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Conserved domains on  [gi|1200742181|ref|NP_001338982|]
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echinoderm microtubule-associated protein-like 2 isoform 6 [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 ...
 168-239 1.91e-38

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: 136.91  E-value: 1.91e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1200742181 168 KMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSV 239
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
404-794 1.24e-34

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 136.96  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 404 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDySKLQEVEVPEDF 483
Cdd:COG2319    42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 484 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWS- 560
Cdd:COG2319   121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 561 RIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 640
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 641 KVSRLGkcsGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADavrnmewatatcvlgfgvfgiwsegADGT 720
Cdd:COG2319   280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1200742181 721 DINAVARSHDGKLLASADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMaLTTGGKDTSVLQWRV 794
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRT-LASGSADGTVRLWDL 401
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 13-60 3.00e-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: 3.00e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1200742181  13 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAALRAR 60
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 super family cl29593
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 245-551 1.44e-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.


The actual alignment was detected with superfamily member cd00200:

Pssm-ID: 475233 [Multi-domain]  Cd Length: 289  Bit Score: 101.64  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 245 RHYLGHNDDIKCLAIHPDMVTIATGQVAGTtkegkplpphVRIWDSVSLSTLHVL-GLGVFDRAVCCVGFSKSnggnLLC 323
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT----------IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 324 AvdeSNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPtDPTVLITCGKSH-IYFWTLEGGSLSKRqglFEKHEKPkyVL 402
Cdd:cd00200    69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 403 CVTFLEGGDVVTGDSG-GNLYVW-GKGGNRItqAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWgsDYSKLQEVEVP 480
Cdd:cd00200   140 SVAFSPDGTFVASSSQdGTIKLWdLRTGKCV--ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTL 215

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1200742181 481 EDF-GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWS 551
Cdd:cd00200   216 RGHeNGVNSVAfSPDGYLLASGSEDGTIRVWDLRTGECVQTlSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 168-239 1.91e-38

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: 136.91  E-value: 1.91e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1200742181 168 KMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSV 239
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
404-794 1.24e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 136.96  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 404 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDySKLQEVEVPEDF 483
Cdd:COG2319    42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 484 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWS- 560
Cdd:COG2319   121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 561 RIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 640
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 641 KVSRLGkcsGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADavrnmewatatcvlgfgvfgiwsegADGT 720
Cdd:COG2319   280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1200742181 721 DINAVARSHDGKLLASADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMaLTTGGKDTSVLQWRV 794
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRT-LASGSADGTVRLWDL 401
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 484-793 1.26e-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: 107.81  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 484 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLwsR 561
Cdd:cd00200    10 GGVTCVAfSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECV--R 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 562 II---EDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAI---HTDGneqISVVSFSPDGAYLAVGSHDNLVYVYTV 635
Cdd:cd00200    88 TLtghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTlrgHTDW---VNSVAFSPDGTFVASSSQDGTIKLWDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 636 DQGgrkvSRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQItsadavrnmewatATCVlGFGVFgiwse 715
Cdd:cd00200   165 RTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL-------------GTLR-GHENG----- 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1200742181 716 gadgtdINAVARSHDGKLLASADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFlWDDSMALTTGGKDTSVLQWR 793
Cdd:cd00200   222 ------VNSVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 13-60 3.00e-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: 3.00e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1200742181  13 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAALRAR 60
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 245-551 1.44e-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: 101.64  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 245 RHYLGHNDDIKCLAIHPDMVTIATGQVAGTtkegkplpphVRIWDSVSLSTLHVL-GLGVFDRAVCCVGFSKSnggnLLC 323
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT----------IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 324 AvdeSNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPtDPTVLITCGKSH-IYFWTLEGGSLSKRqglFEKHEKPkyVL 402
Cdd:cd00200    69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 403 CVTFLEGGDVVTGDSG-GNLYVW-GKGGNRItqAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWgsDYSKLQEVEVP 480
Cdd:cd00200   140 SVAFSPDGTFVASSSQdGTIKLWdLRTGKCV--ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTL 215

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1200742181 481 EDF-GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWS 551
Cdd:cd00200   216 RGHeNGVNSVAfSPDGYLLASGSEDGTIRVWDLRTGECVQTlSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
PTZ00421 PTZ00421
coronin; Provisional
 601-692 3.32e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.11  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 601 IHTDG-NEQISVVSFSPDGA-YLAVGSHDNLVYVYTVDQGgrKVSRLGKCsgHSSFITHLDWAQDSSCFVTNSGDYEILY 678
Cdd:PTZ00421  119 VHLQGhTKKVGIVSFHPSAMnVLASAGADMVVNVWDVERG--KAVEVIKC--HSDQITSLEWNLDGSLLCTTSKDKKLNI 194

