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Conserved domains on  [gi|1676324813|ref|NP_001138548|]
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echinoderm microtubule-associated protein-like 4 isoform b [Homo sapiens]

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 ...
170-238 2.02e-34

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: 125.74  E-value: 2.02e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676324813 170 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFN 238
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
6-64 5.06e-31

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: 115.86  E-value: 5.06e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1676324813   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 ...
444-805 1.37e-26

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 110.89  E-value: 1.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 444 SKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnpereievpdqygtiravaegkadqflvgtsrnfilrgTFN 523
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LET 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 524 DGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTrLVdepGH-----CADFHPSGTVVAIGTHSGR 598
Cdd:cd00200    41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT-LT---GHtsyvsSVAFSPDGRILSSSSRDKT 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 599 WFVLDAETRDLVSI---HTDgneqlSVM--RYSIDGTFLAVGSHDNFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSP 673
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLW----DLRTGKCVATLTGHTGEVNSVAFSP 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 674 DNKYIMSNSGDYEILYWDIPNGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRKVIAVADDFC 753
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASGSEDG 241
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1676324813 754 KVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 805
Cdd:cd00200   242 TIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
245-598 3.57e-19

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


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 88.93  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 245 RHYLGHTDCVKCLAIHPDKIRIATGqiagvDKDGRplqphVRVWDSVTLStlQIIGLGTFERGVGCLDFSkADSGvhlCI 324
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGE--LLRTLKGHTGPVRDVAAS-ADGT---YL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 325 IDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 401
Cdd:cd00200    67 ASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 402 QCLAFLGNGDVLTGDSG-GVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 480
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWDLRTGKCV------------ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 481 dlnpereievpdqygtiravaegkadqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCL 560
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1676324813 561 WNsMEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 598
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 ...
170-238 2.02e-34

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: 125.74  E-value: 2.02e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676324813 170 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFN 238
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
6-64 5.06e-31

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: 115.86  E-value: 5.06e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1676324813   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 ...
444-805 1.37e-26

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 110.89  E-value: 1.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 444 SKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnpereievpdqygtiravaegkadqflvgtsrnfilrgTFN 523
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LET 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 524 DGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTrLVdepGH-----CADFHPSGTVVAIGTHSGR 598
Cdd:cd00200    41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT-LT---GHtsyvsSVAFSPDGRILSSSSRDKT 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 599 WFVLDAETRDLVSI---HTDgneqlSVM--RYSIDGTFLAVGSHDNFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSP 673
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLW----DLRTGKCVATLTGHTGEVNSVAFSP 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 674 DNKYIMSNSGDYEILYWDIPNGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRKVIAVADDFC 753
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASGSEDG 241
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1676324813 754 KVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 805
Cdd:cd00200   242 TIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
450-806 1.16e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.39  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 450 HDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDlNPEREIEVPDQYGTIRAVA---EGKadQFLVGTSRNFILRGTFNDGF 526
Cdd:COG2319    77 HTAAVLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHTGAVRSVAfspDGK--TLASGSADGTVRLWDLATGK 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 527 QI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDA 604
Cdd:COG2319   154 LLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 605 ETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVsENGRKYSRYgrcTGHSSYITHLDWSPDNKYIMSNSGD 684
Cdd:COG2319   234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGKLLASGSDD 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 685 YEILYWDIPNGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRKVIAVADDFCKVHLFQypcSK 764
Cdd:COG2319   310 GTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVRLWD---LA 360
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1676324813 765 AKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 806
Cdd:COG2319   361 TGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
245-598 3.57e-19

