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Conserved domains on  [gi|569002124|ref|XP_006525219|]
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echinoderm microtubule-associated protein-like 4 isoform X2 [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 ...
 250-318 4.85e-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: 4.85e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569002124  250 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 318
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 20-75 2.04e-29

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: 111.23  E-value: 2.04e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569002124  20 DDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 75
Cdd:cd21950    4 DDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 525-885 7.23e-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: 7.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 525 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 604
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 605 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 678
Cdd:cd00200   42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 679 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 749
Cdd:cd00200  117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 750 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 829
Cdd:cd00200  184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569002124 830 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 885
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 ...
 325-678 3.81e-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: 3.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 325 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 404
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 405 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 481
Cdd:cd00200   70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 482 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 560
Cdd:cd00200  139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 561 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 640
Cdd:cd00200  207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 569002124 641 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 678
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 ...
 250-318 4.85e-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: 4.85e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569002124  250 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 318
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 20-75 2.04e-29

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: 111.23  E-value: 2.04e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569002124  20 DDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 75
Cdd:cd21950    4 DDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 525-885 7.23e-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: 7.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 525 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 604
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 605 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 678
Cdd:cd00200   42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 679 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 749
Cdd:cd00200  117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 750 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 829
Cdd:cd00200  184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569002124 830 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 885
Cdd:cd00200  238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
522-886 3.19e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 112.31  E-value: 3.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 522 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 598
Cdd:COG2319   69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 599 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 676
Cdd:COG2319  146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 677 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 756
Cdd:COG2319  226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 757 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 836
Cdd:COG2319  302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 569002124 837 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 886
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 ...
 325-678 3.81e-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: 3.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 325 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 404
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 405 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 481
Cdd:cd00200   70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 482 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 560
Cdd:cd00200  139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 561 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 640
Cdd:cd00200  207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 569002124 641 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 678
Cdd:cd00200  246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
WD40 COG2319
WD40 repeat [General function prediction only];
309-559 9.40e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 77.64  E-value: 9.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 309 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 382
Cdd:COG2319  176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 383 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 460
Cdd:COG2319  244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 461 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 539
Cdd:COG2319  319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380

                        250       260
                 ....*....|....*....|
gi 569002124 540 MRNGMLLTGGGKDRKIILWD 559
Cdd:COG2319  381 SPDGRTLASGSADGTVRLWD 400
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 739-771 1.79e-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: 1.79e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 569002124   739 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 771
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
737-771 3.03e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 3.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 569002124  737 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 771
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
PTZ00420 PTZ00420
coronin; Provisional
 711-774 6.33e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 40.32  E-value: 6.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569002124 711 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 774
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 ...
 250-318 4.85e-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: 4.85e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569002124  250 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFN 318
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 20-75 2.04e-29

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: 111.23  E-value: 2.04e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569002124  20 DDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 75
Cdd:cd21950    4 DDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVKK 59
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 525-885 7.23e-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: 7.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 525 RQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnlereievpdqygtiravaegraeqflvgtsrnfilrgTFND 604
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LETG 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 605 GFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsvehrLEWTRLVDE-PGH-----CADFHPSGTVVAIGTHSGR 678
Cdd:cd00200   42 ELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWD-----LETGECVRTlTGHtsyvsSVAFSPDGRILSSSSRDKT 116

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 679 WFVLDAETRDLVSI---HTDgneqlSVM--RYSVDGTLLAVGSHDNFIYLYTVlengrkysRYGKC----TGHSSYITHL 749
Cdd:cd00200  117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLWDL--------RTGKCvatlTGHTGEVNSV 183

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 750 DWSPDNKHIMSNSGDYEILYWDIENGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRRVIAVA 829
Cdd:cd00200  184 AFSPDGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASG 237

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569002124 830 DDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 885
Cdd:cd00200  238 SEDGTIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
522-886 3.19e-26

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 112.31  E-value: 3.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 522 QINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQyGTIRAVA---EGRaeQFLVGTSRNFIL 598
Cdd:COG2319   69 ALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT-GAVRSVAfspDGK--TLASGSADGTVR 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 599 RGTFNDGFQI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHS 676
Cdd:COG2319  146 LWDLATGKLLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSAD 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 677 GRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNK 756
Cdd:COG2319  226 GTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGK 301

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 757 HIMSNSGDYEILYWDIENGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRRVIAVADDFCKVH 836
Cdd:COG2319  302 LLASGSDDGTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVR 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 569002124 837 LFQypcSKAKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 886
Cdd:COG2319  356 LWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
408-774 2.62e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 109.62  E-value: 2.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 408 SNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 485
Cdd:COG2319   97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 486 FLGNGDVL-TGDSGGVMLIWSktmvePPPGKGPkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnl 564
Cdd:COG2319  170 FSPDGKLLaSGSDDGTVRLWD-----LATGKLL-------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 565 ereievpdqygtiraVAEGRAEQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsV 644
Cdd:COG2319  233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-L 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 645 EHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIY 722
Cdd:COG2319  276 ATGELLRTLTGHSGgvNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVR 355

