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Conserved domains on  [gi|1907126834|ref|XP_036016743|]
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echinoderm microtubule-associated protein-like 4 isoform X7 [Mus musculus]

Protein Classification

HELP and WD40 domain-containing protein( domain architecture ID 13687810)

HELP and WD40 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 174-242 4.47e-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: 4.47e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907126834 174 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 242
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 ...
 449-809 6.34e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 111.66  E-value: 6.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 449 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 528
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 529 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 602
Cdd:cd00200    42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 603 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 673
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 674 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 753
Cdd:cd00200   184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907126834 754 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 809
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 ...
 249-602 3.32e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 92.01  E-value: 3.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 249 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 328
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 329 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 405
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 406 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 484
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 485 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 564
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1907126834 565 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 602
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 ...
 174-242 4.47e-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: 4.47e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907126834 174 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 242
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 449-809 6.34e-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: 111.66  E-value: 6.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 449 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 528
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 529 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 602
Cdd:cd00200    42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 603 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 673
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 674 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 753
Cdd:cd00200   184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907126834 754 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 809
Cdd:cd00200   238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
446-810 1.32e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.47  E-value: 1.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 446 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 522
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 523 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 600
Cdd:COG2319   146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 601 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 680
Cdd:COG2319   226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 681 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 760
Cdd:COG2319   302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907126834 761 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 810
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 ...
 249-602 3.32e-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: 92.01  E-value: 3.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 249 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 328
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 329 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 405
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 406 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 484
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 485 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 564
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1907126834 565 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 602
Cdd:cd00200   246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
WD40 COG2319
WD40 repeat [General function prediction only];
233-483 4.50e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.41  E-value: 4.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 233 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 306
Cdd:COG2319   176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 307 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 384
Cdd:COG2319   244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 385 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 463
Cdd:COG2319   319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380

                         250       260
                  ....*....|....*....|
gi 1907126834 464 MRNGMLLTGGGKDRKIILWD 483
Cdd:COG2319   381 SPDGRTLASGSADGTVRLWD 400
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 663-695 1.69e-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: 1.69e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907126834  663 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 695
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
661-695 2.80e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 2.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907126834 661 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 695
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 635-698 5.87e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 40.32  E-value: 5.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907126834 635 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 698
Cdd:PTZ00420   89 ILASGSEDLTIRVWEIPHNDEsvKEIKDPQCilKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIEN 157
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 174-242 4.47e-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: 4.47e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907126834 174 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 242
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 449-809 6.34e-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: 111.66  E-value: 6.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 449 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 528
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 529 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 602
Cdd:cd00200    42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 603 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 673
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 674 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 753
Cdd:cd00200   184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907126834 754 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 809
Cdd:cd00200   238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
446-810 1.32e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 113.47  E-value: 1.32e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 446 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 522
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 523 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 600
Cdd:COG2319   146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 601 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 680
Cdd:COG2319   226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 681 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 760
Cdd:COG2319   302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907126834 761 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 810
Cdd:COG2319   356 LWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
332-698 9.71e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.77  E-value: 9.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 332 SNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 409
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 410 FLGNGDVL-TGDSGGVMLIWSktmvePPPGKGPkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnl 488
Cdd:COG2319   170 FSPDGKLLaSGSDDGTVRLWD-----LATGKLL-------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 489 ereievpdqygtiraVAEGRAEQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsV 568
Cdd:COG2319   233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-L 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 569 EHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIY 646
Cdd:COG2319   276 ATGELLRTLTGHSGgvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVR 355

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907126834 647 LYTvLENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIEN 698
Cdd:COG2319   356 LWD-LATGELLRTL---TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
337-699 1.28e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 104.61  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 337 LTVWDWQKKSKIAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKyekpkFVQCLAFLGNGDV 416
Cdd:COG2319    18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA-----AVLSVAFSPDGRL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 417 L-TGDSGGVMLIWSktmVEPPpgkgpkgvyQINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWD-HDLNLEREIEV 494
Cdd:COG2319    93 LaSASADGTVRLWD---LATG---------LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 495 PDqyGTIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsVEHRL 572
Cdd:COG2319   161 HS--GAVTSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 573 EWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTV 650
Cdd:COG2319   238 LLRTLTGHSGsvRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1907126834 651 lENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENG 699
Cdd:COG2319   318 -ATGKLLRTL---TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 402-695 2.99e-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: 100.87  E-value: 2.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 402 PKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKII 480
Cdd:cd00200     9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELL------------RTLKGHTGPVRDVAASADGTYLASGSSDKTIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 481 LWD-HDLNLEREIEVPDQYgtIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCA 557
Cdd:cd00200    77 LWDlETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 558 QDRQVCMWNSVEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVD 632
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATL----TGHtgevnSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907126834 633 GTLLAVGSHDNFIYLYtvleNGRKYSRYGKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 695
Cdd:cd00200   231 GYLLASGSEDGTIRVW----DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
465-810 2.23e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 97.67  E-value: 2.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 465 RNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQYGTIRAVAEGRAEQFLVGTSRNFILRGTFNDG-FQIEVQGHTDELWG 543
Cdd:COG2319     4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGaLLATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 544 LATHPFKDLLLTCAQDRQVCMWNsVEHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGN 621
Cdd:COG2319    84 VAFSPDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGavRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 622 EQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcK 701
Cdd:COG2319   163 GAVTSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTL---TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-K 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 702 LIRnrsdckdidwttytcvlgfqvfgvwPEGSDGTDINALVRSHNRRVIAVADDFCKVHLFQypcSKAKAPSHKYSAHSS 781
Cdd:COG2319   238 LLR-------------------------TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSG 289