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.93  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 245 RHYLGHTDCVKCLAIHPDKIRIATGqiagvDKDGRplqphVRVWDSVTLStlQIIGLGTFERGVGCLDFSkADSGvhlCI 324
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGE--LLRTLKGHTGPVRDVAAS-ADGT---YL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 325 IDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 401
Cdd:cd00200    67 ASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 402 QCLAFLGNGDVLTGDSG-GVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 480
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWDLRTGKCV------------ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 481 dlnpereievpdqygtiravaegkadqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCL 560
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1676324813 561 WNsMEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 598
Cdd:cd00200   246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
WD40 COG2319
WD40 repeat [General function prediction only];
222-562 1.51e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.12  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 222 PTGKIvyfIASV-----VVLFNYEERTQRHYL-GHTDCVKCLAIHPDKIRIATGqiagvDKDGRplqphVRVWDSVTLST 295
Cdd:COG2319   130 PDGKT---LASGsadgtVRLWDLATGKLLRTLtGHSGAVTSVAFSPDGKLLASG-----SDDGT-----VRLWDLATGKL 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 296 LQIigLGTFERGVGCLDFSkADSGVhlcIIDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPtDANTIITCGKSH- 374
Cdd:COG2319   197 LRT--LTGHTGAVRSVAFS-PDGKL---LASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGt 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 375 IFFWTW-SGNSLTRKQGIFGKyekpkfVQCLAFLGNGDVL-TGDSGGVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDG 452
Cdd:COG2319   270 VRLWDLaTGELLRTLTGHSGG------VNSVAFSPDGKLLaSGSDDGTVRLWDLATGKLL------------RTLTGHTG 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 453 SVFTLCQMRNGMLLTGGGKDRKIILWDhdlnpereievpdqygtiraVAEGKADQFLvgtsrnfilrgtfndgfqievQG 532
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD--------------------LATGELLRTL---------------------TG 370
                         330       340       350
                  ....*....|....*....|....*....|
gi 1676324813 533 HTDELWGLATHPFKDLLLTCAQDRQVCLWN 562
Cdd:COG2319   371 HTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
659-691 1.18e-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: 39.99  E-value: 1.18e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1676324813  659 CTGHSSYITHLDWSPDNKYIMSNSGDYEILYWD 691
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
660-691 1.66e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.66e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1676324813 660 TGHSSYITHLDWSPDNKYIMSNSGDYEILYWD 691
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
170-238 2.02e-34

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: 125.74  E-value: 2.02e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1676324813 170 KMFMRGRPITMFIPSD-VDNYD-DIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFN 238
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNyYPKDDlDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYD 71
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
6-64 5.06e-31

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: 115.86  E-value: 5.06e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1676324813   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 ...
444-805 1.37e-26