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 569002124 723 LYTvLENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIEN 774
Cdd:COG2319  356 LWD-LATGELLRTL---TGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
413-775 2.91e-23

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 103.45  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 413 LTVWDWQKKSKIAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKyekpkFVQCLAFLGNGDV 492
Cdd:COG2319   18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA-----AVLSVAFSPDGRL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 493 L-TGDSGGVMLIWSktmVEPPpgkgpkgvyQINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWD-HDLNLEREIEV 570
Cdd:COG2319   93 LaSASADGTVRLWD---LATG---------LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 571 PDqyGTIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCMWNsVEHRL 648
Cdd:COG2319  161 HS--GAVTSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 649 EWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTV 726
Cdd:COG2319  238 LLRTLTGHSGsvRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 569002124 727 lENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENG 775
Cdd:COG2319  318 -ATGKLLRTL---TGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 478-771 3.34e-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: 3.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 478 PKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKII 556
Cdd:cd00200    9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGELL------------RTLKGHTGPVRDVAASADGTYLASGSSDKTIR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 557 LWD-HDLNLEREIEVPDQYgtIRAVAEGRAEQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCA 633
Cdd:cd00200   77 LWDlETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 634 QDRQVCMWNSVEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVD 708
Cdd:cd00200  155 QDGTIKLWDLRTGKCVATL----TGHtgevnSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569002124 709 GTLLAVGSHDNFIYLYtvleNGRKYSRYGKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 771
Cdd:cd00200  231 GYLLASGSEDGTIRVW----DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
541-886 4.70e-21

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 96.90  E-value: 4.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 541 RNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQYGTIRAVAEGRAEQFLVGTSRNFILRGTFNDG-FQIEVQGHTDELWG 619
Cdd:COG2319    4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGaLLATLLGHTAAVLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 620 LATHPFKDLLLTCAQDRQVCMWNsVEHRLEWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGN 697
Cdd:COG2319   84 VAFSPDGRLLASASADGTVRLWD-LATGLLLRTLTGHTGavRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 698 EQLSVMRYSVDGTLLAVGSHDNFIYLYTVlENGRKYSRYgkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcK 777
Cdd:COG2319  163 GAVTSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTL---TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-K 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 778 LIRnrsdckdidwttytcvlgfqvfgvwPEGSDGTDINALVRSHNRRVIAVADDFCKVHLFQypcSKAKAPSHKYSAHSS 857
Cdd:COG2319  238 LLR-------------------------TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSG 289

                        330       340
                 ....*....|....*....|....*....
gi 569002124 858 HVTNVSFTHNDSHLIStGGKDMSIIQWKL 886
Cdd:COG2319  290 GVNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 325-678 3.81e-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: 3.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 325 RHYLGHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVIGLGTFerGVGCLDFSkADSGVHLCV 404
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGELLRTLKGHTG--PVRDVAAS-ADGTYLASG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 405 iddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 481
Cdd:cd00200   70 ---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 482 QCLAFLGNGDVLTGDSG-GVMLIWSktmvepppGKGPKGVyqinRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 560
Cdd:cd00200  139 NSVAFSPDGTFVASSSQdGTIKLWD--------LRTGKCV----ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 561 dlnlereievpdqygtiravaegraeqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCM 640
Cdd:cd00200  207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 569002124 641 WNsVEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 678
Cdd:cd00200  246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 20-75 1.79e-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: 1.79e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569002124  20 DDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 75
Cdd:cd21947    2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNR 57
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 316-642 2.14e-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: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 316 LFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiaGVDKDgrplqphVRVWDSVSLTTLHVigLGTFERGVGCLDFS 394
Cdd:cd00200   35 VWDLETGELLRTLkGHTGPVRDVAASADGTYLASG---SSDKT-------IRLWDLETGECVRT--LTGHTSYVSSVAFS 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 395 KaDSGVHLCVIDDSNehmLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTdaNTIITCGKS--HIFFWtwSGNSLTRKQGIF 472
Cdd:cd00200  103 P-DGRILSSSSRDKT---IKVWDVETGKCLTTLRGHTDWVNSVAFSPD--GTFVASSSQdgTIKLW--DLRTGKCVATLT 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 473 GKYekpKFVQCLAFLGNG-DVLTGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQMRNGMLLTGGGK 551
Cdd:cd00200  175 GHT---GEVNSVAFSPDGeKLLSSSSDGTIKLWDLSTGKCL------------GTLRGHENGVNSVAFSPDGYLLASGSE 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 552 DRKIILWDhdlnlereievpdqygtiravaegraeqflvgtSRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLT 631
Cdd:cd00200  240 DGTIRVWD---------------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLAS 278

