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Conserved domains on  [gi|1827393000|ref|NP_001366302|]
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echinoderm microtubule-associated protein-like 4 isoform 6 [Mus musculus]

Protein Classification

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 ...
 228-296 4.74e-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: 4.74e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827393000 228 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 296
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 1.50e-30

trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm microtubule-associated protein-like 4 (EMAP-4), also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to the N-terminal trimerization domain of EMAP-4.


:

Pssm-ID: 409271  Cd Length: 59  Bit Score: 114.31  E-value: 1.50e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1827393000   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950     1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 503-863 9.34e-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: 111.27  E-value: 9.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 503 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 582
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 583 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 656
Cdd:cd00200    42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 657 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 727
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 728 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 807
Cdd:cd00200   184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827393000 808 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 863
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 ...
 303-656 5.76e-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: 91.24  E-value: 5.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 303 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 382
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 383 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 459
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 460 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 538
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 539 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 618
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1827393000 619 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 656
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 ...
 228-296 4.74e-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: 4.74e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827393000 228 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 296
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 1.50e-30

trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm microtubule-associated protein-like 4 (EMAP-4), also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to the N-terminal trimerization domain of EMAP-4.


Pssm-ID: 409271  Cd Length: 59  Bit Score: 114.31  E-value: 1.50e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1827393000   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950     1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 503-863 9.34e-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: 111.27  E-value: 9.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 503 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 582
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 583 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 656
Cdd:cd00200    42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 657 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 727
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 728 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 807
Cdd:cd00200   184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827393000 808 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 863
Cdd:cd00200   238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
500-864 6.29e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.54  E-value: 6.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 500 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 576
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 577 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 654
Cdd:COG2319   146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 655 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 734
Cdd:COG2319   226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 735 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 814
Cdd:COG2319   302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1827393000 815 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 864
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 ...
 303-656 5.76e-20

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 91.24  E-value: 5.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 303 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 382
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 383 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 459
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 460 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 538
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 539 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 618
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1827393000 619 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 656
Cdd:cd00200   246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
WD40 COG2319
WD40 repeat [General function prediction only];
287-537 1.48e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.87  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 287 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 360
Cdd:COG2319   176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 361 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 438
Cdd:COG2319   244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 439 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 517
Cdd:COG2319   319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380

                         250       260
                  ....*....|....*....|
gi 1827393000 518 MRNGMLLTGGGKDRKIILWD 537
Cdd:COG2319   381 SPDGRTLASGSADGTVRLWD 400
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 717-749 1.82e-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: 1.82e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1827393000  717 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 749
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
715-749 3.05e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 3.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1827393000 715 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 749
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 689-752 5.42e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 40.70  E-value: 5.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827393000 689 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 752
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 ...
 228-296 4.74e-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: 4.74e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827393000 228 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 296
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 6-64 1.50e-30

trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm microtubule-associated protein-like 4 (EMAP-4), also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to the N-terminal trimerization domain of EMAP-4.


Pssm-ID: 409271  Cd Length: 59  Bit Score: 114.31  E-value: 1.50e-30
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1827393000   6 GSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21950     1 GSLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 503-863 9.34e-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: 111.27  E-value: 9.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 503 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 582
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 583 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 656
Cdd:cd00200    42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 657 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 727
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 728 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 807
Cdd:cd00200   184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827393000 808 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 863
Cdd:cd00200   238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
500-864 6.29e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 111.54  E-value: 6.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 500 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 576
Cdd:COG2319    69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 577 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 654
Cdd:COG2319   146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 655 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 734
Cdd:COG2319   226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 735 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 814
Cdd:COG2319   302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1827393000 815 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 864
Cdd:COG2319   356 LWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
386-752 4.98e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.85  E-value: 4.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 386 SNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 463
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 464 FLGNGDVL-TGDSGGVMLIWSktmvePPPGKGPkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnl 542
Cdd:COG2319   170 FSPDGKLLaSGSDDGTVRLWD-----LATGKLL-------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 543 ereievpdqygtiraVAEGRAEQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsV 622
Cdd:COG2319   233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-L 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 623 EHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIY 700
Cdd:COG2319   276 ATGELLRTLTGHSGgvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVR 355

