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Conserved domains on  [gi|300795605|ref|NP_001180198|]
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echinoderm microtubule-associated protein-like 2 isoform 3 [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 ...
 169-240 1.92e-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: 1.92e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795605  169 KMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSV 240
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
405-795 1.30e-34

WD40 repeat [General function prediction only];


:

Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 136.96  E-value: 1.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 405 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDySKLQEVEVPEDF 484
Cdd:COG2319   42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 485 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWS- 561
Cdd:COG2319  121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 562 RIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 641
Cdd:COG2319  201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 642 KVSRLGkcsGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADavrnmewatatcvlgfgvfgiwsegADGT 721
Cdd:COG2319  280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795605 722 DINAVARSHDGKLLASADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMaLTTGGKDTSVLQWRV 795
Cdd:COG2319  332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRT-LASGSADGTVRLWDL 401
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 13-60 3.01e-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: 3.01e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 300795605  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 ...
 246-552 1.52e-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: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 246 RHYLGHNDDIKCLAIHPDMVTIATGQVAGTtkegkplpphVRIWDSVSLSTLHVL-GLGVFDRAVCCVGFSKSnggnLLC 324
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT----------IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 325 AvdeSNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPtDPTVLITCGKSH-IYFWTLEGGSLSKRqglFEKHEKPkyVL 403
Cdd:cd00200   69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 404 CVTFLEGGDVVTGDSG-GNLYVW-GKGGNRItqAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWgsDYSKLQEVEVP 481
Cdd:cd00200  140 SVAFSPDGTFVASSSQdGTIKLWdLRTGKCV--ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTL 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795605 482 EDF-GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWS 552
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 ...
 169-240 1.92e-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: 1.92e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795605  169 KMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSV 240
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
405-795 1.30e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 136.96  E-value: 1.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 405 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDySKLQEVEVPEDF 484
Cdd:COG2319   42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 485 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWS- 561
Cdd:COG2319  121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 562 RIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 641
Cdd:COG2319  201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 642 KVSRLGkcsGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADavrnmewatatcvlgfgvfgiwsegADGT 721
Cdd:COG2319  280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795605 722 DINAVARSHDGKLLASADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMaLTTGGKDTSVLQWRV 795
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 ...
 485-794 1.37e-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: 107.42  E-value: 1.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 485 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLwsR 562
Cdd:cd00200   10 GGVTCVAfSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECV--R 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 563 II---EDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAI---HTDGneqISVVSFSPDGAYLAVGSHDNLVYVYTV 636
Cdd:cd00200   88 TLtghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTlrgHTDW---VNSVAFSPDGTFVASSSQDGTIKLWDL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 637 DQGgrkvSRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQItsadavrnmewatATCVlGFGVFgiwse 716
Cdd:cd00200  165 RTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL-------------GTLR-GHENG----- 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300795605 717 gadgtdINAVARSHDGKLLASADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFlWDDSMALTTGGKDTSVLQWR 794
Cdd:cd00200  222 ------VNSVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 13-60 3.01e-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: 3.01e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 300795605  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 ...
 246-552 1.52e-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: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 246 RHYLGHNDDIKCLAIHPDMVTIATGQVAGTtkegkplpphVRIWDSVSLSTLHVL-GLGVFDRAVCCVGFSKSnggnLLC 324
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT----------IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 325 AvdeSNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPtDPTVLITCGKSH-IYFWTLEGGSLSKRqglFEKHEKPkyVL 403
Cdd:cd00200   69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 404 CVTFLEGGDVVTGDSG-GNLYVW-GKGGNRItqAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWgsDYSKLQEVEVP 481
Cdd:cd00200  140 SVAFSPDGTFVASSSQdGTIKLWdLRTGKCV--ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTL 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795605 482 EDF-GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWS 552
Cdd:cd00200  216 RGHeNGVNSVAfSPDGYLLASGSEDGTIRVWDLRTGECVQTlSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
PTZ00421 PTZ00421
coronin; Provisional
 602-693 3.41e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.11  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 602 IHTDG-NEQISVVSFSPDGA-YLAVGSHDNLVYVYTVDQGgrKVSRLGKCsgHSSFITHLDWAQDSSCFVTNSGDYEILY 679
Cdd:PTZ00421 119 VHLQGhTKKVGIVSFHPSAMnVLASAGADMVVNVWDVERG--KAVEVIKC--HSDQITSLEWNLDGSLLCTTSKDKKLNI 194

