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Conserved domains on  [gi|2447069188|ref|NP_620276|]
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echinoderm microtubule-associated protein-like 2 isoform 2 [Rattus norvegicus]

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 ...
214-285 6.46e-37

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: 132.68  E-value: 6.46e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2447069188 214 KMFLRGRPVPMLIPDELAPTYSLDTRSELPSSRLKLDWVYGYRGRDCRANLYLLPTGEVVYFVASVAVLYSV 285
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
450-841 2.48e-36

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.97  E-value: 2.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 450 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQEVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWGSDYSKVQEVEVPEDf 529
Cdd:COG2319    42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 530 GPVRTVA-EGRGDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSETHQPVWS- 606
Cdd:COG2319   121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 607 RSIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTDTRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 686
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 687 KVSRLGkcsGHSSFITHLDWAQDSTCFVTNSGDYEILYWDAATCKQITSADtvrnvqwatatcvlgfgvfgiwpegADGT 766
Cdd:COG2319   280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447069188 767 DINAVARSHDGNLLVSADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMVLtTGGKDTSVLQWRVA 841
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLA-SGSADGTVRLWDLA 402
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
59-106 3.18e-25

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: 98.74  E-value: 3.18e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2447069188  59 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAALRAR 106
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 COG2319
WD40 repeat [General function prediction only];
288-600 1.79e-24

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.92  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 288 QRQRHYLGHNDDIKCLAVHPDMVTIATGQVAGTtkegkplpphVRVWDSVSLSTLHVLGLGvfDRAVCCVAFSkSNGGNL 367
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT----------VRLWDLATGKLLRTLTGH--SGAVTSVAFS-PDGKLL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 368 LCAvdeSNDHVLSVWDWAKESKVVDSKCSNEAVLVATFHPtDPNLLITCGKSH-IYFWSLEGGnlsKRQGLFEKHEKPky 446
Cdd:COG2319   178 ASG---SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATG---KLLRTLTGHSGS-- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 447 VLCVTFLEGGD-VVTGDSGGNLYVWGKGGNRITQeVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWgsDYSKVQEVEV 525
Cdd:COG2319   249 VRSVAFSPDGRlLASGSADGTVRLWDLATGELLR-TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW--DLATGKLLRT 325
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2447069188 526 PEDF-GPVRTVA-EGRGDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSET 600
Cdd:COG2319   326 LTGHtGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGELLRTlTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
214-285 6.46e-37

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: 132.68  E-value: 6.46e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2447069188 214 KMFLRGRPVPMLIPDELAPTYSLDTRSELPSSRLKLDWVYGYRGRDCRANLYLLPTGEVVYFVASVAVLYSV 285
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
450-841 2.48e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.97  E-value: 2.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 450 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQEVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWGSDYSKVQEVEVPEDf 529
Cdd:COG2319    42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 530 GPVRTVA-EGRGDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSETHQPVWS- 606
Cdd:COG2319   121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 607 RSIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTDTRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 686
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 687 KVSRLGkcsGHSSFITHLDWAQDSTCFVTNSGDYEILYWDAATCKQITSADtvrnvqwatatcvlgfgvfgiwpegADGT 766
Cdd:COG2319   280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447069188 767 DINAVARSHDGNLLVSADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMVLtTGGKDTSVLQWRVA 841
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLA-SGSADGTVRLWDLA 402
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
59-106 3.18e-25

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: 98.74  E-value: 3.18e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2447069188  59 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAALRAR 106
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
400-726 8.37e-25