                         330       340
                  ....*....|....*....|....*....
gi 1907126834 782 HVTNVSFTHNDSHLIStGGKDMSIIQWKL 810
Cdd:COG2319   290 GVNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 249-602 3.32e-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: 92.01  E-value: 3.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 249 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 328
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 329 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 405
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 406 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 484
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 485 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 564
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1907126834 565 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 602
Cdd:cd00200   246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 240-566 1.89e-16

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 80.84  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 240 LFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiaGVDKDgrplqphVRVWDSVSLTTLHVigLGTFERGVGCLDFS 318
Cdd:cd00200    35 VWDLETGELLRTLkGHTGPVRDVAASADGTYLASG---SSDKT-------IRLWDLETGECVRT--LTGHTSYVSSVAFS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 319 KaDSGVHLCVIDDSNehmLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKS--HIFFWtwSGNSLTRKQGIF 396
Cdd:cd00200   103 P-DGRILSSSSRDKT---IKVWDVETGKCLTTLRGHTDWVNSVAFSPD--GTFVASSSQdgTIKLW--DLRTGKCVATLT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 397 GKYekpKFVQCLAFLGNG-DVLTGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGK 475
Cdd:cd00200   175 GHT---GEVNSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCL------------GTLRGHENGVNSVAFSPDGYLLASGSE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 476 DRKIILWDhdlnlereievpdqygtiravaegraeqflvgtSRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLT 555
Cdd:cd00200   240 DGTIRVWD---------------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLAS 278

                         330
                  ....*....|.
gi 1907126834 556 CAQDRQVCMWN 566
Cdd:cd00200   279 GSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
233-483 4.50e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 78.41  E-value: 4.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 233 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 306
Cdd:COG2319   176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 307 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 384
Cdd:COG2319   244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 385 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 463
Cdd:COG2319   319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380

                         250       260
                  ....*....|....*....|
gi 1907126834 464 MRNGMLLTGGGKDRKIILWD 483
Cdd:COG2319   381 SPDGRTLASGSADGTVRLWD 400
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 584-810 9.93e-15

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 75.83  E-value: 9.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 584 CADFHPSGTVVAIGTHSGRWFVLDAETRDLVS---IHTDGneqLSVMRYSVDGTLLAVGSHDNFIYLYTvLENGRKYSRY 660
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkGHTGP---VRDVAASADGTYLASGSSDKTIRLWD-LETGECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 661 gkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcKLIRNRSDCKDidwttytcvlgfqvfgvwpegsdgtDINA 740
Cdd:cd00200    90 ---TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTD-------------------------WVNS 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 741 LVRSHNRRVIAVADDFCKVHLFQYPCSKakaPSHKYSAHSSHVTNVSFTHNDSHLISTGGkDMSIIQWKL 810
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 ...
 664-810 6.84e-09

WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions including adaptor/regulatory modules in signal transduction, pre-mRNA processing and cytoskeleton assembly; typically contains a GH dipeptide 11-24 residues from its N-terminus and the WD dipeptide at its C-terminus and is 40 residues long, hence the name WD40; between GH and WD lies a conserved core; serves as a stable propeller-like platform to which proteins can bind either stably or reversibly; forms a propeller-like structure with several blades where each blade is composed of a four-stranded anti-parallel b-sheet; instances with few detectable copies are hypothesized to form larger structures by dimerization; each WD40 sequence repeat forms the first three strands of one blade and the last strand in the next blade; the last C-terminal WD40 repeat completes the blade structure of the first WD40 repeat to create the closed ring propeller-structure; residues on the top and bottom surface of the propeller are proposed to coordinate interactions with other proteins and/or small ligands; 7 copies of the repeat are present in this alignment.


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 58.12  E-value: 6.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 664 TGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGCKLIRNrsdckdidwttytcvlgfqvfgvwpEGSDGTDINALVR 743
Cdd:cd00200     6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-------------------------KGHTGPVRDVAAS 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907126834 744 SHNRRVIAVADD-FCKVhlfqYPcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWKL 810
Cdd:cd00200    61 ADGTYLASGSSDkTIRL----WD-LETGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDV 122
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 663-695 1.69e-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: 1.69e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907126834  663 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 695
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 573-693 1.34e-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: 40.43  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907126834 573 EWTRLVDEPGHCAD--FHPSGTVVAIGT-HSGRW--FVLDAETRDLVSIHTDGNEQLSVmRYSVDGTLLAVGSH-DNFIY 646
Cdd:COG0823    22 EPRRLTNSPGIDTSpaWSPDGRRIAFTSdRGGGPqiYVVDADGGEPRRLTFGGGYNASP-SWSPDGKRLAFVSRsDGRFD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907126834 647 LYTVLENGRKYSRYGKCTGHSSyithldWSPDNKHIM--SNSGDYEILY 693
Cdd:COG0823   101 IYVLDLDGGAPRRLTDGPGSPS------WSPDGRRIVfsSDRGGRPDLY 143
WD40 pfam00400
WD domain, G-beta repeat;
661-695 2.80e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 2.80e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907126834 661 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 695
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
535-566 3.91e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 3.91e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907126834 535 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 566
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 535-566 4.56e-03

WD40 repeats; Note that these repeats are permuted with respect to the structural repeats (blades) of the beta propeller domain.


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.75  E-value: 4.56e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907126834  535 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 566
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 635-698 5.87e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 40.32  E-value: 5.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907126834 635 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 698
Cdd:PTZ00420   89 ILASGSEDLTIRVWEIPHNDEsvKEIKDPQCilKGHKKKISIIDWNPMNYYIMCSSGfDSFVNIWDIEN 157
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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