                          90
                  ....*....|....
gi 1200742181 679 WDPATCKQITSADA 692
Cdd:PTZ00421  195 IDPRDGTIVSSVEA 208
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 645-680 6.12e-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: 6.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1200742181  645 LGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWD 680
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
 
Name Accession Description Interval E-value
HELP pfam03451
HELP motif; The founding member of the EMAP protein family is the 75 kDa Echinoderm ...
 168-239 1.91e-38

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: 136.91  E-value: 1.91e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1200742181 168 KMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSV 239
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
404-794 1.24e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 136.96  E-value: 1.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 404 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDySKLQEVEVPEDF 483
Cdd:COG2319    42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 484 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWS- 560
Cdd:COG2319   121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 561 RIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 640
Cdd:COG2319   201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 641 KVSRLGkcsGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADavrnmewatatcvlgfgvfgiwsegADGT 720
Cdd:COG2319   280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1200742181 721 DINAVARSHDGKLLASADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMaLTTGGKDTSVLQWRV 794
Cdd:COG2319   332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRT-LASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
324-683 1.05e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 134.27  E-value: 1.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 324 AVDESNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPTDPTVLITCGKSHIYFWTLEGGslsKRQGLFEKHEKPkyVLC 403
Cdd:COG2319    51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG---LLLRTLTGHTGA--VRS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 404 VTFLEGGD-VVTGDSGGNLYVWG-KGGNRItqAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDYSKLQEVeVPE 481
Cdd:COG2319   126 VAFSPDGKtLASGSADGTVRLWDlATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTG 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 482 DFGPVRTVAEGH-GDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLW 559
Cdd:COG2319   203 HTGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTlTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 560 S-RIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQG 638
Cdd:COG2319   283 TlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1200742181 639 GrkvsRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPAT 683
Cdd:COG2319   363 E----LLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
406-794 1.10e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.41  E-value: 1.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 406 FLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDYSKLQEVEVPEDFGP 485
Cdd:COG2319     2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 486 VRTVAEGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWS-RII 563
Cdd:COG2319    82 LSVAFSPDGRLLASASADGTVRLWDLATGLLLRTlTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 564 EDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGRKVS 643
Cdd:COG2319   162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA-TGKLLR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 644 RLGkcsGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADAvrnmewatatcvlgfgvfgiwsegaDGTDIN 723
Cdd:COG2319   241 TLT---GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTG-------------------------HSGGVN 292

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1200742181 724 AVARSHDGKLLASADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFLWDDSMALtTGGKDTSVLQWRV 794
Cdd:COG2319   293 SVAFSPDGKLLASGSDDGTVRLWDL---ATGKLLRTLTGHTGAVRSVAFSPDGKTLA-SGSDDGTVRLWDL 359
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 484-793 1.26e-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: 107.81  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 484 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLwsR 561
Cdd:cd00200    10 GGVTCVAfSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECV--R 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 562 II---EDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAI---HTDGneqISVVSFSPDGAYLAVGSHDNLVYVYTV 635
Cdd:cd00200    88 TLtghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTlrgHTDW---VNSVAFSPDGTFVASSSQDGTIKLWDL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 636 DQGgrkvSRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQItsadavrnmewatATCVlGFGVFgiwse 715
Cdd:cd00200   165 RTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL-------------GTLR-GHENG----- 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1200742181 716 gadgtdINAVARSHDGKLLASADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFlWDDSMALTTGGKDTSVLQWR 793
Cdd:cd00200   222 ------VNSVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 13-60 3.00e-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: 3.00e-25
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1200742181  13 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAALRAR 60
Cdd:cd21948     1 MEVDDRISYLEQRLQLQEDEIQVLKAALADALRRLRVCEEQGAALRKR 48
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 245-551 1.44e-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: 101.64  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 245 RHYLGHNDDIKCLAIHPDMVTIATGQVAGTtkegkplpphVRIWDSVSLSTLHVL-GLGVFDRAVCCVGFSKSnggnLLC 323
Cdd:cd00200     3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT----------IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 324 AvdeSNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPtDPTVLITCGKSH-IYFWTLEGGSLSKRqglFEKHEKPkyVL 402
Cdd:cd00200    69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 403 CVTFLEGGDVVTGDSG-GNLYVW-GKGGNRItqAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWgsDYSKLQEVEVP 480
Cdd:cd00200   140 SVAFSPDGTFVASSSQdGTIKLWdLRTGKCV--ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTL 215