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: 105.49  E-value: 8.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 400 VLVATFHPtDPNLLITCGKSH-IYFWSLEGGNLSKRqglFEKHEKPkyVLCVTFLEGGD-VVTGDSGGNLYVWGKGGNRI 477
Cdd:cd00200    12 VTCVAFSP-DGKLLATGSGDGtIKVWDLETGELLRT---LKGHTGP--VRDVAASADGTyLASGSSDKTIRLWDLETGEC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 478 TQEVLGaHDGGVFALCALRDGTLVSGGGRDRRVVLWgsdyskvqevevpeDFGPVRTVAEGRGdtlyvgttrnsillgsv 557
Cdd:cd00200    86 VRTLTG-HTSYVSSVAFSPDGRILSSSSRDKTIKVW--------------DVETGKCLTTLRG----------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 558 HTGFsllvqghveeLWGLATHPSRAQFVSCGQDKLVHLWSSETHQPVWSRSI-EDPARSAGFHPSGSVLAVGTVTGRWLL 636
Cdd:cd00200   134 HTDW----------VNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 637 LDTDTRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQGgrkvSRLGKCSGHSSFITHLDWAQDSTCFVTN 716
Cdd:cd00200   204 WDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG----ECVQTLSGHTNSVTSLAWSPDGKRLASG 279
                         330
                  ....*....|
gi 2447069188 717 SGDYEILYWD 726
Cdd:cd00200   280 SADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
288-600 1.79e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.92  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 288 QRQRHYLGHNDDIKCLAVHPDMVTIATGQVAGTtkegkplpphVRVWDSVSLSTLHVLGLGvfDRAVCCVAFSkSNGGNL 367
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT----------VRLWDLATGKLLRTLTGH--SGAVTSVAFS-PDGKLL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 368 LCAvdeSNDHVLSVWDWAKESKVVDSKCSNEAVLVATFHPtDPNLLITCGKSH-IYFWSLEGGnlsKRQGLFEKHEKPky 446
Cdd:COG2319   178 ASG---SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATG---KLLRTLTGHSGS-- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 447 VLCVTFLEGGD-VVTGDSGGNLYVWGKGGNRITQeVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWgsDYSKVQEVEV 525
Cdd:COG2319   249 VRSVAFSPDGRlLASGSADGTVRLWDLATGELLR-TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW--DLATGKLLRT 325
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2447069188 526 PEDF-GPVRTVA-EGRGDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSET 600
Cdd:COG2319   326 LTGHtGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGELLRTlTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
291-597 5.74e-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: 5.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 291 RHYLGHNDDIKCLAVHPDMVTIATGQVAGTtkegkplpphVRVWDSVSLSTLHVL-GLGVFDRAVCCVAFSKSnggnLLC 369
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT----------IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 370 AvdeSNDHVLSVWDWAKESKVVDSKCSNEAVLVATFHPTDPnLLITCGKSH-IYFWSLEGGNLSKRqglFEKHEKPkyVL 448
Cdd:cd00200    69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 449 CVTFLEGGDVVTGDSG-GNLYVW-GKGGNRITqeVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWgsDYSKVQEVEVP 526
Cdd:cd00200   140 SVAFSPDGTFVASSSQdGTIKLWdLRTGKCVA--TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTL 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2447069188 527 EDF-GPVRTVA-EGRGDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWS 597
Cdd:cd00200   216 RGHeNGVNSVAfSPDGYLLASGSEDGTIRVWDLRTGECVQTlSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
641-679 6.80e-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: 34.98  E-value: 6.80e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2447069188  641 TRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVY 679
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
214-285 6.46e-37

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: 132.68  E-value: 6.46e-37
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2447069188 214 KMFLRGRPVPMLIPDELAPTYSLDTRSELPSSRLKLDWVYGYRGRDCRANLYLLPTGEVVYFVASVAVLYSV 285
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
450-841 2.48e-36

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 141.97  E-value: 2.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 450 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQEVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWGSDYSKVQEVEVPEDf 529
Cdd:COG2319    42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATGLLLRTLTGHT- 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 530 GPVRTVA-EGRGDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSETHQPVWS- 606
Cdd:COG2319   121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 607 RSIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTDTRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 686
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 687 KVSRLGkcsGHSSFITHLDWAQDSTCFVTNSGDYEILYWDAATCKQITSADtvrnvqwatatcvlgfgvfgiwpegADGT 766
Cdd:COG2319   280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2447069188 767 DINAVARSHDGNLLVSADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMVLtTGGKDTSVLQWRVA 841
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRTLA-SGSADGTVRLWDLA 402
WD40 COG2319
WD40 repeat [General function prediction only];
370-729 3.26e-35