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 110.89  E-value: 1.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 444 SKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnpereievpdqygtiravaegkadqflvgtsrnfilrgTFN 523
Cdd:cd00200     2 RRTLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-----------------------------------------LET 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 524 DGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTrLVdepGH-----CADFHPSGTVVAIGTHSGR 598
Cdd:cd00200    41 GELLRTLKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECVRT-LT---GHtsyvsSVAFSPDGRILSSSSRDKT 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 599 WFVLDAETRDLVSI---HTDgneqlSVM--RYSIDGTFLAVGSHDNFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSP 673
Cdd:cd00200   117 IKVWDVETGKCLTTlrgHTD-----WVNsvAFSPDGTFVASSSQDGTIKLW----DLRTGKCVATLTGHTGEVNSVAFSP 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 674 DNKYIMSNSGDYEILYWDIPNGcklirnrsdckdidwttyTCVLGFQVFGVWpegsdgtdINALVRSHNRKVIAVADDFC 753
Cdd:cd00200   188 DGEKLLSSSSDGTIKLWDLSTG------------------KCLGTLRGHENG--------VNSVAFSPDGYLLASGSEDG 241
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1676324813 754 KVHLFQypcSKAKAPSHKYSAHSSHVTNVSFtHNDSHLISTGGKDMSIIQWK 805
Cdd:cd00200   242 TIRVWD---LRTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
450-806 1.16e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.39  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 450 HDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDlNPEREIEVPDQYGTIRAVA---EGKadQFLVGTSRNFILRGTFNDGF 526
Cdd:COG2319    77 HTAAVLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHTGAVRSVAfspDGK--TLASGSADGTVRLWDLATGK 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 527 QI-EVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWT-RLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDA 604
Cdd:COG2319   154 LLrTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTlTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDL 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 605 ETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVsENGRKYSRYgrcTGHSSYITHLDWSPDNKYIMSNSGD 684
Cdd:COG2319   234 ATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDL-ATGELLRTL---TGHSGGVNSVAFSPDGKLLASGSDD 309
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 685 YEILYWDIPNGcKLIRnrsdckdidwttytcvlgfqvfgvWPEGSDGtDINALVRSHNRKVIAVADDFCKVHLFQypcSK 764
Cdd:COG2319   310 GTVRLWDLATG-KLLR------------------------TLTGHTG-AVRSVAFSPDGKTLASGSDDGTVRLWD---LA 360
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1676324813 765 AKAPSHKYSAHSSHVTNVSFTHNDSHLIStGGKDMSIIQWKL 806
Cdd:COG2319   361 TGELLRTLTGHTGAVTSVAFSPDGRTLAS-GSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
328-694 8.27e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 108.07  E-value: 8.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 328 SNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPtDANTIITCGKSH-IFFWTW-SGNSLTRKQGifgkyeKPKFVQCLA 405
Cdd:COG2319    97 SADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSP-DGKTLASGSADGtVRLWDLaTGKLLRTLTG------HSGAVTSVA 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 406 FLGNGDVL-TGDSGGVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDhdlnp 484
Cdd:COG2319   170 FSPDGKLLaSGSDDGTVRLWDLATGKLL------------RTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD----- 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 485 ereievpdqygtiraVAEGKADQFLvgtsrnfilrgtfndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNsm 564
Cdd:COG2319   233 ---------------LATGKLLRTL---------------------TGHSGSVRSVAFSPDGRLLASGSADGTVRLWD-- 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 565 ehrLEWTRLVDEPGHCAD------FHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHD 638
Cdd:COG2319   275 ---LATGELLRTLTGHSGgvnsvaFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDD 351
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1676324813 639 NFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPN 694
Cdd:COG2319   352 GTVRLW----DLATGELLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
398-691 6.24e-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: 100.10  E-value: 6.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 398 PKFVQCLAFLGNGDVL-TGDSGGVMLIWSKTTVEPtpgkgpkgvyqiSKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKII 476
Cdd:cd00200     9 TGGVTCVAFSPDGKLLaTGSGDGTIKVWDLETGEL------------LRTLKGHTGPVRDVAASADGTYLASGSSDKTIR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 477 LWD-HDLNPEREIEVPDQYgtIRAVAEGKADQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCA 553
Cdd:cd00200    77 LWDlETGECVRTLTGHTSY--VSSVAFSPDGRILSSSSRDKTIKvwDVETGKCLTTLRGHTDWVNSVAFSPDGTFVASSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 554 QDRQVCLWNSMEHRLEWTRlvdePGH-----CADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSID 628
Cdd:cd00200   155 QDGTIKLWDLRTGKCVATL----TGHtgevnSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPD 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1676324813 629 GTFLAVGSHDNFIYLYvvseNGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEILYWD 691
Cdd:cd00200   231 GYLLASGSEDGTIRVW----DLRTGECVQTLSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
333-695 3.18e-22

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 100.37  E-value: 3.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 333 LTVWDWQKKAKGAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKyekpkFVQCLAFLGNGDV 412
Cdd:COG2319    18 LALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTA-----AVLSVAFSPDGRL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 413 L-TGDSGGVMLIWSKTTVEPTPgkgpkgvyqiskQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWD-HDLNPEREIEV 490
Cdd:COG2319    93 LaSASADGTVRLWDLATGLLLR------------TLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDlATGKLLRTLTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 491 PDqyGTIRAVAEGKADQFLVGTSRNFILR--GTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNsMEHRL 568
Cdd:COG2319   161 HS--GAVTSVAFSPDGKLLASGSDDGTVRlwDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWD-LATGK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 569 EWTRLVDEPG--HCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVV 646
Cdd:COG2319   238 LLRTLTGHSGsvRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDL 317
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1676324813 647 SEngrkysryGRC----TGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNG 695
Cdd:COG2319   318 AT--------GKLlrtlTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362
WD40 COG2319
WD40 repeat [General function prediction only];
461-806 4.11e-20

