|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
33-101 |
3.64e-36 |
|
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: 130.36 E-value: 3.64e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907126843 33 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 101
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
308-668 |
2.03e-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. The actual alignment was detected with superfamily member cd00200:
Pssm-ID: 475233 [Multi-domain] Cd Length: 289 Bit Score: 109.73 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 308 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 387
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 388 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 461
Cdd:cd00200 42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 462 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 532
Cdd:cd00200 117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 533 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 612
Cdd:cd00200 184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907126843 613 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 668
Cdd:cd00200 238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
|
|
| WD40 super family |
cl29593 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
108-461 |
1.00e-19 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment. The actual alignment was detected with superfamily member cd00200:
Pssm-ID: 475233 [Multi-domain] Cd Length: 289 Bit Score: 90.09 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 108 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 187
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 188 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 264
Cdd:cd00200 70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 265 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 343
Cdd:cd00200 139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 344 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 423
Cdd:cd00200 207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907126843 424 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 461
Cdd:cd00200 246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
33-101 |
3.64e-36 |
|
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: 130.36 E-value: 3.64e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907126843 33 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 101
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
308-668 |
2.03e-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: 109.73 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 308 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 387
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 388 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 461
Cdd:cd00200 42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 462 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 532
Cdd:cd00200 117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 533 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 612
Cdd:cd00200 184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907126843 613 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 668
Cdd:cd00200 238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
305-669 |
3.54e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 111.93 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 305 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 381
Cdd:COG2319 69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 382 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 459
Cdd:COG2319 146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 460 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 539
Cdd:COG2319 226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 540 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 619
Cdd:COG2319 302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907126843 620 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 669
Cdd:COG2319 356 LWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
108-461 |
1.00e-19 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 90.09 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 108 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 187
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 188 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 264
Cdd:cd00200 70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 265 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 343
Cdd:cd00200 139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 344 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 423
Cdd:cd00200 207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907126843 424 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 461
Cdd:cd00200 246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
92-342 |
9.58e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 76.87 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 92 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 165
Cdd:COG2319 176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 166 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 243
Cdd:COG2319 244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 244 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 322
Cdd:COG2319 319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380
|
250 260
....*....|....*....|
gi 1907126843 323 MRNGMLLTGGGKDRKIILWD 342
Cdd:COG2319 381 SPDGRTLASGSADGTVRLWD 400
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
522-554 |
1.83e-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: 1.83e-04
10 20 30
....*....|....*....|....*....|...
gi 1907126843 522 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 554
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
494-557 |
2.82e-03 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 41.09 E-value: 2.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907126843 494 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 557
Cdd:PTZ00420 89 ILASGSEDLTIRVWEIPHNDEsvKEIKDPQCilKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIEN 157
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
520-554 |
3.06e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.78 E-value: 3.06e-03
10 20 30
....*....|....*....|....*....|....*
gi 1907126843 520 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 554
Cdd:pfam00400 5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| HELP |
pfam03451 |
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ... |
33-101 |
3.64e-36 |
|
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: 130.36 E-value: 3.64e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907126843 33 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 101
Cdd:pfam03451 1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
308-668 |
2.03e-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: 109.73 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 308 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 387
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 388 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 461
Cdd:cd00200 42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 462 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 532