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 138.89  E-value: 3.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 370 AVDESNDHVLSVWDWAKESKVVDSKCSNEAVLVATFHPTDPNLLITCGKSHIYFWSLEGGnlsKRQGLFEKHEKPkyVLC 449
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG---LLLRTLTGHTGA--VRS 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 450 VTFLEGGD-VVTGDSGGNLYVWGKGGNRITQeVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWGSDYSKVQEVeVPED 528
Cdd:COG2319   126 VAFSPDGKtLASGSADGTVRLWDLATGKLLR-TLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTGH 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 529 FGPVRTVAEGR-GDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSETHQPVWS 606
Cdd:COG2319   204 TGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTlTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRT 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 607 -RSIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTDTRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQGG 685
Cdd:COG2319   284 lTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATGE 363
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2447069188 686 rkvsRLGKCSGHSSFITHLDWAQDSTCFVTNSGDYEILYWDAAT 729
Cdd:COG2319   364 ----LLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
548-841 1.05e-25

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 110.39  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 548 TRNSILLGSVHTGFSLLVQGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSETHQPVWSRSI-EDPARSAGFHPSGSVLA 626
Cdd:COG2319    15 DLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGhTAAVLSVAFSPDGRLLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 627 VGTVTGRWLLLDTDTRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQgGRKVSRLgkcSGHSSFITHLDW 706
Cdd:COG2319    95 SASADGTVRLWDLATGLLLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLAT-GKLLRTL---TGHSGAVTSVAF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 707 AQDSTCFVTNSGDYEILYWDAATCKQITS----ADTVRNVQWAT-----ATCVLGFGVfGIW---------PEGADGTDI 768
Cdd:COG2319   171 SPDGKLLASGSDDGTVRLWDLATGKLLRTltghTGAVRSVAFSPdgkllASGSADGTV-RLWdlatgkllrTLTGHSGSV 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2447069188 769 NAVARSHDGNLLVSADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFLWDDSMVLtTGGKDTSVLQWRVA 841
Cdd:COG2319   250 RSVAFSPDGRLLASGSADGTVRLWDL---ATGELLRTLTGHSGGVNSVAFSPDGKLLA-SGSDDGTVRLWDLA 318
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
59-106 3.18e-25

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: 98.74  E-value: 3.18e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2447069188  59 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAALRAR 106
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
400-726 8.37e-25

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: 105.49  E-value: 8.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 400 VLVATFHPtDPNLLITCGKSH-IYFWSLEGGNLSKRqglFEKHEKPkyVLCVTFLEGGD-VVTGDSGGNLYVWGKGGNRI 477
Cdd:cd00200    12 VTCVAFSP-DGKLLATGSGDGtIKVWDLETGELLRT---LKGHTGP--VRDVAASADGTyLASGSSDKTIRLWDLETGEC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 478 TQEVLGaHDGGVFALCALRDGTLVSGGGRDRRVVLWgsdyskvqevevpeDFGPVRTVAEGRGdtlyvgttrnsillgsv 557
Cdd:cd00200    86 VRTLTG-HTSYVSSVAFSPDGRILSSSSRDKTIKVW--------------DVETGKCLTTLRG----------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 558 HTGFsllvqghveeLWGLATHPSRAQFVSCGQDKLVHLWSSETHQPVWSRSI-EDPARSAGFHPSGSVLAVGTVTGRWLL 636
Cdd:cd00200   134 HTDW----------VNSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSSSDGTIKL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 637 LDTDTRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQGgrkvSRLGKCSGHSSFITHLDWAQDSTCFVTN 716
Cdd:cd00200   204 WDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG----ECVQTLSGHTNSVTSLAWSPDGKRLASG 279
                         330
                  ....*....|
gi 2447069188 717 SGDYEILYWD 726
Cdd:cd00200   280 SADGTIRIWD 289
WD40 COG2319
WD40 repeat [General function prediction only];
288-600 1.79e-24