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 93.82  E-value: 4.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 461 RNGMLLTGGGKDRKIILWDHDLNPEREIEVPDQYGTIRAVAEGKADQFLVGTSRNFILRGTFNDG-FQIEVQGHTDELWG 539
Cdd:COG2319     4 ADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGaLLATLLGHTAAVLS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 540 LATHPFKDLLLTCAQDRQVCLWN-SMEHRLEWTRLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNE 618
Cdd:COG2319    84 VAFSPDGRLLASASADGTVRLWDlATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTLTGHSG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 619 QLSVMRYSIDGTFLAVGSHDNFIYLYVVsENGRKYSRYgrcTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNGcKL 698
Cdd:COG2319   164 AVTSVAFSPDGKLLASGSDDGTVRLWDL-ATGKLLRTL---TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATG-KL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 699 IRnrsdckdidwttytcvlgfqvfgvwPEGSDGTDINALVRSHNRKVIAVADDFCKVHLFQypcSKAKAPSHKYSAHSSH 778
Cdd:COG2319   239 LR-------------------------TLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWD---LATGELLRTLTGHSGG 290
                         330       340
                  ....*....|....*....|....*...
gi 1676324813 779 VTNVSFTHNDSHLIStGGKDMSIIQWKL 806
Cdd:COG2319   291 VNSVAFSPDGKLLAS-GSDDGTVRLWDL 317
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
245-598 3.57e-19