Cdd:cd00200 117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 533 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 612
Cdd:cd00200 184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907126843 613 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 668
Cdd:cd00200 238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
305-669 |
3.54e-26 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 111.93 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 305 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 381
Cdd:COG2319 69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 382 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 459
Cdd:COG2319 146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 460 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 539
Cdd:COG2319 226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 540 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 619
Cdd:COG2319 302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907126843 620 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 669
Cdd:COG2319 356 LWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
191-557 |
2.86e-25 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 109.23 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 191 SNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 268
Cdd:COG2319 97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 269 FLGNGDVL-TGDSGGVMLIWSktmvePPPGKGPkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnl 347
Cdd:COG2319 170 FSPDGKLLaSGSDDGTVRLWD-----LATGKLL-------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 348 ereievpdqygtiraVAEGRAEQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsV 427
Cdd:COG2319 233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-L 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 428 EHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIY 505
Cdd:COG2319 276 ATGELLRTLTGHSGgvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVR 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907126843 506 LYTvLENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIEN 557
Cdd:COG2319 356 LWD-LATGELLRTL---TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
196-558 |
2.90e-23 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 103.07 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 196 LTVWDWQKKSKIAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKyekpkFVQCLAFLGNGDV 275
Cdd:COG2319 18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA-----AVLSVAFSPDGRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 276 L-TGDSGGVMLIWSktmVEPPpgkgpkgvyQINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWD-HDLNLEREIEV 353
Cdd:COG2319 93 LaSASADGTVRLWD---LATG---------LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 354 PDqyGTIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsVEHRL 431
Cdd:COG2319 161 HS--GAVTSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 432 EWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTV 509
Cdd:COG2319 238 LLRTLTGHSGsvRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907126843 510 lENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENG 558
Cdd:COG2319 318 -ATGKLLRTL---TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
261-554 |
6.71e-23 |
|
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: 99.72 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 261 PKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKII 339
Cdd:cd00200 9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELL------------RTLKGHTGPVRDVAASADGTYLASGSSDKTIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 340 LWD-HDLNLEREIEVPDQYgtIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCA 416
Cdd:cd00200 77 LWDlETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 417 QDRQVCMWNSVEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVD 491
Cdd:cd00200 155 QDGTIKLWDLRTGKCVATL----TGHtgevnSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907126843 492 GTLLAVGSHDNFIYLYtvleNGRKYSRYGKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 554
Cdd:cd00200 231 GYLLASGSEDGTIRVW----DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
324-669 |
4.74e-21 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 96.13 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 324 RNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQYGTIRAVAEGRAEQFLVGTSRNFILRGTFNDG-FQIEVQGHTDELWG 402
Cdd:COG2319 4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGaLLATLLGHTAAVLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 403 LATHPFKDLLLTCAQDRQVCMWNsVEHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGN 480
Cdd:COG2319 84 VAFSPDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGavRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 481 EQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcK 560
Cdd:COG2319 163 GAVTSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTL---TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-K 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 561 LIRnrsdckdidwttytcvlgfqvfgvwPEGSDGTDINALVRSHNRRVIAVADDFCKVHLFQypcSKAKAPSHKYSAHSS 640
Cdd:COG2319 238 LLR-------------------------TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSG 289
|
330 340
....*....|....*....|....*....
gi 1907126843 641 HVTNVSFTHNDSHLIStGGKDMSIIQWKL 669
Cdd:COG2319 290 GVNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
108-461 |
1.00e-19 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 90.09 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 108 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 187
Cdd:cd00200 3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 188 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 264
Cdd:cd00200 70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 265 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 343
Cdd:cd00200 139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 344 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 423
Cdd:cd00200 207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907126843 424 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 461
Cdd:cd00200 246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
99-425 |
4.82e-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: 79.30 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 99 LFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiaGVDKDgrplqphVRVWDSVSLTTLHVigLGTFERGVGCLDFS 177
Cdd:cd00200 35 VWDLETGELLRTLkGHTGPVRDVAASADGTYLASG---SSDKT-------IRLWDLETGECVRT--LTGHTSYVSSVAFS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 178 KaDSGVHLCVIDDSNehmLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKS--HIFFWtwSGNSLTRKQGIF 255
Cdd:cd00200 103 P-DGRILSSSSRDKT---IKVWDVETGKCLTTLRGHTDWVNSVAFSPD--GTFVASSSQdgTIKLW--DLRTGKCVATLT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 256 GKYekpKFVQCLAFLGNG-DVLTGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGK 334
Cdd:cd00200 175 GHT---GEVNSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCL------------GTLRGHENGVNSVAFSPDGYLLASGSE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 335 DRKIILWDhdlnlereievpdqygtiravaegraeqflvgtSRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLT 414
Cdd:cd00200 240 DGTIRVWD---------------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLAS 278
|
330
....*....|.