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 106.92  E-value: 1.79e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 288 QRQRHYLGHNDDIKCLAVHPDMVTIATGQVAGTtkegkplpphVRVWDSVSLSTLHVLGLGvfDRAVCCVAFSkSNGGNL 367
Cdd:COG2319   111 LLLRTLTGHTGAVRSVAFSPDGKTLASGSADGT----------VRLWDLATGKLLRTLTGH--SGAVTSVAFS-PDGKLL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 368 LCAvdeSNDHVLSVWDWAKESKVVDSKCSNEAVLVATFHPtDPNLLITCGKSH-IYFWSLEGGnlsKRQGLFEKHEKPky 446
Cdd:COG2319   178 ASG---SDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSP-DGKLLASGSADGtVRLWDLATG---KLLRTLTGHSGS-- 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 447 VLCVTFLEGGD-VVTGDSGGNLYVWGKGGNRITQeVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWgsDYSKVQEVEV 525
Cdd:COG2319   249 VRSVAFSPDGRlLASGSADGTVRLWDLATGELLR-TLTGHSGGVNSVAFSPDGKLLASGSDDGTVRLW--DLATGKLLRT 325
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2447069188 526 PEDF-GPVRTVA-EGRGDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSET 600
Cdd:COG2319   326 LTGHtGAVRSVAfSPDGKTLASGSDDGTVRLWDLATGELLRTlTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
291-597 5.74e-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: 5.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 291 RHYLGHNDDIKCLAVHPDMVTIATGQVAGTtkegkplpphVRVWDSVSLSTLHVL-GLGVFDRAVCCVAFSKSnggnLLC 369
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT----------IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 370 AvdeSNDHVLSVWDWAKESKVVDSKCSNEAVLVATFHPTDPnLLITCGKSH-IYFWSLEGGNLSKRqglFEKHEKPkyVL 448
Cdd:cd00200    69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSPDGR-ILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 449 CVTFLEGGDVVTGDSG-GNLYVW-GKGGNRITqeVLGAHDGGVFALCALRDGTLVSGGGRDRRVVLWgsDYSKVQEVEVP 526
Cdd:cd00200   140 SVAFSPDGTFVASSSQdGTIKLWdLRTGKCVA--TLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTL 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2447069188 527 EDF-GPVRTVA-EGRGDTLYVGTTRNSILLGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVSCGQDKLVHLWS 597
Cdd:cd00200   216 RGHeNGVNSVAfSPDGYLLASGSEDGTIRVWDLRTGECVQTlSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
565-839 4.49e-20

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


Pssm-ID: 238121 [Multi-domain]  Cd Length: 289  Bit Score: 91.24  E-value: 4.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 565 VQGHVEELWGLATHPSRAQFVSCGQDKLVHLWSSETHQP---------------------------------VWSRSIED 611
Cdd:cd00200     5 LKGHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELlrtlkghtgpvrdvaasadgtylasgssdktirLWDLETGE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 612 PAR----------SAGFHPSGSVLAVGTVTGRWLLLDTDTRDLVAI---HTDGneqISVVSFSPDGAYLAVGSHDNLVYV 678
Cdd:cd00200    85 CVRtltghtsyvsSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTlrgHTDW---VNSVAFSPDGTFVASSSQDGTIKL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 679 YTVDQGgrkvSRLGKCSGHSSFITHLDWAQDSTCFVTNSGDYEILYWDAATCKQItsadtvrnvqwatATCVlGFGVFgi 758
Cdd:cd00200   162 WDLRTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL-------------GTLR-GHENG-- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 759 wpegadgtdINAVARSHDGNLLVSADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFlWDDSMVLTTGGKDTSVLQW 838
Cdd:cd00200   222 ---------VNSVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIW 288

                  .
gi 2447069188 839 R 839
Cdd:cd00200   289 D 289
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
49-103 7.12e-20