                        330
                 ....*....|.
gi 569002124 632 CAQDRQVCMWN 642
Cdd:cd00200  279 GSADGTIRIWD 289
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 29-72 4.26e-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: 4.26e-16
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 569002124  29 SDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVAS 72
Cdd:cd21931    1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
WD40 COG2319
WD40 repeat [General function prediction only];
309-559 9.40e-15

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 77.64  E-value: 9.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 309 FIASV-----VVLFNYEERTQRHYL-GHTDCVRCLAVHPDKIRIATGqiagvDKDGRplqphVRVWDSVSLTTLHVigLG 382
Cdd:COG2319  176 LLASGsddgtVRLWDLATGKLLRTLtGHTGAVRSVAFSPDGKLLASG-----SADGT-----VRLWDLATGKLLRT--LT 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 383 TFERGVGCLDFSkADsGVHLCVIddSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW- 460
Cdd:COG2319  244 GHSGSVRSVAFS-PD-GRLLASG--SADGTVRLWDLATGELLRTLTGHSGGVNSVAFSP-DGKLLASGSDDGtVRLWDLa 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 461 SGNSLTRKQGifgkyeKPKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTMVEPPpgkgpkgvyqinRQIKAHDGSVFTLCQ 539
Cdd:COG2319  319 TGKLLRTLTG------HTGAVRSVAFSPDGKTLaSGSDDGTVRLWDLATGELL------------RTLTGHTGAVTSVAF 380

                        250       260
                 ....*....|....*....|
gi 569002124 540 MRNGMLLTGGGKDRKIILWD 559
Cdd:COG2319  381 SPDGRTLASGSADGTVRLWD 400
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 660-886 1.14e-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: 75.83  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 660 CADFHPSGTVVAIGTHSGRWFVLDAETRDLVS---IHTDGneqLSVMRYSVDGTLLAVGSHDNFIYLYTvLENGRKYSRY 736
Cdd:cd00200   14 CVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkGHTGP---VRDVAASADGTYLASGSSDKTIRLWD-LETGECVRTL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 737 gkcTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGcKLIRNRSDCKDidwttytcvlgfqvfgvwpegsdgtDINA 816
Cdd:cd00200   90 ---TGHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETG-KCLTTLRGHTD-------------------------WVNS 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 817 LVRSHNRRVIAVADDFCKVHLFQYPCSKakaPSHKYSAHSSHVTNVSFTHNDSHLISTGGkDMSIIQWKL 886
Cdd:cd00200  141 VAFSPDGTFVASSSQDGTIKLWDLRTGK---CVATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDL 206
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 30-75 3.27e-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: 67.54  E-value: 3.27e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 569002124  30 DVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 75
Cdd:cd21948    2 EVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRK 47
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 25-69 7.25e-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: 7.25e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 569002124  25 AASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDH 69
Cdd:cd21949    1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 740-886 7.67e-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: 7.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 740 TGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGCKLIRNrsdckdidwttytcvlgfqvfgvwpEGSDGTDINALVR 819
Cdd:cd00200    6 KGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRTL-------------------------KGHTGPVRDVAAS 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569002124 820 SHNRRVIAVADD-FCKVhlfqYPcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWKL 886
Cdd:cd00200   61 ADGTYLASGSSDkTIRL----WD-LETGECVRTLTGHTSYVSSVAF-SPDGRILSSSSRDKTIKVWDV 122
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 739-771 1.79e-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: 1.79e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 569002124   739 CTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 771
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
 649-769 1.54e-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: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569002124 649 EWTRLVDEPGHCAD--FHPSGTVVAIGT-HSGRW--FVLDAETRDLVSIHTDGNEQLSVmRYSVDGTLLAVGSH-DNFIY 722
Cdd:COG0823   22 EPRRLTNSPGIDTSpaWSPDGRRIAFTSdRGGGPqiYVVDADGGEPRRLTFGGGYNASP-SWSPDGKRLAFVSRsDGRFD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 569002124 723 LYTVLENGRKYSRYGKCTGHSSyithldWSPDNKHIM--SNSGDYEILY 769
Cdd:COG0823  101 IYVLDLDGGAPRRLTDGPGSPS------WSPDGRRIVfsSDRGGRPDLY 143
WD40 pfam00400
WD domain, G-beta repeat;
737-771 3.03e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.17  E-value: 3.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 569002124  737 GKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWD 771
Cdd:pfam00400   5 KTLEGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
611-642 4.23e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 35.78  E-value: 4.23e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 569002124  611 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 642
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 611-642 4.98e-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: 4.98e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 569002124   611 QGHTDELWGLATHPFKDLLLTCAQDRQVCMWN 642
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
PTZ00420 PTZ00420
coronin; Provisional
 711-774 6.33e-03

coronin; Provisional


Pssm-ID: 240412 [Multi-domain]  Cd Length: 568  Bit Score: 40.32  E-value: 6.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569002124 711 LLAVGSHDNFIYLYTVLENGR--KYSRYGKC--TGHSSYITHLDWSPDNKHIMSNSG-DYEILYWDIEN 774
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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