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 88.93  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 245 RHYLGHTDCVKCLAIHPDKIRIATGqiagvDKDGRplqphVRVWDSVTLStlQIIGLGTFERGVGCLDFSkADSGvhlCI 324
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATG-----SGDGT-----IKVWDLETGE--LLRTLKGHTGPVRDVAAS-ADGT---YL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 325 IDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTdaNTIITCGKSH--IFFWTW-SGNSLTRKQGIFGkyekpkFV 401
Cdd:cd00200    67 ASGSSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPD--GRILSSSSRDktIKVWDVeTGKCLTTLRGHTD------WV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 402 QCLAFLGNGDVLTGDSG-GVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDH 480
Cdd:cd00200   139 NSVAFSPDGTFVASSSQdGTIKLWDLRTGKCV------------ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 481 dlnpereievpdqygtiravaegkadqflvgtsRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLTCAQDRQVCL 560
Cdd:cd00200   207 ---------------------------------STGKCLGTL--------RGHENGVNSVAFSPDGYLLASGSEDGTIRV 245
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1676324813 561 WNsMEHRLEWTRLV--DEPGHCADFHPSGTVVAIGTHSGR 598
Cdd:cd00200   246 WD-LRTGECVQTLSghTNSVTSLAWSPDGKRLASGSADGT 284
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
9-64 1.65e-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: 1.65e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1676324813   9 DDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21947     2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAMLNR 57
WD40 COG2319
WD40 repeat [General function prediction only];
222-562 1.51e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.12  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 222 PTGKIvyfIASV-----VVLFNYEERTQRHYL-GHTDCVKCLAIHPDKIRIATGqiagvDKDGRplqphVRVWDSVTLST 295
Cdd:COG2319   130 PDGKT---LASGsadgtVRLWDLATGKLLRTLtGHSGAVTSVAFSPDGKLLASG-----SDDGT-----VRLWDLATGKL 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 296 LQIigLGTFERGVGCLDFSkADSGVhlcIIDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPtDANTIITCGKSH- 374
Cdd:COG2319   197 LRT--LTGHTGAVRSVAFS-PDGKL---LASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGt 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 375 IFFWTW-SGNSLTRKQGIFGKyekpkfVQCLAFLGNGDVL-TGDSGGVMLIWSKTTVEPTpgkgpkgvyqisKQIKAHDG 452
Cdd:COG2319   270 VRLWDLaTGELLRTLTGHSGG------VNSVAFSPDGKLLaSGSDDGTVRLWDLATGKLL------------RTLTGHTG 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 453 SVFTLCQMRNGMLLTGGGKDRKIILWDhdlnpereievpdqygtiraVAEGKADQFLvgtsrnfilrgtfndgfqievQG 532
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD--------------------LATGELLRTL---------------------TG 370
                         330       340       350
                  ....*....|....*....|....*....|
gi 1676324813 533 HTDELWGLATHPFKDLLLTCAQDRQVCLWN 562
Cdd:COG2319   371 HTGAVTSVAFSPDGRTLASGSADGTVRLWD 400
WD40 COG2319
WD40 repeat [General function prediction only];
499-806 4.67e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 84.58  E-value: 4.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 499 AVAEGKADQFLVGTSRNFILRGTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTRLV-DEP 577
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGhTAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 578 GHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVsENGRKYSRYg 657
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDL-ATGKLLRTL- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 658 rcTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNGcKLIRnrsdckdidwttytcvlgfqvfgVWPEGSDGtdINAL 737
Cdd:COG2319   159 --TGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATG-KLLR-----------------------TLTGHTGA--VRSV 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1676324813 738 VRSHNRKVIAVADDFCKVHLFQypcSKAKAPSHKYSAHSSHVTNVSFTHnDSHLISTGGKDMSIIQWKL 806
Cdd:COG2319   211 AFSPDGKLLASGSADGTVRLWD---LATGKLLRTLTGHSGSVRSVAFSP-DGRLLASGSADGTVRLWDL 275
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
236-562 1.32e-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: 81.23  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 236 LFNYEERTQRHYL-GHTDCVKCLAIHPDKIRIATGqiaGVDKDgrplqphVRVWDSVTLSTLQIigLGTFERGVGCLDFS 314
Cdd:cd00200    35 VWDLETGELLRTLkGHTGPVRDVAASADGTYLASG---SSDKT-------IRLWDLETGECVRT--LTGHTSYVSSVAFS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 315 KaDSGVHLCIIDDSNehmLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTdaNTIITCGKS--HIFFWtwSGNSLTRKQGIF 392
Cdd:cd00200   103 P-DGRILSSSSRDKT---IKVWDVETGKCLTTLRGHTDWVNSVAFSPD--GTFVASSSQdgTIKLW--DLRTGKCVATLT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 393 GKYekpKFVQCLAFLGNG-DVLTGDSGGVMLIWSKTTVeptpgkgpkgvyQISKQIKAHDGSVFTLCQMRNGMLLTGGGK 471
Cdd:cd00200   175 GHT---GEVNSVAFSPDGeKLLSSSSDGTIKLWDLSTG------------KCLGTLRGHENGVNSVAFSPDGYLLASGSE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 472 DRKIILWDhdlnpereievpdqygtiravaegkadqflvgtSRNFILRGTFndgfqievQGHTDELWGLATHPFKDLLLT 551
Cdd:cd00200   240 DGTIRVWD---------------------------------LRTGECVQTL--------SGHTNSVTSLAWSPDGKRLAS 278
                         330
                  ....*....|.
gi 1676324813 552 CAQDRQVCLWN 562
Cdd:cd00200   279 GSADGTIRIWD 289
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
18-61 2.33e-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: 73.34  E-value: 2.33e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1676324813  18 SDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVAS 61
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
19-64 1.78e-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: 68.31  E-value: 1.78e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1676324813  19 DVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKK 64
Cdd:cd21948     2 EVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRK 47
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
529-806 3.05e-14