                         90
                 ....*....|....
gi 300795605 680 WDPATCKQITSADA 693
Cdd:PTZ00421 195 IDPRDGTIVSSVEA 208
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 646-681 6.07e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 6.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 300795605   646 LGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWD 681
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 ...
 169-240 1.92e-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: 1.92e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300795605  169 KMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSV 240
Cdd:pfam03451   1 KMAIRGRPGAVYPPSNYYPKDDLDQKKEPPDKKLKLEWVYGYRGKDCRSNLYYLPTGEIVYFTAAVVVLYDV 72
WD40 COG2319
WD40 repeat [General function prediction only];
405-795 1.30e-34

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 136.96  E-value: 1.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 405 VTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDySKLQEVEVPEDF 484
Cdd:COG2319   42 LAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLA-TGLLLRTLTGHT 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 485 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWS- 561
Cdd:COG2319  121 GAVRSVAfSPDGKTLASGSADGTVRLWDLATGKLLRTlTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTl 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 562 RIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGR 641
Cdd:COG2319  201 TGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLATGKLLRTLTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLA-TGE 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 642 KVSRLGkcsGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADavrnmewatatcvlgfgvfgiwsegADGT 721
Cdd:COG2319  280 LLRTLT---GHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLT-------------------------GHTG 331

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795605 722 DINAVARSHDGKLLASADDFGKVHLFSypcCQPRALSHKYGGHSSHVTNVAFLWDDSMaLTTGGKDTSVLQWRV 795
Cdd:COG2319  332 AVRSVAFSPDGKTLASGSDDGTVRLWD---LATGELLRTLTGHTGAVTSVAFSPDGRT-LASGSADGTVRLWDL 401
WD40 COG2319
WD40 repeat [General function prediction only];
325-684 1.11e-33

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 134.27  E-value: 1.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 325 AVDESNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPTDPTVLITCGKSHIYFWTLEGGslsKRQGLFEKHEKPkyVLC 404
Cdd:COG2319   51 LAAGAGDLTLLLLDAAAGALLATLLGHTAAVLSVAFSPDGRLLASASADGTVRLWDLATG---LLLRTLTGHTGA--VRS 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 405 VTFLEGGD-VVTGDSGGNLYVWG-KGGNRItqAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDYSKLQEVeVPE 482
Cdd:COG2319  126 VAFSPDGKtLASGSADGTVRLWDlATGKLL--RTLTGHSGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRT-LTG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 483 DFGPVRTVAEGH-GDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLW 560
Cdd:COG2319  203 HTGAVRSVAFSPdGKLLASGSADGTVRLWDLATGKLLRTlTGHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLR 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 561 S-RIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQG 639
Cdd:COG2319  283 TlTGHSGGVNSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKTLASGSDDGTVRLWDLATG 362

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 300795605 640 GrkvsRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPAT 684
Cdd:COG2319  363 E----LLRTLTGHTGAVTSVAFSPDGRTLASGSADGTVRLWDLAT 403
WD40 COG2319
WD40 repeat [General function prediction only];
407-795 1.14e-30

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 125.02  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 407 FLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDYSKLQEVEVPEDFGP 486
Cdd:COG2319    2 LSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 487 VRTVAEGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWS-RII 564
Cdd:COG2319   82 LSVAFSPDGRLLASASADGTVRLWDLATGLLLRTlTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLRTlTGH 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 565 EDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDqGGRKVS 644
Cdd:COG2319  162 SGAVTSVAFSPDGKLLASGSDDGTVRLWDLATGKLLRTLTGHTGAVRSVAFSPDGKLLASGSADGTVRLWDLA-TGKLLR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 645 RLGkcsGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADAvrnmewatatcvlgfgvfgiwsegaDGTDIN 724
Cdd:COG2319  241 TLT---GHSGSVRSVAFSPDGRLLASGSADGTVRLWDLATGELLRTLTG-------------------------HSGGVN 292