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1827393000 701 LYTvLENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIEN 752
Cdd:COG2319   356 LWD-LATGELLRTL---TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 456-749 4.23e-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: 100.49  E-value: 4.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 456 PKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKII 534
Cdd:cd00200     9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELL------------RTLKGHTGPVRDVAASADGTYLASGSSDKTIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 535 LWD-HDLNLEREIEVPDQYgtIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCA 611
Cdd:cd00200    77 LWDlETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 612 QDRQVCMWNSVEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVD 686
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATL----TGHtgevnSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827393000 687 GTLLAVGSHDNFIYLYtvleNGRKYSRYGKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 749
Cdd:cd00200   231 GYLLASGSEDGTIRVW----DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
391-753 4.84e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 102.68  E-value: 4.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 391 LTVWDWQKKSKIAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKyekpkFVQCLAFLGNGDV 470
Cdd:COG2319    18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA-----AVLSVAFSPDGRL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 471 L-TGDSGGVMLIWSktmVEPPpgkgpkgvyQINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWD-HDLNLEREIEV 548
Cdd:COG2319    93 LaSASADGTVRLWD---LATG---------LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 549 PDqyGTIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsVEHRL 626
Cdd:COG2319   161 HS--GAVTSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 627 EWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTV 704
Cdd:COG2319   238 LLRTLTGHSGsvRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1827393000 705 lENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENG 753
Cdd:COG2319   318 -ATGKLLRTL---TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362
WD40 COG2319
WD40 repeat [General function prediction only];
519-864 7.80e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.13  E-value: 7.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 519 RNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQYGTIRAVAEGRAEQFLVGTSRNFILRGTFNDG-FQIEVQGHTDELWG 597
Cdd:COG2319     4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGaLLATLLGHTAAVLS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 598 LATHPFKDLLLTCAQDRQVCMWNsVEHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGN 675
Cdd:COG2319    84 VAFSPDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGavRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 676 EQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcK 755
Cdd:COG2319   163 GAVTSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTL---TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-K 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 756 LIRnrsdckdidwttytcvlgfqvfgvwPEGSDGTDINALVRSHNRRVIAVADDFCKVHLFQypcSKAKAPSHKYSAHSS 835
Cdd:COG2319   238 LLR-------------------------TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSG 289

                         330       340
                  ....*....|....*....|....*....
gi 1827393000 836 HVTNVSFTHNDSHLIStGGKDMSIIQWKL 864
Cdd:COG2319   290 GVNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 303-656 5.76e-20

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 91.24  E-value: 5.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 303 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 382
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 383 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 459
Cdd:cd00200    70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 460 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 538
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 539 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 618
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1827393000 619 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 656
Cdd:cd00200   246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 9-64 1.75e-18

trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm microtubule-associated protein-like 1 (EMAP-1), also called EMAL1, EMAPL, or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. This model corresponds to a conserved region located at the N-terminus of EMAP-1, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-4 and EMAP-2.


Pssm-ID: 409268  Cd Length: 58  Bit Score: 80.15  E-value: 1.75e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1827393000   9 DDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21947     2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNR 57
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 294-620 2.89e-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: 80.46  E-value: 2.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 294 LFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiaGVDKDgrplqphVRVWDSVSLTTLHVigLGTFERGVGCLDFS 372
Cdd:cd00200    35 VWDLETGELLRTLkGHTGPVRDVAASADGTYLASG---SSDKT-------IRLWDLETGECVRT--LTGHTSYVSSVAFS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 373 KaDSGVHLCVIDDSNehmLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKS--HIFFWtwSGNSLTRKQGIF 450
Cdd:cd00200   103 P-DGRILSSSSRDKT---IKVWDVETGKCLTTLRGHTDWVNSVAFSPD--GTFVASSSQdgTIKLW--DLRTGKCVATLT 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 451 GKYekpKFVQCLAFLGNG-DVLTGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGK 529
Cdd:cd00200   175 GHT---GEVNSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCL------------GTLRGHENGVNSVAFSPDGYLLASGSE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 530 DRKIILWDhdlnlereievpdqygtiravaegraeqflvgtSRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLT 609
Cdd:cd00200   240 DGTIRVWD---------------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLAS 278

                         330
                  ....*....|.
gi 1827393000 610 CAQDRQVCMWN 620
Cdd:cd00200   279 GSADGTIRIWD 289
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 18-61 3.64e-16

trimerization domain of the echinoderm microtubule-associated protein-like family; The echinoderm microtubule-associated protein (EMAP)-like (EML) family includes EMAP-1, EMAP-2, EMAP-3, and EMAP-4. EMAP-1, also called EMAL1, EMAPL or EMAPL1, modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. It is required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. EMAP-2, also called EML2 or EMAPL2, is a tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. EMAP-3, also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. EMAP-4, also called EML4, EMAPL4, restrictedly overexpressed proliferation-associated protein, or Ropp 120, may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved trimerization domain located at the N-terminus of EML family members.