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 74.29  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 529 EVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNsMEHRLEWTRLVdepGHcadfhpsgtvvaigTHSGRWFVLDAetrd 608
Cdd:cd00200     4 TLKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWD-LETGELLRTLK---GH--------------TGPVRDVAASA---- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 609 lvsihtdgneqlsvmrysiDGTFLAVGSHDNFIYLYVVsENGRKYSRYgrcTGHSSYITHLDWSPDNKYIMSNSGDYEIL 688
Cdd:cd00200    62 -------------------DGTYLASGSSDKTIRLWDL-ETGECVRTL---TGHTSYVSSVAFSPDGRILSSSSRDKTIK 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 689 YWDIPNGcKLIRNRSDCKDidwttytcvlgfqvfgvwpegsdgtDINALVRSHNRKVIAVADDFCKVHLFQYPCSKakaP 768
Cdd:cd00200   119 VWDVETG-KCLTTLRGHTD-------------------------WVNSVAFSPDGTFVASSSQDGTIKLWDLRTGK---C 169
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1676324813 769 SHKYSAHSSHVTNVSFTHNDSHLISTGGkDMSIIQWKL 806
Cdd:cd00200   170 VATLTGHTGEVNSVAFSPDGEKLLSSSS-DGTIKLWDL 206
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
14-58 6.70e-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: 6.70e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1676324813  14 AASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDH 58
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
569-689 4.64e-05

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: 44.66  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 569 EWTRLVDEPGHCAD--FHPSGTVVAIGT-HSGRW--FVLDAETRDLVSIHTDGNEQLSVmRYSIDGTFLAVGSH-DNFIY 642
Cdd:COG0823    22 EPRRLTNSPGIDTSpaWSPDGRRIAFTSdRGGGPqiYVVDADGGEPRRLTFGGGYNASP-SWSPDGKRLAFVSRsDGRFD 100
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1676324813 643 LYVVSENGRKYSRYGRCTGHSSyithldWSPDNKYIM--SNSGDYEILY 689
Cdd:COG0823   101 IYVLDLDGGAPRRLTDGPGSPS------WSPDGRRIVfsSDRGGRPDLY 143
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
659-691 1.18e-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: 39.99  E-value: 1.18e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1676324813  659 CTGHSSYITHLDWSPDNKYIMSNSGDYEILYWD 691
Cdd:smart00320   8 LKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 pfam00400
WD domain, G-beta repeat;
660-691 1.66e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.94  E-value: 1.66e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1676324813 660 TGHSSYITHLDWSPDNKYIMSNSGDYEILYWD 691
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 pfam00400
WD domain, G-beta repeat;
531-562 2.41e-03

WD domain, G-beta repeat;


Pssm-ID: 459801 [Multi-domain]  Cd Length: 39  Bit Score: 36.55  E-value: 2.41e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1676324813 531 QGHTDELWGLATHPFKDLLLTCAQDRQVCLWN 562
Cdd:pfam00400   8 EGHTGSVTSLAFSPDGKLLASGSDDGTVKVWD 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
531-562 2.96e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 36.14  E-value: 2.96e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1676324813  531 QGHTDELWGLATHPFKDLLLTCAQDRQVCLWN 562
Cdd:smart00320   9 KGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
TolB COG0823
Periplasmic component TolB of the Tol biopolymer transport system [Intracellular trafficking, ...
589-695 7.51e-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: 38.11  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1676324813 589 VVAIGTHSGRW--FVLDAETRDLVSIhTDGNEQLSVMRYSIDGTFLAVGSHDNFIY-LYVVSENGRKYSRYgrcTGHSSY 665
Cdd:COG0823     1 LAFTLSRDGNSdiYVVDLDGGEPRRL-TNSPGIDTSPAWSPDGRRIAFTSDRGGGPqIYVVDADGGEPRRL---TFGGGY 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1676324813 666 ITHLDWSPDNKYIM---SNSGDYEILYWDIPNG 695
Cdd:COG0823    77 NASPSWSPDGKRLAfvsRSDGRFDIYVLDLDGG 109
 
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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