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795605 725 AVARSHDGKLLASADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFLWDDSMALtTGGKDTSVLQWRV 795
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 ...
 485-794 1.37e-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: 107.42  E-value: 1.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 485 GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLwsR 562
Cdd:cd00200   10 GGVTCVAfSPDGKLLATGSGDGTIKVWDLETGELLRTlKGHTGPVRDVAASADGTYLASGSSDKTIRLWDLETGECV--R 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 563 II---EDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAI---HTDGneqISVVSFSPDGAYLAVGSHDNLVYVYTV 636
Cdd:cd00200   88 TLtghTSYVSSVAFSPDGRILSSSSRDKTIKVWDVETGKCLTTlrgHTDW---VNSVAFSPDGTFVASSSQDGTIKLWDL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 637 DQGgrkvSRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQItsadavrnmewatATCVlGFGVFgiwse 716
Cdd:cd00200  165 RTG----KCVATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLWDLSTGKCL-------------GTLR-GHENG----- 221

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300795605 717 gadgtdINAVARSHDGKLLASADDFGKVHLFSYpccQPRALSHKYGGHSSHVTNVAFlWDDSMALTTGGKDTSVLQWR 794
Cdd:cd00200  222 ------VNSVAFSPDGYLLASGSEDGTIRVWDL---RTGECVQTLSGHTNSVTSLAW-SPDGKRLASGSADGTIRIWD 289
TD_EMAP2 cd21948
trimerization domain of echinoderm microtubule-associated protein-like 2; Echinoderm ...
 13-60 3.01e-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: 3.01e-25
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 300795605  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 ...
 246-552 1.52e-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: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 246 RHYLGHNDDIKCLAIHPDMVTIATGQVAGTtkegkplpphVRIWDSVSLSTLHVL-GLGVFDRAVCCVGFSKSnggnLLC 324
Cdd:cd00200    3 RTLKGHTGGVTCVAFSPDGKLLATGSGDGT----------IKVWDLETGELLRTLkGHTGPVRDVAASADGTY----LAS 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 325 AvdeSNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPtDPTVLITCGKSH-IYFWTLEGGSLSKRqglFEKHEKPkyVL 403
Cdd:cd00200   69 G---SSDKTIRLWDLETGECVRTLTGHTSYVSSVAFSP-DGRILSSSSRDKtIKVWDVETGKCLTT---LRGHTDW--VN 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 404 CVTFLEGGDVVTGDSG-GNLYVW-GKGGNRItqAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWgsDYSKLQEVEVP 481
Cdd:cd00200  140 SVAFSPDGTFVASSSQdGTIKLWdLRTGKCV--ATLTGHTGEVNSVAFSPDGEKLLSSSSDGTIKLW--DLSTGKCLGTL 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795605 482 EDF-GPVRTVA-EGHGDTLYVGTTRNSILQGSVHTGFSLLV-QGHVEELWGLATHPSRAQFVTCGQDKLVHLWS 552
Cdd:cd00200  216 RGHeNGVNSVAfSPDGYLLASGSEDGTIRVWDLRTGECVQTlSGHTNSVTSLAWSPDGKRLASGSADGTIRIWD 289
WD40 cd00200
WD40 domain, found in a number of eukaryotic proteins that cover a wide variety of functions ...
 348-681 9.12e-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: 9.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 348 VKCSNEAVLVATFHPtDPTVLITCGKSH-IYFWTLEGGSLSKRqglFEKHEKPkyVLCVTFLEGGD-VVTGDSGGNLYVW 425
Cdd:cd00200    5 LKGHTGGVTCVAFSP-DGKLLATGSGDGtIKVWDLETGELLRT---LKGHTGP--VRDVAASADGTyLASGSSDKTIRLW 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 426 GKGGNRITQaVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWgsdysklqevEVPEdfGPVRTVAEGHGDTLyvgttrn 505
Cdd:cd00200   79 DLETGECVR-TLTGHTSYVSSVAFSPDGRILSSSSRDKTIKVW----------DVET--GKCLTTLRGHTDWV------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 506 silqgsvhtgfsllvqghveelWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWSRII-EDPARSAGFHPSGSVLAVGT 584
Cdd:cd00200  139 ----------------------NSVAFSPDGTFVASSSQDGTIKLWDLRTGKCVATLTGhTGEVNSVAFSPDGEKLLSSS 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 585 VTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQGgrkvSRLGKCSGHSSFITHLDWAQD 664
Cdd:cd00200  197 SDGTIKLWDLSTGKCLGTLRGHENGVNSVAFSPDGYLLASGSEDGTIRVWDLRTG----ECVQTLSGHTNSVTSLAWSPD 272