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1200742181 481 EDF-GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWS 551
Cdd:cd00200   216 RGHeNGVNSVAfSPDGYLLASGSEDGTIRVWDLRTGECVQTlSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 347-680 8.45e-22

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: 96.25  E-value: 8.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 347 VKCSNEAVLVATFHPtDPTVLITCGKSH-IYFWTLEGGSLSKRqglFEKHEKPkyVLCVTFLEGGD-VVTGDSGGNLYVW 424
Cdd:cd00200     5 LKGHTGGVTCVAFSP-DGKLLATGSGDGtIKVWDLETGELLRT---LKGHTGP--VRDVAASADGTyLASGSSDKTIRLW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 425 GKGGNRITQaVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWgsdysklqevEVPEdfGPVRTVAEGHGDTLyvgttrn 504
Cdd:cd00200    79 DLETGECVR-TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW----------DVET--GKCLTTLRGHTDWV------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 505 silqgsvhtgfsllvqghveelWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWSRII-EDPARSAGFHPSGSVLAVGT 583
Cdd:cd00200   139 ----------------------NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSS 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 584 VTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQGgrkvSRLGKCSGHSSFITHLDWAQD 663
Cdd:cd00200   197 SDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG----ECVQTLSGHTNSVTSLAWSPD 272

                         330
                  ....*....|....*..
gi 1200742181 664 SSCFVTNSGDYEILYWD 680
Cdd:cd00200   273 GKRLASGSADGTIRIWD 289
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 4-57 6.26e-19

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: 80.92  E-value: 6.26e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1200742181   4 DDNLSGTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAAL 57
Cdd:cd21947     2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAML 55
WD40 COG2319
WD40 repeat [General function prediction only];
529-794 1.07e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.12  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 529 LATHPSRAQFVTCGQDKLVHLWSSDSHQPLWSRIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQ 608
Cdd:COG2319     1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 609 ISVVSFSPDGAYLAVGSHDNLVYVYTVDQGGrkvsRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQIT 688
Cdd:COG2319    81 VLSVAFSPDGRLLASASADGTVRLWDLATGL----LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 689 S----ADAVRNMEW-------ATATcvlGFGVFGIWS----------EGADGTdINAVARSHDGKLLASADDFGKVHLFS 747
Cdd:COG2319   157 TltghSGAVTSVAFspdgkllASGS---DDGTVRLWDlatgkllrtlTGHTGA-VRSVAFSPDGKLLASGSADGTVRLWD 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1200742181 748 ypcCQPRALSHKYGGHSSHVTNVAFLwDDSMALTTGGKDTSVLQWRV 794
Cdd:COG2319   233 ---LATGKLLRTLTGHSGSVRSVAFS-PDGRLLASGSADGTVRLWDL 275
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 2-58 8.03e-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: 75.02  E-value: 8.03e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1200742181   2 SLDDNLSGTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAALR 58
Cdd:cd21950     2 SLDDSISAASTSDVQDRLSALELRVQQQEDEITVLKAALADVLRRLAISEDSVASVK 58
TD_EMAP-like cd21931
trimerization domain of the echinoderm microtubule-associated protein-like family; The ...
 13-56 1.48e-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: 71.03  E-value: 1.48e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1200742181  13 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAA 56
Cdd:cd21931     1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 9-53 2.00e-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: 65.04  E-value: 2.00e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1200742181   9 GTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQ 53
Cdd:cd21949     1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
PTZ00421 PTZ00421
coronin; Provisional
 601-692 3.32e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.11  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1200742181 601 IHTDG-NEQISVVSFSPDGA-YLAVGSHDNLVYVYTVDQGgrKVSRLGKCsgHSSFITHLDWAQDSSCFVTNSGDYEILY 678
Cdd:PTZ00421  119 VHLQGhTKKVGIVSFHPSAMnVLASAGADMVVNVWDVERG--KAVEVIKC--HSDQITSLEWNLDGSLLCTTSKDKKLNI 194

                          90
                  ....*....|....
gi 1200742181 679 WDPATCKQITSADA 692
Cdd:PTZ00421  195 IDPRDGTIVSSVEA 208
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 645-680 6.12e-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: 6.12e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1200742181  645 LGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWD 680
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 595-633 8.31e-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: 8.31e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1200742181  595 THDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVY 633
Cdd:smart00320   1 SGELLKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLW 39
 
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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