Pssm-ID: 409267  Cd Length: 44  Bit Score: 72.95  E-value: 3.64e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1827393000  18 SDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVAS 61
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 638-864 1.38e-14

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 75.45  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 638 CADFHPSGTVVAIGTHSGRWFVLDAETRDLVS---IHTDGneqLSVMRYSVDGTLLAVGSHDNFIYLYTvLENGRKYSRY 714
Cdd:cd00200    14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkGHTGP---VRDVAASADGTYLASGSSDKTIRLWD-LETGECVRTL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 715 gkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcKLIRNRSDCKDidwttytcvlgfqvfgvwpegsdgtDINA 794
Cdd:cd00200    90 ---TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTD-------------------------WVNS 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 795 LVRSHNRRVIAVADDFCKVHLFQYPCSKakaPSHKYSAHSSHVTNVSFTHNDSHLISTGGkDMSIIQWKL 864
Cdd:cd00200   141 VAFSPDGTFVASSSQDGTIKLWDLRTGK---CVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDL 206
WD40 COG2319
WD40 repeat [General function prediction only];
287-537 1.48e-14

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 76.87  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 287 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 360
Cdd:COG2319   176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 361 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 438
Cdd:COG2319   244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 439 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 517
Cdd:COG2319   319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380

                         250       260
                  ....*....|....*....|
gi 1827393000 518 MRNGMLLTGGGKDRKIILWD 537
Cdd:COG2319   381 SPDGRTLASGSADGTVRLWD 400
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 19-64 2.55e-14

trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm microtubule-associated protein-like 2 (EMAP-2), also called EML2 or EMAPL2, is a tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules. This model corresponds to the N-terminal trimerization domain of EMAP-2.


Pssm-ID: 409269  Cd Length: 48  Bit Score: 67.92  E-value: 2.55e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1827393000  19 DVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21948     2 EVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRK 47
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 14-58 7.09e-12

trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm microtubule-associated protein-like 3 (EMAP-3), also called EML3, is a nuclear microtubule-binding protein required for the correct alignment of chromosomes in metaphase. It may modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic. This model corresponds to a conserved region located at the N-terminus of EMAP-3, which shows high sequence similarity with the N-terminal trimerization domain of EMAP-2 and EMAP-4.


Pssm-ID: 409270  Cd Length: 48  Bit Score: 60.81  E-value: 7.09e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1827393000  14 AASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDH 58
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 718-864 8.72e-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: 57.73  E-value: 8.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 718 TGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGCKLIRNrsdckdidwttytcvlgfqvfgvwpEGSDGTDINALVR 797
Cdd:cd00200     6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-------------------------KGHTGPVRDVAAS 60

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827393000 798 SHNRRVIAVADD-FCKVhlfqYPcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWKL 864
Cdd:cd00200    61 ADGTYLASGSSDkTIRL----WD-LETGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDV 122
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 717-749 1.82e-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: 1.82e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1827393000  717 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 749
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 627-747 1.63e-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: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827393000 627 EWTRLVDEPGHCAD--FHPSGTVVAIGT-HSGRW--FVLDAETRDLVSIHTDGNEQLSVmRYSVDGTLLAVGSH-DNFIY 700
Cdd:COG0823    22 EPRRLTNSPGIDTSpaWSPDGRRIAFTSdRGGGPqiYVVDADGGEPRRLTFGGGYNASP-SWSPDGKRLAFVSRsDGRFD 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1827393000 701 LYTVLENGRKYSRYGKCTGHSSyithldWSPDNKHIM--SNSGDYEILY 747
Cdd:COG0823   101 IYVLDLDGGAPRRLTDGPGSPS------WSPDGRRIVfsSDRGGRPDLY 143
WD40 pfam00400
WD domain, G-beta repeat;
715-749 3.05e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 3.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1827393000 715 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 749
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
589-620 4.22e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 4.22e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1827393000 589 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 620
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 589-620 5.02e-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: 5.02e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1827393000  589 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 620
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 689-752 5.42e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 40.70  E-value: 5.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827393000 689 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 752
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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