                        330
                 ....*....|....*..
gi 300795605 665 SSCFVTNSGDYEILYWD 681
Cdd:cd00200  273 GKRLASGSADGTIRIWD 289
TD_EMAP1 cd21947
trimerization domain of echinoderm microtubule-associated protein-like 1; Echinoderm ...
 4-57 6.27e-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: 6.27e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300795605   4 DDNLSGTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAAL 57
Cdd:cd21947    2 DDSASAASSMEVTDRIASLEQRVQMQEDEIQLLKSALADVVRRLNISEEQQAML 55
WD40 COG2319
WD40 repeat [General function prediction only];
530-795 1.08e-17

WD40 repeat [General function prediction only];


Pssm-ID: 441893 [Multi-domain]  Cd Length: 403  Bit Score: 86.12  E-value: 1.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 530 LATHPSRAQFVTCGQDKLVHLWSSDSHQPLWSRIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQ 609
Cdd:COG2319    1 ALSADGAALAAASADLALALLAAALGALLLLLLGLAAAVASLAASPDGARLAAGAGDLTLLLLDAAAGALLATLLGHTAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 610 ISVVSFSPDGAYLAVGSHDNLVYVYTVDQGGrkvsRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQIT 689
Cdd:COG2319   81 VLSVAFSPDGRLLASASADGTVRLWDLATGL----LLRTLTGHTGAVRSVAFSPDGKTLASGSADGTVRLWDLATGKLLR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 690 S----ADAVRNMEW-------ATATcvlGFGVFGIWS----------EGADGTdINAVARSHDGKLLASADDFGKVHLFS 748
Cdd:COG2319  157 TltghSGAVTSVAFspdgkllASGS---DDGTVRLWDlatgkllrtlTGHTGA-VRSVAFSPDGKLLASGSADGTVRLWD 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 300795605 749 ypcCQPRALSHKYGGHSSHVTNVAFLwDDSMALTTGGKDTSVLQWRV 795
Cdd:COG2319  233 ---LATGKLLRTLTGHSGSVRSVAFS-PDGRLLASGSADGTVRLWDL 275
TD_EMAP4 cd21950
trimerization domain of echinoderm microtubule-associated protein-like 4; Echinoderm ...
 2-58 8.77e-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: 8.77e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795605   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 300795605  13 MEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQGAA 56
Cdd:cd21931    1 EDLRDRVADLEKKVQDQEDEIVCLKSTLADVLRRLNQLETRSSS 44
TD_EMAP3 cd21949
trimerization domain of echinoderm microtubule-associated protein-like 3; Echinoderm ...
 9-53 2.01e-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: 2.01e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 300795605   9 GTSGMEVDDRVSALEQRLQLQEDELAVLKAALADALRRLRACEEQ 53
Cdd:cd21949    1 GPGSGEAPDPLAPLEQRLRTQEEEIALLKAALADALRRLGLYEQQ 45
PTZ00421 PTZ00421
coronin; Provisional
 602-693 3.41e-04

coronin; Provisional


Pssm-ID: 173611 [Multi-domain]  Cd Length: 493  Bit Score: 44.11  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795605 602 IHTDG-NEQISVVSFSPDGA-YLAVGSHDNLVYVYTVDQGgrKVSRLGKCsgHSSFITHLDWAQDSSCFVTNSGDYEILY 679
Cdd:PTZ00421 119 VHLQGhTKKVGIVSFHPSAMnVLASAGADMVVNVWDVERG--KAVEVIKC--HSDQITSLEWNLDGSLLCTTSKDKKLNI 194

                         90
                 ....*....|....
gi 300795605 680 WDPATCKQITSADA 693
Cdd:PTZ00421 195 IDPRDGTIVSSVEA 208
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 646-681 6.07e-03

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


Pssm-ID: 197651 [Multi-domain]  Cd Length: 40  Bit Score: 35.37  E-value: 6.07e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 300795605   646 LGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWD 681
Cdd:smart00320   5 LKTLKGHTGPVTSVAFSPDGKYLASGSDDGTIKLWD 40
WD40 smart00320
WD40 repeats; Note that these repeats are permuted with respect to the structural repeats ...
 596-634 8.32e-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: 8.32e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 300795605   596 THDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVY 634
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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