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: 84.00  E-value: 7.12e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2447069188  49 NDDNLSGTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAAL 103
Cdd:cd21947     1 NDDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAML 55
WD40 COG2319
WD40 repeat [General function prediction only];
575-841 1.51e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 85.73  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 575 LATHPSRAQFVSCGQDKLVHLWSSETHQPVWSRSIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTDTRDLVAIHTDGNEQ 654
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 655 ISVVSFSPDGAYLAVGSHDNLVYVYTVDQGGrkvsRLGKCSGHSSFITHLDWAQDSTCFVTNSGDYEILYWDAATCKQIT 734
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGTVRLWDLATGL----LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 735 S----ADTVRNVQW-------ATATcvlGFGVFGIWpEGADGT----------DINAVARSHDGNLLVSADDFGKVHLFS 793
Cdd:COG2319   157 TltghSGAVTSVAFspdgkllASGS---DDGTVRLW-DLATGKllrtltghtgAVRSVAFSPDGKLLASGSADGTVRLWD 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2447069188 794 ypcCQPRALSHKYGGHSSHVTNVAFLwDDSMVLTTGGKDTSVLQWRVA 841
Cdd:COG2319   233 ---LATGKLLRTLTGHSGSVRSVAFS-PDGRLLASGSADGTVRLWDLA 276
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
48-104 5.12e-17

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: 75.79  E-value: 5.12e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2447069188  48 CNDDNLSGTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAALR 104
Cdd:cd21950     2 SLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVK 58
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
610-840 9.55e-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: 78.53  E-value: 9.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 610 EDPARSAGFHPSGSVLAVGTVTGRWLLLDTDTRDLVA---IHTDGneqISVVSFSPDGAYLAVGSHDNLVYVYTVdQGGR 686
Cdd:cd00200     9 TGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRtlkGHTGP---VRDVAASADGTYLASGSSDKTIRLWDL-ETGE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 687 KVSRLGkcsGHSSFITHLDWAQDSTCFVTNSGDYEILYWDAATCKQITSA----DTVRNVQWATATcvlGFGVFGiwpeG 762
Cdd:cd00200    85 CVRTLT---GHTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTLrghtDWVNSVAFSPDG---TFVASS----S 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 763 ADGT--------------------DINAVARSHDGNLLVSADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDD 822
Cdd:cd00200   155 QDGTiklwdlrtgkcvatltghtgEVNSVAFSPDGEKLLSSSSDGTIKLWD---LSTGKCLGTLRGHENGVNSVAFSPDG 231
                         250
                  ....*....|....*...
gi 2447069188 823 SMvLTTGGKDTSVLQWRV 840
Cdd:cd00200   232 YL-LASGSEDGTIRVWDL 248
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
59-102 1.85e-15

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: 70.64  E-value: 1.85e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2447069188  59 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAA 102
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
55-99 2.65e-13

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: 64.66  E-value: 2.65e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2447069188  55 GTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQ 99
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
696-841 7.46e-07

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: 51.57  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2447069188 696 GHSSFITHLDWAQDSTCFVTNSGDYEILYWDAATCKQITSadtvrnvqwatatcvlgfgvfgiwPEGADGTdINAVARSH 775
Cdd:cd00200     7 GHTGGVTCVAFSPDGKLLATGSGDGTIKVWDLETGELLRT------------------------LKGHTGP-VRDVAASA 61
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2447069188 776 DGNLLVSADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFLWDDSMvLTTGGKDTSVLQWRVA 841
Cdd:cd00200    62 DGTYLASGSSDKTIRLWDL---ETGECVRTLTGHTSYVSSVAFSPDGRI-LSSSSRDKTIKVWDVE 123
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
641-679 6.80e-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: 34.98  E-value: 6.80e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2447069188  641 TRDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVY 679
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
691-726 7.00e-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: 34.98  E-value: 7.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2447069188  691 LGKCSGHSSFITHLDWAQDSTCFVTNSGDYEILYWD 726
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
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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