gi 1907126843 415 CAQDRQVCMWN 425
Cdd:cd00200 279 GSADGTIRIWD 289
|
|
| WD40 |
COG2319 |
WD40 repeat [General function prediction only]; |
92-342 |
9.58e-15 |
|
WD40 repeat [General function prediction only];
Pssm-ID: 441893 [Multi-domain] Cd Length: 403 Bit Score: 76.87 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 92 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 165
Cdd:COG2319 176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 166 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 243
Cdd:COG2319 244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 244 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 322
Cdd:COG2319 319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380
|
250 260
....*....|....*....|
gi 1907126843 323 MRNGMLLTGGGKDRKIILWD 342
Cdd:COG2319 381 SPDGRTLASGSADGTVRLWD 400
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
443-669 |
1.97e-14 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 74.68 E-value: 1.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 443 CADFHPSGTVVAIGTHSGRWFVLDAETRDLVS---IHTDGneqLSVMRYSVDGTLLAVGSHDNFIYLYTvLENGRKYSRY 519
Cdd:cd00200 14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkGHTGP---VRDVAASADGTYLASGSSDKTIRLWD-LETGECVRTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 520 gkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcKLIRNRSDCKDidwttytcvlgfqvfgvwpegsdgtDINA 599
Cdd:cd00200 90 ---TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTD-------------------------WVNS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 600 LVRSHNRRVIAVADDFCKVHLFQYPCSKakaPSHKYSAHSSHVTNVSFTHNDSHLISTGGkDMSIIQWKL 669
Cdd:cd00200 141 VAFSPDGTFVASSSQDGTIKLWDLRTGK---CVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDL 206
|
|
| WD40 |
cd00200 |
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ... |
523-669 |
1.03e-08 |
|
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.
Pssm-ID: 238121 [Multi-domain] Cd Length: 289 Bit Score: 57.34 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 523 TGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGCKLIRNrsdckdidwttytcvlgfqvfgvwpEGSDGTDINALVR 602
Cdd:cd00200 6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-------------------------KGHTGPVRDVAAS 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907126843 603 SHNRRVIAVADDFCkVHLFQYpcsKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWKL 669
Cdd:cd00200 61 ADGTYLASGSSDKT-IRLWDL---ETGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDV 122
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| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
522-554 |
1.83e-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: 1.83e-04
10 20 30
....*....|....*....|....*....|...
gi 1907126843 522 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 554
Cdd:smart00320 8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
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|
| TolB |
COG0823 |
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ... |
432-552 |
1.37e-03 |
|
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440585 [Multi-domain] Cd Length: 158 Bit Score: 40.04 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126843 432 EWTRLVDEPGHCAD--FHPSGTVVAIGT-HSGRW--FVLDAETRDLVSIHTDGNEQLSVmRYSVDGTLLAVGSH-DNFIY 505
Cdd:COG0823 22 EPRRLTNSPGIDTSpaWSPDGRRIAFTSdRGGGPqiYVVDADGGEPRRLTFGGGYNASP-SWSPDGKRLAFVSRsDGRFD 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1907126843 506 LYTVLENGRKYSRYGKCTGHSSyithldWSPDNKHIM--SNSGDYEILY 552
Cdd:COG0823 101 IYVLDLDGGAPRRLTDGPGSPS------WSPDGRRIVfsSDRGGRPDLY 143
|
|
| PTZ00420 |
PTZ00420 |
coronin; Provisional |
494-557 |
2.82e-03 |
|
coronin; Provisional
Pssm-ID: 240412 [Multi-domain] Cd Length: 568 Bit Score: 41.09 E-value: 2.82e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907126843 494 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 557
Cdd:PTZ00420 89 ILASGSEDLTIRVWEIPHNDEsvKEIKDPQCilKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIEN 157
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
520-554 |
3.06e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.78 E-value: 3.06e-03
10 20 30
....*....|....*....|....*....|....*
gi 1907126843 520 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 554
Cdd:pfam00400 5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
pfam00400 |
WD domain, G-beta repeat; |
394-425 |
4.07e-03 |
|
WD domain, G-beta repeat;
Pssm-ID: 459801 [Multi-domain] Cd Length: 39 Bit Score: 35.78 E-value: 4.07e-03
10 20 30
....*....|....*....|....*....|..
gi 1907126843 394 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 425
Cdd:pfam00400 8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
|
|
| WD40 |
smart00320 |
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ... |
394-425 |
4.94e-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: 4.94e-03
10 20 30
....*....|....*....|....*....|..
gi 1907126843 394 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 425
Cdd:smart00320 9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
|
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