgiwpegsDGTDVNTTARSAN 621
Cdd:COG2319 203 HTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLL-----------RTLTG--------------HSGSVRSVAFSPD 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47550919 622 GNLLASGDDFGKINLFRypVNHPKADcTSFKGHSSHVTSVAFNGDSTKLIStGGRDMSCMQWSV 685
Cdd:COG2319 258 GRLLASGSADGTVRLWD--LATGELL-RTLTGHSGGVNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
127-358 |
3.91e-13 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 70.44 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 127 VVLYNVEEQNQRH-YTGHNDDVKSIAVHPDSVTIATGqvaghdPDEGKphVRIWNSITMETLHVLglgffdravcalsfs 205
Cdd:cd00200 117 IKVWDVETGKCLTtLRGHTDWVNSVAFSPDGTFVASS------SQDGT--IKLWDLRTGKCVATL--------------- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47550919 206 kvnvgvhlaavdesnehvlsvwdwkkekklsdtKSSQDPVLACEYHPMNDEQIITLGKGHIHFWNTTGGKLVKksgIFEK 285
Cdd:cd00200 174 ---------------------------------TGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLG---TLRG 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47550919 286 ydKPKFVLSLAFTGNGDVIT-GDSNGNMYIWGKGNTRISQaILGAHEGGIFSLCVMNDGQILSGGGKDKKVILW 358
Cdd:cd00200 218 --HENGVNSVAFSPDGYLLAsGSEDGTIRVWDLRTGECVQ-TLSGHTNSVTSLAWSPDGKRLASGSADGTIRIW 288
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
411-442 |
9.14e-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: 37.29 E-value: 9.14e-04
10 20 30
....*....|....*....|....*....|..
gi 47550919 411 QAHTEELWGLALHPTQGLFLTCGYDKNVIMWD 442
Cdd:smart00320 9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
649-684 |
1.11e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 36.94 E-value: 1.11e-03
10 20 30
....*....|....*....|....*....|....*.
gi 47550919 649 TSFKGHSSHVTSVAFNGDStKLISTGGRDMSCMQWS 684
Cdd:pfam00400 5 KTLEGHTGSVTSLAFSPDG-KLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
650-684 |
1.37e-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: 1.37e-03
10 20 30
....*....|....*....|....*....|....*
gi 47550919 650 SFKGHSSHVTSVAFNGDSTKLIStGGRDMSCMQWS 684
Cdd:smart00320 7 TLKGHTGPVTSVAFSPDGKYLAS-GSDDGTIKLWD 40
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
325-358 |
4.51e-03 |
|
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.
Pssm-ID: 197651 [Multi-domain] Cd Length: 40 Bit Score: 35.37 E-value: 4.51e-03
10 20 30
....*....|....*....|....*....|....
gi 47550919 325 AILGAHEGGIFSLCVMNDGQILSGGGKDKKVILW 358
Cdd:smart00320 6 KTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
404-442 |
5.25e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.01 E-value: 5.25e-03
10 20 30
....*....|....*....|....*....|....*....
gi 47550919 404 GEFNTLVQAHTEELWGLALHPTQGLFLTCGYDKNVIMWD 442
Cdd:pfam00400 1 GKLLKTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
534-571 |
6.82e-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: 34.98 E-value: 6.82e-03
10 20 30
....*....|....*....|....*....|....*...
gi 47550919 534 SKVGKCSGHSSFVTHIDWSADSTKLQSNSGDYELLFWD 571
Cdd:smart00320 3 ELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
|